CEP63_PONAB
ID CEP63_PONAB Reviewed; 541 AA.
AC Q5NVN6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Centrosomal protein of 63 kDa;
DE Short=Cep63;
GN Name=CEP63;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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, KdIAA0753/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; CR925979; CAI29627.1; -; mRNA.
DR RefSeq; NP_001127080.1; NM_001133608.1.
DR AlphaFoldDB; Q5NVN6; -.
DR SMR; Q5NVN6; -.
DR STRING; 9601.ENSPPYP00000015800; -.
DR Ensembl; ENSPPYT00000016423; ENSPPYP00000015800; ENSPPYG00000014122.
DR GeneID; 100174110; -.
DR KEGG; pon:100174110; -.
DR CTD; 80254; -.
DR eggNOG; ENOG502QRYU; Eukaryota.
DR GeneTree; ENSGT00940000153190; -.
DR HOGENOM; CLU_027471_0_0_1; -.
DR InParanoid; Q5NVN6; -.
DR OMA; CLDIREQ; -.
DR OrthoDB; 943593at2759; -.
DR TreeFam; TF330595; -.
DR Proteomes; UP000001595; Chromosome 3.
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; 2.
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..541
FT /note="Centrosomal protein of 63 kDa"
FT /id="PRO_0000381805"
FT REGION 294..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..199
FT /evidence="ECO:0000255"
FT COILED 242..305
FT /evidence="ECO:0000255"
FT COILED 346..485
FT /evidence="ECO:0000255"
FT COILED 514..541
FT /evidence="ECO:0000255"
FT COMPBIAS 294..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 541 AA; 63038 MW; 4DB08E7D02F56D60 CRC64;
MEALLEGIQN RGHGGGFLTS CEAELQELMK QIDIMVAHKK SEWEGRTHAL ETCLKIREQE
LKSLRSQLDV THKEVGMLHQ QVEEHEKIKQ EMTMEYKQEL KKLHEELGIL KRSYEKLQKK
QMREFRGNTK NHREDRSEIE RLTAKIEEFR QKSLDWEKQR LIYQQQVSSL EAQRKALAEQ
SEIIQAQLAN RKQKLESVEL SSQSEIQHLS SKLERANDTI CANELEIERL TMRVNDLVGT
SMTVLQEQQQ KEEKLRESEK LLEALQEEKR ELKAALQSQE NLIHEARIQK EKLQEKVKAT
DTQHAVEAIR PREESPAEKK YTSQGQGDLD SVLFQLNFTH TSEDLLQAEV TRLEGSLESV
SATCKQLSQE LMEKYEELKR MEAHNNEYKA EIKKLKEQIL QGEQSYSSAL EGMKMEISHL
TQELHQRDIT IASTKGSSSD MEKRLRAEMQ KAEDKAVEHK EILDQLESLK LENRHLSEMV
MKLELGLHEC SLPVSPLGSI ATRFLEEEEL RSHHILERLD AHIEELKRES EKTVRQFTAL
K
