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O14777

- NDC80_HUMAN

UniProt

O14777 - NDC80_HUMAN

Protein

Kinetochore protein NDC80 homolog

Gene

NDC80

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore.9 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. attachment of spindle microtubules to kinetochore Source: UniProtKB
    2. cell cycle Source: UniProtKB
    3. chromosome segregation Source: UniProtKB
    4. establishment of mitotic spindle orientation Source: UniProtKB
    5. mitotic cell cycle Source: Reactome
    6. mitotic nuclear division Source: ProtInc
    7. mitotic sister chromatid segregation Source: ProtInc
    8. mitotic spindle organization Source: UniProtKB
    9. phosphatidylinositol-mediated signaling Source: UniProtKB
    10. spindle organization Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.
    SignaLinkiO14777.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinetochore protein NDC80 homolog
    Alternative name(s):
    Highly expressed in cancer protein
    Kinetochore protein Hec1
    Short name:
    HsHec1
    Kinetochore-associated protein 2
    Retinoblastoma-associated protein HEC
    Gene namesi
    Name:NDC80
    Synonyms:HEC, HEC1, KNTC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:16909. NDC80.

    Subcellular locationi

    Nucleus. Chromosomecentromerekinetochore
    Note: Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: ProtInc
    2. condensed chromosome kinetochore Source: UniProtKB
    3. condensed nuclear chromosome outer kinetochore Source: BHF-UCL
    4. cytosol Source: Reactome
    5. kinetochore Source: UniProtKB
    6. membrane Source: UniProtKB
    7. Ndc80 complex Source: UniProtKB
    8. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi234 – 2341E → K: Abrogates binding to RB1. 1 Publication

    Organism-specific databases

    PharmGKBiPA162397359.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 642642Kinetochore protein NDC80 homologPRO_0000249550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691Phosphoserine2 Publications
    Modified residuei165 – 1651Phosphoserine; by NEK22 Publications

    Post-translational modificationi

    Phosphorylation begins in S phase of the cell cycle and peaks in mitosis. Phosphorylated by NEK2. May also be phosphorylated by AURKA and AURKB.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO14777.
    PaxDbiO14777.
    PeptideAtlasiO14777.
    PRIDEiO14777.

    PTM databases

    PhosphoSiteiO14777.

    Expressioni

    Developmental stagei

    Expression peaks in mitosis.3 Publications

    Gene expression databases

    ArrayExpressiO14777.
    BgeeiO14777.
    CleanExiHS_NDC80.
    GenevestigatoriO14777.

    Interactioni

    Subunit structurei

    Component of the NDC80 complex, which consists of NDC80/HEC1, CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed by two subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-SPBC25. Each subcomplex is formed by parallel interactions through the coiled-coil domains of individual subunits. Formation of a tetrameric complex is mediated by interactions between the C-terminal regions of both subunits of the NDC80/HEC1-CDCA1 subcomplex and the N-terminal regions of both subunits of the SPBC24-SPBC25 complex. The tetrameric NDC80 complex has an elongated rod-like structure with globular domains at either end. Interacts with isoform 1 of NEK2 and ZWINT specifically during mitosis. Interacts with CENPH and MIS12. May interact with AURKB, PSMC2, PSMC5 and SMC1A. May interact with RB1 during G2 phase and mitosis.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CENPHQ9H3R53EBI-715849,EBI-1003700
    NUF2Q9BZD410EBI-715849,EBI-724102
    SPC25Q9HBM19EBI-715849,EBI-999909
    ZWINTO9522911EBI-715849,EBI-1001132

    Protein-protein interaction databases

    BioGridi115675. 34 interactions.
    IntActiO14777. 33 interactions.
    MINTiMINT-1411676.
    STRINGi9606.ENSP00000261597.

    Structurei

    Secondary structure

    1
    642
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi89 – 10517
    Turni114 – 1174
    Helixi122 – 13312
    Turni134 – 1363
    Helixi147 – 15711
    Helixi166 – 1705
    Turni171 – 1733
    Turni175 – 1773
    Helixi178 – 19417
    Helixi222 – 23817
    Helixi244 – 25815
    Helixi264 – 28623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IGPX-ray1.80A81-196[»]
    2VE7X-ray2.88A/B80-286[»]
    3IZ0electron microscopy-C/E80-286[»]
    ProteinModelPortaliO14777.
    SMRiO14777. Positions 80-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14777.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 445445Interaction with the N-terminus of CDCA1Add
    BLAST
    Regioni1 – 250250Nuclear localizationAdd
    BLAST
    Regioni128 – 251124Interaction with RB1Add
    BLAST
    Regioni251 – 618368Interaction with NEK2 and ZWINTAdd
    BLAST
    Regioni251 – 431181Interaction with SMC1AAdd
    BLAST
    Regioni361 – 547187Interaction with PSMC2 and SMC1AAdd
    BLAST
    Regioni446 – 642197Interaction with the C-terminus of CDCA1 and the SPBC24-SPBC25 subcomplexAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili261 – 403143Sequence AnalysisAdd
    BLAST
    Coiled coili458 – 642185Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NDC80/HEC1 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5185.
    HOGENOMiHOG000012981.
    HOVERGENiHBG081861.
    InParanoidiO14777.
    KOiK11547.
    OMAiREYEECM.
    OrthoDBiEOG7NSB3P.
    PhylomeDBiO14777.
    TreeFamiTF101177.

    Family and domain databases

    InterProiIPR005550. Kinetochore_Ndc80.
    [Graphical view]
    PANTHERiPTHR10643. PTHR10643. 1 hit.
    PfamiPF03801. Ndc80_HEC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O14777-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRSSVSSGG AGRLSMQELR SQDVNKQGLY TPQTKEKPTF GKLSINKPTS    50
    ERKVSLFGKR TSGHGSRNSQ LGIFSSSEKI KDPRPLNDKA FIQQCIRQLC 100
    EFLTENGYAH NVSMKSLQAP SVKDFLKIFT FLYGFLCPSY ELPDTKFEEE 150
    VPRIFKDLGY PFALSKSSMY TVGAPHTWPH IVAALVWLID CIKIHTAMKE 200
    SSPLFDDGQP WGEETEDGIM HNKLFLDYTI KCYESFMSGA DSFDEMNAEL 250
    QSKLKDLFNV DAFKLESLEA KNRALNEQIA RLEQEREKEP NRLESLRKLK 300
    ASLQGDVQKY QAYMSNLESH SAILDQKLNG LNEEIARVEL ECETIKQENT 350
    RLQNIIDNQK YSVADIERIN HERNELQQTI NKLTKDLEAE QQKLWNEELK 400
    YARGKEAIET QLAEYHKLAR KLKLIPKGAE NSKGYDFEIK FNPEAGANCL 450
    VKYRAQVYVP LKELLNETEE EINKALNKKM GLEDTLEQLN AMITESKRSV 500
    RTLKEEVQKL DDLYQQKIKE AEEEDEKCAS ELESLEKHKH LLESTVNQGL 550
    SEAMNELDAV QREYQLVVQT TTEERRKVGN NLQRLLEMVA THVGSVEKHL 600
    EEQIAKVDRE YEECMSEDLS ENIKEIRDKY EKKATLIKSS EE 642
    Length:642
    Mass (Da):73,913
    Last modified:January 1, 1998 - v1
    Checksum:i6A82DA4D8B77ECDC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti66 – 661S → A.
    Corresponds to variant rs16943490 [ dbSNP | Ensembl ].
    VAR_027436
    Natural varianti348 – 3481E → D.
    Corresponds to variant rs12456560 [ dbSNP | Ensembl ].
    VAR_027437
    Natural varianti605 – 6051A → P.
    Corresponds to variant rs1983346 [ dbSNP | Ensembl ].
    VAR_027438

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017790 mRNA. Translation: AAB80726.1.
    BC010171 mRNA. No translation available.
    CCDSiCCDS11827.1.
    RefSeqiNP_006092.1. NM_006101.2.
    UniGeneiHs.414407.

    Genome annotation databases

    EnsembliENST00000261597; ENSP00000261597; ENSG00000080986.
    GeneIDi10403.
    KEGGihsa:10403.
    UCSCiuc002kli.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017790 mRNA. Translation: AAB80726.1 .
    BC010171 mRNA. No translation available.
    CCDSi CCDS11827.1.
    RefSeqi NP_006092.1. NM_006101.2.
    UniGenei Hs.414407.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IGP X-ray 1.80 A 81-196 [» ]
    2VE7 X-ray 2.88 A/B 80-286 [» ]
    3IZ0 electron microscopy - C/E 80-286 [» ]
    ProteinModelPortali O14777.
    SMRi O14777. Positions 80-302.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115675. 34 interactions.
    IntActi O14777. 33 interactions.
    MINTi MINT-1411676.
    STRINGi 9606.ENSP00000261597.

    Chemistry

    ChEMBLi CHEMBL5660.

    PTM databases

    PhosphoSitei O14777.

    Proteomic databases

    MaxQBi O14777.
    PaxDbi O14777.
    PeptideAtlasi O14777.
    PRIDEi O14777.

    Protocols and materials databases

    DNASUi 10403.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261597 ; ENSP00000261597 ; ENSG00000080986 .
    GeneIDi 10403.
    KEGGi hsa:10403.
    UCSCi uc002kli.3. human.

    Organism-specific databases

    CTDi 10403.
    GeneCardsi GC18P002571.
    HGNCi HGNC:16909. NDC80.
    MIMi 607272. gene.
    neXtProti NX_O14777.
    PharmGKBi PA162397359.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5185.
    HOGENOMi HOG000012981.
    HOVERGENi HBG081861.
    InParanoidi O14777.
    KOi K11547.
    OMAi REYEECM.
    OrthoDBi EOG7NSB3P.
    PhylomeDBi O14777.
    TreeFami TF101177.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.
    SignaLinki O14777.

    Miscellaneous databases

    ChiTaRSi NDC80. human.
    EvolutionaryTracei O14777.
    GeneWikii NDC80.
    GenomeRNAii 10403.
    NextBioi 39424.
    PROi O14777.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14777.
    Bgeei O14777.
    CleanExi HS_NDC80.
    Genevestigatori O14777.

    Family and domain databases

    InterProi IPR005550. Kinetochore_Ndc80.
    [Graphical view ]
    PANTHERi PTHR10643. PTHR10643. 1 hit.
    Pfami PF03801. Ndc80_HEC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "HEC, a novel nuclear protein rich in leucine heptad repeats specifically involved in mitosis."
      Chen Y., Riley D.J., Chen P.-L., Lee W.-H.
      Mol. Cell. Biol. 17:6049-6056(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    2. "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: Brain and Lymph.
    3. "HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins."
      Chen Y., Sharp Z.D., Lee W.-H.
      J. Biol. Chem. 272:24081-24087(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK2; PSMC2; PSMC5 AND SMC1A, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    4. "Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins."
      Zheng L., Chen Y., Lee W.-H.
      Mol. Cell. Biol. 19:5417-5428(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK2; PSMC2; PSMC5; RB1 AND SMC1A.
    5. "Retinoblastoma protein enhances the fidelity of chromosome segregation mediated by hsHec1p."
      Zheng L., Chen Y., Riley D.J., Chen P.-L., Lee W.-H.
      Mol. Cell. Biol. 20:3529-3537(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1 AND SMC1A, MUTAGENESIS OF GLU-234.
    6. "Phosphorylation of the mitotic regulator protein Hec1 by Nek2 kinase is essential for faithful chromosome segregation."
      Chen Y., Riley D.J., Zheng L., Chen P.-L., Lee W.-H.
      J. Biol. Chem. 277:49408-49416(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK2, PHOSPHORYLATION AT SER-165 BY NEK2.
    7. "Role of Hec1 in spindle checkpoint signaling and kinetochore recruitment of Mad1/Mad2."
      Martin-Lluesma S., Stucke V.M., Nigg E.A.
      Science 297:2267-2270(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Nuf2 and Hec1 are required for retention of the checkpoint proteins Mad1 and Mad2 to kinetochores."
      DeLuca J.G., Howell B.J., Canman J.C., Hickey J.M., Fang G., Salmon E.D.
      Curr. Biol. 13:2103-2109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Kinetochore localization and microtubule interaction of the human spindle checkpoint kinase Mps1."
      Stucke V.M., Baumann C., Nigg E.A.
      Chromosoma 113:1-15(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo."
      Joseph J., Liu S.-T., Jablonski S.A., Yen T.J., Dasso M.
      Curr. Biol. 14:611-617(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Timing and checkpoints in the regulation of mitotic progression."
      Meraldi P., Draviam V.M., Sorger P.K.
      Dev. Cell 7:45-60(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: SUBCELLULAR LOCATION.
    13. "Identification of two novel components of the human NDC80 kinetochore complex."
      Bharadwaj R., Qi W., Yu H.
      J. Biol. Chem. 279:13076-13085(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NDC80 COMPLEX.
    14. "NEK2A interacts with MAD1 and possibly functions as a novel integrator of the spindle checkpoint signaling."
      Lou Y., Yao J., Zereshki A., Dou Z., Ahmed K., Wang H., Hu J., Wang Y., Yao X.
      J. Biol. Chem. 279:20049-20057(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "Identification of the substrates and interaction proteins of aurora kinases from a protein-protein interaction model."
      Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G., Lin W.-J., Still I.H., Huang C.-Y.F.
      Mol. Cell. Proteomics 3:93-104(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AURKB AND CDCA1, PHOSPHORYLATION BY AURKA AND AURKB.
    16. "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1."
      Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.
      Nat. Cell Biol. 6:1135-1141(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH MIS12.
    17. "Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores."
      Ahonen L.J., Kallio M.J., Daum J.R., Bolton M., Manke I.A., Yaffe M.B., Stukenberg P.T., Gorbsky G.J.
      Curr. Biol. 15:1078-1089(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. "Architecture of the human Ndc80-Hec1 complex, a critical constituent of the outer kinetochore."
      Ciferri C., De Luca J., Monzani S., Ferrari K.J., Ristic D., Wyman C., Stark H., Kilmartin J., Salmon E.D., Musacchio A.
      J. Biol. Chem. 280:29088-29095(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE NDC80 COMPLEX, SUBCELLULAR LOCATION.
    19. "ZW10 links mitotic checkpoint signaling to the structural kinetochore."
      Kops G.J.P.L., Kim Y., Weaver B.A.A., Mao Y., McLeod I., Yates J.R. III, Tagaya M., Cleveland D.W.
      J. Cell Biol. 169:49-60(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ZWINT.
    20. "Hec1 and Nuf2 are core components of the kinetochore outer plate essential for organizing microtubule attachment sites."
      DeLuca J.G., Dong Y., Hergert P., Strauss J., Hickey J.M., Salmon E.D., McEwen B.F.
      Mol. Biol. Cell 16:519-531(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    21. "The functional region of CENP-H interacts with the Nuf2 complex that localizes to centromere during mitosis."
      Mikami Y., Hori T., Kimura H., Fukagawa T.
      Mol. Cell. Biol. 25:1958-1970(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CENPH.
    22. "Hec1 sequentially recruits Zwint-1 and ZW10 to kinetochores for faithful chromosome segregation and spindle checkpoint control."
      Lin Y.-T., Chen Y., Wu G., Lee W.-H.
      Oncogene 25:6901-6914(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZWINT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNDC80_HUMAN
    AccessioniPrimary (citable) accession number: O14777
    Secondary accession number(s): Q6PJX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 120 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, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: 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