CENPJ_HUMAN
ID CENPJ_HUMAN Reviewed; 1338 AA.
AC Q9HC77; Q2KHM6; Q5JPD5; Q5T6R5; Q96KS5; Q9C067;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Centromere protein J;
DE Short=CENP-J;
DE AltName: Full=Centrosomal P4.1-associated protein;
DE AltName: Full=LAG-3-associated protein;
DE AltName: Full=LYST-interacting protein 1;
GN Name=CENPJ; Synonyms=CPAP, LAP, LIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH EPB41 AND GAMMA-TUBULIN.
RX PubMed=11003675; DOI=10.1128/mcb.20.20.7813-7825.2000;
RA Hung L.-Y., Tang C.J., Tang T.K.;
RT "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which
RT is associated with the gamma-tubulin complex.";
RL Mol. Cell. Biol. 20:7813-7825(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 967-1338 (ISOFORM 1).
RA Andreae S., Triebel P.F.;
RT "LAP, a lymphocyte activation gene-3-associated protein that binds to a
RT repeated EP motif in the intracellular region of LAG-3 may participate in
RT the down-regulation of the CD3/TCR activation pathway.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1142-1338 (ISOFORM 1), AND INTERACTION WITH
RP LYST.
RX PubMed=11984006; DOI=10.1007/bf03402003;
RA Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y.,
RA Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S.,
RA Kingsmore S.F.;
RT "The Chediak-Higashi protein interacts with SNARE complex and signal
RT transduction proteins.";
RL Mol. Med. 8:56-64(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP FUNCTION IN MICROTUBULE DESTABILIZATION.
RX PubMed=15047868; DOI=10.1091/mbc.e04-02-0121;
RA Hung L.-Y., Chen H.-L., Chang C.-W., Li B.-R., Tang T.K.;
RT "Identification of a novel microtubule-destabilizing motif in CPAP that
RT binds to tubulin heterodimers and inhibits microtubule assembly.";
RL Mol. Biol. Cell 15:2697-2706(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17681131; DOI=10.1016/j.devcel.2007.07.002;
RA Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D.,
RA Nigg E.A.;
RT "Plk4-induced centriole biogenesis in human cells.";
RL Dev. Cell 13:190-202(2007).
RN [11]
RP TUBULIN-BINDING.
RX PubMed=19131341; DOI=10.1074/jbc.m808249200;
RA Cormier A., Clement M.J., Knossow M., Lachkar S., Savarin P., Toma F.,
RA Sobel A., Gigant B., Curmi P.A.;
RT "The PN2-3 domain of centrosomal P4.1-associated protein implements a novel
RT mechanism for tubulin sequestration.";
RL J. Biol. Chem. 284:6909-6917(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-589 AND SER-595, AND
RP MUTAGENESIS OF SER-589 AND SER-595.
RX PubMed=20531387; DOI=10.1038/emboj.2010.118;
RA Chang J., Cizmecioglu O., Hoffmann I., Rhee K.;
RT "PLK2 phosphorylation is critical for CPAP function in procentriole
RT formation during the centrosome cycle.";
RL EMBO J. 29:2395-2406(2010).
RN [13]
RP INVOLVEMENT IN SCKL4.
RX PubMed=20522431; DOI=10.1136/jmg.2009.076646;
RA Al-Dosari M.S., Shaheen R., Colak D., Alkuraya F.S.;
RT "Novel CENPJ mutation causes Seckel syndrome.";
RL J. Med. Genet. 47:411-414(2010).
RN [14]
RP INTERACTION WITH CEP152.
RX PubMed=20852615; DOI=10.1038/nature09445;
RA Dzhindzhev N.S., Yu Q.D., Weiskopf K., Tzolovsky G., Cunha-Ferreira I.,
RA Riparbelli M., Rodrigues-Martins A., Bettencourt-Dias M., Callaini G.,
RA Glover D.M.;
RT "Asterless is a scaffold for the onset of centriole assembly.";
RL Nature 467:714-718(2010).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STIL, FORMATION OF A
RP COMPLEX WITH STIL AND SASS8, AND CHARACTERIZATION OF VARIANT MCPH6
RP VAL-1235.
RX PubMed=22020124; DOI=10.1038/emboj.2011.378;
RA Tang C.J., Lin S.Y., Hsu W.B., Lin Y.N., Wu C.T., Lin Y.C., Chang C.W.,
RA Wu K.S., Tang T.K.;
RT "The human microcephaly protein STIL interacts with CPAP and is required
RT for procentriole formation.";
RL EMBO J. 30:4790-4804(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-316 AND SER-540, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP INTERACTION WITH STIL.
RX PubMed=25385835; DOI=10.15252/embj.201488979;
RA Shiratsuchi G., Takaoka K., Ashikawa T., Hamada H., Kitagawa D.;
RT "RBM14 prevents assembly of centriolar protein complexes and maintains
RT mitotic spindle integrity.";
RL EMBO J. 34:97-114(2015).
RN [19]
RP FUNCTION.
RX PubMed=27185865; DOI=10.1242/jcs.186338;
RA Chang C.W., Hsu W.B., Tsai J.J., Tang C.J., Tang T.K.;
RT "CEP295 interacts with microtubules and is required for centriole
RT elongation.";
RL J. Cell Sci. 129:2501-2513(2016).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 311-422 IN COMPLEX WITH TUBULIN
RP HETERODIMER AND DARPIN D1, SELF-ASSOCIATION, FUNCTION, AND MUTAGENESIS OF
RP PHE-338; GLU-339; TYR-341; PHE-375; LYS-377; ARG-378 AND PHE-385.
RX PubMed=27219064; DOI=10.1016/j.devcel.2016.04.024;
RA Sharma A., Aher A., Dynes N.J., Frey D., Katrukha E.A., Jaussi R.,
RA Grigoriev I., Croisier M., Kammerer R.A., Akhmanova A., Gonczy P.,
RA Steinmetz M.O.;
RT "Centriolar CPAP/SAS-4 imparts slow processive microtubule growth.";
RL Dev. Cell 37:362-376(2016).
RN [21] {ECO:0007744|PDB:5EIB}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 372-394, FUNCTION, AND
RP MUTAGENESIS OF GLU-343; GLU-344 AND PHE-375.
RX PubMed=27306797; DOI=10.1038/ncomms11874;
RA Zheng X., Ramani A., Soni K., Gottardo M., Zheng S., Ming Gooi L., Li W.,
RA Feng S., Mariappan A., Wason A., Widlund P., Pozniakovsky A., Poser I.,
RA Deng H., Ou G., Riparbelli M., Giuliano C., Hyman A.A., Sattler M.,
RA Gopalakrishnan J., Li H.;
RT "Molecular basis for CPAP-tubulin interaction in controlling centriolar and
RT ciliary length.";
RL Nat. Commun. 7:11874-11874(2016).
RN [22]
RP VARIANT MCPH6 VAL-1235.
RX PubMed=15793586; DOI=10.1038/ng1539;
RA Bond J., Roberts E., Springell K., Lizarraga S.B., Scott S., Higgins J.,
RA Hampshire D.J., Morrison E.E., Leal G.F., Silva E.O., Costa S.M.R.,
RA Baralle D., Raponi M., Karbani G., Rashid Y., Jafri H., Bennett C.,
RA Corry P., Walsh C.A., Woods C.G.;
RT "A centrosomal mechanism involving CDK5RAP2 and CENPJ controls brain
RT size.";
RL Nat. Genet. 37:353-355(2005).
RN [23]
RP ERRATUM OF PUBMED:15793586.
RA Bond J., Roberts E., Springell K., Lizarraga S.B., Scott S., Higgins J.,
RA Hampshire D.J., Morrison E.E., Leal G.F., Silva E.O., Costa S.M.R.,
RA Baralle D., Raponi M., Karbani G., Rashid Y., Jafri H., Bennett C.,
RA Corry P., Walsh C.A., Woods C.G.;
RL Nat. Genet. 37:555-555(2005).
CC -!- FUNCTION: Plays an important role in cell division and centrosome
CC function by participating in centriole duplication (PubMed:17681131,
CC PubMed:20531387). Inhibits microtubule nucleation from the centrosome.
CC Involved in the regulation of slow processive growth of centriolar
CC microtubules. Acts as microtubule plus-end tracking protein that
CC stabilizes centriolar microtubules and inhibits microtubule
CC polymerization and extension from the distal ends of centrioles
CC (PubMed:15047868, PubMed:27219064, PubMed:27306797). Required for
CC centriole elongation and for STIL-mediated centriole amplification
CC (PubMed:22020124). Required for the recruitment of CEP295 to the
CC proximal end of new-born centrioles at the centriolar microtubule wall
CC during early S phase in a PLK4-dependent manner (PubMed:27185865). May
CC be involved in the control of centriolar-microtubule growth by acting
CC as a regulator of tubulin release (PubMed:27306797).
CC {ECO:0000269|PubMed:15047868, ECO:0000269|PubMed:17681131,
CC ECO:0000269|PubMed:20531387, ECO:0000269|PubMed:22020124,
CC ECO:0000269|PubMed:27185865, ECO:0000269|PubMed:27219064,
CC ECO:0000305|PubMed:27306797}.
CC -!- SUBUNIT: Forms homodimers (PubMed:27219064). Associates with
CC microtubules plus ends; binds to beta-tubulin subunits exposed on
CC microtubule outer surface at its distal tip; also associates with
CC microtubule lattice (PubMed:19131341, PubMed:27219064,
CC PubMed:27306797). Associated with the gamma-tubulin complex. Interacts
CC with the head domain of EPB41 (PubMed:11003675). Interacts with LYST
CC (PubMed:11984006). Interacts with CEP152 (via C-terminus)
CC (PubMed:20852615). Interacts with STIL (PubMed:22020124,
CC PubMed:25385835). Forms a complex with STIL and SASS6
CC (PubMed:22020124). {ECO:0000269|PubMed:11003675,
CC ECO:0000269|PubMed:11984006, ECO:0000269|PubMed:20852615,
CC ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:25385835,
CC ECO:0000269|PubMed:27219064, ECO:0000269|PubMed:27306797}.
CC -!- INTERACTION:
CC Q9HC77; Q9P287: BCCIP; NbExp=3; IntAct=EBI-946194, EBI-711154;
CC Q9HC77; Q9HC77: CENPJ; NbExp=3; IntAct=EBI-946194, EBI-946194;
CC Q9HC77; Q66GS9: CEP135; NbExp=8; IntAct=EBI-946194, EBI-1046993;
CC Q9HC77; Q96RK0: CIC; NbExp=2; IntAct=EBI-946194, EBI-945857;
CC Q9HC77; Q5VTD9: GFI1B; NbExp=2; IntAct=EBI-946194, EBI-946212;
CC Q9HC77; Q9NYY3: PLK2; NbExp=3; IntAct=EBI-946194, EBI-721354;
CC Q9HC77; Q15468: STIL; NbExp=15; IntAct=EBI-946194, EBI-7488405;
CC Q9HC77; O95271: TNKS; NbExp=4; IntAct=EBI-946194, EBI-1105254;
CC Q9HC77; P61981: YWHAG; NbExp=3; IntAct=EBI-946194, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:11003675,
CC ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20531387}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:20531387,
CC ECO:0000269|PubMed:22020124}. Note=Localized within the center of
CC microtubule asters (PubMed:11003675). During centriole biogenesis, it
CC is concentrated within the proximal lumen of both parental centrioles
CC and procentrioles (PubMed:17681131). {ECO:0000269|PubMed:11003675,
CC ECO:0000269|PubMed:17681131}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HC77-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HC77-2; Sequence=VSP_056831, VSP_056832;
CC -!- PTM: Phosphorylation at Ser-589 and Ser-595 by PLK2 is required for
CC procentriole formation and centriole elongation. Phosphorylation by
CC PLK2 oscillates during the cell cycle: it increases at G1/S transition
CC and decreases during the exit from mitosis. Phosphorylation at Ser-595
CC is also mediated by PLK4 but is not a critical step in PLK4 function in
CC procentriole assembly. {ECO:0000269|PubMed:20531387}.
CC -!- DISEASE: Microcephaly 6, primary, autosomal recessive (MCPH6)
CC [MIM:608393]: A disease defined as a head circumference more than 3
CC standard deviations below the age-related mean. Brain weight is
CC markedly reduced and the cerebral cortex is disproportionately small.
CC Despite this marked reduction in size, the gyral pattern is relatively
CC well preserved, with no major abnormality in cortical architecture.
CC Affected individuals are mentally retarded. Primary microcephaly is
CC further defined by the absence of other syndromic features or
CC significant neurological deficits due to degenerative brain disorder.
CC {ECO:0000269|PubMed:15793586, ECO:0000269|PubMed:22020124}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Seckel syndrome 4 (SCKL4) [MIM:613676]: A rare autosomal
CC recessive disorder characterized by proportionate dwarfism of prenatal
CC onset associated with low birth weight, growth retardation, severe
CC microcephaly with a bird-headed like appearance, and intellectual
CC disability. {ECO:0000269|PubMed:20522431}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TCP10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24209.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF139625; AAG21074.1; -; mRNA.
DR EMBL; AL833182; CAI46195.1; -; mRNA.
DR EMBL; AL354798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08354.1; -; Genomic_DNA.
DR EMBL; BC024209; AAH24209.3; ALT_INIT; mRNA.
DR EMBL; BC113110; AAI13111.1; -; mRNA.
DR EMBL; BC113662; AAI13663.1; -; mRNA.
DR EMBL; BC113664; AAI13665.1; -; mRNA.
DR EMBL; AJ303006; CAC80028.1; -; mRNA.
DR EMBL; AF141337; AAG49440.1; -; mRNA.
DR CCDS; CCDS9310.1; -. [Q9HC77-1]
DR RefSeq; NP_060921.3; NM_018451.4. [Q9HC77-1]
DR PDB; 5EIB; X-ray; 2.10 A; F=372-394.
DR PDB; 5ITZ; X-ray; 2.20 A; D=311-422.
DR PDB; 7Q1E; X-ray; 2.70 A; P=319-397.
DR PDB; 7Z0F; X-ray; 2.40 A; P=319-397.
DR PDB; 7Z0G; X-ray; 3.49 A; P/U=319-397.
DR PDBsum; 5EIB; -.
DR PDBsum; 5ITZ; -.
DR PDBsum; 7Q1E; -.
DR PDBsum; 7Z0F; -.
DR PDBsum; 7Z0G; -.
DR AlphaFoldDB; Q9HC77; -.
DR BMRB; Q9HC77; -.
DR SASBDB; Q9HC77; -.
DR SMR; Q9HC77; -.
DR BioGRID; 120939; 174.
DR ComplexPortal; CPX-1159; CPAP-STIL complex.
DR DIP; DIP-49904N; -.
DR IntAct; Q9HC77; 138.
DR MINT; Q9HC77; -.
DR STRING; 9606.ENSP00000371308; -.
DR iPTMnet; Q9HC77; -.
DR PhosphoSitePlus; Q9HC77; -.
DR BioMuta; CENPJ; -.
DR DMDM; 62899891; -.
DR EPD; Q9HC77; -.
DR jPOST; Q9HC77; -.
DR MassIVE; Q9HC77; -.
DR MaxQB; Q9HC77; -.
DR PaxDb; Q9HC77; -.
DR PeptideAtlas; Q9HC77; -.
DR PRIDE; Q9HC77; -.
DR ProteomicsDB; 63008; -.
DR ProteomicsDB; 81646; -. [Q9HC77-1]
DR Antibodypedia; 22520; 201 antibodies from 26 providers.
DR DNASU; 55835; -.
DR Ensembl; ENST00000381884.9; ENSP00000371308.4; ENSG00000151849.16. [Q9HC77-1]
DR Ensembl; ENST00000616936.4; ENSP00000477511.1; ENSG00000151849.16. [Q9HC77-2]
DR GeneID; 55835; -.
DR KEGG; hsa:55835; -.
DR MANE-Select; ENST00000381884.9; ENSP00000371308.4; NM_018451.5; NP_060921.3.
DR UCSC; uc001upt.6; human. [Q9HC77-1]
DR CTD; 55835; -.
DR DisGeNET; 55835; -.
DR GeneCards; CENPJ; -.
DR HGNC; HGNC:17272; CENPJ.
DR HPA; ENSG00000151849; Tissue enhanced (testis).
DR MalaCards; CENPJ; -.
DR MIM; 608393; phenotype.
DR MIM; 609279; gene.
DR MIM; 613676; phenotype.
DR neXtProt; NX_Q9HC77; -.
DR OpenTargets; ENSG00000151849; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR Orphanet; 808; Seckel syndrome.
DR PharmGKB; PA26403; -.
DR VEuPathDB; HostDB:ENSG00000151849; -.
DR eggNOG; ENOG502QQR0; Eukaryota.
DR GeneTree; ENSGT00530000063927; -.
DR HOGENOM; CLU_008072_0_0_1; -.
DR InParanoid; Q9HC77; -.
DR OMA; EPLNFPD; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; Q9HC77; -.
DR TreeFam; TF343156; -.
DR PathwayCommons; Q9HC77; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q9HC77; -.
DR SIGNOR; Q9HC77; -.
DR BioGRID-ORCS; 55835; 122 hits in 1081 CRISPR screens.
DR ChiTaRS; CENPJ; human.
DR GeneWiki; CENPJ; -.
DR GenomeRNAi; 55835; -.
DR Pharos; Q9HC77; Tbio.
DR PRO; PR:Q9HC77; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9HC77; protein.
DR Bgee; ENSG00000151849; Expressed in sperm and 161 other tissues.
DR ExpressionAtlas; Q9HC77; baseline and differential.
DR Genevisible; Q9HC77; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008275; C:gamma-tubulin small complex; NAS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0120099; C:procentriole replication complex; IPI:ComplexPortal.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0030954; P:astral microtubule nucleation; IDA:MGI.
DR GO; GO:0051301; P:cell division; NAS:UniProtKB.
DR GO; GO:0061511; P:centriole elongation; IDA:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; TAS:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:1903724; P:positive regulation of centriole elongation; IMP:UniProtKB.
DR GO; GO:0046601; P:positive regulation of centriole replication; IDA:ComplexPortal.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; IMP:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IC:ComplexPortal.
DR GO; GO:0046599; P:regulation of centriole replication; IMP:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IC:ComplexPortal.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR InterPro; IPR033068; CENP-J.
DR InterPro; IPR009852; Tcp10_C_dom.
DR InterPro; IPR026581; TCP10_fam.
DR PANTHER; PTHR10331; PTHR10331; 1.
DR PANTHER; PTHR10331:SF23; PTHR10331:SF23; 1.
DR Pfam; PF07202; Tcp10_C; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Disease variant; Dwarfism; Intellectual disability; Microtubule;
KW Phosphoprotein; Primary microcephaly; Reference proteome.
FT CHAIN 1..1338
FT /note="Centromere protein J"
FT /id="PRO_0000089480"
FT REGION 190..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..394
FT /note="Alpha/beta-tubulin binding"
FT /evidence="ECO:0000269|PubMed:19131341"
FT REGION 386..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..1338
FT /note="Interaction with STIL"
FT /evidence="ECO:0000269|PubMed:22020124,
FT ECO:0000269|PubMed:25385835"
FT REGION 1096..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 589
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000269|PubMed:20531387"
FT MOD_RES 595
FT /note="Phosphoserine; by PLK2 and PLK4"
FT /evidence="ECO:0000269|PubMed:20531387"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1073..1086
FT /note="NTSVRFQNSQISSG -> AIHLEDPSLHLLVI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_056831"
FT VAR_SEQ 1087..1338
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_056832"
FT VARIANT 21
FT /note="M -> V (in dbSNP:rs35498994)"
FT /id="VAR_032427"
FT VARIANT 55
FT /note="P -> A (in dbSNP:rs17081389)"
FT /id="VAR_032428"
FT VARIANT 63
FT /note="D -> H (in dbSNP:rs7336216)"
FT /id="VAR_032429"
FT VARIANT 85
FT /note="P -> T (in dbSNP:rs9511510)"
FT /id="VAR_032430"
FT VARIANT 151
FT /note="E -> G (in dbSNP:rs34177811)"
FT /id="VAR_032431"
FT VARIANT 879
FT /note="S -> A (in dbSNP:rs17402892)"
FT /id="VAR_032432"
FT VARIANT 1235
FT /note="E -> V (in MCPH6; reduced interaction with STIL;
FT dbSNP:rs121434311)"
FT /evidence="ECO:0000269|PubMed:15793586,
FT ECO:0000269|PubMed:22020124"
FT /id="VAR_032433"
FT MUTAGEN 338
FT /note="F->A: Decreases interaction with alpha/beta-tubulin;
FT when associated with A-339 and A-341."
FT /evidence="ECO:0000269|PubMed:27219064"
FT MUTAGEN 339
FT /note="E->A: Decreases interaction with alpha/beta-tubulin;
FT when associated with A-338 and A-341."
FT /evidence="ECO:0000269|PubMed:27219064"
FT MUTAGEN 341
FT /note="Y->A: Decreases interaction with alpha/beta-tubulin;
FT when associated with A-338 and A-339."
FT /evidence="ECO:0000269|PubMed:27219064"
FT MUTAGEN 343
FT /note="E->A: Slightly decreases interaction with
FT alpha/beta-tubulin; causes overly long daughter centrioles
FT and enhances ciliary length; when associated with A-344."
FT /evidence="ECO:0000269|PubMed:27306797"
FT MUTAGEN 344
FT /note="E->A: Slightly decreases interaction with
FT alpha/beta-tubulin; causes overly long daughter centrioles
FT and enhances ciliary length; when associated with A-343."
FT /evidence="ECO:0000269|PubMed:27306797"
FT MUTAGEN 375
FT /note="F->A: Decreases interaction with alpha/beta-tubulin;
FT disrupts association with microtubule distal tip; no effect
FT on association with microtubule lattice; when associated
FT with A-385."
FT /evidence="ECO:0000269|PubMed:27219064"
FT MUTAGEN 375
FT /note="F->A: Strongly decreases interaction with
FT alpha/beta-tubulin; causes shorter centrioles and doublet
FT microtubules in cilia."
FT /evidence="ECO:0000269|PubMed:27306797"
FT MUTAGEN 377
FT /note="K->E: Decreases interaction with alpha/beta-tubulin;
FT disrupts association with microtubule distal tip; no effect
FT on association with microtubule lattice; when associated
FT with E-378."
FT /evidence="ECO:0000269|PubMed:27219064"
FT MUTAGEN 378
FT /note="R->E: Decreases interaction with alpha/beta-tubulin;
FT disrupts association with microtubule distal tip; no effect
FT on association with microtubule lattice; when associated
FT with E-377."
FT /evidence="ECO:0000269|PubMed:27219064"
FT MUTAGEN 385
FT /note="F->A: Decreases interaction with alpha/beta-tubulin;
FT disrupts association with microtubule distal tip; no effect
FT on association with microtubule lattice; when associated
FT with A-375."
FT /evidence="ECO:0000269|PubMed:27219064"
FT MUTAGEN 589
FT /note="S->A: Abolishes phosphorylation by PLK2 and
FT procentriole formation; when associated with A-595."
FT /evidence="ECO:0000269|PubMed:20531387"
FT MUTAGEN 595
FT /note="S->A: Abolishes phosphorylation by PLK2 and
FT procentriole formation; when associated with A-589."
FT /evidence="ECO:0000269|PubMed:20531387"
FT CONFLICT 129
FT /note="L -> R (in Ref. 1; AAG21074)"
FT /evidence="ECO:0000305"
FT CONFLICT 1142
FT /note="E -> R (in Ref. 7; AAG49440)"
FT /evidence="ECO:0000305"
FT CONFLICT 1224
FT /note="L -> W (in Ref. 7; AAG49440)"
FT /evidence="ECO:0000305"
FT CONFLICT 1333
FT /note="L -> S (in Ref. 1; AAG21074)"
FT /evidence="ECO:0000305"
FT HELIX 380..385
FT /evidence="ECO:0007829|PDB:5EIB"
SQ SEQUENCE 1338 AA; 153000 MW; B4E6531B62A30F2D CRC64;
MFLMPTSSEL NSGQNFLTQW MTNPSRAGVI LNRGFPILEA DKEKRAAVDI STSFPIKGTH
FSDSFSFINE EDSLLEEQKL ESNNPYKPQS DKSETHTAFP CIKKGPQVAA CHSAPGHQEE
NKNDFIPDLA SEFKEGAYKD PLFKKLEQLK EVQQKKQEQL KRQQLEQLQR LMEEQEKLLT
MVSGQCTLPG LSLLPDDQSQ KHRSPGNTTT GERATCCFPS YVYPDPTQEE TYPSNILSHE
QSNFCRTAHG DFVLTSKRAS PNLFSEAQYQ EAPVEKNNLK EENRNHPTGE SILCWEKVTE
QIQEANDKNL QKHDDSSEVA NIEERPIKAA IGERKQTFED YLEEQIQLEE QELKQKQLKE
AEGPLPIKAK PKQPFLKRGE GLARFTNAKS KFQKGKESKL VTNQSTSEDQ PLFKMDRQQL
QRKTALKNKE LCADNPILKK DSKARTKSGS VTLSQKPKML KCSNRKSLSP SGLKIQTGKK
CDGQFRDQIK FENKVTSNNK ENVTECPKPC DTGCTGWNKT QGKDRLPLST GPASRLAAKS
PIRETMKESE SSLDVSLQKK LETWEREKEK ENLELDEFLF LEQAADEISF SSNSSFVLKI
LERDQQICKG HRMSSTPVKA VPQKTNPADP ISHCNRSEDL DHTAREKESE CEVAPKQLHS
LSSADELREQ PCKIRKAVQK STSENQTEWN ARDDEGVPNS DSSTDSEEQL DVTIKPSTED
RERGISSRED SPQVCDDKGP FKDTRTQEDK RRDVDLDLSD KDYSSDESIM ESIKHKVSEP
SRSSSLSLSK MDFDDERTWT DLEENLCNHD VVLGNESTYG TPQTCYPNNE IGILDKTIKR
KIAPVKRGED LSKSRRSRSP PTSELMMKFF PSLKPKPKSD SHLGNELKLN ISQDQPPGDN
ARSQVLREKI IELETEIEKF KAENASLAKL RIERESALEK LRKEIADFEQ QKAKELARIE
EFKKEEMRKL QKERKVFEKY TTAARTFPDK KEREEIQTLK QQIADLREDL KRKETKWSST
HSRLRSQIQM LVRENTDLRE EIKVMERFRL DAWKRAEAIE SSLEVEKKDK LANTSVRFQN
SQISSGTQVE KYKKNYLPMQ GNPPRRSKSA PPRDLGNLDK GQAASPREPL EPLNFPDPEY
KEEEEDQDIQ GEISHPDGKV EKVYKNGCRV ILFPNGTRKE VSADGKTITV TFFNGDVKQV
MPDQRVIYYY AAAQTTHTTY PEGLEVLHFS SGQIEKHYPD GRKEITFPDQ TVKNLFPDGQ
EESIFPDGTI VRVQRDGNKL IEFNNGQREL HTAQFKRREY PDGTVKTVYA NGHQETKYRS
GRIRVKDKEG NVLMDTEL
