CEP63_MOUSE
ID CEP63_MOUSE Reviewed; 700 AA.
AC Q3UPP8; Q80ZM0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Centrosomal protein of 63 kDa {ECO:0000305};
DE Short=Cep63;
GN Name=Cep63 {ECO:0000312|MGI:MGI:2158560}; Synonyms=D9Mgc48e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-700 (ISOFORM 3).
RC TISSUE=Embryo;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 AND SER-492 (ISOFORM 3),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR 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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24240477; DOI=10.1038/ncb2880;
RA Zhao H., Zhu L., Zhu Y., Cao J., Li S., Huang Q., Xu T., Huang X., Yan X.,
RA Zhu X.;
RT "The Cep63 paralogue Deup1 enables massive de novo centriole biogenesis for
RT vertebrate multiciliogenesis.";
RL Nat. Cell Biol. 15:1434-1444(2013).
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. Also recruits CDK1 to centrosomes. Plays a role in DNA
CC damage response. Following DNA damage, such as double-strand breaks
CC (DSBs), is removed from centrosomes; this leads to the inactivation of
CC spindle assembly and in delay mitotic progression.
CC {ECO:0000250|UniProtKB:Q96MT8, ECO:0000269|PubMed:24240477}.
CC -!- SUBUNIT: Interacts with CEP152 and CDK1; these interactions recruit
CC both ligands to centrosomes. Interacts with CDK2, CDK5RAP2, WDR62,
CC CEP90, KIAA0753/moonraker and CCDC14. CEP63, CDK5RAP2, CEP152, WDR62
CC are proposed to form a stepwise assembled complex at the centrosome
CC forming a ring near parental centrioles. Interacts with CCDC57; the
CC interaction is required for their location to proximal end of
CC centrioles (By similarity). {ECO:0000250|UniProtKB:Q96MT8}.
CC -!- INTERACTION:
CC Q3UPP8; A2AUM9: Cep152; NbExp=2; IntAct=EBI-16081652, EBI-2554268;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:21983783}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:24240477}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q96MT8}. Note=Colocalizes with CDK5RAP2, CEP152
CC and WDR62in a discrete ring around the proximal end of the parental
CC centriole. At this site, a cohesive structure is predicted to engage
CC parental centrioles and procentrioles. {ECO:0000250|UniProtKB:Q96MT8,
CC ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:24240477}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UPP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UPP8-2; Sequence=VSP_037843, VSP_037845, VSP_037846;
CC Name=3;
CC IsoId=Q3UPP8-3; Sequence=VSP_037844;
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. {ECO:0000305|PubMed:24240477}.
CC -!- SIMILARITY: Belongs to the CEP63 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48718.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK143341; BAE25347.1; -; mRNA.
DR EMBL; AL450317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT573150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048718; AAH48718.1; ALT_FRAME; mRNA.
DR RefSeq; XP_006511808.1; XM_006511745.3. [Q3UPP8-1]
DR RefSeq; XP_017168899.1; XM_017313410.1. [Q3UPP8-1]
DR RefSeq; XP_017168903.1; XM_017313414.1. [Q3UPP8-3]
DR AlphaFoldDB; Q3UPP8; -.
DR SMR; Q3UPP8; -.
DR BioGRID; 205780; 3.
DR DIP; DIP-61756N; -.
DR IntAct; Q3UPP8; 1.
DR STRING; 10090.ENSMUSP00000091306; -.
DR iPTMnet; Q3UPP8; -.
DR PhosphoSitePlus; Q3UPP8; -.
DR EPD; Q3UPP8; -.
DR jPOST; Q3UPP8; -.
DR MaxQB; Q3UPP8; -.
DR PaxDb; Q3UPP8; -.
DR PeptideAtlas; Q3UPP8; -.
DR PRIDE; Q3UPP8; -.
DR ProteomicsDB; 281377; -. [Q3UPP8-1]
DR ProteomicsDB; 281378; -. [Q3UPP8-2]
DR ProteomicsDB; 281379; -. [Q3UPP8-3]
DR Antibodypedia; 46695; 216 antibodies from 25 providers.
DR Ensembl; ENSMUST00000162655; ENSMUSP00000125621; ENSMUSG00000032534. [Q3UPP8-3]
DR GeneID; 28135; -.
DR UCSC; uc009rfs.1; mouse. [Q3UPP8-1]
DR CTD; 80254; -.
DR MGI; MGI:2158560; Cep63.
DR VEuPathDB; HostDB:ENSMUSG00000032534; -.
DR eggNOG; ENOG502QRYU; Eukaryota.
DR GeneTree; ENSGT00940000153190; -.
DR HOGENOM; CLU_027471_0_0_1; -.
DR InParanoid; Q3UPP8; -.
DR OrthoDB; 943593at2759; -.
DR PhylomeDB; Q3UPP8; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 28135; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Cep63; mouse.
DR PRO; PR:Q3UPP8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3UPP8; protein.
DR Bgee; ENSMUSG00000032534; Expressed in spermatid and 222 other tissues.
DR ExpressionAtlas; Q3UPP8; baseline and differential.
DR Genevisible; Q3UPP8; MM.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0051298; P:centrosome duplication; IMP:MGI.
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:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IGI:MGI.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:MGI.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IGI:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:MGI.
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 Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; DNA damage; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..700
FT /note="Centrosomal protein of 63 kDa"
FT /id="PRO_0000381804"
FT REGION 570..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..283
FT /evidence="ECO:0000255"
FT COILED 343..533
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96MT8"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MT8"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037843"
FT VAR_SEQ 487..648
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037844"
FT VAR_SEQ 487..504
FT /note="AKEISLADLQENYIEALN -> VHTSTLSFCVFEAFERNC (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037845"
FT VAR_SEQ 505..700
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037846"
FT MOD_RES Q3UPP8-3:488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UPP8-3:492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 700 AA; 80449 MW; DAF54534FF243E08 CRC64;
MEALLEGIQN RGHSGGFLTS CEAELQELMK QIDIMVAHKK SEWEGQTHAL ETCLDIRDRE
LKALRSQLDM KHKEVGILHQ QIEEHEKTKQ EMAMEYKEEL LKLQEELSRL KRSYEKLQKK
QLREFRGNTK SFREDRSEIE RLTGKIEEFR QKSLDWEKQR LIYQQQVSSL EAQRKALAEQ
SEIIQAQLAN RKQKLESVEL SSQSEIQHLN SKLERAKDTI CANELEIERL NIRVNDLMGT
NMTILQDHRQ KEEKLRESEK LLEALQEEQK ELKASLQSQE TFILEAKMQE KLQTTLKAVG
TQQSVERPLE DCQKERKYSS PGQGVLDNVL SQLDFSHSSE ELLQAEVTRL EGSLESVSAT
CKQLSQELME KYEELKRMEG HNNEYRTEIK KLKEQILQAD QTYSSALEGM KMEISQLTRE
LHQRDITIAS AKCSSSDMEK QLKAEMQKAE EKAVEHKEIL SQLESLKLEN HRLSETVMKL
ELGLHEAKEI SLADLQENYI EALNKLVSEN QQLQKDLMST KSELEHATNM CKKKDGEIFN
PAHSRAAGFK NAELKPIHGQ HRHDGIKTEQ YKTGHHSPRG QTLDSIDPVA RGPSPLSSHI
SPGSSTVSLP SNFLFEAHSL PSVLDINDVN FSDSLSDCMN DQEEFVSSGS LPTSPLGSIA
TRFLEEEELR SHHILERLDA HIEELKRESE KTVRQFTALV
