ID PCNT_HUMAN Reviewed; 3336 AA. AC O95613; O43152; Q7Z7C9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 4. DT 27-MAR-2024, entry version 211. DE RecName: Full=Pericentrin; DE AltName: Full=Kendrin; DE AltName: Full=Pericentrin-B; GN Name=PCNT; Synonyms=KIAA0402, PCNT2; 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), FUNCTION, SUBUNIT, SUBCELLULAR RP LOCATION, AND VARIANTS GLU-704; ALA-879; ALA-1038; ARG-2188 AND THR-2549. RX PubMed=11171385; DOI=10.1242/jcs.114.4.797; RA Li Q., Hansen D., Killilea A., Joshi H.C., Palazzo R.E., Balczon R.; RT "Kendrin/pericentrin-B, a centrosome protein with homology to pericentrin RT that complexes with PCM-1."; RL J. Cell Sci. 114:797-809(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-704. RA Gromley A.S., Jurczyk A., Sillibourne J.E., Halilovic E., Doxsey S.J.; RT "Vertebrate centrosome proteins that share homology with yeast mitotic exit RT proteins are required for cytokinesis and cell cycle progression."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLU-704 RP AND ALA-1038. RC TISSUE=Brain; RX PubMed=9455477; DOI=10.1093/dnares/4.5.307; RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VIII. 78 RT new cDNA clones from brain which code for large proteins in vitro."; RL DNA Res. 4:307-313(1997). RN [4] RP SEQUENCE REVISION TO 3023. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP SEQUENCE REVISION. RA Ohara O.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 787-1533 (ISOFORM 1), AND VARIANT RP ALA-1038. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CALMODULIN-BINDING RP DOMAIN, AND MUTAGENESIS OF 3196-PHE-ARG-3197; VAL-3203 AND RP 3208-ARG-LEU-3209. RX PubMed=10823944; DOI=10.1073/pnas.97.11.5919; RA Flory M.R., Moser M.J., Monnat R.J. Jr., Davis T.N.; RT "Identification of a human centrosomal calmodulin-binding protein that RT shares homology with pericentrin."; RL Proc. Natl. Acad. Sci. U.S.A. 97:5919-5923(2000). RN [9] 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 [10] RP FUNCTION, INTERACTION WITH DISC1, AND SUBCELLULAR LOCATION. RX PubMed=18955030; DOI=10.1016/j.bbrc.2008.10.100; RA Shimizu S., Matsuzaki S., Hattori T., Kumamoto N., Miyoshi K., Katayama T., RA Tohyama M.; RT "DISC1-kendrin interaction is involved in centrosomal microtubule network RT formation."; RL Biochem. Biophys. Res. Commun. 377:1051-1056(2008). RN [11] RP INVOLVEMENT IN MOPD2. RX PubMed=18157127; DOI=10.1038/ng.2007.80; RA Griffith E., Walker S., Martin C.-A., Vagnarelli P., Stiff T., Vernay B., RA Al Sanna N., Saggar A., Hamel B., Earnshaw W.C., Jeggo P.A., Jackson A.P., RA O'Driscoll M.; RT "Mutations in pericentrin cause Seckel syndrome with defective ATR- RT dependent DNA damage signaling."; RL Nat. Genet. 40:232-236(2008). RN [12] RP INVOLVEMENT IN MOPD2. RX PubMed=18174396; DOI=10.1126/science.1151174; RA Rauch A., Thiel C.T., Schindler D., Wick U., Crow Y.J., Ekici A.B., RA van Essen A.J., Goecke T.O., Al-Gazali L., Chrzanowska K.H., Zweier C., RA Brunner H.G., Becker K., Curry C.J., Dallapiccola B., Devriendt K., RA Doerfler A., Kinning E., Megarbane A., Meinecke P., Semple R.K., RA Spranger S., Toutain A., Trembath R.C., Voss E., Wilson L., Hennekam R., RA de Zegher F., Doerr H.-G., Reis A.; RT "Mutations in the pericentrin (PCNT) gene cause primordial dwarfism."; RL Science 319:816-819(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2177 AND SER-2327, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP FUNCTION, AND INTERACTION WITH NEK2. RX PubMed=20599736; DOI=10.1016/j.bbrc.2010.06.063; RA Matsuo K., Nishimura T., Hayakawa A., Ono Y., Takahashi M.; RT "Involvement of a centrosomal protein kendrin in the maintenance of RT centrosome cohesion by modulating Nek2A kinase activity."; RL Biochem. Biophys. Res. Commun. 398:217-223(2010). RN [15] RP INTERACTION WITH CDK5RAP2. RX PubMed=20466722; DOI=10.1074/jbc.m110.105965; RA Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.; RT "Conserved motif of CDK5RAP2 mediates its localization to centrosomes and RT the Golgi complex."; RL J. Biol. Chem. 285:22658-22665(2010). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-191; SER-682; SER-2044; RP SER-2477; SER-2486 AND SER-3302, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP CLEAVAGE, AND MUTAGENESIS OF ARG-2231 AND LYS-2232. RX PubMed=22722493; DOI=10.4161/cc.20878; RA Lee K., Rhee K.; RT "Separase-dependent cleavage of pericentrin B is necessary and sufficient RT for centriole disengagement during mitosis."; RL Cell Cycle 11:2476-2485(2012). RN [19] RP INTERACTION WITH CEP131, AND SUBCELLULAR LOCATION. RX PubMed=22797915; DOI=10.1242/jcs.104059; RA Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Lee A.J., Swanton C., RA Howell M., Boulton S.J., Collis S.J.; RT "The centriolar satellite protein Cep131 is important for genome RT stability."; RL J. Cell Sci. 125:4770-4779(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-188; THR-191; RP SER-1245; SER-1653; SER-2192; SER-2352; SER-2355 AND SER-2477, 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP SUBCELLULAR LOCATION. RX PubMed=27137183; DOI=10.1007/s00018-016-2236-8; RA Fang C.T., Kuo H.H., Pan T.S., Yu F.C., Yih L.H.; RT "HSP70 regulates the function of mitotic centrosomes."; RL Cell. Mol. Life Sci. 73:3949-3960(2016). RN [23] RP VARIANTS ARG-1452 AND GLN-2424. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). RN [24] RP INTERACTION WITH CCDC13. RX PubMed=24816561; DOI=10.1242/jcs.147785; RA Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Howard A.E., RA Barone G., Lee A.J., Swanton C., Howell M., Maslen S., Skehel J.M., RA Boulton S.J., Collis S.J.; RT "Ccdc13 is a novel human centriolar satellite protein required for RT ciliogenesis and genome stability."; RL J. Cell Sci. 127:2910-2919(2014). RN [25] RP INTERACTION WITH ATF5. RX PubMed=26213385; DOI=10.1016/j.cell.2015.06.055; RA Madarampalli B., Yuan Y., Liu D., Lengel K., Xu Y., Li G., Yang J., Liu X., RA Lu Z., Liu D.X.; RT "ATF5 Connects the Pericentriolar Materials to the Proximal End of the RT Mother Centriole."; RL Cell 162:580-592(2015). RN [26] RP INTERACTION WITH CEP68, AND MUTAGENESIS OF ARG-2231. RX PubMed=25503564; DOI=10.1038/ncb3076; RA Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V., Florens L., RA Washburn M.P., Pagano M.; RT "Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM RT to allow centriole separation, disengagement and licensing."; RL Nat. Cell Biol. 17:31-43(2015). RN [27] RP FUNCTION, SUBCELLULAR LOCATION, AND UBIQUITINATION BY TRIM43. RX PubMed=30420784; DOI=10.1038/s41564-018-0285-5; RA Full F., van Gent M., Sparrer K.M.J., Chiang C., Zurenski M.A., Scherer M., RA Brockmeyer N.H., Heinzerling L., Stuerzl M., Korn K., Stamminger T., RA Ensser A., Gack M.U.; RT "Centrosomal protein TRIM43 restricts herpesvirus infection by regulating RT nuclear lamina integrity."; RL Nat. Microbiol. 4:164-176(2019). CC -!- FUNCTION: Integral component of the filamentous matrix of the CC centrosome involved in the initial establishment of organized CC microtubule arrays in both mitosis and meiosis. Plays a role, together CC with DISC1, in the microtubule network formation. Is an integral CC component of the pericentriolar material (PCM). May play an important CC role in preventing premature centrosome splitting during interphase by CC inhibiting NEK2 kinase activity at the centrosome. CC {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385, CC ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:20599736, CC ECO:0000269|PubMed:30420784}. CC -!- SUBUNIT: Interacts with CHD3. Interacts with CHD4; the interaction CC regulates centrosome integrity (By similarity). Interacts with DISC1 CC and PCM1. Binds calmodulin. Interacts with CDK5RAP2; the interaction is CC leading to centrosomal localization of PCNT and CDK5RAP2. Interacts CC with isoform 1 of NEK2. Interacts with CEP131. Interacts with CCDC13 CC (PubMed:24816561). Interacts with CEP68 (PubMed:25503564). Interacts CC with ATF5; the ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite CC unites the mother centriole and the pericentriolar material (PCM) in CC the centrosome (PubMed:26213385). {ECO:0000250|UniProtKB:P48725, CC ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:18955030, CC ECO:0000269|PubMed:20466722, ECO:0000269|PubMed:20599736, CC ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:24816561, CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:26213385}. CC -!- INTERACTION: CC O95613; Q76N32: CEP68; NbExp=3; IntAct=EBI-530012, EBI-9051024; CC O95613; Q9NRI5: DISC1; NbExp=5; IntAct=EBI-530012, EBI-529989; CC O95613; Q15154: PCM1; NbExp=8; IntAct=EBI-530012, EBI-741421; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:10823944, CC ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:14654843, CC ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:22797915, CC ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:30420784}. CC Note=Centrosomal at all stages of the cell cycle. Remains associated CC with centrosomes following microtubule depolymerization. Colocalized CC with DISC1 at the centrosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95613-1; Sequence=Displayed; CC Name=2; CC IsoId=O95613-2; Sequence=VSP_040104, VSP_040105; CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including CC placenta, liver, kidney and thymus. {ECO:0000269|PubMed:10823944}. CC -!- DOMAIN: Composed of a coiled-coil central region flanked by non-helical CC N- and C-terminals. CC -!- PTM: Cleaved during mitotis which leads to removal of CDK5RAP2 from the CC centrosome and promotes centriole disengagement and subsequent CC centriole separation (PubMed:22722493, PubMed:25503564). The C-terminal CC fragment is rapidly degraded following cleavage (PubMed:22722493). CC {ECO:0000269|PubMed:22722493, ECO:0000269|PubMed:25503564}. CC -!- PTM: Ubiquitinated by TRIM43; leading to proteasomal degradation. CC {ECO:0000269|PubMed:30420784}. CC -!- DISEASE: Microcephalic osteodysplastic primordial dwarfism 2 (MOPD2) CC [MIM:210720]: Adults with this rare inherited condition have an average CC height of 100 centimeters and a brain size comparable to that of a 3- CC month-old baby, but are of near-normal intelligence. CC {ECO:0000269|PubMed:18157127, ECO:0000269|PubMed:18174396}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAD10838.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA23698.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC04252.1; 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; U52962; AAD10838.1; ALT_FRAME; mRNA. DR EMBL; AF515282; AAP46636.1; -; mRNA. DR EMBL; AB007862; BAA23698.3; ALT_INIT; mRNA. DR EMBL; AP000471; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000335; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000336; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000337; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK093923; BAC04252.1; ALT_INIT; mRNA. DR CCDS; CCDS33592.1; -. [O95613-1] DR CCDS; CCDS93109.1; -. [O95613-2] DR RefSeq; NP_001302458.1; NM_001315529.1. [O95613-2] DR RefSeq; NP_006022.3; NM_006031.5. [O95613-1] DR SMR; O95613; -. DR BioGRID; 111146; 200. DR CORUM; O95613; -. DR DIP; DIP-33829N; -. DR ELM; O95613; -. DR IntAct; O95613; 112. DR MINT; O95613; -. DR STRING; 9606.ENSP00000352572; -. DR GlyCosmos; O95613; 1 site, 1 glycan. DR GlyGen; O95613; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; O95613; -. DR MetOSite; O95613; -. DR PhosphoSitePlus; O95613; -. DR SwissPalm; O95613; -. DR BioMuta; PCNT; -. DR EPD; O95613; -. DR jPOST; O95613; -. DR MassIVE; O95613; -. DR MaxQB; O95613; -. DR PaxDb; 9606-ENSP00000352572; -. DR PeptideAtlas; O95613; -. DR ProteomicsDB; 50949; -. [O95613-1] DR ProteomicsDB; 50950; -. [O95613-2] DR Pumba; O95613; -. DR Antibodypedia; 3139; 238 antibodies from 25 providers. DR Ensembl; ENST00000359568.10; ENSP00000352572.5; ENSG00000160299.19. [O95613-1] DR Ensembl; ENST00000480896.5; ENSP00000511989.1; ENSG00000160299.19. [O95613-2] DR GeneID; 5116; -. DR KEGG; hsa:5116; -. DR MANE-Select; ENST00000359568.10; ENSP00000352572.5; NM_006031.6; NP_006022.3. DR UCSC; uc002zji.4; human. [O95613-1] DR AGR; HGNC:16068; -. DR CTD; 5116; -. DR DisGeNET; 5116; -. DR GeneCards; PCNT; -. DR GeneReviews; PCNT; -. DR HGNC; HGNC:16068; PCNT. DR HPA; ENSG00000160299; Tissue enriched (skeletal). DR MalaCards; PCNT; -. DR MIM; 210720; phenotype. DR MIM; 605925; gene. DR neXtProt; NX_O95613; -. DR OpenTargets; ENSG00000160299; -. DR Orphanet; 2637; Microcephalic osteodysplastic primordial dwarfism type II. DR Orphanet; 808; Seckel syndrome. DR PharmGKB; PA33079; -. DR VEuPathDB; HostDB:ENSG00000160299; -. DR eggNOG; ENOG502QV16; Eukaryota. DR GeneTree; ENSGT00730000110871; -. DR HOGENOM; CLU_000160_0_0_1; -. DR InParanoid; O95613; -. DR OMA; EQRGMFT; -. DR OrthoDB; 3030508at2759; -. DR PhylomeDB; O95613; -. DR TreeFam; TF336114; -. DR PathwayCommons; O95613; -. 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-8854518; AURKA Activation by TPX2. DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy. DR Reactome; R-HSA-9615710; Late endosomal microautophagy. DR Reactome; R-HSA-9646399; Aggrephagy. DR SignaLink; O95613; -. DR SIGNOR; O95613; -. DR BioGRID-ORCS; 5116; 86 hits in 1171 CRISPR screens. DR ChiTaRS; PCNT; human. DR GeneWiki; PCNT; -. DR GenomeRNAi; 5116; -. DR Pharos; O95613; Tbio. DR PRO; PR:O95613; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; O95613; Protein. DR Bgee; ENSG00000160299; Expressed in gastrocnemius and 196 other cell types or tissues. DR ExpressionAtlas; O95613; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005814; C:centriole; IDA:MGI. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro. DR GO; GO:0060271; P:cilium assembly; IDA:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0007052; P:mitotic spindle organization; IMP:GO_Central. DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR028745; AKAP9/Pericentrin. DR InterPro; IPR019528; PACT_domain. DR PANTHER; PTHR44981:SF3; PERICENTRIN; 1. DR PANTHER; PTHR44981; PERICENTRIN-LIKE PROTEIN, ISOFORM F; 1. DR Pfam; PF10495; PACT_coil_coil; 1. DR Genevisible; O95613; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calmodulin-binding; Coiled coil; Cytoplasm; KW Cytoskeleton; Dwarfism; Microtubule; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..3336 FT /note="Pericentrin" FT /id="PRO_0000058257" FT REGION 1..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 81..100 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 569..589 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1619..1638 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1954..1974 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2168..2214 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2318..2374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2875..2910 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2983..3246 FT /note="Interaction with NEK2" FT /evidence="ECO:0000269|PubMed:20599736" FT REGION 3084..3126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3195..3208 FT /note="Calmodulin-binding" FT REGION 3224..3300 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 258..553 FT /evidence="ECO:0000255" FT COILED 675..835 FT /evidence="ECO:0000255" FT COILED 1010..1146 FT /evidence="ECO:0000255" FT COILED 1299..1949 FT /evidence="ECO:0000255" FT COILED 2064..2082 FT /evidence="ECO:0000255" FT COILED 2536..3086 FT /evidence="ECO:0000255" FT COMPBIAS 1..47 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2182..2202 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2875..2895 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3084..3099 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3236..3250 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3252..3266 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3279..3300 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 44 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 191 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 610 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 682 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1245 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1653 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1712 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48725" FT MOD_RES 2044 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 2177 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 2192 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2225 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48725" FT MOD_RES 2226 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48725" FT MOD_RES 2327 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 2352 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2355 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2477 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2486 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 3302 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VAR_SEQ 1..118 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9455477" FT /id="VSP_040104" FT VAR_SEQ 2839..2917 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9455477" FT /id="VSP_040105" FT VARIANT 539 FT /note="T -> I (in dbSNP:rs2249060)" FT /id="VAR_043878" FT VARIANT 704 FT /note="G -> E (in dbSNP:rs2839223)" FT /evidence="ECO:0000269|PubMed:11171385, FT ECO:0000269|PubMed:9455477, ECO:0000269|Ref.2" FT /id="VAR_043879" FT VARIANT 879 FT /note="T -> A (in dbSNP:rs2839227)" FT /evidence="ECO:0000269|PubMed:11171385" FT /id="VAR_043880" FT VARIANT 1038 FT /note="V -> A (in dbSNP:rs6518289)" FT /evidence="ECO:0000269|PubMed:11171385, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9455477" FT /id="VAR_043881" FT VARIANT 1163 FT /note="R -> C (in dbSNP:rs7279204)" FT /id="VAR_043882" FT VARIANT 1194 FT /note="A -> T (in dbSNP:rs35044802)" FT /id="VAR_043883" FT VARIANT 1452 FT /note="G -> R (found in a patient with intellectual FT disability, no speech, facial and limbs dysmorphisms; FT dbSNP:rs143796569)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069420" FT VARIANT 1639 FT /note="I -> V (in dbSNP:rs6518291)" FT /id="VAR_043884" FT VARIANT 1841 FT /note="N -> S (in dbSNP:rs35940413)" FT /id="VAR_043885" FT VARIANT 1953 FT /note="R -> H (in dbSNP:rs34268261)" FT /id="VAR_043886" FT VARIANT 1960 FT /note="R -> Q (in dbSNP:rs34813667)" FT /id="VAR_043887" FT VARIANT 2097 FT /note="L -> P (in dbSNP:rs2839245)" FT /id="VAR_043888" FT VARIANT 2125 FT /note="H -> P (in dbSNP:rs35978208)" FT /id="VAR_043889" FT VARIANT 2188 FT /note="M -> R (in dbSNP:rs1044998)" FT /evidence="ECO:0000269|PubMed:11171385" FT /id="VAR_043890" FT VARIANT 2191 FT /note="S -> P (in dbSNP:rs34151633)" FT /id="VAR_043891" FT VARIANT 2239 FT /note="W -> R (in dbSNP:rs35346764)" FT /id="VAR_056961" FT VARIANT 2274 FT /note="P -> L (in dbSNP:rs2070425)" FT /id="VAR_056962" FT VARIANT 2329 FT /note="P -> R (in dbSNP:rs35848602)" FT /id="VAR_056963" FT VARIANT 2361 FT /note="Q -> R (in dbSNP:rs7277175)" FT /id="VAR_056964" FT VARIANT 2424 FT /note="R -> Q (found in a patient with intellectual FT disability, no speech, facial and limbs dysmorphisms; FT dbSNP:rs371893416)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069421" FT VARIANT 2549 FT /note="A -> T (in dbSNP:rs2839256)" FT /evidence="ECO:0000269|PubMed:11171385" FT /id="VAR_056965" FT VARIANT 2625 FT /note="R -> Q (in dbSNP:rs8131693)" FT /id="VAR_056966" FT VARIANT 2659 FT /note="Q -> H (in dbSNP:rs2070426)" FT /id="VAR_056967" FT VARIANT 2753 FT /note="R -> H (in dbSNP:rs743346)" FT /id="VAR_056968" FT VARIANT 2792 FT /note="Q -> R (in dbSNP:rs2073376)" FT /id="VAR_056969" FT VARIANT 2903 FT /note="A -> T (in dbSNP:rs35147998)" FT /id="VAR_056970" FT VARIANT 2975 FT /note="L -> P (in dbSNP:rs35881595)" FT /id="VAR_056971" FT VARIANT 3091 FT /note="S -> G (in dbSNP:rs4818842)" FT /id="VAR_056972" FT VARIANT 3245 FT /note="R -> S (in dbSNP:rs2073380)" FT /id="VAR_056973" FT MUTAGEN 2231 FT /note="R->A: Produces non-cleavable protein which remains FT on centrosomes in late mitosis until its levels eventually FT drop in cells undergoing cytokinesis." FT /evidence="ECO:0000269|PubMed:22722493, FT ECO:0000269|PubMed:25503564" FT MUTAGEN 2232 FT /note="K->M: Stabilizes the C-terminal fragment produced by FT cleavage." FT /evidence="ECO:0000269|PubMed:22722493" FT MUTAGEN 3196..3197 FT /note="FR->AA: Decrease in calmodulin binding." FT /evidence="ECO:0000269|PubMed:10823944" FT MUTAGEN 3203 FT /note="V->A: Decrease in calmodulin binding." FT /evidence="ECO:0000269|PubMed:10823944" FT MUTAGEN 3208..3209 FT /note="RL->AA: Decrease in calmodulin binding." FT /evidence="ECO:0000269|PubMed:10823944" FT CONFLICT 703 FT /note="Y -> F (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 789 FT /note="F -> L (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 819 FT /note="G -> A (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 890..900 FT /note="Missing (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 967 FT /note="S -> T (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 1024 FT /note="E -> K (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 1036 FT /note="T -> A (in Ref. 7; BAC04252)" FT /evidence="ECO:0000305" FT CONFLICT 1287 FT /note="I -> L (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 1317 FT /note="K -> T (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 1534 FT /note="Q -> H (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 3136 FT /note="Y -> S (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" FT CONFLICT 3300 FT /note="E -> G (in Ref. 1; AAD10838)" FT /evidence="ECO:0000305" SQ SEQUENCE 3336 AA; 378037 MW; 4F182D2C201662A8 CRC64; MEVEQEQRRR KVEAGRTKLA HFRQRKTKGD SSHSEKKTAK RKGSAVDASV QEESPVTKED SALCGGGDIC KSTSCDDTPD GAGGAFAAQP EDCDGEKRED LEQLQQKQVN DHPPEQCGMF TVSDHPPEQH GMFTVGDHPP EQRGMFTVSD HPPEQHGMFT VSDHPPEQRG MFTISDHQPE QRGMFTVSDH TPEQRGIFTI SDHPAEQRGM FTKECEQECE LAITDLESGR EDEAGLHQSQ AVHGLELEAL RLSLSNMHTA QLELTQANLQ KEKETALTEL REMLNSRRAQ ELALLQSRQQ HELELLREQH AREKEEVVLR CGQEAAELKE KLQSEMEKNA QIVKTLKEDW ESEKDLCLEN LRKELSAKHQ SEMEDLQNQF QKELAEQRAE LEKIFQDKNQ AERALRNLES HHQAAIEKLR EDLQSEHGRC LEDLEFKFKE SEKEKQLELE NLQASYEDLK AQSQEEIRRL WSQLDSARTS RQELSELHEQ LLARTSRVED LEQLKQREKT QHESELEQLR IYFEKKLRDA EKTYQEDLTL LQQRLQGARE DALLDSVEVG LSCVGLEEKP EKGRKDHVDE LEPERHKESL PRFQAELEES HRHQLEALES PLCIQHEGHV SDRCCVETSA LGHEWRLEPS EGHSQELPWV HLQGVQDGDL EADTERAARV LGLETEHKVQ LSLLQTELKE EIELLKIENR NLYGKLQHET RLKDDLEKVK HNLIEDHQKE LNNAKQKTEL MKQEFQRKET DWKVMKEELQ REAEEKLTLM LLELREKAES EKQTIINKFE LREAEMRQLQ DQQAAQILDL ERSLTEQQGR LQQLEQDLTS DDALHCSQCG REPPTAQDGE LAALHVKEDC ALQLMLARSR FLEERKEITE KFSAEQDAFL QEAQEQHARE LQLLQERHQQ QLLSVTAELE ARHQAALGEL TASLESKQGA LLAARVAELQ TKHAADLGAL ETRHLSSLDS LESCYLSEFQ TIREEHRQAL ELLRADFEEQ LWKKDSLHQT ILTQELEKLK RKHEGELQSV RDHLRTEVST ELAGTVAHEL QGVHQGEFGS EKKTALHEKE ETLRLQSAQA QPFHQEEKES LSLQLQKKNH QVQQLKDQVL SLSHEIEECR SELEVLQQRR ERENREGANL LSMLKADVNL SHSERGALQD ALRRLLGLFG ETLRAAVTLR SRIGERVGLC LDDAGAGLAL STAPALEETW SDVALPELDR TLSECAEMSS VAEISSHMRE SFLMSPESVR ECEQPIRRVF QSLSLAVDGL MEMALDSSRQ LEEARQIHSR FEKEFSFKNE ETAQVVRKHQ ELLECLKEES AAKAELALEL HKTQGTLEGF KVETADLKEV LAGKEDSEHR LVLELESLRR QLQQAAQEQA ALREECTRLW SRGEATATDA EAREAALRKE VEDLTKEQSE TRKQAEKDRS ALLSQMKILE SELEEQLSQH RGCAKQAEAV TALEQQVASL DKHLRNQRQF MDEQAAEREH EREEFQQEIQ RLEGQLRQAA KPQPWGPRDS QQAPLDGEVE LLQQKLREKL DEFNELAIQK ESADRQVLMQ EEEIKRLEEM NINIRKKVAQ LQEEVEKQKN IVKGLEQDKE VLKKQQMSSL LLASTLQSTL DAGRCPEPPS GSPPEGPEIQ LEVTQRALLR RESEVLDLKE QLEKMKGDLE SKNEEILHLN LKLDMQNSQT AVSLRELEEE NTSLKVIYTR SSEIEELKAT IENLQENQKR LQKEKAEEIE QLHEVIEKLQ HELSLMGPVV HEVSDSQAGS LQSELLCSQA GGPRGQALQG ELEAALEAKE ALSRLLADQE RRHSQALEAL QQRLQGAEEA AELQLAELER NVALREAEVE DMASRIQEFE AALKAKEATI AERNLEIDAL NQRKAAHSAE LEAVLLALAR IRRALEQQPL AAGAAPPELQ WLRAQCARLS RQLQVLHQRF LRCQVELDRR QARRATAHTR VPGAHPQPRM DGGAKAQVTG DVEASHDAAL EPVVPDPQGD LQPVLVTLKD APLCKQEGVM SVLTVCQRQL QSELLLVKNE MRLSLEDGGK GKEKVLEDCQ LPKVDLVAQV KQLQEKLNRL LYSMTFQNVD AADTKSLWPM ASAHLLESSW SDDSCDGEEP DISPHIDTCD ANTATGGVTD VIKNQAIDAC DANTTPGGVT DVIKNWDSLI PDEMPDSPIQ EKSECQDMSL SSPTSVLGGS RHQSHTAEAG PRKSPVGMLD LSSWSSPEVL RKDWTLEPWP SLPVTPHSGA LSLCSADTSL GDRADTSLPQ TQGPGLLCSP GVSAAALALQ WAESPPADDH HVQRTAVEKD VEDFITTSFD SQETLSSPPP GLEGKADRSE KSDGSGFGAR LSPGSGGPEA QTAGPVTPAS ISGRFQPLPE AMKEKEVRPK HVKALLQMVR DESHQILALS EGLAPPSGEP HPPRKEDEIQ DISLHGGKTQ EVPTACPDWR GDLLQVVQEA FEKEQEMQGV ELQPRLSGSD LGGHSSLLER LEKIIREQGD LQEKSLEHLR LPDRSSLLSE IQALRAQLRM THLQNQEKLQ HLRTALTSAE ARGSQQEHQL RRQVELLAYK VEQEKCIAGD LQKTLSEEQE KANSVQKLLA AEQTVVRDLK SDLCESRQKS EQLSRSLCEV QQEVLQLRSM LSSKENELKA ALQELESEQG KGRALQSQLE EEQLRHLQRE SQSAKALEEL RASLETQRAQ SSRLCVALKH EQTAKDNLQK ELRIEHSRCE ALLAQERSQL SELQKDLAAE KSRTLELSEA LRHERLLTEQ LSQRTQEACV HQDTQAHHAL LQKLKEEKSR VVDLQAMLEK VQQQALHSQQ QLEAEAQKHC EALRREKEVS ATLKSTVEAL HTQKRELRCS LEREREKPAW LQAELEQSHP RLKEQEGRKA ARRSAEARQS PAAAEQWRKW QRDKEKLREL ELQRQRDLHK IKQLQQTVRD LESKDEVPGS RLHLGSARRA AGSDADHLRE QQRELEAMRQ RLLSAARLLT SFTSQAVDRT VNDWTSSNEK AVMSLLHTLE ELKSDLSRPT SSQKKMAAEL QFQFVDVLLK DNVSLTKALS TVTQEKLELS RAVSKLEKLL KHHLQKGCSP SRSERSAWKP DETAPQSSLR RPDPGRLPPA ASEEAHTSNV KMEKLYLHYL RAESFRKALI YQKKYLLLLI GGFQDSEQET LSMIAHLGVF PSKAERKITS RPFTRFRTAV RVVIAILRLR FLVKKWQEVD RKGALAQGKA PRPGPRARQP QSPPRTRESP PTRDVPSGHT RDPARGRRLA AAASPHSGGR ATPSPNSRLE RSLTASQDPE HSLTEYIHHL EVIQQRLGGV LPDSTSKKSC HPMIKQ //