http://173.199.123.204/Cysteinome/api.php?action=feedcontributions&feedformat=atom&user=Wu3857Cysteinome - User contributions [en]2026-06-04T21:51:36ZUser contributionsMediaWiki 1.30.0http://173.199.123.204/Cysteinome/index.php?title=Cysteinome:About&diff=2239Cysteinome:About2023-09-30T03:01:02Z<p>Wu3857: </p>
<hr />
<div>The covalent modification of intrinsically nucleophilic cysteine in proteins is crucial for diverse biochemical events. Bioinformatics approaches may prove useful in the design and discovery of covalent molecules targeting the cysteine in proteins to tune their functions and activities. <br/><br />
<br />
'''Cysteinome''', the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators. In this database it compiles over '''400 proteins''' with targetable cysteine along with more than '''1200 covalent modulators''' curated from existing literatures. Proteins are annotated with a detailed description of protein families, biological process and related diseases. In addition, covalent modulators are carefully annotated with chemical name, chemical structure, binding affinity, physicochemical properties, molecule type and related diseases etc.<br/><br />
<br />
The Cysteinome database serve as a useful platform for the identification of crucial proteins with targetable cysteine in certain cellular context. Furthermore, it may help biologists and chemists for the design and discovery of covalent chemical probes or inhibitors homing at functional cysteine of critical protein targets implicated in various physiological or disease process.<br/><br />
<br />
==Developers==<br />
'''Cysteinome''' is developed by Center for Molecular Medicine, School of Life Science and Biotechnology, Dalian University of Technology, China, and now maintained by Sijin Wu.<br/><br />
<br />
:'''Sijin Wu''', Ph.D. , Professor (Assistant) at Academy of Pharmacy, Xi'an Jiaotong-Liverpool University (Email: sijin.wu84 AT gmail.com).<br/><br />
:'''Yongliang Yang''', Ph.D. , Professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Cysteinome:About&diff=2238Cysteinome:About2023-09-30T03:00:26Z<p>Wu3857: </p>
<hr />
<div>The covalent modification of intrinsically nucleophilic cysteine in proteins is crucial for diverse biochemical events. Bioinformatics approaches may prove useful in the design and discovery of covalent molecules targeting the cysteine in proteins to tune their functions and activities. <br/><br />
<br />
'''Cysteinome''', the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators. In this database it compiles over '''400 proteins''' with targetable cysteine along with more than '''1200 covalent modulators''' curated from existing literatures. Proteins are annotated with a detailed description of protein families, biological process and related diseases. In addition, covalent modulators are carefully annotated with chemical name, chemical structure, binding affinity, physicochemical properties, molecule type and related diseases etc.<br/><br />
<br />
The Cysteinome database serve as a useful platform for the identification of crucial proteins with targetable cysteine in certain cellular context. Furthermore, it may help biologists and chemists for the design and discovery of covalent chemical probes or inhibitors homing at functional cysteine of critical protein targets implicated in various physiological or disease process.<br/><br />
<br />
==Developers==<br />
'''Cysteinome''' is developed by Center for Molecular Medicine, School of Life Science and Biotechnology, Dalian University of Technology, China, and now maintained by Sijin Wu.<br/><br />
<br />
:'''Sijin Wu''', Ph.D. , Professor (Assistant) at Xi'an Jiaotong-Liverpool University (Email: sijin.wu84 AT gmail.com).<br/><br />
:'''Yongliang Yang''', Ph.D. , Professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Cysteinome&diff=2237Cysteinome2021-04-14T01:35:03Z<p>Wu3857: /* Contact & citaion */</p>
<hr />
<div>__NOTOC__<br />
[[File:Mglogo-large2.png|center|750px]]<br />
<br />
'''Cysteine''' is an unique amino acid with the thiol side chain serving as an intrinsic nucleophile and often participating in various enzymatic reactions. In recent years, covalent probes or inhibitors homing at a cysteine thiol group present in the target proteins have attracted significant attention. But the lack of systematic information for proteins with targetable cysteine has hindered the design and discovery of covalent modulators of protein functions and activities. Therefore, a comprehensive database with an analysis system dedicated to proteins with targetable cysteine could be very useful.<br/><br />
'''Cysteinome''', the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for '''proteins with targetable cysteine''' residues as well as their covalent modulators. It could contribute to the understanding of how protein targets are covalently modified by chemical probes homing at cysteine residues and will serve as a useful resource for the design and development of covalent inhibitors.<br />
<br />
==Announcement==<br />
The old version cysteinome.org website is offline now. I am trying to recover the database by this Wiki site:<br />
:'''http://www.cysteinome.net/Cysteinome''' <br/><br />
<br />
==Category==<br />
<font size="3"><br />
*[[:Category:Targets|Targets]]<br />
:*[[:Category:Species|Species]]<br />
:*[[:Category:Pathway|Pathway]]<br />
:*[[:Category:Type|Function type]]<br />
:*[[:Category:Family|Protein Family/Domain]]<br />
*[[:Category:Ligands|Ligands]]<br />
:*[[:Category:Ligand type|Ligand type]]<br />
:*[[:Category:Bond type|Bond type]]<br />
:*[[:Category:Ligand list|Ligand list]]<br />
</font><br />
<br />
==Contact & citaion==<br />
If you have any question or suggestion, please feel free to connect me:<br />
:sijin_wu AT foxmail.com OR sijin.wu84 AT gmail.com<br />
<br />
And if you find Cysteinome useful, please consider citing the reference:<br/><br />
:'''Cysteinome: The first comprehensive database for proteins with targetable cysteine and their covalent inhibitors.''' Biochemical and biophysical research communications, 2016, 478(3): 1268-1273. [https://www.sciencedirect.com/science/article/pii/S0006291X16313651 Link]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Cysteinome&diff=2236Cysteinome2021-04-14T01:34:49Z<p>Wu3857: /* Contact & citaion */</p>
<hr />
<div>__NOTOC__<br />
[[File:Mglogo-large2.png|center|750px]]<br />
<br />
'''Cysteine''' is an unique amino acid with the thiol side chain serving as an intrinsic nucleophile and often participating in various enzymatic reactions. In recent years, covalent probes or inhibitors homing at a cysteine thiol group present in the target proteins have attracted significant attention. But the lack of systematic information for proteins with targetable cysteine has hindered the design and discovery of covalent modulators of protein functions and activities. Therefore, a comprehensive database with an analysis system dedicated to proteins with targetable cysteine could be very useful.<br/><br />
'''Cysteinome''', the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for '''proteins with targetable cysteine''' residues as well as their covalent modulators. It could contribute to the understanding of how protein targets are covalently modified by chemical probes homing at cysteine residues and will serve as a useful resource for the design and development of covalent inhibitors.<br />
<br />
==Announcement==<br />
The old version cysteinome.org website is offline now. I am trying to recover the database by this Wiki site:<br />
:'''http://www.cysteinome.net/Cysteinome''' <br/><br />
<br />
==Category==<br />
<font size="3"><br />
*[[:Category:Targets|Targets]]<br />
:*[[:Category:Species|Species]]<br />
:*[[:Category:Pathway|Pathway]]<br />
:*[[:Category:Type|Function type]]<br />
:*[[:Category:Family|Protein Family/Domain]]<br />
*[[:Category:Ligands|Ligands]]<br />
:*[[:Category:Ligand type|Ligand type]]<br />
:*[[:Category:Bond type|Bond type]]<br />
:*[[:Category:Ligand list|Ligand list]]<br />
</font><br />
<br />
==Contact & citaion==<br />
If you have any question or suggestion, please feel free to connect me:<br />
:sijin_wu AT foxmail.com OR sijin.wu84 AT gmail.com<br />
<br />
And if you find Cysteinome useful, please consider citing the reference:<br/><br />
:'''Cysteinome: The first comprehensive database for proteins with targetable cysteine and their covalent inhibitors [J].''' Biochemical and biophysical research communications, 2016, 478(3): 1268-1273. [https://www.sciencedirect.com/science/article/pii/S0006291X16313651 Link]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Cysteinome:About&diff=2235Cysteinome:About2021-01-10T14:48:16Z<p>Wu3857: </p>
<hr />
<div>The covalent modification of intrinsically nucleophilic cysteine in proteins is crucial for diverse biochemical events. Bioinformatics approaches may prove useful in the design and discovery of covalent molecules targeting the cysteine in proteins to tune their functions and activities. <br/><br />
<br />
'''Cysteinome''', the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators. In this database it compiles over '''400 proteins''' with targetable cysteine along with more than '''1200 covalent modulators''' curated from existing literatures. Proteins are annotated with a detailed description of protein families, biological process and related diseases. In addition, covalent modulators are carefully annotated with chemical name, chemical structure, binding affinity, physicochemical properties, molecule type and related diseases etc.<br/><br />
<br />
The Cysteinome database serve as a useful platform for the identification of crucial proteins with targetable cysteine in certain cellular context. Furthermore, it may help biologists and chemists for the design and discovery of covalent chemical probes or inhibitors homing at functional cysteine of critical protein targets implicated in various physiological or disease process.<br/><br />
<br />
==Developers==<br />
'''Cysteinome''' is developed by Center for Molecular Medicine, School of Life Science and Biotechnology, Dalian University of Technology, China, and now maintained by Sijin Wu.<br/><br />
<br />
:'''Sijin Wu''', Ph.D. , Associate professor at Dalian Institute of Chemical Physics, Chinese Academy of Sciences (Email: sijin.wu84 AT gmail.com).<br/><br />
:'''Yongliang Yang''', Ph.D. , Associate professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Cysteinome:About&diff=2234Cysteinome:About2021-01-10T14:45:28Z<p>Wu3857: </p>
<hr />
<div>The covalent modification of intrinsically nucleophilic cysteine in proteins is crucial for diverse biochemical events. Bioinformatics approaches may prove useful in the design and discovery of covalent molecules targeting the cysteine in proteins to tune their functions and activities. <br/><br />
<br />
'''Cysteinome''', the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators. In this database it compiles over '''400 proteins''' with targetable cysteine along with more than '''1200 covalent modulators''' curated from existing literatures. Proteins are annotated with a detailed description of protein families, biological process and related diseases. In addition, covalent modulators are carefully annotated with chemical name, chemical structure, binding affinity, physicochemical properties, molecule type and related diseases etc.<br/><br />
<br />
The Cysteinome database serve as a useful platform for the identification of crucial proteins with targetable cysteine in certain cellular context. Furthermore, it may help biologists and chemists for the design and discovery of covalent chemical probes or inhibitors homing at functional cysteine of critical protein targets implicated in various physiological or disease process.<br/><br />
<br />
==Developers==<br />
'''Cysteinome''' is developed by Center for Molecular Medicine, School of Life Science and Biotechnology, Dalian University of Technology, China, and now maintained by Sijin Wu at Dalian Institute of Chemical Physics, Chinese Academy of Sciences, China.<br/><br />
<br />
:'''Sijin Wu''', Ph.D. , Associate professor at Dalian Institute of Chemical Physics, Chinese Academy of Sciences (Email: sijin.wu84 AT gmail.com).<br/><br />
:'''Yongliang Yang''', Ph.D. , Associate professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Cysteinome:About&diff=2233Cysteinome:About2021-01-10T14:41:16Z<p>Wu3857: </p>
<hr />
<div>The covalent modification of intrinsically nucleophilic cysteine in proteins is crucial for diverse biochemical events. Bioinformatics approaches may prove useful in the design and discovery of covalent molecules targeting the cysteine in proteins to tune their functions and activities. <br/><br />
<br />
'''Cysteinome''', the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators. In this database it compiles over '''400 proteins''' with targetable cysteine along with more than '''1200 covalent modulators''' curated from existing literatures. Proteins are annotated with a detailed description of protein families, biological process and related diseases. In addition, covalent modulators are carefully annotated with chemical name, chemical structure, binding affinity, physicochemical properties, molecule type and related diseases etc.<br/><br />
<br />
The Cysteinome database serve as a useful platform for the identification of crucial proteins with targetable cysteine in certain cellular context. Furthermore, it may help biologists and chemists for the design and discovery of covalent chemical probes or inhibitors homing at functional cysteine of critical protein targets implicated in various physiological or disease process.<br/><br />
<br />
==Developers==<br />
'''Cysteinome''' is developed by Center for Molecular Medicine, School of Life Science and Biotechnology, Dalian University of Technology, China, and now maintained by Sijin Wu at Dalian Institute of Chemical Physics, Chinese Academy of Sciences, China.<br/><br />
<br />
:'''Sijin Wu''', Ph.D. , Postdoctoral researcher at Division of Medicinal Chemistry & Pharmacognosy, College of Pharmacy, OSU (Email: wu.3857 AT osu.edu).<br/><br />
:'''Yongliang Yang''', Ph.D. , Associate professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Cysteinome&diff=2232Cysteinome2020-10-19T01:28:28Z<p>Wu3857: /* Contact & citaion */</p>
<hr />
<div>__NOTOC__<br />
[[File:Mglogo-large2.png|center|750px]]<br />
<br />
'''Cysteine''' is an unique amino acid with the thiol side chain serving as an intrinsic nucleophile and often participating in various enzymatic reactions. In recent years, covalent probes or inhibitors homing at a cysteine thiol group present in the target proteins have attracted significant attention. But the lack of systematic information for proteins with targetable cysteine has hindered the design and discovery of covalent modulators of protein functions and activities. Therefore, a comprehensive database with an analysis system dedicated to proteins with targetable cysteine could be very useful.<br/><br />
'''Cysteinome''', the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for '''proteins with targetable cysteine''' residues as well as their covalent modulators. It could contribute to the understanding of how protein targets are covalently modified by chemical probes homing at cysteine residues and will serve as a useful resource for the design and development of covalent inhibitors.<br />
<br />
==Announcement==<br />
The old version cysteinome.org website is offline now. I am trying to recover the database by this Wiki site:<br />
:'''http://www.cysteinome.net/Cysteinome''' <br/><br />
<br />
==Category==<br />
<font size="3"><br />
*[[:Category:Targets|Targets]]<br />
:*[[:Category:Species|Species]]<br />
:*[[:Category:Pathway|Pathway]]<br />
:*[[:Category:Type|Function type]]<br />
:*[[:Category:Family|Protein Family/Domain]]<br />
*[[:Category:Ligands|Ligands]]<br />
:*[[:Category:Ligand type|Ligand type]]<br />
:*[[:Category:Bond type|Bond type]]<br />
:*[[:Category:Ligand list|Ligand list]]<br />
</font><br />
<br />
==Contact & citaion==<br />
If you have any question or suggestion, please feel free to connect me:<br />
:sijin_wu AT foxmail.com OR sijin.wu84 AT gmail.com<br />
<br />
And if you find Cysteinome useful, please consider citing the reference:<br/><br />
:'''Cysteinome: The first comprehensive database for proteins with targetable cysteine and their covalent inhibitors[J].''' Biochemical and biophysical research communications, 2016, 478(3): 1268-1273. [https://www.sciencedirect.com/science/article/pii/S0006291X16313651 Link]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:RNA_demethylase_ALKBH5&diff=2231Category:RNA demethylase ALKBH52020-05-26T20:09:39Z<p>Wu3857: Blanked the page</p>
<hr />
<div></div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2230RNA demethylase ALKBH52020-05-26T20:09:24Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
ALKBH5 belongs to the conserved AlkB family of non-heme Fe(II)/alpha-KG-dependent dioxygenases that repair N-alkylated nucleobases by oxidative demethylation. It could catalyze the demethylation of m6A of ssRNA. N6-Methyladenosine (m6A) is the most prevalent and abundant internal methylated nucleoside in mammalian mRNA and is also found in the RNA of plants and viruses. Mapping of m6A in human and mouse RNA identified that m6A modification happens mainly within the consensus sequence (G/A)(G/A)m6AC(A/C/U) in a non-stoichiometric manner with only three to five m6A sites observed per mRNA molecule.m6A sites are enriched near stop codons and in the 3'-UTR of mRNA. <br/><br />
<br />
ALKBH5 is localized to the nucleus, has 2OG and iron-dependent activity and is upregulated under hypoxic conditions by the hypoxia-inducible factor (HIF) transcription factor pathway. ALKBH5 was observed to be highly expressed in the lung, followed by testis, pancreas, spleen and ovary. It was also reported that ALKBH5 localized to nuclear speckles and that decreased ALKBH5 levels affect mRNA export and processing, leading to altered spermatogenesis. <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
<br />
* SASA:<br />
:Unkown<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:Alkb_family&diff=2229Category:Alkb family2020-05-26T20:09:03Z<p>Wu3857: </p>
<hr />
<div><br />
[[Category:2OG-Fe(II) oxygenase superfamily]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:2OG-Fe(II)_oxygenase_superfamily&diff=2228Category:2OG-Fe(II) oxygenase superfamily2020-05-26T20:08:53Z<p>Wu3857: Blanked the page</p>
<hr />
<div></div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:RNA_demethylase_ALKBH5&diff=2227Category:RNA demethylase ALKBH52020-05-25T17:20:53Z<p>Wu3857: Created page with "Category:Ligand list"</p>
<hr />
<div>[[Category:Ligand list]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2226RNA demethylase ALKBH52020-05-25T17:20:31Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
ALKBH5 belongs to the conserved AlkB family of non-heme Fe(II)/alpha-KG-dependent dioxygenases that repair N-alkylated nucleobases by oxidative demethylation. It could catalyze the demethylation of m6A of ssRNA. N6-Methyladenosine (m6A) is the most prevalent and abundant internal methylated nucleoside in mammalian mRNA and is also found in the RNA of plants and viruses. Mapping of m6A in human and mouse RNA identified that m6A modification happens mainly within the consensus sequence (G/A)(G/A)m6AC(A/C/U) in a non-stoichiometric manner with only three to five m6A sites observed per mRNA molecule.m6A sites are enriched near stop codons and in the 3'-UTR of mRNA. <br/><br />
<br />
ALKBH5 is localized to the nucleus, has 2OG and iron-dependent activity and is upregulated under hypoxic conditions by the hypoxia-inducible factor (HIF) transcription factor pathway. ALKBH5 was observed to be highly expressed in the lung, followed by testis, pancreas, spleen and ovary. It was also reported that ALKBH5 localized to nuclear speckles and that decreased ALKBH5 levels affect mRNA export and processing, leading to altered spermatogenesis. <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
<br />
* SASA:<br />
:Unkown<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2225RNA demethylase ALKBH52020-05-25T17:20:21Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
ALKBH5 belongs to the conserved AlkB family of non-heme Fe(II)/alpha-KG-dependent dioxygenases that repair N-alkylated nucleobases by oxidative demethylation. It could catalyze the demethylation of m6A of ssRNA. N6-Methyladenosine (m6A) is the most prevalent and abundant internal methylated nucleoside in mammalian mRNA and is also found in the RNA of plants and viruses. Mapping of m6A in human and mouse RNA identified that m6A modification happens mainly within the consensus sequence (G/A)(G/A)m6AC(A/C/U) in a non-stoichiometric manner with only three to five m6A sites observed per mRNA molecule.m6A sites are enriched near stop codons and in the 3'-UTR of mRNA. <br/><br/><br />
<br />
ALKBH5 is localized to the nucleus, has 2OG and iron-dependent activity and is upregulated under hypoxic conditions by the hypoxia-inducible factor (HIF) transcription factor pathway. ALKBH5 was observed to be highly expressed in the lung, followed by testis, pancreas, spleen and ovary. It was also reported that ALKBH5 localized to nuclear speckles and that decreased ALKBH5 levels affect mRNA export and processing, leading to altered spermatogenesis. <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
<br />
* SASA:<br />
:Unkown<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2224RNA demethylase ALKBH52020-05-25T17:20:11Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
ALKBH5 belongs to the conserved AlkB family of non-heme Fe(II)/alpha-KG-dependent dioxygenases that repair N-alkylated nucleobases by oxidative demethylation. It could catalyze the demethylation of m6A of ssRNA. N6-Methyladenosine (m6A) is the most prevalent and abundant internal methylated nucleoside in mammalian mRNA and is also found in the RNA of plants and viruses. Mapping of m6A in human and mouse RNA identified that m6A modification happens mainly within the consensus sequence (G/A)(G/A)m6AC(A/C/U) in a non-stoichiometric manner with only three to five m6A sites observed per mRNA molecule.m6A sites are enriched near stop codons and in the 3'-UTR of mRNA. <br/><br/><br />
<br />
ALKBH5 is localized to the nucleus, has 2OG and iron-dependent activity and is upregulated under hypoxic conditions by the hypoxia-inducible factor (HIF) transcription factor pathway. ALKBH5 was observed to be highly expressed in the lung, followed by testis, pancreas, spleen and ovary. It was also reported that ALKBH5 localized to nuclear speckles and that decreased ALKBH5 levels affect mRNA export and processing, leading to altered spermatogenesis. <br/> <br />
<br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
<br />
* SASA:<br />
:Unkown<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2223RNA demethylase ALKBH52020-05-25T17:19:51Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
ALKBH5 belongs to the conserved AlkB family of non-heme Fe(II)/alpha-KG-dependent dioxygenases that repair N-alkylated nucleobases by oxidative demethylation. It could catalyze the demethylation of m6A of ssRNA. N6-Methyladenosine (m6A) is the most prevalent and abundant internal methylated nucleoside in mammalian mRNA and is also found in the RNA of plants and viruses. Mapping of m6A in human and mouse RNA identified that m6A modification happens mainly within the consensus sequence (G/A)(G/A)m6AC(A/C/U) in a non-stoichiometric manner with only three to five m6A sites observed per mRNA molecule.m6A sites are enriched near stop codons and in the 3'-UTR ofmRNA <br/><br />
<br />
ALKBH5 is localized to the nucleus, has 2OG and iron-dependent activity and is upregulated under hypoxic conditions by the hypoxia-inducible factor (HIF) transcription factor pathway. ALKBH5 was observed to be highly expressed in the lung, followed by testis, pancreas, spleen and ovary. It was also reported that ALKBH5 localized to nuclear speckles and that decreased ALKBH5 levels affect mRNA export and processing, leading to altered spermatogenesis. <br/> <br />
<br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
<br />
* SASA:<br />
:Unkown<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2222RNA demethylase ALKBH52020-05-25T17:14:55Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
<br />
* SASA:<br />
:Unkown<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2221RNA demethylase ALKBH52020-05-25T17:13:45Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
:[[File:ALKBH5-hydro.png||600px]]<br />
* SASA:<br />
:Unkown<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
[[File:ALKBH5.png|center|800px]]<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2220RNA demethylase ALKBH52020-05-25T17:12:04Z<p>Wu3857: /* Reference */</p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
:[[File:ALKBH5-hydro.png||600px]]<br />
* SASA:<br />
:Cys200: ? A^2<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
[[File:ALKBH5.png|center|800px]]<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2219RNA demethylase ALKBH52020-05-25T17:11:41Z<p>Wu3857: /* Reference */</p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
:[[File:ALKBH5-hydro.png||600px]]<br />
* SASA:<br />
:Cys200: ? A^2<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
[[File:ALKBH5.png|center|800px]]<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119] <br/><br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2218RNA demethylase ALKBH52020-05-25T17:11:21Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
:[[File:ALKBH5-hydro.png||600px]]<br />
* SASA:<br />
:Cys200: ? A^2<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
[[File:ALKBH5.png|center|800px]]<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119] <br/><br />
<br />
<br />
[[Category:Homo sapiens]]<br />
[[Category:Targets]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2217RNA demethylase ALKBH52020-05-25T17:09:55Z<p>Wu3857: /* Reference */</p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
:[[File:ALKBH5-hydro.png||600px]]<br />
* SASA:<br />
:Cys200: ? A^2<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
[[File:ALKBH5.png|center|800px]]<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119] <br/><br />
<br />
<br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:Alkb_family&diff=2216Category:Alkb family2020-05-25T17:09:21Z<p>Wu3857: </p>
<hr />
<div>[[Category:Family]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:Alkb_family&diff=2215Category:Alkb family2020-05-25T17:09:01Z<p>Wu3857: Created page with "Category:Family"</p>
<hr />
<div>[[Category:Family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:2OG-Fe(II)_oxygenase_superfamily&diff=2214Category:2OG-Fe(II) oxygenase superfamily2020-05-25T17:08:50Z<p>Wu3857: Created page with "Category:Family"</p>
<hr />
<div>[[Category:Family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:Nucleic_acid_modification&diff=2213Category:Nucleic acid modification2020-05-25T17:08:41Z<p>Wu3857: Created page with "Category:Type"</p>
<hr />
<div>[[Category:Type]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2212RNA demethylase ALKBH52020-05-25T17:08:11Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
:[[File:ALKBH5-hydro.png||600px]]<br />
* SASA:<br />
:Cys200: ? A^2<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
[[File:ALKBH5.png|center|800px]]<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
<br />
<br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2211RNA demethylase ALKBH52020-05-25T17:07:21Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],<br/>Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
:[[File:ALKBH5-hydro.png||600px]]<br />
* SASA:<br />
:Cys200: ? A^2<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
[[File:ALKBH5.png|center|800px]]<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
<br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=RNA_demethylase_ALKBH5&diff=2210RNA demethylase ALKBH52020-05-25T17:06:51Z<p>Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532..."</p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|ALKBH5|[https://www.uniprot.org/uniprot/Q6P6C2 Q6P6C2]|Homo sapiens|Cys200|[http://pfam.xfam.org/family/PF13532 2OG-Fe(II) oxygenase superfamily],Alkb family|[[:Category:RNA demethylase ALKBH5|Ligand list]]|Nucleic acid modification}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/><br />
<br />
Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/> <br />
<br />
===Cys Function & Property===<br />
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.<br/><br />
<br />
* Hydrophobic property:<br />
:[[File:ALKBH5-hydro.png||600px]]<br />
* SASA:<br />
:Cys200: ? A^2<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP <br/><br />
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC <br/><br />
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP <br/><br />
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGG<span style="background:#ffff00">'''C'''</span> <br/><br />
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR <br/><br />
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS <br/><br />
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS <br/><br />
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/4NJ4 4NJ4]<br/> <br />
<br />
*Protein structure:<br />
[[File:ALKBH5.png|center|800px]]<br />
<br />
==Related Pathway==<br />
:Unknown<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography <br />
<br />
==Reference==<br />
# Aik W S, Scotti J S, Choi H, et al. '''Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation[J].''' Nucleic acids research, 2014, 42(7): 4741-4754. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24489119 24489119]<br/><br />
<br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Nucleic acid modification]]<br />
[[Category:2OG-Fe(II) oxygenase superfamily]]<br />
[[Category:Alkb family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:Protein-glutamine_gamma-glutamyltransferase_2&diff=2209Category:Protein-glutamine gamma-glutamyltransferase 22020-04-30T01:54:34Z<p>Wu3857: Created page with "Category:Ligand list"</p>
<hr />
<div>[[Category:Ligand list]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:Transglutaminase-like_superfamily&diff=2208Category:Transglutaminase-like superfamily2020-04-30T01:54:20Z<p>Wu3857: Created page with "Category:Family"</p>
<hr />
<div>[[Category:Family]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Protein-glutamine_gamma-glutamyltransferase_2&diff=2207Protein-glutamine gamma-glutamyltransferase 22020-04-30T01:53:56Z<p>Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|TGM2, TGC, TGase H, TGase-2|[https://www.uniprot.org/uniprot/P21980 P21980]|Homo sapiens|Cys277|[http://pfam.xf..."</p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|TGM2, TGC, TGase H, TGase-2|[https://www.uniprot.org/uniprot/P21980 P21980]|Homo sapiens|Cys277|[http://pfam.xfam.org/family/PF00656 Transglutaminase-like superfamily]|[[:Category:Protein-glutamine gamma-glutamyltransferase 2|Ligand list]]|Metabolic enzyme}}<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Transglutaminases play important roles in diverse biological functions by selectively crosslinking proteins. They catalyze, in a Ca2+dependent manner, the transamidation of glutamine residues to lysine residues, resulting in proteolytically resistant NƐ(ƴ-glutamyl)lysyl isopeptide bonds.<br/> <br />
Transglutaminase 2 (TG2, also known as tissue transglutaminase) s structurally and mechanistically complex, and has both intracellular and extracellular functions. The catalytic mechanism, related to that of cysteine Metabolic enzymes, involves an active site thiol that reacts with a glutamine side chain of a protein or peptide substrate to form a thioester intermediate from which the acyl group is transferred to an amine substrate. In the absence of a suitable amine, water can act as an alternative nucleophile, leading to deamidation of the glutamine residue to glutamate. (PMID: 18092889)<br />
<br/> <br />
[[File:603-function.png|center|600px]]<br />
<br />
===Cys Function & Property===<br />
Cys227 is one of the active site of TGM2. <br/><br />
<br />
* Hydrophobic property:<br />
:[[File:603-hydro.png||600px]]<br />
* SASA:<br />
:Cys277: 1.107 A^2<br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MAEELVLERC DLELETNGRD HHTADLCREK LVVRRGQPFW LTLHFEGRNY <br/><br />
EASVDSLTFS VVTGPAPSQE AGTKARFPLR DAVEEGDWTA TVVDQQDCTL <br/><br />
SLQLTTPANA PIGLYRLSLE ASTGYQGSSF VLGHFILLFN AWCPADAVYL <br/><br />
DSEEERQEYV LTQQGFIYQG SAKFIKNIPW NFGQFEDGIL DICLILLDVN <br/><br />
PKFLKNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR WDNNYGDGVS <br/><br />
PMSWIGSVDI LRRWKNHGCQ RVKYGQ<span style="background:#ffff00">'''C'''</span>WVF AAVACTVLRC LGIPTRVVTN <br/><br />
YNSAHDQNSN LLIEYFRNEF GEIQGDKSEM IWNFHCWVES WMTRPDLQPG <br/><br />
YEGWQALDPT PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD <br/><br />
VVDWIQQDDG SVHKSINRSL IVGLKISTKS VGRDEREDIT HTYKYPEGSS <br/><br />
EEREAFTRAN HLNKLAEKEE TGMAMRIRVG QSMNMGSDFD VFAHITNNTA <br/><br />
EEYVCRLLLC ARTVSYNGIL GPECGTKYLL NLNLEPFSEK SVPLCILYEK <br/><br />
YRDCLTESNL IKVRALLVEP VINSYLLAER DLYLENPEIK IRILGEPKQK <br/><br />
RKLVAEVSLQ NPLPVALEGC TFTVEGAGLT EEQKTVEIPD PVEAGEEVKV <br/><br />
RMDLLPLHMG LHKLVVNFES DKLKAVKGFR NVIIGPA <br/><br />
</font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:[https://www.rcsb.org/structure/3S3S 3S3S]<br/> <br />
:[https://www.rcsb.org/structure/3S3P 3S3P]<br/><br />
:[https://www.rcsb.org/structure/3S3J 3S3J]<br/><br />
<br />
*Protein structure:<br />
[[File:603.png|center|800px]]<br />
<br />
==Related Pathway==<br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05016 Huntington disease]<br/><br />
<br />
==Experimental Evidence==<br />
:Crystallography<br />
<br />
==Reference==<br />
# Pinkas D M, Strop P, Brunger A T, et al. Transglutaminase 2 undergoes a large conformational change upon activation[J]. PLoS biology, 2007, 5(12). [https://www.ncbi.nlm.nih.gov/pubmed/?term=18092889 18092889]<br/><br />
<br />
[[Category:Targets]]<br />
[[Category:Homo sapiens]]<br />
[[Category:Metabolic enzyme]]<br />
[[Category:Transglutaminase-like superfamily]]<br />
[[Category:Huntington disease]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:Hemoglobin_subunit_beta-2_(Rattus_norvegicus)&diff=2206Category:Hemoglobin subunit beta-2 (Rattus norvegicus)2020-04-29T20:28:28Z<p>Wu3857: Created page with "Category:Ligand list"</p>
<hr />
<div>[[Category:Ligand list]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Hemoglobin_subunit_beta-2_(Rattus_norvegicus)&diff=2205Hemoglobin subunit beta-2 (Rattus norvegicus)2020-04-29T20:28:01Z<p>Wu3857: /* Protein Function */</p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|Beta-2-globin|[https://www.uniprot.org/uniprot/P11517 P11517]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/family/PF00042 Globin family]|[[:Category:Hemoglobin subunit beta-2 (Rattus norvegicus)|Ligand list]]|Transporter}}<br />
<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Beta globin (also referred to as HBB, β-globin, haemoglobin beta, hemoglobin beta, or preferably haemoglobin subunit beta) is a globin protein, which along with alpha globin (HBA), makes up the most common form of haemoglobin in adult humans, the HbA. It is 146 amino acids long and has a molecular weight of 15,867 Da. Normal adult human HbA is a heterotetramer consisting of two alpha chains and two beta chains. <br/><br />
HBB is encoded by the HBB gene on human chromosome 11. Mutations in the gene produce several variants of the proteins which are implicated with genetic disorders such as sickle-cell disease and beta thalassemia, as well as beneficial traits such as genetic resistance to malaria. (From Wikipedia) <br/><br />
<br/><br />
<br />
===Cys Function & Property===<br />
The covalent modification on Cys126 could inhibit the fomration of dimer with HBA. <br/><br />
<br />
* Hydrophobic property:<br />
:[[File:602-hydro.png||600px]]<br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MVHLTDAEKA TVSGLWGKVN ADNVGAEALG RLLVVYPWTQ RYFSKFGDLS <br/><br />
SASAIMGNPQ VKAHGKKVIN AFNDGLKHLD NLKGTFAHLS ELH<span style="background:#ffff00">'''C'''</span>DKLHVD <br/><br />
PENFRLLGNM IVIVLGHHLG KEFTPCAQAA FQKVVAGVAS ALAHKYH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:Unknown<br/> <br />
<br />
*Protein structure:<br />
:[[File:601.png|center|800px]]<br />
<div align="center">HBB1 structure (the sequence of Beta-2-globin is conserved with HBB1 (94.6% identity))</div><br/><br />
<br />
==Related Pathway==<br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05143 African trypanosomiasis] <br/><br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05144 Malaria] <br/><br />
<br />
==Experimental Evidence==<br />
:Cys modification assay, MALDI-TOF/MS, LC/MS/MS, Glu-C endoproteinase digest<br />
<br />
==Reference==<br />
# Erve J C L, Jensen O N, Valentine H S, et al. Disulfiram generates a stable N, N-diethylcarbamoyl adduct on Cys-125 of rat hemoglobin β-chains in vivo[J]. Chemical research in toxicology, 2000, 13(4): 237-244. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10775322 10775322]<br/> <br />
# Zimmerman L J, Valentine H S, Amarnath K, et al. Identification of a S-Hexahydro-1 H-azepine-1-carbonyl Adduct Produced by Molinate on Rat Hemoglobin β2 and β3 Chains in Vivo[J]. Chemical research in toxicology, 2002, 15(2): 209-217. [https://www.ncbi.nlm.nih.gov/pubmed/?term=11849047 11849047]<br/> <br />
<br />
<br />
[[Category:Targets]]<br />
[[Category:Rattus norvegicus]]<br />
[[Category:Transporter]]<br />
[[Category:Globin family]]<br />
[[Category:African trypanosomiasis]]<br />
[[Category:Malaria]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Hemoglobin_subunit_beta-2_(Rattus_norvegicus)&diff=2204Hemoglobin subunit beta-2 (Rattus norvegicus)2020-04-29T20:27:48Z<p>Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|Beta-2-globin|[https://www.uniprot.org/uniprot/P11517 P11517]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/fa..."</p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|Beta-2-globin|[https://www.uniprot.org/uniprot/P11517 P11517]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/family/PF00042 Globin family]|[[:Category:Hemoglobin subunit beta-2 (Rattus norvegicus)|Ligand list]]|Transporter}}<br />
<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Beta globin (also referred to as HBB, β-globin, haemoglobin beta, hemoglobin beta, or preferably haemoglobin subunit beta) is a globin protein, which along with alpha globin (HBA), makes up the most common form of haemoglobin in adult humans, the HbA. It is 146 amino acids long and has a molecular weight of 15,867 Da. Normal adult human HbA is a heterotetramer consisting of two alpha chains and two beta chains. <br/><br />
HBB is encoded by the HBB gene on human chromosome 11. Mutations in the gene produce several variants of the proteins which are implicated with genetic disorders such as sickle-cell disease and beta thalassemia, as well as beneficial traits such as genetic resistance to malaria. (From Wikipedia) <br/><br />
<br />
===Cys Function & Property===<br />
The covalent modification on Cys126 could inhibit the fomration of dimer with HBA. <br/><br />
<br />
* Hydrophobic property:<br />
:[[File:602-hydro.png||600px]]<br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MVHLTDAEKA TVSGLWGKVN ADNVGAEALG RLLVVYPWTQ RYFSKFGDLS <br/><br />
SASAIMGNPQ VKAHGKKVIN AFNDGLKHLD NLKGTFAHLS ELH<span style="background:#ffff00">'''C'''</span>DKLHVD <br/><br />
PENFRLLGNM IVIVLGHHLG KEFTPCAQAA FQKVVAGVAS ALAHKYH <br/> </font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:Unknown<br/> <br />
<br />
*Protein structure:<br />
:[[File:601.png|center|800px]]<br />
<div align="center">HBB1 structure (the sequence of Beta-2-globin is conserved with HBB1 (94.6% identity))</div><br/><br />
<br />
==Related Pathway==<br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05143 African trypanosomiasis] <br/><br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05144 Malaria] <br/><br />
<br />
==Experimental Evidence==<br />
:Cys modification assay, MALDI-TOF/MS, LC/MS/MS, Glu-C endoproteinase digest<br />
<br />
==Reference==<br />
# Erve J C L, Jensen O N, Valentine H S, et al. Disulfiram generates a stable N, N-diethylcarbamoyl adduct on Cys-125 of rat hemoglobin β-chains in vivo[J]. Chemical research in toxicology, 2000, 13(4): 237-244. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10775322 10775322]<br/> <br />
# Zimmerman L J, Valentine H S, Amarnath K, et al. Identification of a S-Hexahydro-1 H-azepine-1-carbonyl Adduct Produced by Molinate on Rat Hemoglobin β2 and β3 Chains in Vivo[J]. Chemical research in toxicology, 2002, 15(2): 209-217. [https://www.ncbi.nlm.nih.gov/pubmed/?term=11849047 11849047]<br/> <br />
<br />
<br />
[[Category:Targets]]<br />
[[Category:Rattus norvegicus]]<br />
[[Category:Transporter]]<br />
[[Category:Globin family]]<br />
[[Category:African trypanosomiasis]]<br />
[[Category:Malaria]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Category:Hemoglobin_subunit_beta-1_(Rattus_norvegicus)&diff=2203Category:Hemoglobin subunit beta-1 (Rattus norvegicus)2020-04-28T21:20:06Z<p>Wu3857: Created page with "Category:Ligand list"</p>
<hr />
<div>[[Category:Ligand list]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Hemoglobin_subunit_beta-1_(Rattus_norvegicus)&diff=2202Hemoglobin subunit beta-1 (Rattus norvegicus)2020-04-28T16:02:55Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|HBB|[https://www.uniprot.org/uniprot/P02091 P02091]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/family/PF00042 Globin family]|[[:Category:Hemoglobin subunit beta-1 (Rattus norvegicus)|Ligand list]]|Transporter}}<br />
<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Beta globin (also referred to as HBB, β-globin, haemoglobin beta, hemoglobin beta, or preferably haemoglobin subunit beta) is a globin protein, which along with alpha globin (HBA), makes up the most common form of haemoglobin in adult humans, the HbA. It is 146 amino acids long and has a molecular weight of 15,867 Da. Normal adult human HbA is a heterotetramer consisting of two alpha chains and two beta chains. <br/><br />
HBB is encoded by the HBB gene on human chromosome 11. Mutations in the gene produce several variants of the proteins which are implicated with genetic disorders such as sickle-cell disease and beta thalassemia, as well as beneficial traits such as genetic resistance to malaria. (From Wikipedia) <br/><br />
<br/><br />
===Cys Function & Property===<br />
The covalent modification on Cys126 could inhibit the fomration of dimer with Hemoglobin subunit alpha-1 (HBA1). <br/><br />
<br />
* Hydrophobic property:<br />
:[[File:601-hydro.png||600px]]<br />
* SASA：<br />
:Cys126: 88.89 A^2 <br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS <br/><br />
TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELH<span style="background:#ffff00">'''C'''</span>DKLHVD <br/><br />
PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH<br/><br />
</font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:Unknown<br/> <br />
<br />
*Protein structure:<br />
:[[File:601.png|center|800px]]<br />
<br />
==Related Pathway==<br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05143 African trypanosomiasis] <br/><br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05144 Malaria] <br/><br />
<br />
==Experimental Evidence==<br />
:FTIR spectra, Electrospray Mass Spectra <br />
<br />
==Reference==<br />
# Erve J C L, Jensen O N, Valentine H S, et al. Disulfiram generates a stable N, N-diethylcarbamoyl adduct on Cys-125 of rat hemoglobin β-chains in vivo[J]. Chemical research in toxicology, 2000, 13(4): 237-244. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10775322 10775322]<br/> <br />
# Zimmerman L J, Valentine H S, Amarnath K, et al. Identification of a S-Hexahydro-1 H-azepine-1-carbonyl Adduct Produced by Molinate on Rat Hemoglobin β2 and β3 Chains in Vivo[J]. Chemical research in toxicology, 2002, 15(2): 209-217. [https://www.ncbi.nlm.nih.gov/pubmed/?term=11849047 11849047]<br/> <br />
<br />
<br />
[[Category:Targets]]<br />
[[Category:Rattus norvegicus]]<br />
[[Category:Transporter]]<br />
[[Category:Globin family]]<br />
[[Category:African trypanosomiasis]]<br />
[[Category:Malaria]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=Hemoglobin_subunit_beta-1_(Rattus_norvegicus)&diff=2201Hemoglobin subunit beta-1 (Rattus norvegicus)2020-04-28T16:02:12Z<p>Wu3857: </p>
<hr />
<div>{| align="left"<br />
| __TOC__<br />
|}<br />
{{#invoke:InfoboxforTarget|run|HBB|[https://www.uniprot.org/uniprot/P02091 P02091]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/family/PF00042 Globin family]|[[:Category:Hemoglobin subunit beta-1 (Rattus norvegicus)|Ligand list]]|Transporter}}<br />
<br />
==Summary==<br />
<br />
===Protein Function ===<br />
Beta globin (also referred to as HBB, β-globin, haemoglobin beta, hemoglobin beta, or preferably haemoglobin subunit beta) is a globin protein, which along with alpha globin (HBA), makes up the most common form of haemoglobin in adult humans, the HbA. It is 146 amino acids long and has a molecular weight of 15,867 Da. Normal adult human HbA is a heterotetramer consisting of two alpha chains and two beta chains. <br/><br />
HBB is encoded by the HBB gene on human chromosome 11. Mutations in the gene produce several variants of the proteins which are implicated with genetic disorders such as sickle-cell disease and beta thalassemia, as well as beneficial traits such as genetic resistance to malaria. (From Wikipedia) <br/><br />
<br/><br />
===Cys Function & Property===<br />
The covalent modification on Cys126 could inhibit the fomration of dimer with HBA1. <br/><br />
<br />
* Hydrophobic property:<br />
:[[File:601-hydro.png||600px]]<br />
* SASA：<br />
:Cys126: 88.89 A^2 <br/><br />
<br />
==Protein Sequence==<br />
<font face="Courier"><br />
MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS <br/><br />
TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELH<span style="background:#ffff00">'''C'''</span>DKLHVD <br/><br />
PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH<br/><br />
</font><br />
<br />
==Structural Information==<br />
*Known structure with covalent ligand: <br/><br />
:Unknown<br/> <br />
<br />
*Protein structure:<br />
:[[File:601.png|center|800px]]<br />
<br />
==Related Pathway==<br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05143 African trypanosomiasis] <br/><br />
*[https://www.genome.jp/kegg-bin/show_pathway?ko05144 Malaria] <br/><br />
<br />
==Experimental Evidence==<br />
:FTIR spectra, Electrospray Mass Spectra <br />
<br />
==Reference==<br />
# Erve J C L, Jensen O N, Valentine H S, et al. Disulfiram generates a stable N, N-diethylcarbamoyl adduct on Cys-125 of rat hemoglobin β-chains in vivo[J]. Chemical research in toxicology, 2000, 13(4): 237-244. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10775322 10775322]<br/> <br />
# Zimmerman L J, Valentine H S, Amarnath K, et al. Identification of a S-Hexahydro-1 H-azepine-1-carbonyl Adduct Produced by Molinate on Rat Hemoglobin β2 and β3 Chains in Vivo[J]. Chemical research in toxicology, 2002, 15(2): 209-217. [https://www.ncbi.nlm.nih.gov/pubmed/?term=11849047 11849047]<br/> <br />
<br />
<br />
[[Category:Targets]]<br />
[[Category:Rattus norvegicus]]<br />
[[Category:Transporter]]<br />
[[Category:Globin family]]<br />
[[Category:African trypanosomiasis]]<br />
[[Category:Malaria]]</div>Wu3857http://173.199.123.204/Cysteinome/index.php?title=File:639-function.png&diff=2200File:639-function.png2020-04-28T04:50:50Z<p>Wu3857: </p>
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