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Q03188

- CENPC_HUMAN

UniProt

Q03188 - CENPC_HUMAN

Protein

Centromere protein C

Gene

CENPC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions.2 Publications

    GO - Molecular functioni

    1. centromeric DNA binding Source: InterPro
    2. DNA binding Source: ProtInc

    GO - Biological processi

    1. chromosome segregation Source: UniProtKB
    2. kinetochore assembly Source: UniProtKB
    3. mitotic cell cycle Source: UniProtKB
    4. mitotic nuclear division Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centromere protein C
    Short name:
    CENP-C
    Alternative name(s):
    Centromere autoantigen C
    Centromere protein C 1
    Short name:
    CENP-C 1
    Interphase centromere complex protein 7
    Gene namesi
    Name:CENPC
    Synonyms:CENPC1, ICEN7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:1854. CENPC.

    Subcellular locationi

    Nucleus. Chromosomecentromerekinetochore
    Note: Localizes exclusively in the kinetochore domain of centromeres.

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. condensed nuclear chromosome, centromeric region Source: BHF-UCL
    3. cytoplasm Source: HPA
    4. cytosol Source: Reactome
    5. kinetochore Source: UniProtKB
    6. nucleus Source: HPA
    7. pericentric heterochromatin Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26398.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 943943Centromere protein CPRO_0000089474Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei96 – 961Phosphoserine1 Publication
    Modified residuei130 – 1301Phosphothreonine1 Publication
    Modified residuei146 – 1461Phosphoserine1 Publication
    Modified residuei183 – 1831Phosphothreonine1 Publication
    Modified residuei189 – 1891Phosphoserine1 Publication
    Modified residuei225 – 2251Phosphoserine3 Publications
    Modified residuei261 – 2611Phosphoserine1 Publication
    Modified residuei316 – 3161Phosphoserine1 Publication
    Modified residuei439 – 4391Phosphoserine2 Publications
    Modified residuei538 – 5381Phosphoserine2 Publications
    Modified residuei709 – 7091Phosphoserine1 Publication
    Modified residuei710 – 7101Phosphoserine1 Publication
    Modified residuei734 – 7341Phosphothreonine1 Publication
    Modified residuei763 – 7631Phosphoserine2 Publications
    Modified residuei773 – 7731Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ03188.
    PaxDbiQ03188.
    PRIDEiQ03188.

    PTM databases

    PhosphoSiteiQ03188.

    Expressioni

    Gene expression databases

    ArrayExpressiQ03188.
    BgeeiQ03188.
    CleanExiHS_CENPC1.
    GenevestigatoriQ03188.

    Organism-specific databases

    HPAiHPA049740.

    Interactioni

    Subunit structurei

    Oligomer. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to DAXX. Interacts directly with CENPA.3 Publications

    Protein-protein interaction databases

    BioGridi107489. 15 interactions.
    IntActiQ03188. 11 interactions.
    MINTiMINT-4786577.
    STRINGi9606.ENSP00000273853.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03188.
    SMRiQ03188. Positions 908-936.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni737 – 75923MIF2 homology domain IIAdd
    BLAST
    Regioni890 – 94354MIF2 homology domain IIIAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi259 – 27315Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi484 – 49916Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi558 – 57417Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi780 – 79819Nuclear localization signalSequence AnalysisAdd
    BLAST

    Domaini

    The MIF2 homology domain II targets centromeres and binds the alpha satellite DNA in vivo. The MIF2 homology domain III can induce CENPC dimerization/oligomerization.1 Publication

    Sequence similaritiesi

    Belongs to the CENPC family.Curated

    Phylogenomic databases

    eggNOGiNOG329217.
    HOGENOMiHOG000090256.
    HOVERGENiHBG050891.
    InParanoidiQ03188.
    KOiK11497.
    OMAiGYRRRFC.
    OrthoDBiEOG73FQQ8.
    PhylomeDBiQ03188.
    TreeFamiTF101132.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    InterProiIPR028386. CENP-C/Mif2/cnp3.
    IPR028931. CENP-C_mid.
    IPR028052. CENP_C_N_dom.
    IPR025974. Mif2/CENP-C_cupin.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR16684. PTHR16684. 1 hit.
    PfamiPF11699. CENP-C_C. 1 hit.
    PF15620. CENP-C_mid. 1 hit.
    PF15622. CENP_C_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51182. SSF51182. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q03188-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASGLDHLK NGYRRRFCRP SRARDINTEQ GQNVLEILQD CFEEKSLAND    50
    FSTNSTKSVP NSTRKIKDTC IQSPSKECQK SHPKSVPVSS KKKEASLQFV 100
    VEPSEATNRS VQAHEVHQKI LATDVSSKNT PDSKKISSRN INDHHSEADE 150
    EFYLSVGSPS VLLDAKTSVS QNVIPSSAQK RETYTFENSV NMLPSSTEVS 200
    VKTKKRLNFD DKVMLKKIEI DNKVSDEEDK TSEGQERKPS GSSQNRIRDS 250
    EYEIQRQAKK SFSTLFLETV KRKSESSPIV RHAATAPPHS CPPDDTKLIE 300
    DEFIIDESDQ SFASRSWITI PRKAGSLKQR TISPAESTAL LQGRKSREKH 350
    HNILPKTLAN DKHSHKPHPV ETSQPSDKTV LDTSYALIGE TVNNYRSTKY 400
    EMYSKNAEKP SRSKRTIKQK QRRKFMAKPA EEQLDVGQSK DENIHTSHIT 450
    QDEFQRNSDR NMEEHEEMGN DCVSKKQMPP VGSKKSSTRK DKEESKKKRF 500
    SSESKNKLVP EEVTSTVTKS RRISRRPSDW WVVKSEESPV YSNSSVRNEL 550
    PMHHNSSRKS TKKTNQSSKN IRKKTIPLKR QKTATKGNQR VQKFLNAEGS 600
    GGIVGHDEIS RCSLSEPLES DEADLAKKKN LDCSRSTRSS KNEDNIMTAQ 650
    NVPLKPQTSG YTCNIPTESN LDSGEHKTSV LEESGPSRLN NNYLMSGKND 700
    VDDEEVHGSS DDSKQSKVIP KNRIHHKLVL PSNTPNVRRT KRTRLKPLEY 750
    WRGERIDYQG RPSGGFVISG VLSPDTISSK RKAKENIGKV NKKSNKKRIC 800
    LDNDERKTNL MVNLGIPLGD PLQPTRVKDP ETREIILMDL VRPQDTYQFF 850
    VKHGELKVYK TLDTPFFSTG KLILGPQEEK GKQHVGQDIL VFYVNFGDLL 900
    CTLHETPYIL STGDSFYVPS GNYYNIKNLR NEESVLLFTQ IKR 943
    Length:943
    Mass (Da):106,834
    Last modified:May 18, 2010 - v2
    Checksum:i2AA5AF82BA88C809
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti179 – 1791Q → K in AAA51974. (PubMed:1339310)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti341 – 3411L → F.4 Publications
    Corresponds to variant rs11250 [ dbSNP | Ensembl ].
    VAR_069295
    Natural varianti389 – 3891G → D.1 Publication
    Corresponds to variant rs1056787 [ dbSNP | Ensembl ].
    VAR_069296

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95724 mRNA. Translation: AAA51974.1.
    AC104806 Genomic DNA. No translation available.
    AC109356 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05545.1.
    BC041117 mRNA. Translation: AAH41117.1.
    AF151723 Genomic DNA. Translation: AAF73191.1.
    CCDSiCCDS47063.1.
    PIRiA42681.
    RefSeqiNP_001803.2. NM_001812.2.
    UniGeneiHs.479867.

    Genome annotation databases

    EnsembliENST00000273853; ENSP00000273853; ENSG00000145241.
    GeneIDi1060.
    KEGGihsa:1060.
    UCSCiuc003hdd.1. human.

    Polymorphism databases

    DMDMi296434446.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95724 mRNA. Translation: AAA51974.1 .
    AC104806 Genomic DNA. No translation available.
    AC109356 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05545.1 .
    BC041117 mRNA. Translation: AAH41117.1 .
    AF151723 Genomic DNA. Translation: AAF73191.1 .
    CCDSi CCDS47063.1.
    PIRi A42681.
    RefSeqi NP_001803.2. NM_001812.2.
    UniGenei Hs.479867.

    3D structure databases

    ProteinModelPortali Q03188.
    SMRi Q03188. Positions 908-936.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107489. 15 interactions.
    IntActi Q03188. 11 interactions.
    MINTi MINT-4786577.
    STRINGi 9606.ENSP00000273853.

    PTM databases

    PhosphoSitei Q03188.

    Polymorphism databases

    DMDMi 296434446.

    Proteomic databases

    MaxQBi Q03188.
    PaxDbi Q03188.
    PRIDEi Q03188.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273853 ; ENSP00000273853 ; ENSG00000145241 .
    GeneIDi 1060.
    KEGGi hsa:1060.
    UCSCi uc003hdd.1. human.

    Organism-specific databases

    CTDi 1060.
    GeneCardsi GC04M068337.
    H-InvDB HIX0024603.
    HGNCi HGNC:1854. CENPC.
    HPAi HPA049740.
    MIMi 117141. gene.
    neXtProti NX_Q03188.
    PharmGKBi PA26398.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG329217.
    HOGENOMi HOG000090256.
    HOVERGENi HBG050891.
    InParanoidi Q03188.
    KOi K11497.
    OMAi GYRRRFC.
    OrthoDBi EOG73FQQ8.
    PhylomeDBi Q03188.
    TreeFami TF101132.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi CENPC1. human.
    GeneWikii CENPC1.
    GenomeRNAii 1060.
    NextBioi 4436.
    PROi Q03188.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03188.
    Bgeei Q03188.
    CleanExi HS_CENPC1.
    Genevestigatori Q03188.

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    InterProi IPR028386. CENP-C/Mif2/cnp3.
    IPR028931. CENP-C_mid.
    IPR028052. CENP_C_N_dom.
    IPR025974. Mif2/CENP-C_cupin.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    PANTHERi PTHR16684. PTHR16684. 1 hit.
    Pfami PF11699. CENP-C_C. 1 hit.
    PF15620. CENP-C_mid. 1 hit.
    PF15622. CENP_C_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51182. SSF51182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "CENP-C, an autoantigen in scleroderma, is a component of the human inner kinetochore plate."
      Saitoh H., Tomkiel J., Cooke C.A., Ratrie H. III, Maurer M., Rothfield N.F., Earnshaw W.C.
      Cell 70:115-125(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PHE-341 AND ASP-389.
      Tissue: Placenta.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-341.
    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], VARIANT PHE-341.
      Tissue: Blood.
    5. "Promoter characterization of centromere protein C reveals its participation in cell cycle regulation in late G1-phase and expression control by E2F-1, pRb, p107 and Sp-1."
      Poppe M., Botz J., Hahm B., Dobat K., Eickelbaum W., Paweletz N., Arand M., Knehr M.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Comprehensive analysis of the ICEN (Interphase Centromere Complex) components enriched in the CENP-A chromatin of human cells."
      Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., Goshima N., Nomura F., Nomura N., Yoda K.
      Genes Cells 11:673-684(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    8. Cited for: IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPH; CENPM; CENPN; CENPT AND CENPU.
    9. "Co-localization of CENP-C and CENP-H to discontinuous domains of CENP-A chromatin at human neocentromeres."
      Alonso A., Fritz B., Hasson D., Abrusan G., Cheung F., Yoda K., Radlwimmer B., Ladurner A.G., Warburton P.E.
      Genome Biol. 8:R148.1-R148.19(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261; SER-316 AND SER-773, VARIANT [LARGE SCALE ANALYSIS] PHE-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "The C-terminal domain of CENP-C displays multiple and critical functions for mammalian centromere formation."
      Trazzi S., Perini G., Bernardoni R., Zoli M., Reese J.C., Musacchio A., Della Valle G.
      PLoS ONE 4:E5832-E5832(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, SUBUNIT, INTERACTION WITH CENPA.
    12. "DNMT3B interacts with constitutive centromere protein CENP-C to modulate DNA methylation and the histone code at centromeric regions."
      Gopalakrishnan S., Sullivan B.A., Trazzi S., Della Valle G., Robertson K.D.
      Hum. Mol. Genet. 18:3178-3193(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DNMT3B.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; THR-183; SER-189; SER-538; SER-763 AND SER-773, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-96; THR-130; SER-225; SER-439; SER-538; THR-734; SER-763 AND SER-773, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Induced ectopic kinetochore assembly bypasses the requirement for CENP-A nucleosomes."
      Gascoigne K.E., Takeuchi K., Suzuki A., Hori T., Fukagawa T., Cheeseman I.M.
      Cell 145:410-422(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-439; SER-709 AND SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCENPC_HUMAN
    AccessioniPrimary (citable) accession number: Q03188
    Secondary accession number(s): Q8IW27, Q9P0M5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 124 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3