Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02100

- HBE_HUMAN

UniProt

P02100 - HBE_HUMAN

Protein

Hemoglobin subunit epsilon

Gene

HBE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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: UniProt
    2. cytosol Source: Reactome
    3. hemoglobin complex Source: ProtInc

    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

    ArrayExpressiP02100.
    BgeeiP02100.
    CleanExiHS_HBE1.
    GenevestigatoriP02100.

    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 – 1813
    Turni21 – 233
    Helixi24 – 3512
    Helixi37 – 415
    Helixi44 – 463
    Helixi52 – 576
    Helixi59 – 7618
    Beta strandi79 – 813
    Turni83 – 864
    Helixi87 – 948
    Turni95 – 973
    Helixi102 – 11918
    Helixi120 – 1223
    Helixi125 – 14218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MVHFTAEEKA AVTSLWSKMN VEEAGGEALG RLLVVYPWTQ RFFDSFGNLS    50
    SPSAILGNPK VKAHGKKVLT SFGDAIKNMD NLKPAFAKLS ELHCDKLHVD 100
    PENFKLLGNV MVIILATHFG KEFTPEVQAA WQKLVSAVAI ALAHKYH 147
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS7756.1.
    PIRi A90802. HEHU.
    RefSeqi NP_005321.1. NM_005330.3.
    UniGenei Hs.655195.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A9W X-ray 2.90 E/F 2-147 [» ]
    ProteinModelPortali P02100.
    SMRi P02100. Positions 2-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109296. 2 interactions.
    IntActi P02100. 4 interactions.
    STRINGi 9606.ENSP00000292896.

    PTM databases

    PhosphoSitei P02100.

    Polymorphism databases

    DMDMi 122726.

    Proteomic databases

    MaxQBi P02100.
    PaxDbi P02100.
    PeptideAtlasi P02100.
    PRIDEi P02100.

    Protocols and materials databases

    DNASUi 3046.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292896 ; ENSP00000292896 ; ENSG00000213931 .
    ENST00000380237 ; ENSP00000369586 ; ENSG00000213931 .
    GeneIDi 3046.
    KEGGi hsa:3046.
    UCSCi uc001mal.1. human.

    Organism-specific databases

    CTDi 3046.
    GeneCardsi GC11M005289.
    HGNCi HGNC:4830. HBE1.
    MIMi 142100. gene.
    neXtProti NX_P02100.
    PharmGKBi PA29205.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325823.
    HOGENOMi HOG000036868.
    HOVERGENi HBG009709.
    InParanoidi P02100.
    KOi K13825.
    OMAi MDNLKGA.
    OrthoDBi EOG7B8S5H.
    PhylomeDBi P02100.
    TreeFami TF333268.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    EvolutionaryTracei P02100.
    GeneWikii HBE1.
    GenomeRNAii 3046.
    NextBioi 12059.
    PROi P02100.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02100.
    Bgeei P02100.
    CleanExi HS_HBE1.
    Genevestigatori P02100.

    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 ]
    PANTHERi PTHR11442:SF7. PTHR11442:SF7. 1 hit.
    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. "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: October 1, 2014
    This is version 147 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