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P20827

- EFNA1_HUMAN

UniProt

P20827 - EFNA1_HUMAN

Protein

Ephrin-A1

Gene

EFNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis.2 Publications

    GO - Molecular functioni

    1. ephrin receptor binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. receptor binding Source: ProtInc

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. angiogenesis Source: RefGenome
    3. aortic valve morphogenesis Source: BHF-UCL
    4. axon guidance Source: RefGenome
    5. cell-cell signaling Source: ProtInc
    6. cell migration Source: UniProtKB
    7. endocardial cushion to mesenchymal transition involved in heart valve formation Source: BHF-UCL
    8. ephrin receptor signaling pathway Source: UniProtKB
    9. mitral valve morphogenesis Source: BHF-UCL
    10. negative regulation of dendritic spine morphogenesis Source: UniProtKB
    11. negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
    12. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    13. notochord formation Source: Ensembl
    14. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    15. regulation of angiogenesis Source: Ensembl
    16. regulation of axonogenesis Source: Ensembl
    17. regulation of blood vessel endothelial cell migration Source: Ensembl
    18. regulation of cell adhesion mediated by integrin Source: UniProtKB
    19. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    20. substrate adhesion-dependent cell spreading Source: UniProtKB

    Keywords - Biological processi

    Angiogenesis

    Enzyme and pathway databases

    SignaLinkiP20827.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin-A1
    Alternative name(s):
    EPH-related receptor tyrosine kinase ligand 1
    Short name:
    LERK-1
    Immediate early response protein B61
    Tumor necrosis factor alpha-induced protein 4
    Short name:
    TNF alpha-induced protein 4
    Cleaved into the following chain:
    Gene namesi
    Name:EFNA1
    Synonyms:EPLG1, LERK1, TNFAIP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3221. EFNA1.

    Subcellular locationi

    Cell membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication

    GO - Cellular componenti

    1. anchored component of plasma membrane Source: RefGenome
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA27656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 182164Ephrin-A1PRO_0000008353Add
    BLAST
    Chaini19 – ?Ephrin-A1, secreted formPRO_0000389630
    Propeptidei183 – 20523Removed in mature formSequence AnalysisPRO_0000008354Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi26 – 261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi51 ↔ 92
    Disulfide bondi80 ↔ 140
    Lipidationi182 – 1821GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

    Undergoes proteolysis by a metalloprotease to give rise to a soluble monomeric form.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiP20827.
    PRIDEiP20827.

    PTM databases

    PhosphoSiteiP20827.

    Expressioni

    Tissue specificityi

    Brain. Down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells (at protein level).1 Publication

    Inductioni

    By TNF and IL1B/interleukin-1 beta.

    Gene expression databases

    BgeeiP20827.
    CleanExiHS_EFNA1.
    GenevestigatoriP20827.

    Organism-specific databases

    HPAiCAB032498.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Forms heterodimers with EPHA2. Binds to the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6 and EPHA7. Also binds with low affinity to EPHA1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EPHA2P293177EBI-715194,EBI-702104

    Protein-protein interaction databases

    BioGridi108262. 6 interactions.
    DIPiDIP-98N.
    IntActiP20827. 6 interactions.
    MINTiMINT-1393983.
    STRINGi9606.ENSP00000357392.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 245
    Helixi30 – 323
    Beta strandi38 – 414
    Beta strandi46 – 505
    Helixi61 – 633
    Beta strandi67 – 726
    Helixi74 – 796
    Helixi85 – 873
    Beta strandi88 – 925
    Beta strandi98 – 1003
    Beta strandi103 – 1075
    Beta strandi125 – 13410
    Beta strandi142 – 1476

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CZUX-ray2.65B17-171[»]
    3HEIX-ray2.00B/D/F/H/J/L/N/P18-147[»]
    3MBWX-ray2.81B17-171[»]
    ProteinModelPortaliP20827.
    SMRiP20827. Positions 18-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20827.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 151133Ephrin RBDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ephrin family.PROSITE-ProRule annotation
    Contains 1 ephrin RBD (ephrin receptor-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG296825.
    HOGENOMiHOG000234373.
    HOVERGENiHBG051447.
    InParanoidiP20827.
    KOiK05462.
    OMAiPIHHQED.
    OrthoDBiEOG70W3FD.
    PhylomeDBiP20827.

    Family and domain databases

    Gene3Di2.60.40.420. 1 hit.
    InterProiIPR008972. Cupredoxin.
    IPR001799. Ephrin.
    IPR019765. Ephrin_CS.
    [Graphical view]
    PANTHERiPTHR11304. PTHR11304. 1 hit.
    PfamiPF00812. Ephrin. 1 hit.
    [Graphical view]
    PRINTSiPR01347. EPHRIN.
    ProDomiPD002533. Ephrin. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF49503. SSF49503. 1 hit.
    PROSITEiPS01299. EPHRIN_RBD_1. 1 hit.
    PS51551. EPHRIN_RBD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P20827-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEFLWAPLLG LCCSLAAADR HTVFWNSSNP KFRNEDYTIH VQLNDYVDII    50
    CPHYEDHSVA DAAMEQYILY LVEHEEYQLC QPQSKDQVRW QCNRPSAKHG 100
    PEKLSEKFQR FTPFTLGKEF KEGHSYYYIS KPIHQHEDRC LRLKVTVSGK 150
    ITHSPQAHDN PQEKRLAADD PEVRVLHSIG HSAAPRLFPL AWTVLLLPLL 200
    LLQTP 205
    Length:205
    Mass (Da):23,787
    Last modified:August 30, 2005 - v2
    Checksum:iEFF026BF4C12461F
    GO
    Isoform 2 (identifier: P20827-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         131-152: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:183
    Mass (Da):21,246
    Checksum:i8B9A70B6402577BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1801G → A in AAH32698. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti159 – 1591D → V.4 Publications
    Corresponds to variant rs4745 [ dbSNP | Ensembl ].
    VAR_014791

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei131 – 15222Missing in isoform 2. CuratedVSP_017543Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57730 mRNA. Translation: AAA58388.1.
    CR457416 mRNA. Translation: CAG33697.1.
    AL691442 Genomic DNA. Translation: CAI15319.1.
    AL691442 Genomic DNA. Translation: CAI15320.1.
    CH471121 Genomic DNA. Translation: EAW53131.1.
    CH471121 Genomic DNA. Translation: EAW53132.1.
    BC032698 mRNA. Translation: AAH32698.1.
    BC095432 mRNA. Translation: AAH95432.1.
    CCDSiCCDS1091.1. [P20827-1]
    CCDS1092.1. [P20827-2]
    PIRiA36377.
    RefSeqiNP_004419.2. NM_004428.2. [P20827-1]
    NP_872626.1. NM_182685.1. [P20827-2]
    UniGeneiHs.516664.

    Genome annotation databases

    EnsembliENST00000368406; ENSP00000357391; ENSG00000169242. [P20827-2]
    ENST00000368407; ENSP00000357392; ENSG00000169242. [P20827-1]
    GeneIDi1942.
    KEGGihsa:1942.
    UCSCiuc001fhh.3. human. [P20827-1]
    uc001fhi.3. human. [P20827-2]

    Polymorphism databases

    DMDMi73920206.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57730 mRNA. Translation: AAA58388.1 .
    CR457416 mRNA. Translation: CAG33697.1 .
    AL691442 Genomic DNA. Translation: CAI15319.1 .
    AL691442 Genomic DNA. Translation: CAI15320.1 .
    CH471121 Genomic DNA. Translation: EAW53131.1 .
    CH471121 Genomic DNA. Translation: EAW53132.1 .
    BC032698 mRNA. Translation: AAH32698.1 .
    BC095432 mRNA. Translation: AAH95432.1 .
    CCDSi CCDS1091.1. [P20827-1 ]
    CCDS1092.1. [P20827-2 ]
    PIRi A36377.
    RefSeqi NP_004419.2. NM_004428.2. [P20827-1 ]
    NP_872626.1. NM_182685.1. [P20827-2 ]
    UniGenei Hs.516664.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CZU X-ray 2.65 B 17-171 [» ]
    3HEI X-ray 2.00 B/D/F/H/J/L/N/P 18-147 [» ]
    3MBW X-ray 2.81 B 17-171 [» ]
    ProteinModelPortali P20827.
    SMRi P20827. Positions 18-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108262. 6 interactions.
    DIPi DIP-98N.
    IntActi P20827. 6 interactions.
    MINTi MINT-1393983.
    STRINGi 9606.ENSP00000357392.

    PTM databases

    PhosphoSitei P20827.

    Polymorphism databases

    DMDMi 73920206.

    Proteomic databases

    PaxDbi P20827.
    PRIDEi P20827.

    Protocols and materials databases

    DNASUi 1942.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368406 ; ENSP00000357391 ; ENSG00000169242 . [P20827-2 ]
    ENST00000368407 ; ENSP00000357392 ; ENSG00000169242 . [P20827-1 ]
    GeneIDi 1942.
    KEGGi hsa:1942.
    UCSCi uc001fhh.3. human. [P20827-1 ]
    uc001fhi.3. human. [P20827-2 ]

    Organism-specific databases

    CTDi 1942.
    GeneCardsi GC01P155099.
    H-InvDB HIX0116282.
    HIX0116386.
    HGNCi HGNC:3221. EFNA1.
    HPAi CAB032498.
    MIMi 191164. gene.
    neXtProti NX_P20827.
    PharmGKBi PA27656.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296825.
    HOGENOMi HOG000234373.
    HOVERGENi HBG051447.
    InParanoidi P20827.
    KOi K05462.
    OMAi PIHHQED.
    OrthoDBi EOG70W3FD.
    PhylomeDBi P20827.

    Enzyme and pathway databases

    SignaLinki P20827.

    Miscellaneous databases

    EvolutionaryTracei P20827.
    GeneWikii Ephrin_A1.
    GenomeRNAii 1942.
    NextBioi 7865.
    PROi P20827.
    SOURCEi Search...

    Gene expression databases

    Bgeei P20827.
    CleanExi HS_EFNA1.
    Genevestigatori P20827.

    Family and domain databases

    Gene3Di 2.60.40.420. 1 hit.
    InterProi IPR008972. Cupredoxin.
    IPR001799. Ephrin.
    IPR019765. Ephrin_CS.
    [Graphical view ]
    PANTHERi PTHR11304. PTHR11304. 1 hit.
    Pfami PF00812. Ephrin. 1 hit.
    [Graphical view ]
    PRINTSi PR01347. EPHRIN.
    ProDomi PD002533. Ephrin. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF49503. SSF49503. 1 hit.
    PROSITEi PS01299. EPHRIN_RBD_1. 1 hit.
    PS51551. EPHRIN_RBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel immediate-early response gene of endothelium is induced by cytokines and encodes a secreted protein."
      Holzman L.B., Marks R.M., Dixit V.M.
      Mol. Cell. Biol. 10:5830-5838(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-159.
    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] (ISOFORM 1), VARIANT VAL-159.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-159.
    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] (ISOFORM 1), VARIANT VAL-159.
      Tissue: Liver.
    6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-33.
    7. "Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins."
      Kozlosky C.J., Maraskovsky E., McGrew J.T., Vanden Bos T., Teepe M., Lyman S.D., Srinivasan S., Fletcher F.A., Gayle R.B. III, Cerretti D.P., Beckmann M.P.
      Oncogene 10:299-306(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR.
    8. "Ephrin-A1 is a negative regulator in glioma through down-regulation of EphA2 and FAK."
      Liu D.-P., Wang Y., Koeffler H.P., Xie D.
      Int. J. Oncol. 30:865-871(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    9. "Soluble monomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor."
      Wykosky J., Palma E., Gibo D.M., Ringler S., Turner C.P., Debinski W.
      Oncogene 27:7260-7273(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
    10. "Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex."
      Himanen J.P., Goldgur Y., Miao H., Myshkin E., Guo H., Buck M., Nguyen M., Rajashankar K.R., Wang B., Nikolov D.B.
      EMBO Rep. 10:722-728(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-147 IN COMPLEX WITH EPHA2, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-26.
    11. "Ephrin A1 bound to the ligand binding domain of the human ephrin A2 (EPHA2) receptor protein kinase."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 19-171 IN COMPLEX WITH EPHA2, DISULFIDE BONDS.

    Entry informationi

    Entry nameiEFNA1_HUMAN
    AccessioniPrimary (citable) accession number: P20827
    Secondary accession number(s): D3DV86
    , Q5SR60, Q5SR61, Q6I9T9, Q8N578
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 144 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3