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P02062

- HBB_HORSE

UniProt

P02062 - HBB_HORSE

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Protein

Hemoglobin subunit beta

Gene

HBB

Organism
Equus caballus (Horse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Involved in oxygen transport from the lung to the various peripheral tissues.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Iron (heme distal ligand)
Metal bindingi92 – 921Iron (heme proximal ligand)

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. oxygen binding Source: InterPro
  4. oxygen transporter activity Source: UniProtKB-KW
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
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus ›
ProteomesiUP000002281: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. hemoglobin complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146Hemoglobin subunit betaPRO_0000052975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylvalineBy similarity
Modified residuei59 – 591N6-acetyllysineBy similarity
Modified residuei82 – 821N6-acetyllysineBy similarity
Modified residuei93 – 931S-nitrosocysteineBy similarity
Modified residuei144 – 1441N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, S-nitrosylation

Proteomic databases

PRIDEiP02062.

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Protein-protein interaction databases

MINTiMINT-242194.
STRINGi9796.ENSECAP00000008056.

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511Combined sources
Helixi20 – 3415Combined sources
Helixi36 – 4510Combined sources
Helixi51 – 566Combined sources
Helixi58 – 7518Combined sources
Helixi76 – 805Combined sources
Helixi81 – 9414Combined sources
Helixi101 – 11818Combined sources
Helixi119 – 1213Combined sources
Helixi124 – 14118Combined sources
Helixi143 – 1453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP02062.
SMRiP02062. Positions 1-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02062.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG269316.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP02062.
KOiK13823.
OMAiWTRRFFE.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
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.

P02062-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
VQLSGEEKAA VLALWDKVNE EEVGGEALGR LLVVYPWTQR FFDSFGDLSN 
        60         70         80         90        100
PGAVMGNPKV KAHGKKVLHS FGEGVHHLDN LKGTFAALSE LHCDKLHVDP 
       110        120        130        140 
ENFRLLGNVL VVVLARHFGK DFTPELQASY QKVVAGVANA LAHKYH
Length:146
Mass (Da):16,008
Last modified:July 21, 1986 - v1
Checksum:i734664793DA642EE
GO

Sequence databases

PIRiB91688. HBHO.
RefSeqiNP_001157490.1. NM_001164018.1.
UniGeneiEca.16920.

Genome annotation databases

GeneIDi100054109.
KEGGiecb:100054109.

Cross-referencesi

Web resourcesi

Protein Spotlight

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

Sequence databases

PIRi B91688. HBHO.
RefSeqi NP_001157490.1. NM_001164018.1.
UniGenei Eca.16920.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G0B X-ray 1.90 B 1-146 [» ]
1IBE X-ray 1.80 B 1-146 [» ]
1IWH X-ray 1.55 B 1-146 [» ]
1NS6 X-ray 2.05 B 1-146 [» ]
1NS9 X-ray 1.60 B 1-146 [» ]
1Y8H X-ray 3.10 B/D 1-146 [» ]
1Y8I X-ray 2.60 B/D 1-146 [» ]
1Y8K X-ray 2.30 B/D 1-146 [» ]
2D5X X-ray 1.45 B 1-146 [» ]
2DHB X-ray 2.80 B 1-146 [» ]
2MHB X-ray 2.00 B 1-146 [» ]
2ZLT X-ray 1.90 B 1-146 [» ]
2ZLU X-ray 2.00 B 1-146 [» ]
2ZLV X-ray 2.00 B 1-146 [» ]
2ZLW X-ray 2.90 B/D 1-146 [» ]
2ZLX X-ray 2.80 B/D 1-146 [» ]
ProteinModelPortali P02062.
SMRi P02062. Positions 1-146.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-242194.
STRINGi 9796.ENSECAP00000008056.

Proteomic databases

PRIDEi P02062.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100054109.
KEGGi ecb:100054109.

Organism-specific databases

CTDi 3043.

Phylogenomic databases

eggNOGi NOG269316.
HOGENOMi HOG000036868.
HOVERGENi HBG009709.
InParanoidi P02062.
KOi K13823.
OMAi WTRRFFE.

Miscellaneous databases

EvolutionaryTracei P02062.

Family and domain databases

Gene3Di 1.10.490.10. 1 hit.
InterProi IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view ]
Pfami PF00042. Globin. 1 hit.
[Graphical view ]
PRINTSi PR00814. BETAHAEM.
SUPFAMi SSF46458. SSF46458. 1 hit.
PROSITEi PS01033. GLOBIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiHBB_HORSE
AccessioniPrimary (citable) accession number: P02062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 119 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.
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