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Protein

Hemoglobin subunit alpha-1/2

Gene

Hba1

Organism
Rattus norvegicus (Rat)
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

GO - Biological processi

  • negative regulation of blood pressure Source: RGD
  • regulation of sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit alpha-1/2
Alternative name(s):
Alpha-1/2-globin
Hemoglobin alpha-1/2 chain
Gene namesi
Name:Hba1
Synonyms:Hba-a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2782. Hba1.

Subcellular locationi

GO - Cellular componenti

  • hemoglobin complex Source: InterPro
  • synapse Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000527512 – 142Hemoglobin subunit alpha-1/2Add BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4PhosphoserineBy similarity1
Modified residuei8N6-succinyllysineBy similarity1
Modified residuei9PhosphothreonineBy similarity1
Modified residuei12N6-succinyllysineBy similarity1
Modified residuei17N6-acetyllysine; alternateBy similarity1
Modified residuei17N6-succinyllysine; alternateBy similarity1
Modified residuei25PhosphotyrosineBy similarity1
Modified residuei41N6-succinyllysineBy similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei103PhosphoserineBy similarity1
Modified residuei109PhosphothreonineBy similarity1
Modified residuei125PhosphoserineBy similarity1
Modified residuei132PhosphoserineBy similarity1
Modified residuei135PhosphothreonineBy similarity1
Modified residuei138PhosphothreonineBy similarity1
Modified residuei139PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP01946.
PRIDEiP01946.

PTM databases

iPTMnetiP01946.
PhosphoSitePlusiP01946.

Expressioni

Tissue specificityi

Red blood cells.

Gene expression databases

BgeeiENSRNOG00000029886.
ExpressionAtlasiP01946. differential.
GenevisibleiP01946. RN.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Protein-protein interaction databases

BioGridi247661. 1 interactor.
261987. 1 interactor.
IntActiP01946. 1 interactor.
STRINGi10116.ENSRNOP00000044233.

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 – 44Combined sources7
Beta strandi50 – 52Combined sources3
Helixi54 – 72Combined sources19
Helixi74 – 76Combined sources3
Helixi77 – 80Combined sources4
Helixi82 – 89Combined sources8
Helixi96 – 113Combined sources18
Turni115 – 117Combined sources3
Helixi120 – 137Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DHTX-ray2.98A2-142[»]
3HF4X-ray2.70A/E2-142[»]
ProteinModelPortaliP01946.
SMRiP01946.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01946.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP01946.
KOiK13822.
OMAiGAYMGEA.
OrthoDBiEOG091G0S0X.
PhylomeDBiP01946.
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.

P01946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSADDKTN IKNCWGKIGG HGGEYGEEAL QRMFAAFPTT KTYFSHIDVS
60 70 80 90 100
PGSAQVKAHG KKVADALAKA ADHVEDLPGA LSTLSDLHAH KLRVDPVNFK
110 120 130 140
FLSHCLLVTL ACHHPGDFTP AMHASLDKFL ASVSTVLTSK YR
Length:142
Mass (Da):15,329
Last modified:January 23, 2007 - v3
Checksum:iDEF6857594C42A99
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21H → S AA sequence (PubMed:8334153).Curated1
Sequence conflicti71 – 79ADHVEDLPG → GAHLBBVPZ AA sequence (PubMed:1191258).Curated9

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti6D → A in alpha-2. 3 Publications1
Natural varianti45S → N.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17083 mRNA. Translation: AAA41308.1.
X56325 Genomic DNA. Translation: CAA39764.1.
X65495 Genomic DNA. Translation: CAA46476.1.
U29528 Genomic DNA. Translation: AAA99054.1.
BC059150 mRNA. Translation: AAH59150.1.
BC091567 mRNA. Translation: AAH91567.1.
S66657 Genomic DNA. Translation: AAP13984.1.
M32510 mRNA. Translation: AAA41315.1.
PIRiI54239. HART1.
RefSeqiNP_001007723.1. NM_001007722.1.
NP_037228.1. NM_013096.1.
UniGeneiRn.107334.
Rn.203003.

Genome annotation databases

EnsembliENSRNOT00000051483; ENSRNOP00000044233; ENSRNOG00000029886.
GeneIDi25632.
360504.
KEGGirno:25632.
rno:360504.
UCSCiRGD:2782. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17083 mRNA. Translation: AAA41308.1.
X56325 Genomic DNA. Translation: CAA39764.1.
X65495 Genomic DNA. Translation: CAA46476.1.
U29528 Genomic DNA. Translation: AAA99054.1.
BC059150 mRNA. Translation: AAH59150.1.
BC091567 mRNA. Translation: AAH91567.1.
S66657 Genomic DNA. Translation: AAP13984.1.
M32510 mRNA. Translation: AAA41315.1.
PIRiI54239. HART1.
RefSeqiNP_001007723.1. NM_001007722.1.
NP_037228.1. NM_013096.1.
UniGeneiRn.107334.
Rn.203003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DHTX-ray2.98A2-142[»]
3HF4X-ray2.70A/E2-142[»]
ProteinModelPortaliP01946.
SMRiP01946.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247661. 1 interactor.
261987. 1 interactor.
IntActiP01946. 1 interactor.
STRINGi10116.ENSRNOP00000044233.

PTM databases

iPTMnetiP01946.
PhosphoSitePlusiP01946.

Proteomic databases

PaxDbiP01946.
PRIDEiP01946.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000051483; ENSRNOP00000044233; ENSRNOG00000029886.
GeneIDi25632.
360504.
KEGGirno:25632.
rno:360504.
UCSCiRGD:2782. rat.

Organism-specific databases

CTDi3039.
3040.
RGDi2782. Hba1.

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP01946.
KOiK13822.
OMAiGAYMGEA.
OrthoDBiEOG091G0S0X.
PhylomeDBiP01946.
TreeFamiTF332328.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP01946.
PROiP01946.

Gene expression databases

BgeeiENSRNOG00000029886.
ExpressionAtlasiP01946. differential.
GenevisibleiP01946. RN.

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_RAT
AccessioniPrimary (citable) accession number: P01946
Secondary accession number(s): P33583
, Q63243, Q80XV2, Q91V15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In rats there are two non-allelic alpha chains and two non-allelic beta chains. The alpha-1 chain sequence is shown.

Caution

PubMed:8334153 incorrectly assigned their sequence fragment as a fatty acid-binding protein.Curated

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.