Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hemoglobin subunit beta

Gene

HBB

Organism
Bos taurus (Bovine)
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.1 Publication
Spinorphin: functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and may thereby play a role as a regulator of pain and inflammation.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi62Iron (heme distal ligand)1
Metal bindingi91Iron (heme proximal ligand)1

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-BTA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-BTA-2168880. Scavenging of heme from plasma.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit beta
Alternative name(s):
Beta-globin
Hemoglobin beta chain
Cleaved into the following chain:
Gene namesi
Name:HBB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Protein family/group databases

Allergomei8242. Bos d HG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000528921 – 145Hemoglobin subunit betaAdd BLAST145
PeptideiPRO_000042422531 – 37Spinorphin7

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11PhosphothreonineBy similarity1
Modified residuei43PhosphoserineBy similarity1
Modified residuei58N6-acetyllysineBy similarity1
Modified residuei81N6-acetyllysineBy similarity1
Modified residuei92S-nitrosocysteineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP02070.
PeptideAtlasiP02070.
PRIDEiP02070.

Miscellaneous databases

PMAP-CutDBP02070.

Expressioni

Tissue specificityi

Red blood cells.

Gene expression databases

BgeeiENSBTAG00000038748.
ExpressionAtlasiP02070. baseline and differential.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000043063.

Structurei

Secondary structure

1145
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Helixi21 – 33Combined sources13
Helixi35 – 44Combined sources10
Helixi50 – 55Combined sources6
Helixi57 – 73Combined sources17
Helixi77 – 79Combined sources3
Helixi80 – 83Combined sources4
Helixi85 – 93Combined sources9
Helixi100 – 117Combined sources18
Helixi118 – 120Combined sources3
Helixi123 – 140Combined sources18
Helixi141 – 144Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FSXX-ray2.10B/D1-145[»]
1G08X-ray1.90B/D1-145[»]
1G09X-ray2.04B/D1-145[»]
1G0AX-ray2.04B/D1-145[»]
1HDAX-ray2.20B/D1-145[»]
2QSPX-ray1.85B/D1-145[»]
2QSSX-ray1.75B/D1-145[»]
3CIUX-ray3.50B/D1-145[»]
3PI8X-ray2.20B/D1-145[»]
3PI9X-ray2.90B/D1-145[»]
3PIAX-ray2.10B/D1-145[»]
ProteinModelPortaliP02070.
SMRiP02070.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02070.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP02070.
KOiK13823.
OMAiWTRRFFE.
OrthoDBiEOG091G0R7W.
TreeFamiTF333268.

Family and domain databases

CDDicd08925. Hb-beta_like. 1 hit.
Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002337. Haemoglobin_b.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00814. BETAHAEM.
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.

P02070-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTAEEKAAV TAFWGKVKVD EVGGEALGRL LVVYPWTQRF FESFGDLSTA
60 70 80 90 100
DAVMNNPKVK AHGKKVLDSF SNGMKHLDDL KGTFAALSEL HCDKLHVDPE
110 120 130 140
NFKLLGNVLV VVLARNFGKE FTPVLQADFQ KVVAGVANAL AHRYH
Length:145
Mass (Da):15,954
Last modified:July 21, 1986 - v1
Checksum:iFD62217E8477CFD4
GO

Polymorphismi

Four allelic beta chains have been found in bovine hemoglobins. A and B alleles were found in Jersey cattle and C and D alleles were found in Angoni cattle (East African short-horn zebu). The sequence shown is that of the allele A.3 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti15G → S in allele B. 1 Publication1
Natural varianti18K → H in allele B. 1 Publication1
Natural varianti20D → G in allele D-Zambia. 1 Publication1
Natural varianti43S → T in allele D-Zambia. 1 Publication1
Natural varianti119K → N in allele B. 1
Natural varianti131K → Q in allele C-Rhodesia. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00376 Genomic DNA. Translation: CAA25111.1.
M63453 Genomic DNA. Translation: AAA30408.1.
PIRiB93504. HBBOB.
RefSeqiNP_776342.1. NM_173917.2.
UniGeneiBt.23726.

Genome annotation databases

EnsembliENSBTAT00000045694; ENSBTAP00000043063; ENSBTAG00000038748.
GeneIDi280813.
KEGGibta:280813.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00376 Genomic DNA. Translation: CAA25111.1.
M63453 Genomic DNA. Translation: AAA30408.1.
PIRiB93504. HBBOB.
RefSeqiNP_776342.1. NM_173917.2.
UniGeneiBt.23726.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FSXX-ray2.10B/D1-145[»]
1G08X-ray1.90B/D1-145[»]
1G09X-ray2.04B/D1-145[»]
1G0AX-ray2.04B/D1-145[»]
1HDAX-ray2.20B/D1-145[»]
2QSPX-ray1.85B/D1-145[»]
2QSSX-ray1.75B/D1-145[»]
3CIUX-ray3.50B/D1-145[»]
3PI8X-ray2.20B/D1-145[»]
3PI9X-ray2.90B/D1-145[»]
3PIAX-ray2.10B/D1-145[»]
ProteinModelPortaliP02070.
SMRiP02070.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000043063.

Protein family/group databases

Allergomei8242. Bos d HG.

Proteomic databases

PaxDbiP02070.
PeptideAtlasiP02070.
PRIDEiP02070.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000045694; ENSBTAP00000043063; ENSBTAG00000038748.
GeneIDi280813.
KEGGibta:280813.

Organism-specific databases

CTDi3043.

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP02070.
KOiK13823.
OMAiWTRRFFE.
OrthoDBiEOG091G0R7W.
TreeFamiTF333268.

Enzyme and pathway databases

ReactomeiR-BTA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-BTA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-BTA-2168880. Scavenging of heme from plasma.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP02070.
PMAP-CutDBP02070.

Gene expression databases

BgeeiENSBTAG00000038748.
ExpressionAtlasiP02070. baseline and differential.

Family and domain databases

CDDicd08925. Hb-beta_like. 1 hit.
Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002337. Haemoglobin_b.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00814. BETAHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHBB_BOVIN
AccessioniPrimary (citable) accession number: P02070
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.