CEP63_HUMAN
ID CEP63_HUMAN Reviewed; 703 AA.
AC Q96MT8; D3DND8; D3DND9; D3DNE0; Q96CR0; Q9H8F5; Q9H8N0;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Centrosomal protein of 63 kDa {ECO:0000305};
DE Short=Cep63;
GN Name=CEP63 {ECO:0000312|HGNC:HGNC:25815};
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Placenta, and Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Pancreas;
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 [4]
RP IDENTIFICATION (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION [LARGE SCALE 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 [5]
RP FUNCTION, INTERACTION WITH CDK1 AND CDK2, AND SUBCELLULAR LOCATION.
RX PubMed=21406398; DOI=10.1158/0008-5472.can-10-2684;
RA Loffler H., Fechter A., Matuszewska M., Saffrich R., Mistrik M.,
RA Marhold J., Hornung C., Westermann F., Bartek J., Kramer A.;
RT "Cep63 recruits Cdk1 to the centrosome: implications for regulation of
RT mitotic entry, centrosome amplification, and genome maintenance.";
RL Cancer Res. 71:2129-2139(2011).
RN [6]
RP INVOLVEMENT IN SCKL6, FUNCTION, INTERACTION WITH CEP152, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21983783; DOI=10.1038/ng.971;
RA Sir J.H., Barr A.R., Nicholas A.K., Carvalho O.P., Khurshid M., Sossick A.,
RA Reichelt S., D'Santos C., Woods C.G., Gergely F.;
RT "A primary microcephaly protein complex forms a ring around parental
RT centrioles.";
RL Nat. Genet. 43:1147-1153(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CCDC14 AND KIAA0753.
RX PubMed=24613305; DOI=10.1016/j.cub.2014.01.067;
RA Firat-Karalar E.N., Rauniyar N., Yates J.R. III, Stearns T.;
RT "Proximity interactions among centrosome components identify regulators of
RT centriole duplication.";
RL Curr. Biol. 24:664-670(2014).
RN [10]
RP FUNCTION, INTERACTION WITH CDK5RAP2; CEP152; WDR62; CEP90; CCDC14 AND CDK2,
RP AND SUBCELLULAR LOCATION.
RX PubMed=26297806; DOI=10.7554/elife.07519;
RA Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L.,
RA Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N.,
RA Walsh C.A., Reiter J.F.;
RT "Centriolar satellites assemble centrosomal microcephaly proteins to
RT recruit CDK2 and promote centriole duplication.";
RL Elife 4:0-0(2015).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CCDC57.
RX PubMed=32402286; DOI=10.1016/j.celrep.2020.107630;
RA Gurkaslar H.K., Culfa E., Arslanhan M.D., Lince-Faria M.,
RA Firat-Karalar E.N.;
RT "CCDC57 Cooperates with Microtubules and Microcephaly Protein CEP63 and
RT Regulates Centriole Duplication and Mitotic Progression.";
RL Cell Rep. 31:107630-107630(2020).
CC -!- FUNCTION: Required for normal spindle assembly. Plays a key role in
CC mother-centriole-dependent centriole duplication; the function seems
CC also to involve CEP152, CDK5RAP2 and WDR62 through a stepwise assembled
CC complex at the centrosome that recruits CDK2 required for centriole
CC duplication. Reported to be required for centrosomal recruitment of
CC CEP152; however, this function has been questioned (PubMed:21983783,
CC PubMed:26297806). Also recruits CDK1 to centrosomes (PubMed:21406398).
CC Plays a role in DNA damage response. Following DNA damage, such as
CC double-strand breaks (DSBs), is removed from centrosomes; this leads to
CC the inactivation of spindle assembly and delay in mitotic progression
CC (PubMed:21406398). {ECO:0000269|PubMed:21406398,
CC ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806}.
CC -!- SUBUNIT: Interacts with CEP152 and CDK1; these interactions recruit
CC both ligands to centrosomes (PubMed:21406398). Interacts with CDK2,
CC CDK5RAP2, WDR62, CEP90, KIAA0753/moonraker and CCDC14. CEP63, CDK5RAP2,
CC CEP152, WDR62 are proposed to form a stepwise assembled complex at the
CC centrosome forming a ring near parental centrioles (PubMed:21406398,
CC PubMed:26297806). Interacts with CCDC57; the interaction is required
CC for their location to proximal end of centrioles (PubMed:32402286).
CC {ECO:0000269|PubMed:21406398, ECO:0000269|PubMed:21983783,
CC ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:32402286}.
CC -!- INTERACTION:
CC Q96MT8; P09917: ALOX5; NbExp=4; IntAct=EBI-741977, EBI-79934;
CC Q96MT8; P53365: ARFIP2; NbExp=3; IntAct=EBI-741977, EBI-638194;
CC Q96MT8; Q49A88: CCDC14; NbExp=5; IntAct=EBI-741977, EBI-751035;
CC Q96MT8; Q86XR8: CEP57; NbExp=3; IntAct=EBI-741977, EBI-308614;
CC Q96MT8; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-741977, EBI-1104570;
CC Q96MT8; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-741977, EBI-10181988;
CC Q96MT8; Q9NRI5: DISC1; NbExp=7; IntAct=EBI-741977, EBI-529989;
CC Q96MT8; O60941: DTNB; NbExp=5; IntAct=EBI-741977, EBI-740402;
CC Q96MT8; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-741977, EBI-948630;
CC Q96MT8; Q15910: EZH2; NbExp=4; IntAct=EBI-741977, EBI-530054;
CC Q96MT8; Q3B820: FAM161A; NbExp=3; IntAct=EBI-741977, EBI-719941;
CC Q96MT8; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-741977, EBI-10244131;
CC Q96MT8; Q96CS2: HAUS1; NbExp=4; IntAct=EBI-741977, EBI-2514791;
CC Q96MT8; Q9NPJ8: NXT2; NbExp=3; IntAct=EBI-741977, EBI-752122;
CC Q96MT8; Q8WXW3: PIBF1; NbExp=6; IntAct=EBI-741977, EBI-2558770;
CC Q96MT8; Q9BT08: POLR3C; NbExp=3; IntAct=EBI-741977, EBI-10297880;
CC Q96MT8; Q969G3: SMARCE1; NbExp=4; IntAct=EBI-741977, EBI-455078;
CC Q96MT8; Q99909: SSX3; NbExp=4; IntAct=EBI-741977, EBI-10295431;
CC Q96MT8; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-741977, EBI-745392;
CC Q96MT8; Q92844: TANK; NbExp=4; IntAct=EBI-741977, EBI-356349;
CC Q96MT8; Q8TC07: TBC1D15; NbExp=5; IntAct=EBI-741977, EBI-1048247;
CC Q96MT8; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-741977, EBI-9053916;
CC Q96MT8; P40222: TXLNA; NbExp=4; IntAct=EBI-741977, EBI-359793;
CC Q96MT8; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-741977, EBI-6116822;
CC Q96MT8; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-741977, EBI-597063;
CC Q96MT8; A2AUM9: Cep152; Xeno; NbExp=3; IntAct=EBI-741977, EBI-2554268;
CC Q96MT8; P03410: tax; Xeno; NbExp=4; IntAct=EBI-741977, EBI-9676218;
CC Q96MT8; P14079: tax; Xeno; NbExp=5; IntAct=EBI-741977, EBI-9675698;
CC Q96MT8-3; P09917: ALOX5; NbExp=8; IntAct=EBI-11522539, EBI-79934;
CC Q96MT8-3; Q13515: BFSP2; NbExp=3; IntAct=EBI-11522539, EBI-10229433;
CC Q96MT8-3; P55201-2: BRPF1; NbExp=3; IntAct=EBI-11522539, EBI-12065306;
CC Q96MT8-3; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-11522539, EBI-1765641;
CC Q96MT8-3; Q49A88-3: CCDC14; NbExp=3; IntAct=EBI-11522539, EBI-12105646;
CC Q96MT8-3; Q8TD31-3: CCHCR1; NbExp=7; IntAct=EBI-11522539, EBI-10175300;
CC Q96MT8-3; Q86XR8-3: CEP57; NbExp=4; IntAct=EBI-11522539, EBI-11752486;
CC Q96MT8-3; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-11522539, EBI-5453285;
CC Q96MT8-3; Q9UER7: DAXX; NbExp=3; IntAct=EBI-11522539, EBI-77321;
CC Q96MT8-3; O60941-5: DTNB; NbExp=3; IntAct=EBI-11522539, EBI-11984733;
CC Q96MT8-3; Q3B820: FAM161A; NbExp=3; IntAct=EBI-11522539, EBI-719941;
CC Q96MT8-3; Q96JP0: FEM1C; NbExp=3; IntAct=EBI-11522539, EBI-2515330;
CC Q96MT8-3; O14964: HGS; NbExp=6; IntAct=EBI-11522539, EBI-740220;
CC Q96MT8-3; P42858: HTT; NbExp=12; IntAct=EBI-11522539, EBI-466029;
CC Q96MT8-3; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-11522539, EBI-2556193;
CC Q96MT8-3; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-11522539, EBI-14086479;
CC Q96MT8-3; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-11522539, EBI-743811;
CC Q96MT8-3; O14777: NDC80; NbExp=3; IntAct=EBI-11522539, EBI-715849;
CC Q96MT8-3; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-11522539, EBI-14066006;
CC Q96MT8-3; Q9BUI4: POLR3C; NbExp=5; IntAct=EBI-11522539, EBI-5452779;
CC Q96MT8-3; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-11522539, EBI-1504830;
CC Q96MT8-3; Q9GZN7: ROGDI; NbExp=3; IntAct=EBI-11522539, EBI-713255;
CC Q96MT8-3; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-11522539, EBI-455078;
CC Q96MT8-3; Q8TC07: TBC1D15; NbExp=3; IntAct=EBI-11522539, EBI-1048247;
CC Q96MT8-3; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-11522539, EBI-8787464;
CC Q96MT8-3; Q99816: TSG101; NbExp=3; IntAct=EBI-11522539, EBI-346882;
CC Q96MT8-3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-11522539, EBI-10241197;
CC Q96MT8-3; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-11522539, EBI-6116822;
CC Q96MT8-3; Q8N6Y0: USHBP1; NbExp=5; IntAct=EBI-11522539, EBI-739895;
CC Q96MT8-3; O75604: USP2; NbExp=3; IntAct=EBI-11522539, EBI-743272;
CC Q96MT8-3; Q9UQR1-2: ZNF148; NbExp=3; IntAct=EBI-11522539, EBI-11742222;
CC Q96MT8-3; P15622-3: ZNF250; NbExp=3; IntAct=EBI-11522539, EBI-10177272;
CC Q96MT8-3; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-11522539, EBI-10251462;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:32402286}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806,
CC ECO:0000269|PubMed:32402286}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:24613305, ECO:0000269|PubMed:32402286}.
CC Note=Colocalizes with CDK5RAP2, CEP152 and WDR62 in a discrete ring
CC around the proximal end of the parental centriole. At this site, a
CC cohesive structure is predicted to engage parental centrioles and
CC procentrioles. {ECO:0000269|PubMed:21983783,
CC ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:32402286}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96MT8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96MT8-2; Sequence=VSP_012252;
CC Name=3;
CC IsoId=Q96MT8-3; Sequence=VSP_012251, VSP_012252;
CC Name=4;
CC IsoId=Q96MT8-4; Sequence=VSP_012251, VSP_012253, VSP_012254;
CC -!- DISEASE: Seckel syndrome 6 (SCKL6) [MIM:614728]: 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:21983783}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: CEP63 and DEUP1 paralogs are both involved in centriole
CC amplification: while CEP63 mediates mother-centriole-dependent
CC centriole duplication, DEUP1 mediates de novo centriole amplification
CC in multiciliated cells.
CC -!- SIMILARITY: Belongs to the CEP63 family. {ECO:0000305}.
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DR EMBL; AK023448; BAB14578.1; -; mRNA.
DR EMBL; AK023738; BAB14662.1; -; mRNA.
DR EMBL; AK056465; BAB71192.1; -; mRNA.
DR EMBL; CH471052; EAW79136.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79137.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79138.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79139.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79140.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79141.1; -; Genomic_DNA.
DR EMBL; BC014050; AAH14050.1; -; mRNA.
DR EMBL; BC068997; AAH68997.1; -; mRNA.
DR EMBL; BK005503; DAA05503.1; -; mRNA.
DR CCDS; CCDS3086.1; -. [Q96MT8-1]
DR CCDS; CCDS43152.1; -. [Q96MT8-4]
DR CCDS; CCDS43153.1; -. [Q96MT8-2]
DR CCDS; CCDS43154.1; -. [Q96MT8-3]
DR RefSeq; NP_001035842.1; NM_001042383.1. [Q96MT8-3]
DR RefSeq; NP_001035843.1; NM_001042384.1. [Q96MT8-4]
DR RefSeq; NP_001035859.1; NM_001042400.1. [Q96MT8-2]
DR RefSeq; NP_079456.2; NM_025180.3. [Q96MT8-1]
DR RefSeq; XP_005247854.1; XM_005247797.3. [Q96MT8-1]
DR RefSeq; XP_006713823.1; XM_006713760.3. [Q96MT8-1]
DR RefSeq; XP_011511496.1; XM_011513194.2.
DR RefSeq; XP_016862743.1; XM_017007254.1.
DR RefSeq; XP_016862744.1; XM_017007255.1.
DR RefSeq; XP_016862745.1; XM_017007256.1.
DR RefSeq; XP_016862751.1; XM_017007262.1.
DR RefSeq; XP_016862752.1; XM_017007263.1.
DR RefSeq; XP_016862753.1; XM_017007264.1.
DR RefSeq; XP_016862755.1; XM_017007266.1.
DR RefSeq; XP_016862756.1; XM_017007267.1.
DR PDB; 6CSU; X-ray; 2.50 A; A/C=664-703.
DR PDB; 6CSV; X-ray; 2.50 A; A/B/C/D=664-703.
DR PDBsum; 6CSU; -.
DR PDBsum; 6CSV; -.
DR AlphaFoldDB; Q96MT8; -.
DR SMR; Q96MT8; -.
DR BioGRID; 123200; 179.
DR DIP; DIP-36374N; -.
DR IntAct; Q96MT8; 167.
DR MINT; Q96MT8; -.
DR STRING; 9606.ENSP00000336524; -.
DR iPTMnet; Q96MT8; -.
DR PhosphoSitePlus; Q96MT8; -.
DR BioMuta; CEP63; -.
DR DMDM; 56748851; -.
DR EPD; Q96MT8; -.
DR jPOST; Q96MT8; -.
DR MassIVE; Q96MT8; -.
DR MaxQB; Q96MT8; -.
DR PaxDb; Q96MT8; -.
DR PeptideAtlas; Q96MT8; -.
DR PRIDE; Q96MT8; -.
DR ProteomicsDB; 77406; -. [Q96MT8-1]
DR ProteomicsDB; 77407; -. [Q96MT8-2]
DR ProteomicsDB; 77408; -. [Q96MT8-3]
DR ProteomicsDB; 77409; -. [Q96MT8-4]
DR Antibodypedia; 46695; 216 antibodies from 25 providers.
DR DNASU; 80254; -.
DR Ensembl; ENST00000332047.10; ENSP00000328382.5; ENSG00000182923.20. [Q96MT8-3]
DR Ensembl; ENST00000354446.7; ENSP00000346432.3; ENSG00000182923.20. [Q96MT8-4]
DR Ensembl; ENST00000383229.8; ENSP00000372716.3; ENSG00000182923.20. [Q96MT8-2]
DR Ensembl; ENST00000512894.6; ENSP00000423225.2; ENSG00000182923.20. [Q96MT8-4]
DR Ensembl; ENST00000513612.7; ENSP00000426129.1; ENSG00000182923.20. [Q96MT8-1]
DR Ensembl; ENST00000606977.5; ENSP00000475903.1; ENSG00000182923.20. [Q96MT8-1]
DR Ensembl; ENST00000620544.5; ENSP00000482219.1; ENSG00000182923.20. [Q96MT8-4]
DR Ensembl; ENST00000675561.1; ENSP00000502085.1; ENSG00000182923.20. [Q96MT8-1]
DR Ensembl; ENST00000682042.1; ENSP00000507228.1; ENSG00000182923.20. [Q96MT8-3]
DR Ensembl; ENST00000682800.1; ENSP00000506791.1; ENSG00000182923.20. [Q96MT8-3]
DR Ensembl; ENST00000682858.1; ENSP00000507703.1; ENSG00000182923.20. [Q96MT8-3]
DR Ensembl; ENST00000683177.1; ENSP00000506828.1; ENSG00000182923.20. [Q96MT8-3]
DR Ensembl; ENST00000683596.1; ENSP00000506896.1; ENSG00000182923.20. [Q96MT8-1]
DR Ensembl; ENST00000683608.1; ENSP00000507704.1; ENSG00000182923.20. [Q96MT8-2]
DR Ensembl; ENST00000683861.1; ENSP00000506728.1; ENSG00000182923.20. [Q96MT8-3]
DR Ensembl; ENST00000684217.1; ENSP00000508291.1; ENSG00000182923.20. [Q96MT8-2]
DR Ensembl; ENST00000684677.1; ENSP00000507217.1; ENSG00000182923.20. [Q96MT8-2]
DR GeneID; 80254; -.
DR KEGG; hsa:80254; -.
DR MANE-Select; ENST00000675561.1; ENSP00000502085.1; NM_001353108.3; NP_001340037.1.
DR UCSC; uc003eql.2; human. [Q96MT8-1]
DR CTD; 80254; -.
DR DisGeNET; 80254; -.
DR GeneCards; CEP63; -.
DR HGNC; HGNC:25815; CEP63.
DR HPA; ENSG00000182923; Low tissue specificity.
DR MalaCards; CEP63; -.
DR MIM; 614724; gene.
DR MIM; 614728; phenotype.
DR neXtProt; NX_Q96MT8; -.
DR OpenTargets; ENSG00000182923; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA142672124; -.
DR VEuPathDB; HostDB:ENSG00000182923; -.
DR eggNOG; ENOG502QRYU; Eukaryota.
DR GeneTree; ENSGT00940000153190; -.
DR HOGENOM; CLU_027471_1_0_1; -.
DR InParanoid; Q96MT8; -.
DR OMA; CLDIREQ; -.
DR OrthoDB; 943593at2759; -.
DR PhylomeDB; Q96MT8; -.
DR TreeFam; TF330595; -.
DR PathwayCommons; Q96MT8; -.
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 SignaLink; Q96MT8; -.
DR BioGRID-ORCS; 80254; 18 hits in 1084 CRISPR screens.
DR ChiTaRS; CEP63; human.
DR GeneWiki; CEP63; -.
DR GenomeRNAi; 80254; -.
DR Pharos; Q96MT8; Tbio.
DR PRO; PR:Q96MT8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96MT8; protein.
DR Bgee; ENSG00000182923; Expressed in calcaneal tendon and 202 other tissues.
DR ExpressionAtlas; Q96MT8; baseline and differential.
DR Genevisible; Q96MT8; HS.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
DR InterPro; IPR029608; Cep63.
DR InterPro; IPR031470; Cep63/Deup1_N.
DR PANTHER; PTHR18875:SF7; PTHR18875:SF7; 1.
DR Pfam; PF17045; CEP63; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; DNA damage; Dwarfism;
KW Intellectual disability; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..703
FT /note="Centrosomal protein of 63 kDa"
FT /id="PRO_0000089493"
FT COILED 22..199
FT /evidence="ECO:0000255"
FT COILED 242..306
FT /evidence="ECO:0000255"
FT COILED 353..533
FT /evidence="ECO:0000255"
FT COILED 676..703
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 310..355
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012251"
FT VAR_SEQ 490..651
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012252"
FT VAR_SEQ 490..521
FT /note="AKEISLADLQENYIEALNKLVSENQQLQKDLM -> RWGFTMLSSLVLNFGI
FT QAIRQPQRPKVLELQV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012253"
FT VAR_SEQ 522..703
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012254"
FT VARIANT 651
FT /note="S -> L (in dbSNP:rs1127826)"
FT /id="VAR_020604"
FT CONFLICT 365
FT /note="K -> R (in Ref. 1; BAB14662)"
FT /evidence="ECO:0000305"
FT HELIX 664..701
FT /evidence="ECO:0007829|PDB:6CSU"
SQ SEQUENCE 703 AA; 81344 MW; D5406B75BB19B5D0 CRC64;
MEALLEGIQN RGHGGGFLTS CEAELQELMK QIDIMVAHKK SEWEGRTHAL ETCLKIREQE
LKSLRSQLDV THKEVGMLHQ QVEEHEKIKQ EMTMEYKQEL KKLHEELCIL KRSYEKLQKK
QMREFRGNTK NHREDRSEIE RLTAKIEEFR QKSLDWEKQR LIYQQQVSSL EAQRKALAEQ
SEIIQAQLVN RKQKLESVEL SSQSEIQHLS SKLERANDTI CANELEIERL TMRVNDLVGT
SMTVLQEQQQ KEEKLRESEK LLEALQEEKR ELKAALQSQE NLIHEARIQK EKLQEKVKAT
NTQHAVEAIR PREESLAEKK YTSQGQGDLD SVLSQLNFTH TSEDLLQAEV TCLEGSLESV
SATCKQLSQE LMEKYEELKR MEAHNNEYKA EIKKLKEQIL QGEQSYSSAL EGMKMEISHL
TQELHQRDIT IASTKGSSSD MEKRLRAEMQ KAEDKAVEHK EILDQLESLK LENRHLSEMV
MKLELGLHEA KEISLADLQE NYIEALNKLV SENQQLQKDL MNTKSQLEIS TQMCKKQNDR
IFKPTHSRTT EFKNTEFKPT HGQHRHDGIK TEHYKTDLHS PRGQASDSIN PMSRVLSPLS
PQISPCSSTR SLTSYSLCKT HSLPSALDTN EANFSDTMSE SMNDQEEFIS SCSLPVSPLG
SIATRFLEEE ELRSHHILER LDAHIEELKR ESEKTVRQFT ALK
