CEP63_CHICK
ID CEP63_CHICK Reviewed; 711 AA.
AC P0CB05;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Centrosomal protein of 63 kDa;
DE Short=Cep63;
GN Name=CEP63;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-248.
RA Evock-Clover C.M., Ashwell C.M., McMurtry J.P., Lillehoj H.S.,
RA Matukumalli L.K., Van Tassell C.P.;
RT "Characterization of expressed sequence tags generated from multiple
RT chicken tissues.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 damage, such as double-strand breaks
CC (DSBs), is removed from centrosomes; this leads to the inactivation of
CC spindle assembly and delay in 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 -!- SIMILARITY: Belongs to the CEP63 family. {ECO:0000305}.
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DR EMBL; DN928209; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015132426.1; XM_015276940.1.
DR AlphaFoldDB; P0CB05; -.
DR SMR; P0CB05; -.
DR STRING; 9031.ENSGALP00000010701; -.
DR PaxDb; P0CB05; -.
DR Ensembl; ENSGALT00000010715; ENSGALP00000010701; ENSGALG00000006632.
DR GeneID; 424873; -.
DR CTD; 80254; -.
DR VEuPathDB; HostDB:geneid_424873; -.
DR eggNOG; ENOG502QRYU; Eukaryota.
DR GeneTree; ENSGT00940000153190; -.
DR HOGENOM; CLU_027471_0_0_1; -.
DR InParanoid; P0CB05; -.
DR OMA; CLDIREQ; -.
DR PhylomeDB; P0CB05; -.
DR PRO; PR:P0CB05; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000006632; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; P0CB05; baseline and differential.
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: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; 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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW DNA damage; Mitosis; Reference proteome.
FT CHAIN 1..711
FT /note="Centrosomal protein of 63 kDa"
FT /id="PRO_0000381807"
FT REGION 529..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..192
FT /evidence="ECO:0000255"
FT COILED 224..535
FT /evidence="ECO:0000255"
FT COMPBIAS 529..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 82000 MW; C64180F51FE4E174 CRC64;
MEALLEGMQR NGQGSSGFLT SCEAELQELM KQIDIMVAHK KAEWEGQTQA LEACLGVREQ
ELSSARAALE EKHKEVGKLR QQLEDMEAAK QDLVREYEQQ LKKFQEELAR LRRSYEKLQK
KQLREAREEA TKRQGDDQCE MSRLSRKLEE FRQKSLDWEK QRLLYQQQVA SLEAQRKALA
EQSELIQTQL ASRKQILESV ELASRSEIQH LTSKLERAND TICANELEVE RLNMRVDDLT
ENNRMILEDQ QRVAEELRQS KKMLEVLQDE KMELRATLQS QEDFIDSSKL HQEQLQKELA
RVTETLHTKE ILIRALEERL QEKQLSSPGL EHILLQLDVA QEKEQHLQAE VTHLEDSLVS
SNARCVQLSE ELAESIKELQ SMEEHRAESK VEIKKLKEQL SQAEQIHRGE LEGMRKEILR
LTQELHQRDI TIASAGGSTS DLEQRLRMEI ERAERKAVEH RMILVQLETL KLENRHLSEM
LEKVELGVLE GKDATLRALS EDYVVELNKL KSENQQLKKD LSEAREKLEL TTQSQPEGTA
QQLQSEEPEP RDVQHRPTQE SQHKQDEQTE KIHHKPDKTT QHHQRWKIQP LPAEIPVAVI
PEASVLPTQT SRKSCVESPT LAAGALQGTD SLLLVLDDSK GFPDATSRQS NHEQESVPLC
PLPTSSVGSV AARYLEEEEL RSQHILECLD AHIEELKKES EKIVRHFGHQ E
