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P02089 (HBB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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 beta-2
Alternative name(s):
Beta-2-globin
Hemoglobin beta-2 chain
Hemoglobin beta-minor chain
Gene names
Name:Hbb-b2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length147 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

Inbred mouse strains possess 1 of 3 alleles at the HBB locus: D (diffuse), S (single), and P. The D and P alleles are actually closely linked doublets that coordinately express a major and a minor chain, the minor chain being slightly different in the two alleles. The S allele produces only 1 chain, it is characteristic of North American wild mice.

Miscellaneous

The D-minor sequence is shown. See also the entry for the beta D-major chain and the S allele.

Sequence similarities

Belongs to the globin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 147146Hemoglobin subunit beta-2
PRO_0000053025

Sites

Metal binding641Iron (heme distal ligand)
Metal binding931Iron (heme proximal ligand)

Amino acid modifications

Modified residue181N6-succinyllysine Ref.5
Modified residue601N6-succinyllysine Ref.5

Natural variations

Natural variant23 – 242EV → AI in allele P.

Sequences

Sequence LengthMass (Da)Tools
P02089 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1FABBDC2D0ABC4FD

FASTA14715,878
        10         20         30         40         50         60 
MVHLTDAEKS AVSCLWAKVN PDEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNPK 

        70         80         90        100        110        120 
VKAHGKKVIT AFNEGLKNLD NLKGTFASLS ELHCDKLHVD PENFRLLGNA IVIVLGHHLG 

       130        140 
KDFTPAAQAA FQKVVAGVAT ALAHKYH 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the BALB/c mouse beta-globin complex."
Shehee W.R., Loeb D.D., Adey N.B., Burton F.H., Casavant N.C., Cole P., Davies C.J., McGraw R.A., Schichman S.A., Severynse D.M., Voliva C.F., Weyter F.W., Wisely G.B., Edgell M.H., Hutchison C.A. III
J. Mol. Biol. 205:41-62(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The evolution and sequence comparison of two recently diverged mouse chromosomal beta-globin genes."
Konkel D.A., Maizel J.V. Jr., Leder P.
Cell 18:865-873(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT 24-ALA--ILE-25.
Strain: Czech II and FVB/N.
Tissue: Mammary gland and Salivary gland.
[4]"Mouse haemoglobin beta chains. Comparative sequence data on adult major and minor beta chains from two species, Mus musculus and Mus cervicolor."
Gilman J.G.
Biochem. J. 159:43-53(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, VARIANT 23-ALA-ILE-24.
[5]"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-18 AND LYS-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00722 Genomic DNA. Translation: CAA24101.1.
X14061 Genomic DNA. Translation: CAA32225.1. Sequence problems.
BC027434 mRNA. Translation: AAH27434.1.
BC032264 mRNA. Translation: AAH32264.1.
PIRHBMSN1. B90790.
RefSeqNP_058652.1. NM_016956.3.
UniGeneMm.288567.
Mm.467412.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNEX-ray1.90B/D65-77[»]
1FNGX-ray1.90B/D65-77[»]
1I3RX-ray2.40B/D/F/H65-77[»]
ProteinModelPortalP02089.
SMRP02089. Positions 2-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200220. 1 interaction.
IntActP02089. 11 interactions.
MINTMINT-4097249.

Chemistry

ChEMBLCHEMBL4007.

PTM databases

PhosphoSiteP02089.

Proteomic databases

MaxQBP02089.
PRIDEP02089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID15130.
KEGGmmu:15130.

Organism-specific databases

CTD15130.
MGIMGI:96022. Hbb-b2.

Phylogenomic databases

HOVERGENHBG009709.
InParanoidQ5D0E8.
KOK13823.

Gene expression databases

GenevestigatorP02089.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00814. BETAHAEM.
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02089.
NextBio287586.
PROP02089.
SOURCESearch...

Entry information

Entry nameHBB2_MOUSE
AccessionPrimary (citable) accession number: P02089
Secondary accession number(s): Q5D0E8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 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