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P02062 (HBB_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 116. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemoglobin subunit beta
Alternative name(s):
Beta-globin
Hemoglobin beta chain
Gene names
Name:HBB
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus ›

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
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.

Sequence similarities

Belongs to the globin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Hemoglobin subunit beta
PRO_0000052975

Sites

Metal binding631Iron (heme distal ligand)
Metal binding921Iron (heme proximal ligand)

Amino acid modifications

Modified residue11N-acetylvaline By similarity
Modified residue591N6-acetyllysine By similarity
Modified residue821N6-acetyllysine By similarity
Modified residue931S-nitrosocysteine By similarity
Modified residue1441N6-acetyllysine By similarity

Secondary structure

1 .................... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02062 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 734664793DA642EE

FASTA14616,008
        10         20         30         40         50         60 
VQLSGEEKAA VLALWDKVNE EEVGGEALGR LLVVYPWTQR FFDSFGDLSN PGAVMGNPKV 

        70         80         90        100        110        120 
KAHGKKVLHS FGEGVHHLDN LKGTFAALSE LHCDKLHVDP ENFRLLGNVL VVVLARHFGK 

       130        140 
DFTPELQASY QKVVAGVANA LAHKYH

« Hide

References

[1]"Hemoglobins, XXXIII. Note on the sequence of the hemoglobins of the horse."
Matsuda G., Maita T., Braunitzer G., Schrank B.
Hoppe-Seyler's Z. Physiol. Chem. 361:1107-1116(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Amino acid sequences of some tryptic peptides from the beta-chain of horse hemoglobin."
Smith D.B.
Can. J. Biochem. 46:825-843(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-82 AND 117-146.
[3]"Amide groups of some tryptic peptides from the beta-chain of horse hemoglobin."
Smith D.B., Chung W.P.
Can. J. Biochem. 48:1160-1164(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: DETERMINATION OF AMIDES, PROTEIN SEQUENCE OF 52-54.
[4]"Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8-A resolution: (1) X-ray analysis."
Perutz M.F., Miurhead H., Cox J.M., Goaman L.C., Mathews F.S., McGandy E.L., Webb L.E.
Nature 219:29-32(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[5]"Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: the atomic model."
Perutz M.F., Muirhead H., Cox J.M., Goaman L.C.
Nature 219:131-139(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]"The structure of horse methaemoglobin at 2.0-A resolution."
Ladner R.C., Heidner E.J., Perutz M.F.
J. Mol. Biol. 114:385-414(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Protein Spotlight

The man behind the molecular lung - Issue 21 of April 2002

Cross-references

Sequence databases

PIRHBHO. B91688.
RefSeqNP_001157490.1. NM_001164018.1.
UniGeneEca.16920.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G0BX-ray1.90B1-146[»]
1IBEX-ray1.80B1-146[»]
1IWHX-ray1.55B1-146[»]
1NS6X-ray2.05B1-146[»]
1NS9X-ray1.60B1-146[»]
1Y8HX-ray3.10B/D1-146[»]
1Y8IX-ray2.60B/D1-146[»]
1Y8KX-ray2.30B/D1-146[»]
2D5XX-ray1.45B1-146[»]
2DHBX-ray2.80B1-146[»]
2MHBX-ray2.00B1-146[»]
2ZLTX-ray1.90B1-146[»]
2ZLUX-ray2.00B1-146[»]
2ZLVX-ray2.00B1-146[»]
2ZLWX-ray2.90B/D1-146[»]
2ZLXX-ray2.80B/D1-146[»]
ProteinModelPortalP02062.
SMRP02062. Positions 1-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-242194.
STRING9796.ENSECAP00000008056.

Proteomic databases

PRIDEP02062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100054109.
KEGGecb:100054109.

Organism-specific databases

CTD3043.

Phylogenomic databases

eggNOGNOG269316.
HOGENOMHOG000036868.
HOVERGENHBG009709.
InParanoidP02062.
KOK13823.
OMAAVMNNPK.

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

EvolutionaryTraceP02062.

Entry information

Entry nameHBB_HORSE
AccessionPrimary (citable) accession number: P02062
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 116 of the entry and version 1 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents