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 27-MAR-2024, entry version 200. 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="https://atlasgeneticsoncology.org/gene/280/H4"; 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; 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; 187. DR IntAct; Q16204; 77. DR MINT; Q16204; -. DR STRING; 9606.ENSP00000263102; -. DR BindingDB; Q16204; -. DR GlyCosmos; Q16204; 3 sites, 1 glycan. DR GlyGen; Q16204; 4 sites, 1 O-linked glycan (4 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; 9606-ENSP00000263102; -. DR PeptideAtlas; Q16204; -. DR ProteomicsDB; 60837; -. DR Pumba; Q16204; -. DR Antibodypedia; 14268; 249 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 AGR; HGNC:18782; -. 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; KMQQFAQ; -. DR OrthoDB; 2910065at2759; -. DR PhylomeDB; Q16204; -. DR TreeFam; TF321211; -. DR PathwayCommons; Q16204; -. DR SignaLink; Q16204; -. DR SIGNOR; Q16204; -. DR BioGRID-ORCS; 8030; 79 hits in 1162 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 201 other cell types or tissues. 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:SF0; COILED-COIL DOMAIN-CONTAINING PROTEIN 6; 1. DR PANTHER; PTHR15276; H4 D10S170 PROTEIN-RELATED; 1. DR Pfam; PF09755; DUF2046; 1. DR Genevisible; Q16204; HS. 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 //