CE170_HUMAN
ID CE170_HUMAN Reviewed; 1584 AA.
AC Q5SW79; O75058; Q5SW77; Q5SW78; Q7LGA9; Q86W31; Q9UQ08; Q9UQ09;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Centrosomal protein of 170 kDa;
DE Short=Cep170;
DE AltName: Full=KARP-1-binding protein;
DE Short=KARP1-binding protein;
GN Name=CEP170; Synonyms=FAM68A, KAB, KIAA0470;
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 [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT SER-213.
RC TISSUE=Brain, and Cervix carcinoma;
RA Hara Y., Adachi Y.;
RT "Molecular cloning and initial characterization of KAB.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-213.
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543 (ISOFORM 2), AND VARIANT
RP SER-213.
RC TISSUE=Testis;
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 [6]
RP FUNCTION, INTERACTION WITH PLK1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=15616186; DOI=10.1091/mbc.e04-10-0939;
RA Guarguaglini G., Duncan P.I., Stierhof Y.D., Holmstroem T., Duensing S.,
RA Nigg E.A.;
RT "The forkhead-associated domain protein Cep170 interacts with Polo-like
RT kinase 1 and serves as a marker for mature centrioles.";
RL Mol. Biol. Cell 16:1095-1107(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-359 AND SER-933, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633 AND SER-636, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-359; THR-501;
RP SER-633; SER-636; SER-838; SER-930; SER-958; SER-1112; SER-1165 AND
RP SER-1251, AND IDENTIFICATION BY 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1112 AND SER-1160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-359; TYR-364;
RP SER-1112 AND SER-1114, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-359; SER-446 AND
RP SER-497, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=23386061; DOI=10.1038/emboj.2013.3;
RA Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
RA Reiter J.F.;
RT "Kif3a interacts with Dynactin subunit p150 Glued to organize centriole
RT subdistal appendages.";
RL EMBO J. 32:597-607(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-141; SER-356;
RP SER-359; SER-446; SER-466; SER-571; SER-580; SER-630; SER-636; THR-644;
RP SER-667; SER-725; THR-760; SER-879; SER-881; THR-914; THR-920; SER-958;
RP THR-1058; SER-1059; SER-1112; SER-1132; SER-1133; SER-1145; SER-1160;
RP SER-1165; SER-1198; SER-1205; SER-1210; SER-1241; SER-1270; SER-1280 AND
RP SER-1362, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP FUNCTION, AND INTERACTION WITH CCDC68 AND CCDC120.
RX PubMed=28422092; DOI=10.1038/ncomms15057;
RA Huang N., Xia Y., Zhang D., Wang S., Bao Y., He R., Teng J., Chen J.;
RT "Hierarchical assembly of centriole subdistal appendages via centrosome
RT binding proteins CCDC120 and CCDC68.";
RL Nat. Commun. 8:15057-15057(2017).
RN [20]
RP INTERACTION WITH TBK1 AND CCDC61, AND SUBCELLULAR LOCATION.
RX PubMed=30354798; DOI=10.1091/mbc.e18-02-0115;
RA Baerenz F., Kschonsak Y.T., Meyer A., Jafarpour A., Lorenz H., Hoffmann I.;
RT "Ccdc61 controls centrosomal localization of Cep170 and is required for
RT spindle assembly and symmetry.";
RL Mol. Biol. Cell 29:3105-3118(2018).
RN [21]
RP INTERACTION WITH CCDC61, AND SUBCELLULAR LOCATION.
RX PubMed=31789463; DOI=10.1111/boc.201900038;
RA Pizon V., Gaudin N., Poteau M., Cifuentes-Diaz C., Demdou R., Heyer V.,
RA Reina San Martin B., Azimzadeh J.;
RT "hVFL3/CCDC61 is a component of mother centriole subdistal appendages
RT required for centrosome cohesion and positioning.";
RL Biol. Cell 112:22-37(2020).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-126.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a centrosomal protein 170kDA, transcript variant beta
RT (CEP170) from Homo sapiens at 2.15 A resolution (PSI community target,
RT Sundstrom).";
RL Submitted (APR-2013) to the PDB data bank.
CC -!- FUNCTION: Plays a role in microtubule organization (PubMed:15616186).
CC Required for centriole subdistal appendage assembly (PubMed:28422092).
CC {ECO:0000269|PubMed:15616186, ECO:0000269|PubMed:28422092}.
CC -!- SUBUNIT: Interacts with CCDC68 and CCDC120; leading to recruitment to
CC centrosomes (PubMed:28422092). Interacts with PLK1 (PubMed:15616186).
CC Interacts with NIN (By similarity). Interacts with FHDC1 (By
CC similarity). Interacts with CCDC61 (PubMed:30354798, PubMed:31789463).
CC Interacts with TBK1; efficient complex formation may be dependent on
CC the presence of CCDC61 (PubMed:30354798).
CC {ECO:0000250|UniProtKB:Q6A065, ECO:0000269|PubMed:15616186,
CC ECO:0000269|PubMed:28422092, ECO:0000269|PubMed:30354798,
CC ECO:0000269|PubMed:31789463}.
CC -!- INTERACTION:
CC Q5SW79; Q96HB5: CCDC120; NbExp=12; IntAct=EBI-1104799, EBI-744556;
CC Q5SW79; Q9Y6R9: CCDC61; NbExp=3; IntAct=EBI-1104799, EBI-10961230;
CC Q5SW79; Q9H2F9: CCDC68; NbExp=6; IntAct=EBI-1104799, EBI-2813327;
CC Q5SW79; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-1104799, EBI-529989;
CC Q5SW79; P12520: vpr; Xeno; NbExp=4; IntAct=EBI-1104799, EBI-6164519;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:30354798,
CC ECO:0000269|PubMed:31789463}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:15616186,
CC ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:31789463}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:15616186}. Note=Associated
CC with the mature mother centriole. Associated with spindle microtubules
CC during mitosis. Localizes to the distal appendage region of the
CC centriole (PubMed:31789463). Localizes at the centriole proximal ends
CC (PubMed:31789463). {ECO:0000269|PubMed:23386061,
CC ECO:0000269|PubMed:31789463}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q5SW79-1; Sequence=Displayed;
CC Name=2; Synonyms=Gamma, 3;
CC IsoId=Q5SW79-2; Sequence=VSP_024240, VSP_024241, VSP_024242;
CC Name=3; Synonyms=Beta, KAB2;
CC IsoId=Q5SW79-3; Sequence=VSP_024240;
CC -!- PTM: Phosphorylated; probably by PLK1. {ECO:0000269|PubMed:15616186}.
CC -!- SIMILARITY: Belongs to the CEP170 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32315.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB022657; BAA83378.1; -; mRNA.
DR EMBL; AB022658; BAA83379.1; -; mRNA.
DR EMBL; AB022659; BAA83380.1; -; mRNA.
DR EMBL; AB007939; BAA32315.2; ALT_INIT; mRNA.
DR EMBL; AC092782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050722; AAH50722.1; ALT_TERM; mRNA.
DR CCDS; CCDS44337.1; -. [Q5SW79-3]
DR CCDS; CCDS44338.1; -. [Q5SW79-2]
DR CCDS; CCDS44339.1; -. [Q5SW79-1]
DR PIR; T00095; T00095.
DR RefSeq; NP_001035863.1; NM_001042404.1. [Q5SW79-3]
DR RefSeq; NP_001035864.1; NM_001042405.1. [Q5SW79-2]
DR RefSeq; NP_055627.2; NM_014812.2. [Q5SW79-1]
DR RefSeq; XP_016858425.1; XM_017002936.1. [Q5SW79-1]
DR PDB; 4JON; X-ray; 2.15 A; A/B/C/D/E=1-126.
DR PDBsum; 4JON; -.
DR AlphaFoldDB; Q5SW79; -.
DR SMR; Q5SW79; -.
DR BioGRID; 115193; 277.
DR DIP; DIP-37594N; -.
DR IntAct; Q5SW79; 218.
DR MINT; Q5SW79; -.
DR STRING; 9606.ENSP00000355500; -.
DR GlyGen; Q5SW79; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5SW79; -.
DR MetOSite; Q5SW79; -.
DR PhosphoSitePlus; Q5SW79; -.
DR BioMuta; CEP170; -.
DR DMDM; 74743919; -.
DR EPD; Q5SW79; -.
DR jPOST; Q5SW79; -.
DR MassIVE; Q5SW79; -.
DR MaxQB; Q5SW79; -.
DR PaxDb; Q5SW79; -.
DR PeptideAtlas; Q5SW79; -.
DR PRIDE; Q5SW79; -.
DR ProteomicsDB; 63964; -. [Q5SW79-1]
DR ProteomicsDB; 63965; -. [Q5SW79-2]
DR ProteomicsDB; 63966; -. [Q5SW79-3]
DR Antibodypedia; 34708; 116 antibodies from 21 providers.
DR DNASU; 9859; -.
DR Ensembl; ENST00000366542.6; ENSP00000355500.1; ENSG00000143702.16. [Q5SW79-1]
DR Ensembl; ENST00000366543.5; ENSP00000355501.1; ENSG00000143702.16. [Q5SW79-2]
DR Ensembl; ENST00000366544.5; ENSP00000355502.1; ENSG00000143702.16. [Q5SW79-3]
DR Ensembl; ENST00000450306.5; ENSP00000482707.1; ENSG00000276725.4. [Q5SW79-3]
DR Ensembl; ENST00000612450.4; ENSP00000483344.1; ENSG00000276725.4. [Q5SW79-1]
DR Ensembl; ENST00000621831.4; ENSP00000484359.2; ENSG00000276725.4. [Q5SW79-2]
DR GeneID; 9859; -.
DR KEGG; hsa:9859; -.
DR MANE-Select; ENST00000366542.6; ENSP00000355500.1; NM_014812.3; NP_055627.2.
DR UCSC; uc057qug.1; human. [Q5SW79-1]
DR CTD; 9859; -.
DR DisGeNET; 9859; -.
DR GeneCards; CEP170; -.
DR HGNC; HGNC:28920; CEP170.
DR HPA; ENSG00000143702; Group enriched (bone marrow, brain, testis).
DR MIM; 613023; gene.
DR neXtProt; NX_Q5SW79; -.
DR OpenTargets; ENSG00000143702; -.
DR PharmGKB; PA128395757; -.
DR VEuPathDB; HostDB:ENSG00000143702; -.
DR eggNOG; ENOG502QSH8; Eukaryota.
DR GeneTree; ENSGT00940000155103; -.
DR HOGENOM; CLU_003940_1_0_1; -.
DR InParanoid; Q5SW79; -.
DR OMA; IDKCRED; -.
DR OrthoDB; 83451at2759; -.
DR PhylomeDB; Q5SW79; -.
DR TreeFam; TF328469; -.
DR PathwayCommons; Q5SW79; -.
DR SignaLink; Q5SW79; -.
DR BioGRID-ORCS; 9859; 15 hits in 1043 CRISPR screens.
DR ChiTaRS; CEP170; human.
DR GeneWiki; CEP170; -.
DR GenomeRNAi; 9859; -.
DR Pharos; Q5SW79; Tbio.
DR PRO; PR:Q5SW79; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5SW79; protein.
DR Bgee; ENSG00000143702; Expressed in cortical plate and 101 other tissues.
DR ExpressionAtlas; Q5SW79; baseline and differential.
DR Genevisible; Q5SW79; HS.
DR GO; GO:0120103; C:centriolar subdistal appendage; IDA:GO_Central.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR026644; CEP170.
DR InterPro; IPR029300; CEP170_C.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR15715:SF17; PTHR15715:SF17; 1.
DR Pfam; PF15308; CEP170_C; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1584
FT /note="Centrosomal protein of 170 kDa"
FT /id="PRO_0000282887"
FT DOMAIN 23..73
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 368..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..1584
FT /note="Targeting to microtubules"
FT REGION 906..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1460
FT /note="Interaction with CCDC61"
FT /evidence="ECO:0000269|PubMed:30354798"
FT REGION 1113..1584
FT /note="Targeting to centrosomes"
FT REGION 1238..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1467..1495
FT /evidence="ECO:0000255"
FT COMPBIAS 368..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 364
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 644
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 760
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 914
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 920
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 958
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A065"
FT MOD_RES 1023
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6A065"
FT MOD_RES 1058
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A065"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A065"
FT MOD_RES 1522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A065"
FT VAR_SEQ 425..522
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9455484, ECO:0000303|Ref.1"
FT /id="VSP_024240"
FT VAR_SEQ 1226..1261
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9455484, ECO:0000303|Ref.1"
FT /id="VSP_024241"
FT VAR_SEQ 1353
FT /note="E -> EVGDLHGEMHK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9455484, ECO:0000303|Ref.1"
FT /id="VSP_024242"
FT VARIANT 213
FT /note="G -> S (in dbSNP:rs2631092)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9455484, ECO:0000269|Ref.1"
FT /id="VAR_031437"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:4JON"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:4JON"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:4JON"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4JON"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:4JON"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:4JON"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4JON"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4JON"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:4JON"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:4JON"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:4JON"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:4JON"
SQ SEQUENCE 1584 AA; 175293 MW; 50E981650D21B2E6 CRC64;
MSLTSWFLVS SGGTRHRLPR EMIFVGRDDC ELMLQSRSVD KQHAVINYDA STDEHLVKDL
GSLNGTFVND VRIPEQTYIT LKLEDKLRFG YDTNLFTVVQ GEMRVPEEAL KHEKFTIQLQ
LSQKSSESEL SKSASAKSID SKVADAATEV QHKTTEALKS EEKAMDISAM PRGTPLYGQP
SWWGDDEVDE KRAFKTNGKP EEKNHEAGTS GCGIDAKQVE EQSAAANEEV LFPFCREPSY
FEIPTKEFQQ PSQITESTIH EIPTKDTPSS HITGAGHASF TIEFDDSTPG KVTIRDHVTK
FTSDQRHKSK KSSPGTQDLL GIQTGMMAPE NKVADWLAQN NPPQMLWERT EEDSKSIKSD
VPVYLKRLKG NKHDDGTQSD SENAGAHRRC SKRATLEEHL RRHHSEHKKL QKVQATEKHQ
DQAVTSSAHH RGGHGVPHGK LLKQKSEEPS VSIPFLQTAL LRSSGSLGHR PSQEMDKMLK
NQATSATSEK DNDDDQSDKG TYTIELENPN SEEVEARKMI DKVFGVDDNQ DYNRPVINEK
HKDLIKDWAL SSAAAVMEER KPLTTSGFHH SEEGTSSSGS KRWVSQWASL AANHTRHDQE
ERIMEFSAPL PLENETEISE SGMTVRSTGS ATSLASQGER RRRTLPQLPN EEKSLESHRA
KVVTQRSEIG EKQDTELQEK ETPTQVYQKD KQDADRPLSK MNRAVNGETL KTGGDNKTLL
HLGSSAPGKE KSETDKETSL VKQTLAKLQQ QEQREEAQWT PTKLSSKNVS GQTDKCREET
FKQESQPPEK NSGHSTSKGD RVAQSESKRR KAEEILKSQT PKGGDKKESS KSLVRQGSFT
IEKPSPNIPI ELIPHINKQT SSTPSSLALT SASRIRERSE SLDPDSSMDT TLILKDTEAV
MAFLEAKLRE DNKTDEGPDT PSYNRDNSIS PESDVDTAST ISLVTGETER KSTQKRKSFT
SLYKDRCSTG SPSKDVTKSS SSGAREKMEK KTKSRSTDVG SRADGRKFVQ SSGRIRQPSV
DLTDDDQTSS VPHSAISDIM SSDQETYSCK PHGRTPLTSA DEHVHSKLEG SKVTKSKTSP
VVSGSSSKST TLPRPRPTRT SLLRRARLGE ASDSELADAD KASVASEVST TSSTSKPPTG
RRNISRIDLL AQPRRTRLGS LSARSDSEAT ISRSSASSRT AEAIIRSGAR LVPSDKFSPR
IRANSISRLS DSKVKSMTSA HGSASVNSRW RRFPTDYAST SEDEFGSNRN SPKHTRLRTS
PALKTTRLQS AGSAMPTSSS FKHRIKEQED YIRDWTAHRE EIARISQDLA LIAREINDVA
GEIDSVTSSG TAPSTTVSTA ATTPGSAIDT REELVDRVFD ESLNFRKIPP LVHSKTPEGN
NGRSGDPRPQ AAEPPDHLTI TRRRTWSRDE VMGDNLLLSS VFQFSKKIRQ SIDKTAGKIR
ILFKDKDRNW DDIESKLRAE SEVPIVKTSS MEISSILQEL KRVEKQLQAI NAMIDPDGTL
EALNNMGFPS AMLPSPPKQK SSPVNNHHSP GQTPTLGQPE ARALHPAAVS AAAEFENAES
EADFSIHFNR FNPDGEEEDV TVQE
