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
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 bindingi63Iron (heme distal ligand)1
Metal bindingi92Iron (heme proximal ligand)1

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit beta
Alternative name(s):
Beta-globin
Hemoglobin beta chain
Gene namesi
Name:HBB
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000529071 – 146Hemoglobin subunit betaAdd BLAST146

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylvalineBy similarity1
Modified residuei44PhosphoserineBy similarity1
Modified residuei59N6-acetyllysineBy similarity1
Modified residuei82N6-acetyllysineBy similarity1
Modified residuei93S-nitrosocysteineBy similarity1
Modified residuei144N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP60524.
PRIDEiP60524.

Miscellaneous databases

PMAP-CutDBP60524.

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.1 Publication

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000009258.

Structurei

Secondary structure

1146
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 15Combined sources11
Turni20 – 22Combined sources3
Helixi23 – 34Combined sources12
Helixi36 – 45Combined sources10
Helixi51 – 55Combined sources5
Helixi58 – 75Combined sources18
Helixi78 – 80Combined sources3
Helixi81 – 94Combined sources14
Helixi101 – 118Combined sources18
Helixi119 – 121Combined sources3
Helixi124 – 141Combined sources18
Helixi143 – 145Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QLSX-ray3.50B/D1-146[»]
3GOUX-ray3.00B/D1-146[»]
3PELX-ray1.90B1-146[»]
ProteinModelPortaliP60524.
SMRiP60524.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60524.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP60524.

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.

P60524-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VHLTAEEKSL VSGLWGKVNV DEVGGEALGR LLIVYPWTQR FFDSFGDLST
60 70 80 90 100
PDAVMSNAKV KAHGKKVLNS FSDGLKNLDN LKGTFAKLSE LHCDKLHVDP
110 120 130 140
ENFKLLGNVL VCVLAHHFGK EFTPQVQAAY QKVVAGVANA LAHKYH
Length:146
Mass (Da):15,996
Last modified:July 21, 1986 - v1
Checksum:iECD68B81D53608F1
GO

Sequence databases

PIRiA02374. HBDG.

Cross-referencesi

Sequence databases

PIRiA02374. HBDG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QLSX-ray3.50B/D1-146[»]
3GOUX-ray3.00B/D1-146[»]
3PELX-ray1.90B1-146[»]
ProteinModelPortaliP60524.
SMRiP60524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000009258.

Proteomic databases

PaxDbiP60524.
PRIDEiP60524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP60524.

Miscellaneous databases

EvolutionaryTraceiP60524.
PMAP-CutDBP60524.

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_CANLF
AccessioniPrimary (citable) accession number: P60524
Secondary accession number(s): P02056
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 89 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.