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Protein

Hemoglobin subunit beta-1

Gene

Hbb

Organism
Rattus norvegicus (Rat)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Iron (heme distal ligand)
Metal bindingi93 – 931Iron (heme proximal ligand)

GO - Molecular functioni

  • heme binding Source: InterPro
  • hemoglobin alpha binding Source: RGD
  • hemoglobin beta binding Source: RGD
  • iron ion binding Source: InterPro
  • oxygen binding Source: InterPro
  • oxygen transporter activity Source: UniProtKB-KW

GO - Biological processi

  • glutathione metabolic process Source: RGD
  • oxygen transport Source: RGD
  • protein heterooligomerization Source: RGD
Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit beta-1
Alternative name(s):
Beta-1-globin
Hemoglobin beta chain, major-form
Hemoglobin beta-1 chain
Gene namesi
Name:Hbb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2783. Hbb.

Subcellular locationi

GO - Cellular componenti

  • hemoglobin complex Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity3 Publications
Chaini2 – 147146Hemoglobin subunit beta-1PRO_0000053090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylvalineBy similarity
Modified residuei18 – 181N6-succinyllysineBy similarity
Modified residuei45 – 451PhosphoserineCombined sources
Modified residuei51 – 511PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei60 – 601N6-succinyllysineBy similarity
Modified residuei124 – 1241PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP02091.
PRIDEiP02091.

PTM databases

iPTMnetiP02091.
PhosphoSiteiP02091.

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

GO - Molecular functioni

  • hemoglobin alpha binding Source: RGD
  • hemoglobin beta binding Source: RGD

Protein-protein interaction databases

BioGridi246605. 2 interactions.
STRINGi10116.ENSRNOP00000048250.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1611Combined sources
Helixi21 – 3515Combined sources
Helixi37 – 426Combined sources
Helixi44 – 463Combined sources
Helixi52 – 576Combined sources
Helixi59 – 7719Combined sources
Helixi79 – 813Combined sources
Helixi82 – 854Combined sources
Helixi87 – 959Combined sources
Helixi102 – 11918Combined sources
Helixi120 – 1223Combined sources
Helixi125 – 14218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DHTX-ray2.98B2-147[»]
3HF4X-ray2.70B/F2-147[»]
ProteinModelPortaliP02091.
SMRiP02091. Positions 2-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02091.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP02091.
KOiK13823.
OrthoDBiEOG7B8S5H.
PhylomeDBiP02091.
TreeFamiTF333268.

Family and domain databases

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.

P02091-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHLTDAEKA AVNGLWGKVN PDDVGGEALG RLLVVYPWTQ RYFDSFGDLS
60 70 80 90 100
SASAIMGNPK VKAHGKKVIN AFNDGLKHLD NLKGTFAHLS ELHCDKLHVD
110 120 130 140
PENFRLLGNM IVIVLGHHLG KEFTPCAQAA FQKVVAGVAS ALAHKYH
Length:147
Mass (Da):15,979
Last modified:January 23, 2007 - v3
Checksum:i77A715901BC44D26
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141G → A in AAA41309 (PubMed:3619896).Curated

Polymorphismi

In rats there are two non-allelic alpha chains and two non-allelic beta chains.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591P → A.
Natural varianti88 – 881H → N.
Natural varianti90 – 901S → T.
Natural varianti124 – 1241T → S.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16417 mRNA. Translation: CAA34439.1.
X15009 Genomic DNA. Translation: CAA33114.1.
M17084 mRNA. Translation: AAA41309.1.
X67613 Genomic DNA. Translation: CAA47873.1.
BC058448 mRNA. Translation: AAH58448.1.
PIRiS04588.
S06748. HBRT.
RefSeqiNP_150237.1. NM_033234.1.
UniGeneiRn.202945.

Genome annotation databases

GeneIDi24440.
KEGGirno:24440.
UCSCiRGD:2783. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16417 mRNA. Translation: CAA34439.1.
X15009 Genomic DNA. Translation: CAA33114.1.
M17084 mRNA. Translation: AAA41309.1.
X67613 Genomic DNA. Translation: CAA47873.1.
BC058448 mRNA. Translation: AAH58448.1.
PIRiS04588.
S06748. HBRT.
RefSeqiNP_150237.1. NM_033234.1.
UniGeneiRn.202945.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DHTX-ray2.98B2-147[»]
3HF4X-ray2.70B/F2-147[»]
ProteinModelPortaliP02091.
SMRiP02091. Positions 2-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246605. 2 interactions.
STRINGi10116.ENSRNOP00000048250.

PTM databases

iPTMnetiP02091.
PhosphoSiteiP02091.

Proteomic databases

PaxDbiP02091.
PRIDEiP02091.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24440.
KEGGirno:24440.
UCSCiRGD:2783. rat.

Organism-specific databases

CTDi3043.
RGDi2783. Hbb.

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP02091.
KOiK13823.
OrthoDBiEOG7B8S5H.
PhylomeDBiP02091.
TreeFamiTF333268.

Miscellaneous databases

EvolutionaryTraceiP02091.
PROiP02091.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequences of two beta-globin genes in a Sprague-Dawley rat."
    Woo C., Lam V.M.S., Tam J.W.O.
    Nucleic Acids Res. 17:8870-8870(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Genomic sequence of rat beta-globin major gene."
    Radosavlevic D., Crkvenjakov R.
    Nucleic Acids Res. 17:4368-4368(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
  3. "Molecular cloning and sequence analysis of two rat major globin cDNAs."
    Satoh H., Fujii H., Okazaki T.
    Biochem. Biophys. Res. Commun. 146:618-624(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Inokuchi N., Iwahara S., Satoh H., Nagoe Y., Okazaki T.
    Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Wistar.
    Tissue: Liver.
  5. "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].
    Tissue: Pituitary.
  6. "Primary structure of the major beta chain of rat hemoglobin."
    Garrick L.M., Klonowski T.J., Sloan R.L., Ryan T.W., Garrick M.D.
    Fed. Proc. 36:758-758(1977)
    Cited for: PROTEIN SEQUENCE OF 2-147.
  7. "Purification and characterization of fatty acid-binding proteins from brown adipose tissue of the rat."
    Dutta-Roy A.K., Huang Y., Dunbar B., Trayhurn P.
    Biochim. Biophys. Acta 1169:73-79(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-36.
    Tissue: Brown adipose tissue.
  8. Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-60; 67-145; 84-104 AND 106-145, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-51 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHBB1_RAT
AccessioniPrimary (citable) accession number: P02091
Secondary accession number(s): P33584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

PubMed:8334153 incorrectly assigned their sequence fragment as a fatty acid-binding protein.Curated

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.