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 27-MAR-2024, entry version 177. 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 a 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; 7Q1F; X-ray; 2.35 A; P/V=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; 7Q1F; -. DR PDBsum; 7Z0F; -. DR PDBsum; 7Z0G; -. DR AlphaFoldDB; Q9HC77; -. DR BMRB; Q9HC77; -. DR SASBDB; Q9HC77; -. DR SMR; Q9HC77; -. DR BioGRID; 120939; 179. DR ComplexPortal; CPX-1159; CPAP-STIL complex. DR DIP; DIP-49904N; -. DR IntAct; Q9HC77; 139. DR MINT; Q9HC77; -. DR STRING; 9606.ENSP00000371308; -. DR GlyGen; Q9HC77; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000371308; -. DR PeptideAtlas; Q9HC77; -. DR ProteomicsDB; 63008; -. DR ProteomicsDB; 81646; -. [Q9HC77-1] DR Pumba; Q9HC77; -. DR Antibodypedia; 22520; 232 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 AGR; HGNC:17272; -. 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; EENSCKH; -. DR OrthoDB; 69779at2759; -. 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; 125 hits in 1161 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 163 other cell types or tissues. DR ExpressionAtlas; Q9HC77; baseline and differential. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:HPA. 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: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; NAS:ComplexPortal. DR GO; GO:0046599; P:regulation of centriole replication; IMP:UniProtKB. DR GO; GO:0060236; P:regulation of mitotic spindle organization; NAS:ComplexPortal. DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl. DR Gene3D; 2.60.450.20; -; 1. DR InterPro; IPR009852; CENPJ_C_dom. DR InterPro; IPR047002; Tcp10_C_sf. DR InterPro; IPR026581; TCP10_fam. DR PANTHER; PTHR10331:SF23; CENTROMERE PROTEIN J; 1. DR PANTHER; PTHR10331; T COMPLEX PROTEIN 10; 1. DR Pfam; PF07202; Tcp10_C; 4. DR Genevisible; Q9HC77; HS. 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 322..324 FT /evidence="ECO:0007829|PDB:7Q1F" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:7Q1F" FT HELIX 339..350 FT /evidence="ECO:0007829|PDB:7Q1F" 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 //