CEP68_MOUSE
ID CEP68_MOUSE Reviewed; 733 AA.
AC Q8C0D9; Q3US49; Q5SW85; Q8R2V0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Centrosomal protein of 68 kDa;
DE Short=Cep68;
GN Name=Cep68;
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 1).
RC STRAIN=C57BL/6J; TISSUE=Head, and Testis;
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] (ISOFORM 2).
RC STRAIN=129; TISSUE=Mammary gland;
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-453 AND SER-459, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Involved in maintenance of centrosome cohesion, probably as
CC part of a linker structure which prevents centrosome splitting.
CC Required for localization of CDK5RAP2 to the centrosome during
CC interphase. {ECO:0000250|UniProtKB:Q76N32}.
CC -!- SUBUNIT: Interacts with CNTLN; the interaction recruits CEP68 to the
CC centrosome. Interacts with the SCF(FBXW11) complex which contains SKP1,
CC CUL1 and FBXW11; the interaction is probably mediated by FBXW11 and the
CC complex also contains CDK5RAP2 and PCNT. Also interacts with F-box
CC protein BTRC. Interacts with serine/threonine-protein kinase PLK1; the
CC interaction leads to phosphorylation of CEP68 and its subsequent
CC degradation. Interacts with NEK2; the interaction leads to
CC phosphorylation of CEP68. {ECO:0000250|UniProtKB:Q76N32}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Note=Localizes to thin fibers
CC protruding away from the proximal ends of the two centrioles.
CC Dissociates from interphase centrosomes at the onset of mitosis.
CC {ECO:0000250|UniProtKB:Q76N32}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C0D9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0D9-2; Sequence=VSP_013477;
CC -!- PTM: Phosphorylation by PLK1 is required for binding to BTRC in
CC prometaphase. Phosphorylated directly or indirectly by NEK2. NEK2-
CC mediated phosphorylation promotes CEP68 dissociation from the
CC centrosome and its degradation at the onset of mitosis.
CC {ECO:0000250|UniProtKB:Q76N32}.
CC -!- PTM: Ubiquitinated and targeted for proteasomal degradation in early
CC mitosis by the SCF(BTRC) and/or SCF(FBXW11) E3 ubiquitin-protein ligase
CC complexes. Degradation is complete by prometaphase and is required for
CC removal of CDK5RAP2 from the peripheral pericentriolar material and
CC subsequent centriole separation. {ECO:0000250|UniProtKB:Q76N32}.
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DR EMBL; AK031622; BAC27484.1; -; mRNA.
DR EMBL; AK140820; BAE24488.1; -; mRNA.
DR EMBL; AL606522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027174; AAH27174.1; -; mRNA.
DR CCDS; CCDS24456.1; -. [Q8C0D9-1]
DR RefSeq; NP_758464.2; NM_172260.3. [Q8C0D9-1]
DR AlphaFoldDB; Q8C0D9; -.
DR SMR; Q8C0D9; -.
DR STRING; 10090.ENSMUSP00000054943; -.
DR iPTMnet; Q8C0D9; -.
DR PhosphoSitePlus; Q8C0D9; -.
DR MaxQB; Q8C0D9; -.
DR PaxDb; Q8C0D9; -.
DR PeptideAtlas; Q8C0D9; -.
DR PRIDE; Q8C0D9; -.
DR ProteomicsDB; 280069; -. [Q8C0D9-1]
DR ProteomicsDB; 280070; -. [Q8C0D9-2]
DR Antibodypedia; 47440; 222 antibodies from 24 providers.
DR DNASU; 216543; -.
DR Ensembl; ENSMUST00000050611; ENSMUSP00000054943; ENSMUSG00000044066. [Q8C0D9-1]
DR Ensembl; ENSMUST00000109596; ENSMUSP00000105225; ENSMUSG00000044066. [Q8C0D9-2]
DR GeneID; 216543; -.
DR KEGG; mmu:216543; -.
DR UCSC; uc007icw.1; mouse. [Q8C0D9-1]
DR UCSC; uc007icx.1; mouse. [Q8C0D9-2]
DR CTD; 23177; -.
DR MGI; MGI:2667663; Cep68.
DR VEuPathDB; HostDB:ENSMUSG00000044066; -.
DR eggNOG; ENOG502RK93; Eukaryota.
DR GeneTree; ENSGT00810000125473; -.
DR HOGENOM; CLU_370860_0_0_1; -.
DR InParanoid; Q8C0D9; -.
DR OMA; IPAPACW; -.
DR OrthoDB; 1235573at2759; -.
DR PhylomeDB; Q8C0D9; -.
DR TreeFam; TF333570; -.
DR BioGRID-ORCS; 216543; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cep68; mouse.
DR PRO; PR:Q8C0D9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C0D9; protein.
DR Bgee; ENSMUSG00000044066; Expressed in brain blood vessel and 252 other tissues.
DR ExpressionAtlas; Q8C0D9; baseline and differential.
DR Genevisible; Q8C0D9; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISO:MGI.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; ISO:MGI.
DR InterPro; IPR030265; CEP68.
DR PANTHER; PTHR14514:SF3; PTHR14514:SF3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..733
FT /note="Centrosomal protein of 68 kDa"
FT /id="PRO_0000089495"
FT REGION 71..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76N32"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 647..733
FT /note="QFKKDVDEHQSLTESVLEKGEILLQCLLDNTPVLKDVLERIAKQSGELESRA
FT DHLYDSILASLDMLAGCTLIPDNRPTAAEHPHEGL -> VICSPGLFIHGDGS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013477"
FT CONFLICT 228
FT /note="P -> Q (in Ref. 1; BAC27484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 733 AA; 78749 MW; 15D93FCECDDC92A9 CRC64;
MALSEDEAEA EVSVNTKVPS CGRWNSGKLL PSGLEPDQPL HLGVEGGPLW RAEADPGCIS
GVFLSRVHTA SKEPVADRSK PPLRGPLPSA SVGTGEVLHS MGSQMEEDRL PASQDLLPAL
QVFGTITVCS GQEADSEDFQ ATLDPSQVLG LSQQPHTSGL PLPPQWKSTV SPGAPQLSSR
SISASSVGSS LQDHQEKAGP QRASFANVSS PELTVPQAAH SVVGAGPPLQ GSAQPLTSGS
DATGLGKRHL SFQAEYWACA LPNSLPPSPN RHSALWDPNK EYEDLLDYTY PLRPGPQLPK
QPESHVLTEP VLQDSGVDLD SLSVSPASTL KSPTNVSHNC SSAEVPTLPF SGARESCLKR
WPLGIFQKQG GTSLSSWNQL ASTPRAPGTE DASWENREAA LRGTAEDCLP IGEDLRMGSP
QLKTKEKEPP FPRQKRGRQH VSCPACVTPG WPSEEEVGSD EEYLALPTRL TQVSSLVSYS
GARPSFVNLH TGAAEEHSSL QVSDSDKPAS PTLDSSHRKH PSGTSFQGPV GQNPCFRHSI
QPQDSRGKSS LMSNQTLGVS SKPLKTQPAS KAMTDRRLFS ELVAGETLPR TTDEQEKASL
VQCVQTFCCR LEELICWLYN VTDVADLSAP PRTSLTGLKS SLQLYRQFKK DVDEHQSLTE
SVLEKGEILL QCLLDNTPVL KDVLERIAKQ SGELESRADH LYDSILASLD MLAGCTLIPD
NRPTAAEHPH EGL
