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Protein

Hemoglobin subunit epsilon

Gene

HBE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin.

Sites

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

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. protein heterooligomerization Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit epsilon
Alternative name(s):
Epsilon-globin
Hemoglobin epsilon chain
Gene namesi
Name:HBE1
Synonyms:HBE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:4830. HBE1.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProtKB
  2. cytosol Source: Reactome
  3. hemoglobin complex Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29205.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 147146Hemoglobin subunit epsilonPRO_0000053212Add
BLAST

Proteomic databases

MaxQBiP02100.
PaxDbiP02100.
PeptideAtlasiP02100.
PRIDEiP02100.

PTM databases

PhosphoSiteiP02100.

Expressioni

Tissue specificityi

Red blood cells.

Gene expression databases

BgeeiP02100.
CleanExiHS_HBE1.
ExpressionAtlasiP02100. baseline and differential.
GenevestigatoriP02100.

Organism-specific databases

HPAiHPA043234.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two epsilon chains in early embryonic hemoglobin Gower-2; two zeta chains and two epsilon chains in early embryonic hemoglobin Gower-1.1 Publication

Protein-protein interaction databases

BioGridi109296. 2 interactions.
IntActiP02100. 4 interactions.
STRINGi9606.ENSP00000292896.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Turni21 – 233Combined sources
Helixi24 – 3512Combined sources
Helixi37 – 415Combined sources
Helixi44 – 463Combined sources
Helixi52 – 576Combined sources
Helixi59 – 7618Combined sources
Beta strandi79 – 813Combined sources
Turni83 – 864Combined sources
Helixi87 – 948Combined sources
Turni95 – 973Combined 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
1A9WX-ray2.90E/F2-147[»]
ProteinModelPortaliP02100.
SMRiP02100. Positions 2-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02100.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG325823.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP02100.
KOiK13825.
OMAiMDNLKGA.
OrthoDBiEOG7B8S5H.
PhylomeDBiP02100.
TreeFamiTF333268.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]
PANTHERiPTHR11442:SF7. PTHR11442:SF7. 1 hit.
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.

P02100-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHFTAEEKA AVTSLWSKMN VEEAGGEALG RLLVVYPWTQ RFFDSFGNLS
60 70 80 90 100
SPSAILGNPK VKAHGKKVLT SFGDAIKNMD NLKPAFAKLS ELHCDKLHVD
110 120 130 140
PENFKLLGNV MVIILATHFG KEFTPEVQAA WQKLVSAVAI ALAHKYH
Length:147
Mass (Da):16,203
Last modified:January 23, 2007 - v2
Checksum:i223388816EDDE8D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431A → G AA sequence (PubMed:6172865).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01317 Genomic DNA. Translation: AAA16330.1.
V00508 Genomic DNA. Translation: CAA23766.1.
CR541912 mRNA. Translation: CAG46710.1.
CH471064 Genomic DNA. Translation: EAW68802.1.
BC015537 mRNA. Translation: AAH15537.1.
CCDSiCCDS7756.1.
PIRiA90802. HEHU.
RefSeqiNP_005321.1. NM_005330.3.
UniGeneiHs.655195.

Genome annotation databases

EnsembliENST00000292896; ENSP00000292896; ENSG00000213931.
ENST00000380237; ENSP00000369586; ENSG00000213931.
GeneIDi3046.
KEGGihsa:3046.
UCSCiuc001mal.1. human.

Polymorphism databases

DMDMi122726.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01317 Genomic DNA. Translation: AAA16330.1.
V00508 Genomic DNA. Translation: CAA23766.1.
CR541912 mRNA. Translation: CAG46710.1.
CH471064 Genomic DNA. Translation: EAW68802.1.
BC015537 mRNA. Translation: AAH15537.1.
CCDSiCCDS7756.1.
PIRiA90802. HEHU.
RefSeqiNP_005321.1. NM_005330.3.
UniGeneiHs.655195.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9WX-ray2.90E/F2-147[»]
ProteinModelPortaliP02100.
SMRiP02100. Positions 2-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109296. 2 interactions.
IntActiP02100. 4 interactions.
STRINGi9606.ENSP00000292896.

PTM databases

PhosphoSiteiP02100.

Polymorphism databases

DMDMi122726.

Proteomic databases

MaxQBiP02100.
PaxDbiP02100.
PeptideAtlasiP02100.
PRIDEiP02100.

Protocols and materials databases

DNASUi3046.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000292896; ENSP00000292896; ENSG00000213931.
ENST00000380237; ENSP00000369586; ENSG00000213931.
GeneIDi3046.
KEGGihsa:3046.
UCSCiuc001mal.1. human.

Organism-specific databases

CTDi3046.
GeneCardsiGC11M005289.
HGNCiHGNC:4830. HBE1.
HPAiHPA043234.
MIMi142100. gene.
neXtProtiNX_P02100.
PharmGKBiPA29205.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG325823.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036868.
HOVERGENiHBG009709.
InParanoidiP02100.
KOiK13825.
OMAiMDNLKGA.
OrthoDBiEOG7B8S5H.
PhylomeDBiP02100.
TreeFamiTF333268.

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP02100.
GeneWikiiHBE1.
GenomeRNAii3046.
NextBioi12059.
PROiP02100.
SOURCEiSearch...

Gene expression databases

BgeeiP02100.
CleanExiHS_HBE1.
ExpressionAtlasiP02100. baseline and differential.
GenevestigatoriP02100.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]
PANTHERiPTHR11442:SF7. PTHR11442:SF7. 1 hit.
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. "The primary structure of the human epsilon-globin gene."
    Baralle F.E., Shoulders C.C., Proudfoot N.J.
    Cell 21:621-626(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Lung.
  5. "Embryonic hemoglobin: sequence of the epsilon and zeta chains."
    Clegg J.B.
    Tex. Rep. Biol. Med. 40:23-28(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-147.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution."
    Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T., Baker E.N.
    J. Mol. Biol. 280:475-484(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2, SUBUNIT.

Entry informationi

Entry nameiHBE_HUMAN
AccessioniPrimary (citable) accession number: P02100
Secondary accession number(s): Q6FH44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.