ID   CEP63_MACFA             Reviewed;         703 AA.
AC   Q4R703;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Centrosomal protein of 63 kDa;
DE            Short=Cep63;
GN   Name=CEP63; ORFNames=QtsA-16693;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Plays a
CC       role in DNA damage response. Following DNA damage, such as double-
CC       strand breaks (DSBs), is removed from centrosomes; this leads to the
CC       inactivation of spindle assembly and delay in mitotic progression (By
CC       similarity). {ECO:0000250|UniProtKB:Q96MT8}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q3UPP8,
CC       ECO:0000250|UniProtKB:Q96MT8}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q3UPP8,
CC       ECO:0000250|UniProtKB:Q96MT8}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriolar satellite
CC       {ECO:0000250|UniProtKB:Q96MT8}. Note=Colocalizes with CDK5RAP2, CEP152
CC       and WDR62 in 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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q3UPP8, ECO:0000250|UniProtKB:Q96MT8}.
CC   -!- SIMILARITY: Belongs to the CEP63 family. {ECO:0000305}.
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DR   EMBL; AB169027; BAE01121.1; -; mRNA.
DR   AlphaFoldDB; Q4R703; -.
DR   SMR; Q4R703; -.
DR   STRING; 9541.XP_005545865.1; -.
DR   eggNOG; ENOG502QRYU; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
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; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; DNA damage; Mitosis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..703
FT                   /note="Centrosomal protein of 63 kDa"
FT                   /id="PRO_0000381803"
FT   COILED          77..199
FT                   /evidence="ECO:0000255"
FT   COILED          242..303
FT                   /evidence="ECO:0000255"
FT   COILED          346..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"
SQ   SEQUENCE   703 AA;  81463 MW;  F447F33F25764B00 CRC64;
     MEALLERMQN RGHGGGFLTS CEAELQELMK QIDIMVAHKK SEWEGRTHAL ETCLKIREQE
     LKTLRGQLDV THKEVGMLHQ QVEEHEKIKQ EMTMEYKQEL KKLHEELGIL KRSYEKLQKK
     QMREFRGNTK NHREDRSEIE RLTAKIEEFR QKSLDWEKQR LIYQQQVSSL EAQRKALAEQ
     SEIIQAQLAN RKQKLESVEL SSQSEIQHLS SKLERANDTI CANELEIERL TMRVNDLVGT
     SMTVLQEQQQ KEEKLRESEK LLEALQEEKR ELRAALQSQE NLIHEGRMQK EKLQEKVKAA
     DTQHAVEAIR LREESLAEKK YTSQGQGDLD SVLSQLNFTH TSEELLQAEV TRLEGSLESV
     SATCKQLSQE LMEKYEELKR MEAHNNEYRA EIKKLKEQIL QGEQSYSSAL EGMKMEISHL
     TQELHQRDIS IASTKGSSSD MEKRLKAEMQ KAEEKAVEHK EILDQLESLK LENRHLSEMV
     MKFELGLHEA KEISLADLQE NYIEALNKLV SENQQLQKDL MNTKSQLEIS TQMCKKQNDR
     IFKPTHRRTT EFKNTEFKPT HGQHRHDGIK TEHYKTGLHS PRGQASDSID PMSRVLSPLS
     PQISPCSSTR SLTSYSLCKS HSLPSALDTN EANFSDTVSE SMNDQEEFMS SCSLPVSPLG
     SIATRFLEEE ELRSHHILER LDAHTEELKR ESEKTVRQFT ALK