Hemoglobin subunit beta-1 (Rattus norvegicus) - Revision history

Wu3857 at 16:02, 28 April 2020

2020-04-28T16:02:55Z

Wu3857 at 16:02, 28 April 2020

2020-04-28T16:02:12Z

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|HBB|[https://www.uniprot.org/uniprot/P02091 P02091]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/family/PF000..."

2020-04-28T04:08:32Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|HBB|[https://www.uniprot.org/uniprot/P02091 P02091]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/family/PF000..."

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{| align="left"
| __TOC__
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{{#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}}

==Summary==

===Protein Function ===
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. 
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) 

===Cys Function & Property===
The covalent modification on Cys126 could inhibit the fomration of dimer with HBA1. 

* Hydrophobic property:
:[[File:601-hydro.png||600px]]
* SASA：
:Cys126: 88.89 A^2 

==Protein Sequence==

MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS 
TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELH'''C'''DKLHVD 
PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH 


==Structural Information==
*Known structure with covalent ligand: 
:Unknown 

*Protein structure:
:[[File:601.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko05143 African trypanosomiasis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05144 Malaria] 

==Experimental Evidence==
:FTIR spectra, Electrospray Mass Spectra

==Reference==
# 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] 
# 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] 

[[Category:Targets]]
[[Category:Rattus norvegicus]]
[[Category:Transporter]]
[[Category:Globin family]]
[[Category:African trypanosomiasis]]
[[Category:Malaria]]

@@ Line 11: / Line 11: @@
 <br/>
 ===Cys Function & Property===
-The covalent modification on Cys126 could inhibit the fomration of dimer with HBA1. <br/>
+The covalent modification on Cys126 could inhibit the fomration of dimer with Hemoglobin subunit alpha-1 (HBA1). <br/>
 * Hydrophobic property:

@@ Line 9: / Line 9: @@
 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/>
 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/>
 ===Cys Function & Property===
 The covalent modification on Cys126 could inhibit the fomration of dimer with HBA1. <br/>

Hemoglobin subunit beta-1 (Rattus norvegicus) - Revision history

Wu3857 at 16:02, 28 April 2020

Wu3857 at 16:02, 28 April 2020

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|HBB|[https://www.uniprot.org/uniprot/P02091 P02091]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/family/PF000..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|HBB|[https://www.uniprot.org/uniprot/P02091 P02091]|Rattus norvegicus|Cys126|[http://pfam.xfam.org/family/PF000..."