CCDC6_HUMAN
ID CCDC6_HUMAN Reviewed; 474 AA.
AC Q16204; Q15250; Q6GSG7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Coiled-coil domain-containing protein 6;
DE AltName: Full=Papillary thyroid carcinoma-encoded protein;
DE AltName: Full=Protein H4;
GN Name=CCDC6; Synonyms=D10S170, TST1;
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], AND VARIANT THR-470.
RC TISSUE=Thyroid;
RX PubMed=8058316;
RA Grieco M., Cerrato A., Santoro M., Fusco A., Melillo R.M., Vecchio G.;
RT "Cloning and characterization of H4 (D10S170), a gene involved in RET
RT rearrangements in vivo.";
RL Oncogene 9:2531-2535(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-470.
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-470.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-470.
RC TISSUE=Blood, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-101, AND CHROMOSOMAL TRANSLOCATION WITH
RP RET.
RC TISSUE=Thyroid papillary carcinoma;
RX PubMed=2406025; DOI=10.1016/0092-8674(90)90659-3;
RA Grieco M., Santoro M., Berlingieri M.T., Melillo R.M., Donghi R.,
RA Bongarzone I., Pierotti M.A., Della Porta G., Fusco A., Vecchio G.;
RT "PTC is a novel rearranged form of the ret proto-oncogene and is frequently
RT detected in vivo in human thyroid papillary carcinomas.";
RL Cell 60:557-563(1990).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-244, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-244, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-240 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-349; SER-363 AND
RP SER-367, 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-240; SER-244; SER-254
RP AND SER-367, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-240; SER-244;
RP SER-249; SER-254; SER-284 AND SER-323, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-244 AND SER-323, AND
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-240; SER-244;
RP SER-254; SER-323; SER-395 AND SER-413, AND IDENTIFICATION BY MASS
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- INTERACTION:
CC Q16204; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-1045350, EBI-5661893;
CC Q16204; Q9Y2D1: ATF5; NbExp=3; IntAct=EBI-1045350, EBI-492509;
CC Q16204; Q16204: CCDC6; NbExp=3; IntAct=EBI-1045350, EBI-1045350;
CC Q16204; Q7L2Z9: CENPQ; NbExp=3; IntAct=EBI-1045350, EBI-2350265;
CC Q16204; Q9UIA0: CYTH4; NbExp=3; IntAct=EBI-1045350, EBI-11521003;
CC Q16204; Q969H0: FBXW7; NbExp=9; IntAct=EBI-1045350, EBI-359574;
CC Q16204; O95995: GAS8; NbExp=3; IntAct=EBI-1045350, EBI-1052570;
CC Q16204; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-1045350, EBI-740641;
CC Q16204; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-1045350, EBI-12039345;
CC Q16204; Q6UWE0: LRSAM1; NbExp=3; IntAct=EBI-1045350, EBI-720984;
CC Q16204; Q9P127: LUZP4; NbExp=3; IntAct=EBI-1045350, EBI-10198848;
CC Q16204; Q13164: MAPK7; NbExp=3; IntAct=EBI-1045350, EBI-1213983;
CC Q16204; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1045350, EBI-16439278;
CC Q16204; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-1045350, EBI-11522433;
CC Q16204; P26367: PAX6; NbExp=3; IntAct=EBI-1045350, EBI-747278;
CC Q16204; Q13526: PIN1; NbExp=6; IntAct=EBI-1045350, EBI-714158;
CC Q16204; Q15311: RALBP1; NbExp=7; IntAct=EBI-1045350, EBI-749285;
CC Q16204; Q16533: SNAPC1; NbExp=3; IntAct=EBI-1045350, EBI-11915024;
CC Q16204; O60504: SORBS3; NbExp=3; IntAct=EBI-1045350, EBI-741237;
CC Q16204; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-1045350, EBI-1105213;
CC Q16204; Q14142: TRIM14; NbExp=3; IntAct=EBI-1045350, EBI-2820256;
CC Q16204; P15622-3: ZNF250; NbExp=3; IntAct=EBI-1045350, EBI-10177272;
CC Q16204; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-1045350, EBI-4395669;
CC Q16204; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-1045350, EBI-10251462;
CC Q16204; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-1045350, EBI-5667516;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000305}.
CC Note=May be a cytoskeletal protein.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: The protein has mostly an alpha helical conformation similar to
CC myosin heavy-chain tail that might adopt a coiled-coil conformation.
CC -!- DISEASE: Note=A chromosomal aberration involving CCDC6 is found in
CC papillary thyroid carcinomas (PTCs). Inversion inv(10)(q11.2;q21)
CC generates the RET/CCDC6 (PTC1) oncogene. {ECO:0000269|PubMed:2406025}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC60637.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/H4ID280.html";
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DR EMBL; S72869; AAC60637.1; ALT_FRAME; mRNA.
DR EMBL; AK292593; BAF85282.1; -; mRNA.
DR EMBL; AC060231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54196.1; -; Genomic_DNA.
DR EMBL; BC036757; AAH36757.2; -; mRNA.
DR EMBL; BC064391; AAH64391.1; -; mRNA.
DR EMBL; M31213; AAA36524.1; ALT_TERM; mRNA.
DR CCDS; CCDS7257.1; -.
DR PIR; I58403; I58403.
DR RefSeq; NP_005427.2; NM_005436.4.
DR AlphaFoldDB; Q16204; -.
DR SMR; Q16204; -.
DR BioGRID; 113725; 139.
DR IntAct; Q16204; 71.
DR MINT; Q16204; -.
DR STRING; 9606.ENSP00000263102; -.
DR BindingDB; Q16204; -.
DR GlyGen; Q16204; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q16204; -.
DR PhosphoSitePlus; Q16204; -.
DR BioMuta; CCDC6; -.
DR DMDM; 292494979; -.
DR EPD; Q16204; -.
DR jPOST; Q16204; -.
DR MassIVE; Q16204; -.
DR MaxQB; Q16204; -.
DR PaxDb; Q16204; -.
DR PeptideAtlas; Q16204; -.
DR PRIDE; Q16204; -.
DR ProteomicsDB; 60837; -.
DR Antibodypedia; 14268; 230 antibodies from 29 providers.
DR DNASU; 8030; -.
DR Ensembl; ENST00000263102.7; ENSP00000263102.6; ENSG00000108091.11.
DR GeneID; 8030; -.
DR KEGG; hsa:8030; -.
DR MANE-Select; ENST00000263102.7; ENSP00000263102.6; NM_005436.5; NP_005427.2.
DR UCSC; uc001jks.5; human.
DR CTD; 8030; -.
DR DisGeNET; 8030; -.
DR GeneCards; CCDC6; -.
DR HGNC; HGNC:18782; CCDC6.
DR HPA; ENSG00000108091; Low tissue specificity.
DR MalaCards; CCDC6; -.
DR MIM; 601985; gene.
DR neXtProt; NX_Q16204; -.
DR OpenTargets; ENSG00000108091; -.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR PharmGKB; PA134904022; -.
DR VEuPathDB; HostDB:ENSG00000108091; -.
DR eggNOG; KOG2129; Eukaryota.
DR GeneTree; ENSGT00390000013594; -.
DR HOGENOM; CLU_033433_2_0_1; -.
DR InParanoid; Q16204; -.
DR OMA; NLSAHIQ; -.
DR OrthoDB; 1142037at2759; -.
DR PhylomeDB; Q16204; -.
DR TreeFam; TF321211; -.
DR PathwayCommons; Q16204; -.
DR SignaLink; Q16204; -.
DR SIGNOR; Q16204; -.
DR BioGRID-ORCS; 8030; 75 hits in 1083 CRISPR screens.
DR ChiTaRS; CCDC6; human.
DR GeneWiki; CCDC6; -.
DR GenomeRNAi; 8030; -.
DR Pharos; Q16204; Tbio.
DR PRO; PR:Q16204; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q16204; protein.
DR Bgee; ENSG00000108091; Expressed in secondary oocyte and 199 other tissues.
DR Genevisible; Q16204; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR InterPro; IPR019152; DUF2046.
DR PANTHER; PTHR15276; PTHR15276; 1.
DR Pfam; PF09755; DUF2046; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosomal rearrangement; Coiled coil; Cytoplasm;
KW Cytoskeleton; Methylation; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repeat; SH3-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..474
FT /note="Coiled-coil domain-containing protein 6"
FT /id="PRO_0000089398"
FT REPEAT 106..134
FT /note="1"
FT REPEAT 135..163
FT /note="2"
FT REPEAT 164..192
FT /note="3"
FT REPEAT 193..206
FT /note="4; approximate"
FT REPEAT 207..235
FT /note="5"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..235
FT /note="5 X 29 AA tandem repeats"
FT REGION 342..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..237
FT /evidence="ECO:0000255"
FT COILED 253..332
FT /evidence="ECO:0000255"
FT MOTIF 442..451
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 101..102
FT /note="Breakpoint for translocation to form RET-CCDC6
FT oncogene"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 387
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:D3YZP9"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 470
FT /note="P -> T (in dbSNP:rs1053266)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8058316,
FT ECO:0000269|Ref.4"
FT /id="VAR_062971"
FT CONFLICT 157
FT /note="A -> G (in Ref. 1; AAC60637)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="K -> T (in Ref. 1; AAC60637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53291 MW; DF055DBF20304D26 CRC64;
MADSASESDT DGAGGNSSSS AAMQSSCSST SGGGGGGGGG GGGGKSGGIV ISPFRLEELT
NRLASLQQEN KVLKIELETY KLKCKALQEE NRDLRKASVT IQARAEQEEE FISNTLFKKI
QALQKEKETL AVNYEKEEEF LTNELSRKLM QLQHEKAELE QHLEQEQEFQ VNKLMKKIKK
LENDTISKQL TLEQLRREKI DLENTLEQEQ EALVNRLWKR MDKLEAEKRI LQEKLDQPVS
APPSPRDISM EIDSPENMMR HIRFLKNEVE RLKKQLRAAQ LQHSEKMAQY LEEERHMREE
NLRLQRKLQR EMERREALCR QLSESESSLE MDDERYFNEM SAQGLRPRTV SSPIPYTPSP
SSSRPISPGL SYASHTVGFT PPTSLTRAGM SYYNSPGLHV QHMGTSHGIT RPSPRRSNSP
DKFKRPTPPP SPNTQTPVQP PPPPPPPPMQ PTVPSAATSQ PTPSQHSAHP SSQP
