ID CEP68_HUMAN Reviewed; 757 AA. AC Q76N32; B4DRQ1; D6W5F1; D6W5F2; O60326; Q9BQ18; Q9UDM9; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 27-MAR-2024, entry version 162. DE RecName: Full=Centrosomal protein of 68 kDa; DE Short=Cep68; GN Name=CEP68; Synonyms=KIAA0582; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9628581; DOI=10.1093/dnares/5.1.31; RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., RA Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. IX. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:31-39(1998). RN [2] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-74. RC TISSUE=Lymph; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18042621; DOI=10.1242/jcs.020248; RA Graser S., Stierhof Y.D., Nigg E.A.; RT "Cep68 and Cep215 (Cdk5rap2) are required for centrosome cohesion."; RL J. Cell Sci. 120:4321-4331(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP FUNCTION, INTERACTION WITH CNTLN AND NEK2, AND PHOSPHORYLATION. RX PubMed=24554434; DOI=10.1242/jcs.139451; RA Fang G., Zhang D., Yin H., Zheng L., Bi X., Yuan L.; RT "Centlein mediates an interaction between C-Nap1 and Cep68 to maintain RT centrosome cohesion."; RL J. Cell Sci. 127:1631-1639(2014). RN [12] RP INTERACTION WITH BTRC, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND RP PROTEOLYTIC DEGRADATION. RX PubMed=25704143; DOI=10.1016/j.ejcb.2015.01.004; RA Man X., Megraw T.L., Lim Y.P.; RT "Cep68 can be regulated by Nek2 and SCF complex."; RL Eur. J. Cell Biol. 94:162-172(2015). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SCF(FBXW11) COMPLEX AND RP BTRC, MUTAGENESIS OF 331-ASP--ASP-337; SER-332 AND ASP-337, PHOSPHORYLATION RP AT SER-332, AND PROTEOLYTIC DEGRADATION. RX PubMed=25503564; DOI=10.1038/ncb3076; RA Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V., Florens L., RA Washburn M.P., Pagano M.; RT "Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM RT to allow centriole separation, disengagement and licensing."; RL Nat. Cell Biol. 17:31-43(2015). RN [14] RP FUNCTION. RX PubMed=30404835; DOI=10.1242/jcs.222901; RA Xia Y., Huang N., Chen Z., Li F., Fan G., Ma D., Chen J., Teng J.; RT "CCDC102B functions in centrosome linker assembly and centrosome RT cohesion."; RL J. Cell Sci. 131:0-0(2018). RN [15] RP SUBCELLULAR LOCATION. RX PubMed=31974111; DOI=10.1242/jcs.239616; RA Hossain D., Shih S.Y., Xiao X., White J., Tsang W.Y.; RT "Cep44 functions in centrosome cohesion by stabilizing rootletin."; RL J. Cell Sci. 133:0-0(2020). CC -!- FUNCTION: Involved in maintenance of centrosome cohesion, probably as CC part of a linker structure which prevents centrosome splitting CC (PubMed:18042621). Required for localization of CDK5RAP2 to the CC centrosome during interphase (PubMed:24554434, PubMed:25503564). CC Contributes to CROCC/rootletin filament formation (PubMed:30404835). CC {ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:24554434, CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:30404835}. CC -!- SUBUNIT: Interacts with CNTLN; the interaction recruits CEP68 to the CC centrosome (PubMed:24554434). Interacts with the SCF(FBXW11) complex CC which contains SKP1, CUL1 and FBXW11; the interaction is probably CC mediated by FBXW11 and the complex also contains CDK5RAP2 and PCNT CC (PubMed:25503564). Also interacts with F-box protein BTRC CC (PubMed:25704143, PubMed:25503564). Interacts with serine/threonine- CC protein kinase PLK1; the interaction leads to phosphorylation of CEP68 CC and its subsequent degradation (PubMed:25503564). Interacts with NEK2; CC the interaction leads to phosphorylation of CEP68 (PubMed:24554434). CC {ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:24554434, CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143}. CC -!- INTERACTION: CC Q76N32; Q9Y297: BTRC; NbExp=2; IntAct=EBI-9051024, EBI-307461; CC Q76N32; Q96SN8: CDK5RAP2; NbExp=8; IntAct=EBI-9051024, EBI-308374; CC Q76N32; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-9051024, EBI-10171858; CC Q76N32; O95613: PCNT; NbExp=3; IntAct=EBI-9051024, EBI-530012; CC Q76N32; P53350: PLK1; NbExp=2; IntAct=EBI-9051024, EBI-476768; CC Q76N32; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-9051024, EBI-739895; CC Q76N32-2; Q14746: COG2; NbExp=3; IntAct=EBI-11975967, EBI-389449; CC Q76N32-2; P56545-3: CTBP2; NbExp=3; IntAct=EBI-11975967, EBI-10171902; CC Q76N32-2; O14964: HGS; NbExp=3; IntAct=EBI-11975967, EBI-740220; CC Q76N32-2; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-11975967, EBI-765817; CC Q76N32-2; Q99598: TSNAX; NbExp=3; IntAct=EBI-11975967, EBI-742638; CC Q76N32-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-11975967, EBI-739895; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:14654843, CC ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:25503564, CC ECO:0000269|PubMed:25704143, ECO:0000269|PubMed:31974111}. CC Note=Localizes to thin fibers protruding away from the proximal ends of CC the two centrioles. Dissociates from interphase centrosomes at the CC onset of mitosis. {ECO:0000269|PubMed:18042621, CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q76N32-1; Sequence=Displayed; CC Name=2; CC IsoId=Q76N32-2; Sequence=VSP_013476; CC -!- PTM: Phosphorylation by PLK1 is required for binding to BTRC in CC prometaphase (PubMed:25503564). Phosphorylated directly or indirectly CC by NEK2 (PubMed:24554434). NEK2-mediated phosphorylation promotes CEP68 CC dissociation from the centrosome and its degradation at the onset of CC mitosis (PubMed:25704143). {ECO:0000269|PubMed:24554434, CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143}. 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 (PubMed:25704143, PubMed:25503564). Degradation is complete CC by prometaphase and is required for removal of CDK5RAP2 from the CC peripheral pericentriolar material and subsequent centriole separation CC (PubMed:25503564). {ECO:0000269|PubMed:25503564, CC ECO:0000269|PubMed:25704143}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA25508.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB011154; BAA25508.2; ALT_INIT; mRNA. DR EMBL; AC007386; AAF03518.2; -; Genomic_DNA. DR EMBL; AK299373; BAG61363.1; -; mRNA. DR EMBL; CH471053; EAW99926.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99927.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99928.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99929.1; -; Genomic_DNA. DR EMBL; BC002982; AAH02982.1; -; mRNA. DR EMBL; BC004873; AAH04873.1; -; mRNA. DR CCDS; CCDS1880.2; -. [Q76N32-1] DR CCDS; CCDS82457.1; -. [Q76N32-2] DR RefSeq; NP_001306029.1; NM_001319100.1. [Q76N32-1] DR RefSeq; NP_001306030.1; NM_001319101.1. [Q76N32-2] DR RefSeq; NP_055962.2; NM_015147.2. [Q76N32-1] DR AlphaFoldDB; Q76N32; -. DR SMR; Q76N32; -. DR BioGRID; 116789; 24. DR DIP; DIP-57845N; -. DR IntAct; Q76N32; 24. DR STRING; 9606.ENSP00000367229; -. DR GlyGen; Q76N32; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q76N32; -. DR PhosphoSitePlus; Q76N32; -. DR BioMuta; CEP68; -. DR DMDM; 62899863; -. DR EPD; Q76N32; -. DR jPOST; Q76N32; -. DR MassIVE; Q76N32; -. DR MaxQB; Q76N32; -. DR PaxDb; 9606-ENSP00000367229; -. DR PeptideAtlas; Q76N32; -. DR ProteomicsDB; 68690; -. [Q76N32-1] DR ProteomicsDB; 68691; -. [Q76N32-2] DR Pumba; Q76N32; -. DR Antibodypedia; 47440; 246 antibodies from 24 providers. DR DNASU; 23177; -. DR Ensembl; ENST00000260569.4; ENSP00000260569.4; ENSG00000011523.15. [Q76N32-2] DR Ensembl; ENST00000377990.7; ENSP00000367229.2; ENSG00000011523.15. [Q76N32-1] DR GeneID; 23177; -. DR KEGG; hsa:23177; -. DR MANE-Select; ENST00000377990.7; ENSP00000367229.2; NM_015147.3; NP_055962.2. DR UCSC; uc002sdk.5; human. [Q76N32-1] DR AGR; HGNC:29076; -. DR CTD; 23177; -. DR DisGeNET; 23177; -. DR GeneCards; CEP68; -. DR HGNC; HGNC:29076; CEP68. DR HPA; ENSG00000011523; Low tissue specificity. DR MIM; 616889; gene. DR neXtProt; NX_Q76N32; -. DR OpenTargets; ENSG00000011523; -. DR PharmGKB; PA134991391; -. DR VEuPathDB; HostDB:ENSG00000011523; -. DR eggNOG; ENOG502RK93; Eukaryota. DR GeneTree; ENSGT00810000125473; -. DR HOGENOM; CLU_370860_0_0_1; -. DR InParanoid; Q76N32; -. DR OMA; WDRGWPL; -. DR OrthoDB; 4636462at2759; -. DR PhylomeDB; Q76N32; -. DR TreeFam; TF333570; -. DR PathwayCommons; Q76N32; -. DR SignaLink; Q76N32; -. DR BioGRID-ORCS; 23177; 115 hits in 1164 CRISPR screens. DR ChiTaRS; CEP68; human. DR GeneWiki; CEP68; -. DR GenomeRNAi; 23177; -. DR Pharos; Q76N32; Tbio. DR PRO; PR:Q76N32; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q76N32; Protein. DR Bgee; ENSG00000011523; Expressed in biceps brachii and 214 other cell types or tissues. DR ExpressionAtlas; Q76N32; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB. DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB. DR GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB. 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; Q76N32; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Cytoskeleton; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..757 FT /note="Centrosomal protein of 68 kDa" FT /id="PRO_0000089494" FT REGION 1..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 67..158 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 192..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 311..480 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 509..551 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 597..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..34 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 119..145 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 192..210 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 335..358 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 406..429 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 444..476 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 522..543 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 332 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000269|PubMed:25503564" FT MOD_RES 472 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C0D9" FT MOD_RES 478 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 492..628 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_013476" FT VARIANT 27 FT /note="R -> G (in dbSNP:rs12611491)" FT /id="VAR_050794" FT VARIANT 74 FT /note="G -> S (in dbSNP:rs7572857)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_022363" FT VARIANT 397 FT /note="L -> P (in dbSNP:rs35501092)" FT /id="VAR_050795" FT VARIANT 462 FT /note="R -> C (in dbSNP:rs35694840)" FT /id="VAR_050796" FT VARIANT 473 FT /note="E -> Q (in dbSNP:rs35089924)" FT /id="VAR_050797" FT MUTAGEN 331..337 FT /note="Missing: Prevents binding to BTRC and FT down-regulation of CEP68 during mitosis." FT /evidence="ECO:0000269|PubMed:25503564" FT MUTAGEN 332 FT /note="S->A: Prevents binding to BTRC and down-regulation FT of CEP68 during mitosis." FT /evidence="ECO:0000269|PubMed:25503564" FT MUTAGEN 337 FT /note="D->A: Reduces CEP68 binding to BTRC." FT /evidence="ECO:0000269|PubMed:12168954" SQ SEQUENCE 757 AA; 81102 MW; 3FC969065CD5D2D7 CRC64; MALGEEKAEA EASEDTKAQS YGRGSCRERE LDIPGPMSGE QPPRLEAEGG LISPVWGAEG IPAPTCWIGT DPGGPSRAHQ PQASDANREP VAERSEPALS GLPPATMGSG DLLLSGESQV EKTKLSSSEE FPQTLSLPRT TTICSGHDAD TEDDPSLADL PQALDLSQQP HSSGLSCLSQ WKSVLSPGSA AQPSSCSISA SSTGSSLQGH QERAEPRGGS LAKVSSSLEP VVPQEPSSVV GLGPRPQWSP QPVFSGGDAS GLGRRRLSFQ AEYWACVLPD SLPPSPDRHS PLWNPNKEYE DLLDYTYPLR PGPQLPKHLD SRVPADPVLQ DSGVDLDSFS VSPASTLKSP TNVSPNCPPA EATALPFSGP REPSLKQWPS RVPQKQGGMG LASWSQLAST PRAPGSRDAR WERREPALRG AKDRLTIGKH LDMGSPQLRT RDRGWPSPRP EREKRTSQSA RRPTCTESRW KSEEEVESDD EYLALPARLT QVSSLVSYLG SISTLVTLPT GDIKGQSPLE VSDSDGPASF PSSSSQSQLP PGAALQGSGD PEGQNPCFLR SFVRAHDSAG EGSLGSSQAL GVSSGLLKTR PSLPARLDRW PFSDPDVEGQ LPRKGGEQGK ESLVQCVKTF CCQLEELICW LYNVADVTDH GTAARSNLTS LKSSLQLYRQ FKKDIDEHQS LTESVLQKGE ILLQCLLENT PVLEDVLGRI AKQSGELESH ADRLYDSILA SLDMLAGCTL IPDKKPMAAM EHPCEGV //