CEP68_HUMAN
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 03-AUG-2022, entry version 153.
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 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 {ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:24554434,
CC ECO:0000269|PubMed:25503564}.
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=5; 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};
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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; 23.
DR DIP; DIP-57845N; -.
DR IntAct; Q76N32; 25.
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; Q76N32; -.
DR PeptideAtlas; Q76N32; -.
DR PRIDE; Q76N32; -.
DR ProteomicsDB; 68690; -. [Q76N32-1]
DR ProteomicsDB; 68691; -. [Q76N32-2]
DR Antibodypedia; 47440; 222 antibodies from 24 providers.
DR DNASU; 23177; -.
DR Ensembl; ENST00000260569.4; ENSP00000260569.4; ENSG00000011523.14. [Q76N32-2]
DR Ensembl; ENST00000377990.7; ENSP00000367229.2; ENSG00000011523.14. [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 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; IPAPACW; -.
DR OrthoDB; 1235573at2759; -.
DR PhylomeDB; Q76N32; -.
DR TreeFam; TF333570; -.
DR PathwayCommons; Q76N32; -.
DR SignaLink; Q76N32; -.
DR BioGRID-ORCS; 23177; 113 hits in 1087 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 212 other tissues.
DR ExpressionAtlas; Q76N32; baseline and differential.
DR Genevisible; Q76N32; HS.
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 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..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 down-
FT 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
