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Q9HC77

- CENPJ_HUMAN

UniProt

Q9HC77 - CENPJ_HUMAN

Protein

Centromere protein J

Gene

CENPJ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein domain specific binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB
    4. tubulin binding Source: UniProtKB

    GO - Biological processi

    1. cell division Source: UniProtKB
    2. centriole replication Source: UniProtKB
    3. G2/M transition of mitotic cell cycle Source: Reactome
    4. microtubule nucleation Source: UniProtKB
    5. microtubule polymerization Source: UniProtKB
    6. mitotic cell cycle Source: Reactome
    7. regulation of centriole replication Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centromere protein J
    Short name:
    CENP-J
    Alternative name(s):
    Centrosomal P4.1-associated protein
    LAG-3-associated protein
    LYST-interacting protein 1
    Gene namesi
    Name:CENPJ
    Synonyms:CPAP, LAP, LIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:17272. CENPJ.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole
    Note: Localized within the center of microtubule asters. During centriole biogenesis, it is concentrated within the proximal lumen of both parental centrioles and procentrioles.

    GO - Cellular componenti

    1. centriole Source: UniProtKB
    2. centrosome Source: UniProtKB
    3. cytosol Source: Reactome
    4. gamma-tubulin small complex Source: UniProtKB
    5. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Microcephaly 6, primary, autosomal recessive (MCPH6) [MIM:608393]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1235 – 12351E → V in MCPH6. 1 Publication
    VAR_032433
    Seckel syndrome 4 (SCKL4) [MIM:613676]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi589 – 5891S → A: Abolishes phosphorylation by PLK2 and procentriole formation; when associated with A-595. 1 Publication
    Mutagenesisi595 – 5951S → A: Abolishes phosphorylation by PLK2 and procentriole formation; when associated with A-589. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dwarfism, Mental retardation, Primary microcephaly

    Organism-specific databases

    MIMi608393. phenotype.
    613676. phenotype.
    Orphaneti2512. Autosomal recessive primary microcephaly.
    808. Seckel syndrome.
    PharmGKBiPA26403.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13381338Centromere protein JPRO_0000089480Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei589 – 5891Phosphoserine; by PLK21 Publication
    Modified residuei595 – 5951Phosphoserine; by PLK2 and PLK41 Publication
    Modified residuei759 – 7591Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-589 and Ser-595 by PLK2 is required for procentriole formation and centriole elongation. Phosphorylation by PLK2 oscillates during the cell cycle: it increases at G1/S transition and decreases during the exit from mitosis. Phosphorylation at Ser-595 is also mediated by PLK4 but is not a critical step in PLK4 function in procentriole assembly.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9HC77.
    PaxDbiQ9HC77.
    PRIDEiQ9HC77.

    PTM databases

    PhosphoSiteiQ9HC77.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HC77.
    BgeeiQ9HC77.
    CleanExiHS_CENPJ.
    GenevestigatoriQ9HC77.

    Interactioni

    Subunit structurei

    Part of a ternary complex composed of SASS6, CENPJ and CEP350. Associated with the gamma-tubulin complex. Interacts with the head domain of EPB41. Interacts with LYST. Interacts with CEP152 (via C-terminus).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CEP135Q66GS98EBI-946194,EBI-1046993
    CICQ96RK02EBI-946194,EBI-945857
    GFI1BQ5VTD92EBI-946194,EBI-946212
    PLK2Q9NYY33EBI-946194,EBI-721354
    STILQ1546812EBI-946194,EBI-7488405
    TNKSO952714EBI-946194,EBI-1105254

    Protein-protein interaction databases

    BioGridi120939. 13 interactions.
    DIPiDIP-49904N.
    IntActiQ9HC77. 16 interactions.
    STRINGi9606.ENSP00000371308.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HC77.
    SMRiQ9HC77. Positions 1166-1318.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TCP10 family.Curated

    Phylogenomic databases

    eggNOGiNOG83204.
    HOGENOMiHOG000111541.
    HOVERGENiHBG050894.
    InParanoidiQ9HC77.
    KOiK11502.
    OMAiDSPQVCD.
    OrthoDBiEOG77DJ60.
    PhylomeDBiQ9HC77.
    TreeFamiTF343156.

    Family and domain databases

    InterProiIPR009852. Tcp10_C_dom.
    IPR026581. TCP10_fam.
    [Graphical view]
    PANTHERiPTHR10331. PTHR10331. 1 hit.
    PfamiPF07202. Tcp10_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9HC77-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLMPTSSEL NSGQNFLTQW MTNPSRAGVI LNRGFPILEA DKEKRAAVDI     50
    STSFPIKGTH FSDSFSFINE EDSLLEEQKL ESNNPYKPQS DKSETHTAFP 100
    CIKKGPQVAA CHSAPGHQEE NKNDFIPDLA SEFKEGAYKD PLFKKLEQLK 150
    EVQQKKQEQL KRQQLEQLQR LMEEQEKLLT MVSGQCTLPG LSLLPDDQSQ 200
    KHRSPGNTTT GERATCCFPS YVYPDPTQEE TYPSNILSHE QSNFCRTAHG 250
    DFVLTSKRAS PNLFSEAQYQ EAPVEKNNLK EENRNHPTGE SILCWEKVTE 300
    QIQEANDKNL QKHDDSSEVA NIEERPIKAA IGERKQTFED YLEEQIQLEE 350
    QELKQKQLKE AEGPLPIKAK PKQPFLKRGE GLARFTNAKS KFQKGKESKL 400
    VTNQSTSEDQ PLFKMDRQQL QRKTALKNKE LCADNPILKK DSKARTKSGS 450
    VTLSQKPKML KCSNRKSLSP SGLKIQTGKK CDGQFRDQIK FENKVTSNNK 500
    ENVTECPKPC DTGCTGWNKT QGKDRLPLST GPASRLAAKS PIRETMKESE 550
    SSLDVSLQKK LETWEREKEK ENLELDEFLF LEQAADEISF SSNSSFVLKI 600
    LERDQQICKG HRMSSTPVKA VPQKTNPADP ISHCNRSEDL DHTAREKESE 650
    CEVAPKQLHS LSSADELREQ PCKIRKAVQK STSENQTEWN ARDDEGVPNS 700
    DSSTDSEEQL DVTIKPSTED RERGISSRED SPQVCDDKGP FKDTRTQEDK 750
    RRDVDLDLSD KDYSSDESIM ESIKHKVSEP SRSSSLSLSK MDFDDERTWT 800
    DLEENLCNHD VVLGNESTYG TPQTCYPNNE IGILDKTIKR KIAPVKRGED 850
    LSKSRRSRSP PTSELMMKFF PSLKPKPKSD SHLGNELKLN ISQDQPPGDN 900
    ARSQVLREKI IELETEIEKF KAENASLAKL RIERESALEK LRKEIADFEQ 950
    QKAKELARIE EFKKEEMRKL QKERKVFEKY TTAARTFPDK KEREEIQTLK 1000
    QQIADLREDL KRKETKWSST HSRLRSQIQM LVRENTDLRE EIKVMERFRL 1050
    DAWKRAEAIE SSLEVEKKDK LANTSVRFQN SQISSGTQVE KYKKNYLPMQ 1100
    GNPPRRSKSA PPRDLGNLDK GQAASPREPL EPLNFPDPEY KEEEEDQDIQ 1150
    GEISHPDGKV EKVYKNGCRV ILFPNGTRKE VSADGKTITV TFFNGDVKQV 1200
    MPDQRVIYYY AAAQTTHTTY PEGLEVLHFS SGQIEKHYPD GRKEITFPDQ 1250
    TVKNLFPDGQ EESIFPDGTI VRVQRDGNKL IEFNNGQREL HTAQFKRREY 1300
    PDGTVKTVYA NGHQETKYRS GRIRVKDKEG NVLMDTEL 1338
    Length:1,338
    Mass (Da):153,000
    Last modified:April 26, 2005 - v2
    Checksum:iB4E6531B62A30F2D
    GO

    Sequence cautioni

    The sequence AAH24209.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti129 – 1291L → R in AAG21074. (PubMed:11003675)Curated
    Sequence conflicti1142 – 11421E → R in AAG49440. (PubMed:11984006)Curated
    Sequence conflicti1224 – 12241L → W in AAG49440. (PubMed:11984006)Curated
    Sequence conflicti1333 – 13331L → S in AAG21074. (PubMed:11003675)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211M → V.
    Corresponds to variant rs35498994 [ dbSNP | Ensembl ].
    VAR_032427
    Natural varianti55 – 551P → A.
    Corresponds to variant rs17081389 [ dbSNP | Ensembl ].
    VAR_032428
    Natural varianti63 – 631D → H.
    Corresponds to variant rs7336216 [ dbSNP | Ensembl ].
    VAR_032429
    Natural varianti85 – 851P → T.
    Corresponds to variant rs9511510 [ dbSNP | Ensembl ].
    VAR_032430
    Natural varianti151 – 1511E → G.
    Corresponds to variant rs34177811 [ dbSNP | Ensembl ].
    VAR_032431
    Natural varianti879 – 8791S → A.
    Corresponds to variant rs17402892 [ dbSNP | Ensembl ].
    VAR_032432
    Natural varianti1235 – 12351E → V in MCPH6. 1 Publication
    VAR_032433

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF139625 mRNA. Translation: AAG21074.1.
    AL354798 Genomic DNA. Translation: CAI16635.1.
    BC024209 mRNA. Translation: AAH24209.3. Different initiation.
    BC113110 mRNA. Translation: AAI13111.1.
    BC113662 mRNA. Translation: AAI13663.1.
    BC113664 mRNA. Translation: AAI13665.1.
    AJ303006 mRNA. Translation: CAC80028.1.
    AF141337 mRNA. Translation: AAG49440.1.
    CCDSiCCDS9310.1.
    RefSeqiNP_060921.3. NM_018451.4.
    UniGeneiHs.513379.
    Hs.741581.

    Genome annotation databases

    EnsembliENST00000381884; ENSP00000371308; ENSG00000151849.
    GeneIDi55835.
    KEGGihsa:55835.
    UCSCiuc001upt.5. human.

    Polymorphism databases

    DMDMi62899891.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF139625 mRNA. Translation: AAG21074.1 .
    AL354798 Genomic DNA. Translation: CAI16635.1 .
    BC024209 mRNA. Translation: AAH24209.3 . Different initiation.
    BC113110 mRNA. Translation: AAI13111.1 .
    BC113662 mRNA. Translation: AAI13663.1 .
    BC113664 mRNA. Translation: AAI13665.1 .
    AJ303006 mRNA. Translation: CAC80028.1 .
    AF141337 mRNA. Translation: AAG49440.1 .
    CCDSi CCDS9310.1.
    RefSeqi NP_060921.3. NM_018451.4.
    UniGenei Hs.513379.
    Hs.741581.

    3D structure databases

    ProteinModelPortali Q9HC77.
    SMRi Q9HC77. Positions 1166-1318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120939. 13 interactions.
    DIPi DIP-49904N.
    IntActi Q9HC77. 16 interactions.
    STRINGi 9606.ENSP00000371308.

    PTM databases

    PhosphoSitei Q9HC77.

    Polymorphism databases

    DMDMi 62899891.

    Proteomic databases

    MaxQBi Q9HC77.
    PaxDbi Q9HC77.
    PRIDEi Q9HC77.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381884 ; ENSP00000371308 ; ENSG00000151849 .
    GeneIDi 55835.
    KEGGi hsa:55835.
    UCSCi uc001upt.5. human.

    Organism-specific databases

    CTDi 55835.
    GeneCardsi GC13M025456.
    GeneReviewsi CENPJ.
    HGNCi HGNC:17272. CENPJ.
    MIMi 608393. phenotype.
    609279. gene.
    613676. phenotype.
    neXtProti NX_Q9HC77.
    Orphaneti 2512. Autosomal recessive primary microcephaly.
    808. Seckel syndrome.
    PharmGKBi PA26403.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG83204.
    HOGENOMi HOG000111541.
    HOVERGENi HBG050894.
    InParanoidi Q9HC77.
    KOi K11502.
    OMAi DSPQVCD.
    OrthoDBi EOG77DJ60.
    PhylomeDBi Q9HC77.
    TreeFami TF343156.

    Enzyme and pathway databases

    Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    GeneWikii CENPJ.
    GenomeRNAii 55835.
    NextBioi 61057.
    PROi Q9HC77.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HC77.
    Bgeei Q9HC77.
    CleanExi HS_CENPJ.
    Genevestigatori Q9HC77.

    Family and domain databases

    InterProi IPR009852. Tcp10_C_dom.
    IPR026581. TCP10_fam.
    [Graphical view ]
    PANTHERi PTHR10331. PTHR10331. 1 hit.
    Pfami PF07202. Tcp10_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex."
      Hung L.-Y., Tang C.J., Tang T.K.
      Mol. Cell. Biol. 20:7813-7825(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH EPB41.
    2. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Muscle.
    4. "LAP, a lymphocyte activation gene-3-associated protein that binds to a repeated EP motif in the intracellular region of LAG-3 may participate in the down-regulation of the CD3/TCR activation pathway."
      Andreae S., Triebel P.F.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 967-1338.
    5. "The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins."
      Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y., Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S., Kingsmore S.F.
      Mol. Med. 8:56-64(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1142-1338, INTERACTION WITH LYST.
    6. "Identification of a novel microtubule-destabilizing motif in CPAP that binds to tubulin heterodimers and inhibits microtubule assembly."
      Hung L.-Y., Chen H.-L., Chang C.-W., Li B.-R., Tang T.K.
      Mol. Biol. Cell 15:2697-2706(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MICROTUBULE DESTABILIZATION.
    7. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Role of CAP350 in centriolar tubule stability and centriole assembly."
      Le Clech M.
      PLoS ONE 3:E3855-E3855(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH SASS6 AND CEP350.
    9. "PLK2 phosphorylation is critical for CPAP function in procentriole formation during the centrosome cycle."
      Chang J., Cizmecioglu O., Hoffmann I., Rhee K.
      EMBO J. 29:2395-2406(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-589 AND SER-595, MUTAGENESIS OF SER-589 AND SER-595.
    10. Cited for: INVOLVEMENT IN SCKL4.
    11. Cited for: INTERACTION WITH CEP152.
    12. "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-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: VARIANT MCPH6 VAL-1235.

    Entry informationi

    Entry nameiCENPJ_HUMAN
    AccessioniPrimary (citable) accession number: Q9HC77
    Secondary accession number(s): Q2KHM6
    , Q5T6R5, Q96KS5, Q9C067
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 109 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 13
      Human chromosome 13: 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