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Protein

Hemoglobin subunit alpha-1/2

Gene
N/A
Organism
Odocoileus virginianus virginianus (Virginia white-tailed deer)
Status
Reviewed-Annotation score: -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 bindingi58Iron (heme distal ligand)1
Metal bindingi87Iron (heme proximal ligand)1

GO - Molecular functioni

Keywordsi

Biological processOxygen transport, Transport
LigandHeme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit alpha-1/2
Alternative name(s):
Alpha-1/2-globin
Hemoglobin alpha-1/2 chain
OrganismiOdocoileus virginianus virginianus (Virginia white-tailed deer)
Taxonomic identifieri9875 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraCervidaeOdocoileinaeOdocoileus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000527081 – 141Hemoglobin subunit alpha-1/2Add BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineBy similarity1
Modified residuei7N6-succinyllysineBy similarity1
Modified residuei11N6-succinyllysineBy similarity1
Modified residuei16N6-acetyllysine; alternateBy similarity1
Modified residuei16N6-succinyllysine; alternateBy similarity1
Modified residuei24PhosphotyrosineBy similarity1
Modified residuei35PhosphoserineBy similarity1
Modified residuei40N6-succinyllysineBy similarity1
Modified residuei49PhosphoserineBy similarity1
Modified residuei102PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei124PhosphoserineBy similarity1
Modified residuei134PhosphothreonineBy similarity1
Modified residuei137PhosphothreonineBy similarity1
Modified residuei138PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP01972

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Structurei

Secondary structure

1141
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Turni15 – 17Combined sources3
Helixi22 – 28Combined sources7
Turni33 – 35Combined sources3
Helixi40 – 42Combined sources3
Helixi54 – 69Combined sources16
Helixi76 – 79Combined sources4
Turni81 – 83Combined sources3
Helixi84 – 88Combined sources5
Turni89 – 91Combined sources3
Helixi95 – 97Combined sources3
Helixi98 – 112Combined sources15
Turni114 – 116Combined sources3
Helixi119 – 135Combined sources17
Turni136 – 139Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HDSX-ray1.98A/C1-141[»]
SMRiP01972
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01972

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG009709

Family and domain databases

CDDicd08927 Hb-alpha_like, 1 hit
Gene3Di1.10.490.10, 1 hit
InterProiView protein in InterPro
IPR000971 Globin
IPR009050 Globin-like_sf
IPR012292 Globin/Proto
IPR002338 Haemoglobin_a-typ
PfamiView protein in Pfam
PF00042 Globin, 1 hit
PRINTSiPR00612 ALPHAHAEM
SUPFAMiSSF46458 SSF46458, 1 hit
PROSITEiView protein in PROSITE
PS01033 GLOBIN, 1 hit

Sequencei

Sequence statusi: Complete.

P01972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VLSAABKSBV KAAWGKVGGN AAPYGAZALZ RMFLSFPTTK TYFPHFBLSH
60 70 80 90 100
GSAZVKAHGZ KVABALTKAV GHLBBLPGTL SBLSBLHAHK LRVBPVBFKL
110 120 130 140
LSHSLLVTLA THLPBBFTPA VHASLBKFLA BVSTVLTSKY R
Length:141
Mass (Da):15,127
Last modified:July 21, 1986 - v1
Checksum:i5B2EBB566F902D4F
GO

Polymorphismi

There are three alleles of the alpha-1 chain (alpha-1*1, alpha-1*2 and alpha-1*3). The sequence shown is alpha-1*1. The alpha-2 chain is non-allelic.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti5A → T in alpha-1*2 chain. 1
Natural varianti20N → K in alpha-2 chain. 1
Natural varianti24Y → F in alpha-2 chain and alpha-1*3 chain. 1

Sequence databases

PIRiA02296 HADE1V

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiHBA_ODOVI
AccessioniPrimary (citable) accession number: P01972
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 25, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
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Main funding by: National Institutes of Health