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   27-MAR-2024, entry version 139.
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. Contributes to CROCC/rootletin filament formation.
CC       {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; 10090-ENSMUSP00000054943; -.
DR   PeptideAtlas; Q8C0D9; -.
DR   ProteomicsDB; 280069; -. [Q8C0D9-1]
DR   ProteomicsDB; 280070; -. [Q8C0D9-2]
DR   Pumba; Q8C0D9; -.
DR   Antibodypedia; 47440; 246 antibodies from 24 providers.
DR   DNASU; 216543; -.
DR   Ensembl; ENSMUST00000050611.14; ENSMUSP00000054943.8; ENSMUSG00000044066.15. [Q8C0D9-1]
DR   Ensembl; ENSMUST00000109596.8; ENSMUSP00000105225.2; ENSMUSG00000044066.15. [Q8C0D9-2]
DR   GeneID; 216543; -.
DR   KEGG; mmu:216543; -.
DR   UCSC; uc007icw.1; mouse. [Q8C0D9-1]
DR   UCSC; uc007icx.1; mouse. [Q8C0D9-2]
DR   AGR; MGI:2667663; -.
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; WDRGWPL; -.
DR   OrthoDB; 4636462at2759; -.
DR   PhylomeDB; Q8C0D9; -.
DR   TreeFam; TF333570; -.
DR   BioGRID-ORCS; 216543; 1 hit in 77 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 255 other cell types or tissues.
DR   ExpressionAtlas; Q8C0D9; baseline and differential.
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   Gene3D; 1.20.58.60; -; 1.
DR   InterPro; IPR026696; AKAP6/CEP68.
DR   PANTHER; PTHR14514:SF8; CENTROSOMAL PROTEIN OF 68 KDA; 1.
DR   PANTHER; PTHR14514; PKA ANCHORING PROTEIN; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 1.
DR   Genevisible; Q8C0D9; MM.
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
//