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Q99075

- HBEGF_HUMAN

UniProt

Q99075 - HBEGF_HUMAN

Protein

Proheparin-binding EGF-like growth factor

Gene

HBEGF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei141 – 1411Plays a critical role in diphtheria toxin binding and toxin sensitivityBy similarity

    GO - Molecular functioni

    1. epidermal growth factor receptor binding Source: ProtInc
    2. growth factor activity Source: UniProtKB
    3. heparin binding Source: UniProtKB

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: BHF-UCL
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. innate immune response Source: Reactome
    5. muscle organ development Source: ProtInc
    6. negative regulation of elastin biosynthetic process Source: Ensembl
    7. neurotrophin TRK receptor signaling pathway Source: Reactome
    8. phosphatidylinositol-mediated signaling Source: Reactome
    9. positive regulation of cell growth Source: Ensembl
    10. positive regulation of cell migration Source: BHF-UCL
    11. positive regulation of keratinocyte migration Source: Ensembl
    12. positive regulation of protein kinase B signaling Source: BHF-UCL
    13. positive regulation of smooth muscle cell proliferation Source: Ensembl
    14. positive regulation of wound healing Source: BHF-UCL
    15. regulation of heart contraction Source: Ensembl
    16. signal transduction Source: ProtInc
    17. wound healing, spreading of epidermal cells Source: Ensembl

    Keywords - Molecular functioni

    Growth factor, Receptor

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_115596. Signaling by ERBB4.
    REACT_115755. Signaling by ERBB2.
    REACT_115854. GRB2 events in ERBB2 signaling.
    REACT_115961. PI3K events in ERBB4 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116005. SHC1 events in ERBB4 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_116022. Nuclear signaling by ERBB4.
    REACT_121096. EGFR Transactivation by Gastrin.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiQ99075.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proheparin-binding EGF-like growth factor
    Cleaved into the following chain:
    Heparin-binding EGF-like growth factor
    Short name:
    HB-EGF
    Short name:
    HBEGF
    Alternative name(s):
    Diphtheria toxin receptor
    Short name:
    DT-R
    Gene namesi
    Name:HBEGF
    Synonyms:DTR, DTS, HEGFL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:3059. HBEGF.

    Subcellular locationi

    Chain Heparin-binding EGF-like growth factor : Secretedextracellular space
    Note: Mature HB-EGF is released into the extracellular space and probably binds to a receptor.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27513.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 208189Proheparin-binding EGF-like growth factorPRO_0000302803Add
    BLAST
    Propeptidei20 – 6243Or 72, or 73, or 76, or 811 PublicationPRO_0000007611Add
    BLAST
    Chaini63 – 14886Heparin-binding EGF-like growth factorPRO_0000007612Add
    BLAST
    Propeptidei149 – 20860C-terminalSequence AnalysisPRO_0000007613Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371O-linked (GalNAc...)1 Publication
    Glycosylationi38 – 381O-linked (GalNAc...)1 Publication
    Glycosylationi44 – 441O-linked (GalNAc...)2 Publications
    Glycosylationi47 – 471O-linked (GalNAc...)1 Publication
    Glycosylationi75 – 751O-linked (GalNAc...)1 Publication
    Glycosylationi85 – 851O-linked (GalNAc...)1 Publication
    Disulfide bondi108 ↔ 121PROSITE-ProRule annotation
    Disulfide bondi116 ↔ 132PROSITE-ProRule annotation
    Disulfide bondi134 ↔ 143PROSITE-ProRule annotation

    Post-translational modificationi

    Several N-termini have been identified by direct sequencing. The forms with N-termini 63, 73 and 74 have been tested and found to be biologically active.
    O-glycosylated with core 1 or possibly core 8 glycans. Thr-47 is a minor glycosylation site compared to Thr-44.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ99075.
    PRIDEiQ99075.

    PTM databases

    PhosphoSiteiQ99075.

    Miscellaneous databases

    PMAP-CutDBQ99075.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99075.
    BgeeiQ99075.
    CleanExiHS_HBEGF.
    GenevestigatoriQ99075.

    Organism-specific databases

    HPAiHPA053243.

    Interactioni

    Subunit structurei

    Interacts with FBLN1 By similarity. Interacts with EGFR and ERBB4.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi108172. 9 interactions.
    DIPiDIP-114N.
    IntActiQ99075. 1 interaction.
    MINTiMINT-1511911.
    STRINGi9606.ENSP00000230990.

    Structurei

    Secondary structure

    1
    208
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni108 – 1147
    Beta strandi117 – 1215
    Turni125 – 1284
    Beta strandi132 – 1343
    Beta strandi138 – 1403
    Beta strandi188 – 1958

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XDTX-ray2.65R73-147[»]
    2M8SNMR-B185-208[»]
    ProteinModelPortaliQ99075.
    SMRiQ99075. Positions 107-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99075.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 160141ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini185 – 20824CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei161 – 18424HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini104 – 14441EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 EGF-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG45526.
    HOGENOMiHOG000026782.
    HOVERGENiHBG053952.
    InParanoidiQ99075.
    KOiK08523.
    OMAiYSYDHTT.
    OrthoDBiEOG7VQJGP.
    PhylomeDBiQ99075.
    TreeFamiTF332773.

    Family and domain databases

    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR015497. EGF_rcpt_ligand.
    [Graphical view]
    PANTHERiPTHR10740. PTHR10740. 1 hit.
    PfamiPF00008. EGF. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99075-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLLPSVVLK LFLAAVLSAL VTGESLERLR RGLAAGTSNP DPPTVSTDQL    50
    LPLGGGRDRK VRDLQEADLD LLRVTLSSKP QALATPNKEE HGKRKKKGKG 100
    LGKKRDPCLR KYKDFCIHGE CKYVKELRAP SCICHPGYHG ERCHGLSLPV 150
    ENRLYTYDHT TILAVVAVVL SSVCLLVIVG LLMFRYHRRG GYDVENEEKV 200
    KLGMTNSH 208
    Length:208
    Mass (Da):23,067
    Last modified:June 1, 1994 - v1
    Checksum:i2C43C9D1D8291B51
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60278 mRNA. Translation: AAA35956.1.
    AY164533 Genomic DNA. Translation: AAN46738.1.
    AK313202 mRNA. Translation: BAG36018.1.
    AC004634 Genomic DNA. Translation: AAC15470.1.
    CH471062 Genomic DNA. Translation: EAW62069.1.
    BC033097 mRNA. Translation: AAH33097.1.
    CCDSiCCDS4223.1.
    PIRiA38432.
    RefSeqiNP_001936.1. NM_001945.2.
    UniGeneiHs.592942.
    Hs.799.

    Genome annotation databases

    EnsembliENST00000230990; ENSP00000230990; ENSG00000113070.
    GeneIDi1839.
    KEGGihsa:1839.
    UCSCiuc003lfi.3. human.

    Polymorphism databases

    DMDMi544477.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60278 mRNA. Translation: AAA35956.1 .
    AY164533 Genomic DNA. Translation: AAN46738.1 .
    AK313202 mRNA. Translation: BAG36018.1 .
    AC004634 Genomic DNA. Translation: AAC15470.1 .
    CH471062 Genomic DNA. Translation: EAW62069.1 .
    BC033097 mRNA. Translation: AAH33097.1 .
    CCDSi CCDS4223.1.
    PIRi A38432.
    RefSeqi NP_001936.1. NM_001945.2.
    UniGenei Hs.592942.
    Hs.799.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XDT X-ray 2.65 R 73-147 [» ]
    2M8S NMR - B 185-208 [» ]
    ProteinModelPortali Q99075.
    SMRi Q99075. Positions 107-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108172. 9 interactions.
    DIPi DIP-114N.
    IntActi Q99075. 1 interaction.
    MINTi MINT-1511911.
    STRINGi 9606.ENSP00000230990.

    PTM databases

    PhosphoSitei Q99075.

    Polymorphism databases

    DMDMi 544477.

    Proteomic databases

    PaxDbi Q99075.
    PRIDEi Q99075.

    Protocols and materials databases

    DNASUi 1839.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230990 ; ENSP00000230990 ; ENSG00000113070 .
    GeneIDi 1839.
    KEGGi hsa:1839.
    UCSCi uc003lfi.3. human.

    Organism-specific databases

    CTDi 1839.
    GeneCardsi GC05M139694.
    HGNCi HGNC:3059. HBEGF.
    HPAi HPA053243.
    MIMi 126150. gene.
    neXtProti NX_Q99075.
    PharmGKBi PA27513.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45526.
    HOGENOMi HOG000026782.
    HOVERGENi HBG053952.
    InParanoidi Q99075.
    KOi K08523.
    OMAi YSYDHTT.
    OrthoDBi EOG7VQJGP.
    PhylomeDBi Q99075.
    TreeFami TF332773.

    Enzyme and pathway databases

    Reactomei REACT_115596. Signaling by ERBB4.
    REACT_115755. Signaling by ERBB2.
    REACT_115854. GRB2 events in ERBB2 signaling.
    REACT_115961. PI3K events in ERBB4 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116005. SHC1 events in ERBB4 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_116022. Nuclear signaling by ERBB4.
    REACT_121096. EGFR Transactivation by Gastrin.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki Q99075.

    Miscellaneous databases

    EvolutionaryTracei Q99075.
    GeneWikii Heparin-binding_EGF-like_growth_factor.
    GenomeRNAii 1839.
    NextBioi 7529.
    PMAP-CutDB Q99075.
    PROi Q99075.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99075.
    Bgeei Q99075.
    CleanExi HS_HBEGF.
    Genevestigatori Q99075.

    Family and domain databases

    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR015497. EGF_rcpt_ligand.
    [Graphical view ]
    PANTHERi PTHR10740. PTHR10740. 1 hit.
    Pfami PF00008. EGF. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF."
      Higashiyama S., Abraham J.A., Miller J., Fiddes J.C., Klagsbrun M.
      Science 251:936-939(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-93.
      Tissue: Macrophage.
    2. NIEHS SNPs program
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Eye.
    7. "Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein."
      Higashiyama S., Lau K., Besner G.E., Abraham J.A., Klagsbrun M.
      J. Biol. Chem. 267:6205-6212(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 63-141 AND 143-148, GLYCOSYLATION AT THR-75 AND THR-85.
      Tissue: Histiocytic lymphoma.
    8. "Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diphtheria toxin receptor and inhibits specifically its mitogenic activity."
      Mitamura T., Higashiyama S., Taniguchi N., Klagsbrun M., Mekada E.
      J. Biol. Chem. 270:1015-1019(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN TOXIN BINDING.
    9. "Activation of HER4 by heparin-binding EGF-like growth factor stimulates chemotaxis but not proliferation."
      Elenius K., Paul S., Allison G., Sun J., Klagsbrun M.
      EMBO J. 16:1268-1278(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB4.
    10. "ErbB and HB-EGF signaling in heart development and function."
      Iwamoto R., Mekada E.
      Cell Struct. Funct. 31:1-14(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    11. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-44 AND THR-47, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
      Halim A., Ruetschi U., Larson G., Nilsson J.
      J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-37; SER-38 AND THR-44, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor."
      Louie G.V., Yang W., Bowman M.E., Choe S.
      Mol. Cell 1:67-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 73-147 IN COMPLEX WITH TOX.

    Entry informationi

    Entry nameiHBEGF_HUMAN
    AccessioniPrimary (citable) accession number: Q99075
    Secondary accession number(s): B2R821
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 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 5
      Human chromosome 5: 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