ID   CE63A_XENLA             Reviewed;         649 AA.
AC   B9V5F5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Centrosomal protein of 63 kDa-A;
DE            Short=Cep63-A;
DE            Short=Xcep63;
GN   Name=cep63-a; Synonyms=cep63;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION
RP   AT SER-560, AND MUTAGENESIS OF SER-560.
RX   PubMed=19182792; DOI=10.1038/ncb1835;
RA   Smith E., Dejsuphong D., Balestrini A., Hampel M., Lenz C., Takeda S.,
RA   Vindigni A., Costanzo V.;
RT   "An ATM- and ATR-dependent checkpoint inactivates spindle assembly by
RT   targeting CEP63.";
RL   Nat. Cell Biol. 11:278-285(2009).
CC   -!- FUNCTION: Required for normal spindle assembly. Plays a key role in
CC       mother-centriole-dependent centriole duplication. Plays a role in DNA
CC       damage response: following DNA double strand breaks (DSBs), it is
CC       delocalized from centrosomes due to phosphorylation by atm and atr,
CC       leading to inactivate spindle assembly and delay mitotic progression.
CC       {ECO:0000269|PubMed:19182792}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:19182792}.
CC   -!- PTM: Phosphorylation at Ser-560 by atm and atr promotes its
CC       delocalization from the centrosome and impairs its ability to promote
CC       centrosome dependent spindle assembly. {ECO:0000269|PubMed:19182792}.
CC   -!- SIMILARITY: Belongs to the CEP63 family. {ECO:0000305}.
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DR   EMBL; FJ464988; ACM45719.1; -; mRNA.
DR   RefSeq; NP_001088987.2; NM_001095518.2.
DR   AlphaFoldDB; B9V5F5; -.
DR   SMR; B9V5F5; -.
DR   iPTMnet; B9V5F5; -.
DR   DNASU; 496369; -.
DR   GeneID; 496369; -.
DR   KEGG; xla:496369; -.
DR   CTD; 496369; -.
DR   Xenbase; XB-GENE-952551; cep63.L.
DR   OrthoDB; 943593at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 496369; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
DR   GO; GO:0042770; P:signal transduction in response to DNA damage; IMP:UniProtKB.
DR   GO; GO:0051225; P:spindle assembly; IMP: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   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   DNA damage; Mitosis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..649
FT                   /note="Centrosomal protein of 63 kDa-A"
FT                   /id="PRO_0000381809"
FT   COILED          19..185
FT                   /evidence="ECO:0000255"
FT   COILED          222..556
FT                   /evidence="ECO:0000255"
FT   COILED          612..645
FT                   /evidence="ECO:0000255"
FT   MOD_RES         560
FT                   /note="Phosphoserine; by atm and atr"
FT                   /evidence="ECO:0000269|PubMed:19182792"
FT   MUTAGEN         560
FT                   /note="S->A: Abolishes phosphorylation by atm and atr
FT                   preventing spindle assembly inactivation."
FT                   /evidence="ECO:0000269|PubMed:19182792"
SQ   SEQUENCE   649 AA;  75463 MW;  601BDA3CABC091C6 CRC64;
     MEALLQGLQR QDRMGALQDS CEAELQELMK QIDIMLDHKR SQWEAETETM KTRLELKEQE
     LNCALDREER LNQEVRRLRQ QLIQQEEETQ NKTTQYEAQL SGFKEELNRL KKSYEKVQKK
     HLRSEMKAKA EEERSEVSRL TRRLEEFRQR SLDWEKQRLL YQQQLAGLEA QRKTLIEQTE
     MYQHQSHNRK QMLEQTSLVG RSELQNLSGQ LHRANDSLCA KEEELETLKI QLRCAVEGQK
     RAEHETELSK QAVQALKEEK AELRATLQAH TEFLQGSRVQ KHELLPEGYR GSEVLRENNS
     IRSVEERLQE MGQVGGETEV EAIRSKLSVS RMNEHRLQAE VTCLEDSVES VTSQCQLLAK
     ELKGKEEYFH GVKEDHQKCL SENKKLKGQL SQAELTHKSV LDGMRKEISQ LTQELHQRDI
     RMASSAGIDW ERKIKAERQR AEREAAEHRM SLNALENLRQ ENCRLSELLQ TQEPDVAQAL
     VNLEQANQRL QRELLQTQEK LELIAQRRES EIQNAVDSIS QELLNKQEQE LRIMQERLKV
     YEQEMQTFRS QQDAASSGSS LESIFSEVWK EQATGSPISA ASVDSAIEPV EDLASSLPVP
     PTSPANAVAS RFLQEEEQRS HELLQRLNAH IEELKQESQR TVEHFTQAR