Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Iron (heme distal ligand)
Metal bindingi88 – 881Iron (heme proximal ligand)

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 142141Hemoglobin subunit alphaPRO_0000052568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei8 – 81N6-succinyllysineBy similarity
Modified residuei12 – 121N6-succinyllysineBy similarity
Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
Modified residuei17 – 171N6-succinyllysine; alternateBy similarity
Modified residuei25 – 251PhosphotyrosineBy similarity
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei41 – 411N6-succinyllysineBy similarity
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei103 – 1031PhosphoserineBy similarity
Modified residuei109 – 1091PhosphothreonineBy similarity
Modified residuei125 – 1251PhosphoserineBy similarity
Modified residuei135 – 1351PhosphothreonineBy similarity
Modified residuei138 – 1381PhosphothreonineBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP01966.
PRIDEiP01966.

Miscellaneous databases

PMAP-CutDBP01966.

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Protein-protein interaction databases

BioGridi169070. 1 interaction.
STRINGi9913.ENSBTAP00000037374.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814Combined sources
Helixi19 – 213Combined sources
Helixi22 – 3615Combined sources
Helixi38 – 436Combined sources
Beta strandi45 – 473Combined sources
Helixi54 – 7219Combined sources
Helixi73 – 764Combined sources
Helixi77 – 804Combined sources
Helixi82 – 898Combined sources
Helixi97 – 11317Combined sources
Turni115 – 1173Combined sources
Helixi120 – 13718Combined sources
Turni138 – 1403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-142.
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.
OrthoDBiEOG7KH9MP.
TreeFamiTF332328.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002338. Haemoglobin_a.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901H → Y in allele Y. 1 Publication
Natural varianti132 – 1321N → S in allele S. 1 Publication

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
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. Positions 2-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi169070. 1 interaction.
STRINGi9913.ENSBTAP00000037374.

Protein family/group databases

Allergomei8242. Bos d HG.

Proteomic databases

PaxDbiP01966.
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.
OrthoDBiEOG7KH9MP.
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.
NextBioi20790730.
PMAP-CutDBP01966.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002338. Haemoglobin_a.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of Podolian cattle (Bos taurus primigenius) alpha globin genes."
    Rullo R., Pieragostini E., Vincenti D., Campanile C., Di Luccia A.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES N; S AND Y).
    Strain: Podolian.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal liver.
  3. "Amino acid sequence of the alpha-chain of bovine fetal hemoglobin."
    Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Babin D.R.
    Arch. Biochem. Biophys. 120:1-14(1967) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-142.
    Strain: Holstein.
  4. "Predominant low-molecular-weight proteins in isolated brain capillaries are histones."
    Pardridge W.M., Nowlin D.M., Calaycay J., Shively J.E.
    J. Neurochem. 53:1014-1018(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-24.
    Tissue: Brain capillary.
  5. "A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin."
    Perutz M.F., Fermi G., Poyart C., Pagnier J., Kister J.
    J. Mol. Biol. 233:536-545(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  6. "The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 A resoultion and its relationship to the quaternary structures of other hemoglobin crystal froms."
    Safo M.K., Abraham D.J.
    Protein Sci. 10:1091-1099(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

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: January 20, 2016
This is version 144 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.