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P01942 (HBA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemoglobin subunit alpha
Alternative name(s):
Alpha-globin
Hemoglobin alpha chain
Gene names
Name:Hba
Synonyms:Hba-a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Heterotetramer of two alpha chains and two beta chains.

Tissue specificity

Red blood cells.

Polymorphism

In inbred mouse strains there are at least 6 alleles that can occur at the HBA locus: A, B, C, D, F, or G. Strains carrying the A and F alleles produce a single kind of alpha chain, whereas those carrying B, C, D, or G each produce 2 kinds of chains. The sequence shown is that of the B1 and D1 allele chains.

Sequence similarities

Belongs to the globin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 142141Hemoglobin subunit alpha
PRO_0000052694

Sites

Metal binding591Iron (heme distal ligand)
Metal binding881Iron (heme proximal ligand)

Amino acid modifications

Modified residue81N6-succinyllysine Ref.6
Modified residue121N6-succinyllysine Ref.6
Modified residue171N6-acetyllysine; alternate By similarity
Modified residue171N6-succinyllysine; alternate Ref.6
Modified residue411N6-succinyllysine Ref.6

Natural variations

Natural variant261G → V in allele chain C(1) and in strain NB. Ref.7 Ref.8 Ref.9
Natural variant631V → I in allele chain C(1) and in strain NB. Ref.7 Ref.8 Ref.9
Natural variant691S → N in allele chains A, C(2), D(2), F, G(1) and G(2) and in strain C57BL. Ref.7 Ref.8 Ref.9
Natural variant691S → T in allele chain B(2) and in 1 BALB/C strain sequence. Ref.7 Ref.8 Ref.9
Natural variant791G → A in allele chains F and G(2). Ref.7 Ref.8 Ref.9

Secondary structure

....................... 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01942 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2F70043BFF66E24A

FASTA14215,085
        10         20         30         40         50         60 
MVLSGEDKSN IKAAWGKIGG HGAEYGAEAL ERMFASFPTT KTYFPHFDVS HGSAQVKGHG 

        70         80         90        100        110        120 
KKVADALASA AGHLDDLPGA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL ASHHPADFTP 

       130        140 
AVHASLDKFL ASVSTVLTSK YR 

« Hide

References

« Hide 'large scale' references
[1]"The complete sequence of a chromosomal mouse alpha-globin gene reveals elements conserved throughout vertebrate evolution."
Nishioka Y., Leder P.
Cell 18:875-882(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BALB/c.
[2]"Hemoglobins of mice: sequence and possible ambiguity at one position of the alpha chain."
Popp R.A.
J. Mol. Biol. 27:9-16(1967) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-142.
Strain: BALB/c, C57BL/6 and NB.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 18-57; 94-100 AND 129-140, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[4]"Comparison of cloned mouse alpha- and beta-globin genes: conservation of intervening sequence locations and extragenic homology."
Leder A., Miller H.I., Hamer D.H., Seidman J.G., Norman B., Sullivan M., Leder P.
Proc. Natl. Acad. Sci. U.S.A. 75:6187-6191(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-99.
[5]"Characterization and kinetics of synthesis of 15S beta-globin RNA, a putative precursor of beta-globin mRNA."
Curtis P.J., Mantei N., Weissmann C.
Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 84-109.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-12; LYS-17 AND LYS-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Studies on the mouse hemoglobin loci. 8. A fourth alpha-chain phenotype."
Popp R.A.
J. Hered. 60:126-133(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
[8]Popp R.A.
(In) Altman P.A., Katz D.D. (eds.); Inbred and genetically defined strains of laboratory animals, pp.105-105, Federation of American Societies for Experimental Biology, Bethesda (1979)
Cited for: VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
[9]"The primary structure of genetic variants of mouse hemoglobin."
Popp R.A., Bailiff E.G., Skow L.C., Whitney J.B. III
Biochem. Genet. 20:199-208(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00714 Genomic DNA. Translation: CAA24095.1.
M10703 Genomic DNA. Translation: AAA37782.2.
M10840 mRNA. Translation: AAA37784.1.
PIRHAMS. A90791.
UniGeneMm.196110.
Mm.459653.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HRWX-ray2.80A/C2-142[»]
ProteinModelPortalP01942.
SMRP01942. Positions 2-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-34118N.
IntActP01942. 8 interactions.
MINTMINT-1869504.

PTM databases

PhosphoSiteP01942.

2D gel databases

REPRODUCTION-2DPAGEIPI00469114.
P01942.
SWISS-2DPAGEP01942.

Proteomic databases

PaxDbP01942.
PRIDEP01942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:96015. Hba-a1.

Phylogenomic databases

eggNOGNOG283543.
HOGENOMHOG000036867.
HOVERGENHBG009709.
InParanoidP01942.
PhylomeDBP01942.

Gene expression databases

CleanExMM_HBA-A1.
GenevestigatorP01942.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002338. Haemoglobin_a.
IPR018331. Haemoglobin_alpha_chain.
IPR002339. Haemoglobin_pi.
[Graphical view]
PANTHERPTHR11442:SF14. PTHR11442:SF14. 1 hit.
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01942.
PROP01942.
SOURCESearch...

Entry information

Entry nameHBA_MOUSE
AccessionPrimary (citable) accession number: P01942
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot