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Protein

Hemoglobin subunit alpha

Gene

HBA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in oxygen transport from the lung to the various peripheral tissues.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Iron (heme distal ligand)1
Metal bindingi88Iron (heme proximal ligand)1

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-BTA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-BTA-2168880. Scavenging of heme from plasma.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit alpha
Alternative name(s):
Alpha-globin
Hemoglobin alpha chain
Gene namesi
Name:HBA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Protein family/group databases

Allergomei8242. Bos d HG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000525682 – 142Hemoglobin subunit alphaAdd BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4PhosphoserineBy similarity1
Modified residuei8N6-succinyllysineBy similarity1
Modified residuei12N6-succinyllysineBy similarity1
Modified residuei17N6-acetyllysine; alternateBy similarity1
Modified residuei17N6-succinyllysine; alternateBy similarity1
Modified residuei25PhosphotyrosineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei41N6-succinyllysineBy similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei103PhosphoserineBy similarity1
Modified residuei109PhosphothreonineBy similarity1
Modified residuei125PhosphoserineBy similarity1
Modified residuei135PhosphothreonineBy similarity1
Modified residuei138PhosphothreonineBy similarity1
Modified residuei139PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP01966.
PeptideAtlasiP01966.
PRIDEiP01966.

Miscellaneous databases

PMAP-CutDBP01966.

Expressioni

Tissue specificityi

Red blood cells.

Gene expression databases

BgeeiENSBTAG00000026417.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Protein-protein interaction databases

BioGridi169070. 1 interactor.
STRINGi9913.ENSBTAP00000037374.

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 18Combined sources14
Helixi19 – 21Combined sources3
Helixi22 – 36Combined sources15
Helixi38 – 43Combined sources6
Beta strandi45 – 47Combined sources3
Helixi54 – 72Combined sources19
Helixi73 – 76Combined sources4
Helixi77 – 80Combined sources4
Helixi82 – 89Combined sources8
Helixi97 – 113Combined sources17
Turni115 – 117Combined sources3
Helixi120 – 137Combined sources18
Turni138 – 140Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FSXX-ray2.10A/C2-142[»]
1G08X-ray1.90A/C2-142[»]
1G09X-ray2.04A/C2-142[»]
1G0AX-ray2.04A/C2-142[»]
1HDAX-ray2.20A/C2-142[»]
2QSPX-ray1.85A/C2-142[»]
2QSSX-ray1.75A/C2-142[»]
3CIUX-ray3.50A/C2-142[»]
3PI8X-ray2.20A/C2-142[»]
3PI9X-ray2.90A/C2-142[»]
3PIAX-ray2.10A/C2-142[»]
ProteinModelPortaliP01966.
SMRiP01966.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01966.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP01966.
KOiK13822.
OMAiDKFLCAV.
OrthoDBiEOG091G0S0X.
TreeFamiTF332328.

Family and domain databases

CDDicd08927. Hb-alpha_like. 1 hit.
Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002338. Haemoglobin_a-typ.
IPR002339. Haemoglobin_pi.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01966-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSAADKGN VKAAWGKVGG HAAEYGAEAL ERMFLSFPTT KTYFPHFDLS
60 70 80 90 100
HGSAQVKGHG AKVAAALTKA VEHLDDLPGA LSELSDLHAH KLRVDPVNFK
110 120 130 140
LLSHSLLVTL ASHLPSDFTP AVHASLDKFL ANVSTVLTSK YR
Length:142
Mass (Da):15,184
Last modified:January 23, 2007 - v2
Checksum:i6D20CADDA05C0DC5
GO

Polymorphismi

There are 3 alleles in Podolian cattle; N, S and Y.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti90H → Y in allele Y. 1 Publication1
Natural varianti132N → S in allele S. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ242797 Genomic DNA. Translation: CAB56827.1.
AJ242798 Genomic DNA. Translation: CAB56828.1.
AJ242799 Genomic DNA. Translation: CAB56829.1.
BC102940 mRNA. Translation: AAI02941.1.
BC133477 mRNA. Translation: AAI33478.1.
PIRiA02289. HABO.
RefSeqiNP_001070890.2. NM_001077422.3.
XP_001788728.1. XM_001788676.4.
XP_003585623.1. XM_003585575.2.
UniGeneiBt.10591.

Genome annotation databases

EnsembliENSBTAT00000022034; ENSBTAP00000022034; ENSBTAG00000026417.
ENSBTAT00000037545; ENSBTAP00000037374; ENSBTAG00000026418.
GeneIDi100140149.
512439.
KEGGibta:100140149.
bta:512439.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ242797 Genomic DNA. Translation: CAB56827.1.
AJ242798 Genomic DNA. Translation: CAB56828.1.
AJ242799 Genomic DNA. Translation: CAB56829.1.
BC102940 mRNA. Translation: AAI02941.1.
BC133477 mRNA. Translation: AAI33478.1.
PIRiA02289. HABO.
RefSeqiNP_001070890.2. NM_001077422.3.
XP_001788728.1. XM_001788676.4.
XP_003585623.1. XM_003585575.2.
UniGeneiBt.10591.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FSXX-ray2.10A/C2-142[»]
1G08X-ray1.90A/C2-142[»]
1G09X-ray2.04A/C2-142[»]
1G0AX-ray2.04A/C2-142[»]
1HDAX-ray2.20A/C2-142[»]
2QSPX-ray1.85A/C2-142[»]
2QSSX-ray1.75A/C2-142[»]
3CIUX-ray3.50A/C2-142[»]
3PI8X-ray2.20A/C2-142[»]
3PI9X-ray2.90A/C2-142[»]
3PIAX-ray2.10A/C2-142[»]
ProteinModelPortaliP01966.
SMRiP01966.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi169070. 1 interactor.
STRINGi9913.ENSBTAP00000037374.

Protein family/group databases

Allergomei8242. Bos d HG.

Proteomic databases

PaxDbiP01966.
PeptideAtlasiP01966.
PRIDEiP01966.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022034; ENSBTAP00000022034; ENSBTAG00000026417.
ENSBTAT00000037545; ENSBTAP00000037374; ENSBTAG00000026418.
GeneIDi100140149.
512439.
KEGGibta:100140149.
bta:512439.

Organism-specific databases

CTDi15121.
3039.

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP01966.
KOiK13822.
OMAiDKFLCAV.
OrthoDBiEOG091G0S0X.
TreeFamiTF332328.

Enzyme and pathway databases

ReactomeiR-BTA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-BTA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-BTA-2168880. Scavenging of heme from plasma.

Miscellaneous databases

EvolutionaryTraceiP01966.
PMAP-CutDBP01966.

Gene expression databases

BgeeiENSBTAG00000026417.

Family and domain databases

CDDicd08927. Hb-alpha_like. 1 hit.
Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002338. Haemoglobin_a-typ.
IPR002339. Haemoglobin_pi.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHBA_BOVIN
AccessioniPrimary (citable) accession number: P01966
Secondary accession number(s): A3KN13
, Q3SZE0, Q9TTR9, Q9TTS0, Q9TTS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.