CC120_HUMAN
ID CC120_HUMAN Reviewed; 630 AA.
AC Q96HB5; A8K5Q5; B4DF24; B4DFC1; B4DTU2; F5GZU4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Coiled-coil domain-containing protein 120;
GN Name=CCDC120; ORFNames=JM11;
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).
RA Rolfs A., Kelley F., McCarron S., Jepson D., Shen B., Shi Z., Hu Y.,
RA Taycher E., Zuo D., Ebert L., Hoerlein A., Ernst U., Korn B., LaBaer J.;
RT "Cloning of human full-length CDS FLEXGene in Gateway(TM) recombinational
RT vector system.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC TISSUE=Cerebellum, Fetal brain, and Placenta;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Choriocarcinoma;
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 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION, INTERACTION WITH CYTH2, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=25326380; DOI=10.1074/jbc.m114.575787;
RA Torii T., Miyamoto Y., Tago K., Sango K., Nakamura K., Sanbe A., Tanoue A.,
RA Yamauchi J.;
RT "Arf6 guanine nucleotide exchange factor cytohesin-2 binds to CCDC120 and
RT is transported along neurites to mediate neurite growth.";
RL J. Biol. Chem. 289:33887-33903(2014).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NIN AND CEP170.
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).
CC -!- FUNCTION: Centriolar protein required for centriole subdistal appendage
CC assembly and microtubule anchoring in interphase cells
CC (PubMed:28422092). Together with CCDC68, cooperate with subdistal
CC appendage components ODF2, NIN and CEP170 for hierarchical subdistal
CC appendage assembly (PubMed:28422092). Recruits NIN and CEP170 to
CC centrosomes (PubMed:28422092). Also required for neurite growth.
CC Localizes CYTH2 to vesicles to allow its transport along neurites, and
CC subsequent ARF6 activation and neurite growth.
CC {ECO:0000269|PubMed:25326380}.
CC -!- SUBUNIT: Interacts with NIN and CEP170; leading to recruit them to
CC centrosomes (PubMed:28422092). Directly interacts with CYTH2; this
CC interaction stabilizes CCDC120, possibly by preventing ubiquitination.
CC {ECO:0000269|PubMed:25326380, ECO:0000269|PubMed:28422092}.
CC -!- INTERACTION:
CC Q96HB5; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-744556, EBI-357530;
CC Q96HB5; Q03989: ARID5A; NbExp=3; IntAct=EBI-744556, EBI-948603;
CC Q96HB5; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-744556, EBI-12811889;
CC Q96HB5; O75934: BCAS2; NbExp=3; IntAct=EBI-744556, EBI-1050106;
CC Q96HB5; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-744556, EBI-11519926;
CC Q96HB5; Q9H2G9: BLZF1; NbExp=5; IntAct=EBI-744556, EBI-2548012;
CC Q96HB5; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-744556, EBI-8643161;
CC Q96HB5; A2RRN7: CADPS; NbExp=3; IntAct=EBI-744556, EBI-10179719;
CC Q96HB5; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-744556, EBI-739580;
CC Q96HB5; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-744556, EBI-11530605;
CC Q96HB5; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-744556, EBI-10171570;
CC Q96HB5; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-744556, EBI-10961312;
CC Q96HB5; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-744556, EBI-10961624;
CC Q96HB5; Q01850: CDR2; NbExp=3; IntAct=EBI-744556, EBI-1181367;
CC Q96HB5; Q5SW79: CEP170; NbExp=12; IntAct=EBI-744556, EBI-1104799;
CC Q96HB5; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-744556, EBI-747776;
CC Q96HB5; P61024: CKS1B; NbExp=3; IntAct=EBI-744556, EBI-456371;
CC Q96HB5; Q9BYD5: CNFN; NbExp=3; IntAct=EBI-744556, EBI-12819063;
CC Q96HB5; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-744556, EBI-3866319;
CC Q96HB5; P56545-3: CTBP2; NbExp=3; IntAct=EBI-744556, EBI-10171902;
CC Q96HB5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-744556, EBI-3867333;
CC Q96HB5; Q15438: CYTH1; NbExp=9; IntAct=EBI-744556, EBI-997830;
CC Q96HB5; Q99418: CYTH2; NbExp=4; IntAct=EBI-744556, EBI-448974;
CC Q96HB5; O43739-2: CYTH3; NbExp=4; IntAct=EBI-744556, EBI-11974015;
CC Q96HB5; Q9UIA0: CYTH4; NbExp=8; IntAct=EBI-744556, EBI-11521003;
CC Q96HB5; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-744556, EBI-2349927;
CC Q96HB5; O00303: EIF3F; NbExp=3; IntAct=EBI-744556, EBI-711990;
CC Q96HB5; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-744556, EBI-11958845;
CC Q96HB5; P22607: FGFR3; NbExp=3; IntAct=EBI-744556, EBI-348399;
CC Q96HB5; P01100: FOS; NbExp=3; IntAct=EBI-744556, EBI-852851;
CC Q96HB5; P15407: FOSL1; NbExp=3; IntAct=EBI-744556, EBI-744510;
CC Q96HB5; A1L4K1: FSD2; NbExp=3; IntAct=EBI-744556, EBI-5661036;
CC Q96HB5; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-744556, EBI-7960826;
CC Q96HB5; P14136: GFAP; NbExp=3; IntAct=EBI-744556, EBI-744302;
CC Q96HB5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-744556, EBI-618309;
CC Q96HB5; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-744556, EBI-5916454;
CC Q96HB5; P31943: HNRNPH1; NbExp=3; IntAct=EBI-744556, EBI-351590;
CC Q96HB5; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-744556, EBI-748420;
CC Q96HB5; P49639: HOXA1; NbExp=5; IntAct=EBI-744556, EBI-740785;
CC Q96HB5; P01112: HRAS; NbExp=3; IntAct=EBI-744556, EBI-350145;
CC Q96HB5; O75031: HSF2BP; NbExp=3; IntAct=EBI-744556, EBI-7116203;
CC Q96HB5; P42858: HTT; NbExp=3; IntAct=EBI-744556, EBI-466029;
CC Q96HB5; Q13099: IFT88; NbExp=3; IntAct=EBI-744556, EBI-347427;
CC Q96HB5; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-744556, EBI-8638439;
CC Q96HB5; Q5TA45: INTS11; NbExp=3; IntAct=EBI-744556, EBI-748258;
CC Q96HB5; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-744556, EBI-749265;
CC Q96HB5; Q15323: KRT31; NbExp=3; IntAct=EBI-744556, EBI-948001;
CC Q96HB5; O76011: KRT34; NbExp=3; IntAct=EBI-744556, EBI-1047093;
CC Q96HB5; Q92764: KRT35; NbExp=3; IntAct=EBI-744556, EBI-1058674;
CC Q96HB5; O76015: KRT38; NbExp=3; IntAct=EBI-744556, EBI-1047263;
CC Q96HB5; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-744556, EBI-10241252;
CC Q96HB5; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-744556, EBI-12811111;
CC Q96HB5; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-744556, EBI-12111050;
CC Q96HB5; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-744556, EBI-11962084;
CC Q96HB5; Q03252: LMNB2; NbExp=3; IntAct=EBI-744556, EBI-2830427;
CC Q96HB5; P61968: LMO4; NbExp=3; IntAct=EBI-744556, EBI-2798728;
CC Q96HB5; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-744556, EBI-1216080;
CC Q96HB5; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-744556, EBI-716006;
CC Q96HB5; Q9P086: MED11; NbExp=3; IntAct=EBI-744556, EBI-394704;
CC Q96HB5; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-744556, EBI-8487781;
CC Q96HB5; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-744556, EBI-10172526;
CC Q96HB5; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-744556, EBI-2801965;
CC Q96HB5; Q8TD10: MIPOL1; NbExp=6; IntAct=EBI-744556, EBI-2548751;
CC Q96HB5; Q13064: MKRN3; NbExp=3; IntAct=EBI-744556, EBI-2340269;
CC Q96HB5; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-744556, EBI-720441;
CC Q96HB5; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-744556, EBI-11522433;
CC Q96HB5; P15173: MYOG; NbExp=3; IntAct=EBI-744556, EBI-3906629;
CC Q96HB5; O43639: NCK2; NbExp=3; IntAct=EBI-744556, EBI-713635;
CC Q96HB5; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-744556, EBI-11750983;
CC Q96HB5; Q8N4C6: NIN; NbExp=11; IntAct=EBI-744556, EBI-1164022;
CC Q96HB5; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-744556, EBI-17490746;
CC Q96HB5; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-744556, EBI-398874;
CC Q96HB5; Q5BJF6: ODF2; NbExp=5; IntAct=EBI-744556, EBI-8744243;
CC Q96HB5; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-744556, EBI-11022007;
CC Q96HB5; P16284: PECAM1; NbExp=3; IntAct=EBI-744556, EBI-716404;
CC Q96HB5; Q99959-2: PKP2; NbExp=3; IntAct=EBI-744556, EBI-10987518;
CC Q96HB5; O15496: PLA2G10; NbExp=3; IntAct=EBI-744556, EBI-726466;
CC Q96HB5; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-744556, EBI-2876622;
CC Q96HB5; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-744556, EBI-949255;
CC Q96HB5; Q16633: POU2AF1; NbExp=3; IntAct=EBI-744556, EBI-943588;
CC Q96HB5; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-744556, EBI-11320284;
CC Q96HB5; P41219: PRPH; NbExp=3; IntAct=EBI-744556, EBI-752074;
CC Q96HB5; P20339: RAB5A; NbExp=3; IntAct=EBI-744556, EBI-399437;
CC Q96HB5; Q15276: RABEP1; NbExp=3; IntAct=EBI-744556, EBI-447043;
CC Q96HB5; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-744556, EBI-740343;
CC Q96HB5; Q9P2R6: RERE; NbExp=3; IntAct=EBI-744556, EBI-948076;
CC Q96HB5; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-744556, EBI-726876;
CC Q96HB5; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-744556, EBI-6257312;
CC Q96HB5; O60504: SORBS3; NbExp=3; IntAct=EBI-744556, EBI-741237;
CC Q96HB5; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-744556, EBI-11959123;
CC Q96HB5; O75558: STX11; NbExp=3; IntAct=EBI-744556, EBI-714135;
CC Q96HB5; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-744556, EBI-1105213;
CC Q96HB5; Q08117-2: TLE5; NbExp=6; IntAct=EBI-744556, EBI-11741437;
CC Q96HB5; Q12888: TP53BP1; NbExp=3; IntAct=EBI-744556, EBI-396540;
CC Q96HB5; Q13077: TRAF1; NbExp=3; IntAct=EBI-744556, EBI-359224;
CC Q96HB5; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-744556, EBI-5235829;
CC Q96HB5; Q15654: TRIP6; NbExp=3; IntAct=EBI-744556, EBI-742327;
CC Q96HB5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-744556, EBI-12806590;
CC Q96HB5; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-744556, EBI-10241197;
CC Q96HB5; P08670: VIM; NbExp=3; IntAct=EBI-744556, EBI-353844;
CC Q96HB5; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-744556, EBI-11962760;
CC Q96HB5; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-744556, EBI-7850213;
CC Q96HB5; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-744556, EBI-740727;
CC Q96HB5; Q5T619: ZNF648; NbExp=3; IntAct=EBI-744556, EBI-11985915;
CC Q96HB5; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-744556, EBI-527853;
CC Q96HB5; Q9Y649; NbExp=3; IntAct=EBI-744556, EBI-25900580;
CC Q96HB5-4; Q68D86: CCDC102B; NbExp=4; IntAct=EBI-10185348, EBI-10171570;
CC Q96HB5-4; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-10185348, EBI-2808286;
CC Q96HB5-4; Q96L14: CEP170P1; NbExp=4; IntAct=EBI-10185348, EBI-743488;
CC Q96HB5-4; Q99418: CYTH2; NbExp=4; IntAct=EBI-10185348, EBI-448974;
CC Q96HB5-4; O43739: CYTH3; NbExp=3; IntAct=EBI-10185348, EBI-741648;
CC Q96HB5-4; Q5JST6: EFHC2; NbExp=4; IntAct=EBI-10185348, EBI-2349927;
CC Q96HB5-4; Q15323: KRT31; NbExp=4; IntAct=EBI-10185348, EBI-948001;
CC Q96HB5-4; Q6A162: KRT40; NbExp=4; IntAct=EBI-10185348, EBI-10171697;
CC Q96HB5-4; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-10185348, EBI-10172526;
CC Q96HB5-4; Q13077: TRAF1; NbExp=4; IntAct=EBI-10185348, EBI-359224;
CC Q96HB5-4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10185348, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:28422092}. Cytoplasm
CC {ECO:0000269|PubMed:25326380}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:25326380}. Cell projection, growth cone
CC {ECO:0000269|PubMed:25326380}. Endosome {ECO:0000269|PubMed:25326380}.
CC Note=Localizes to the subdistal appendages of mother centrioles and
CC proximal ends of both centrioles in interphase cells (PubMed:28422092).
CC Recruited to subdistal appendages by ODF2 (PubMed:28422092). In
CC differentiating neuroblastoma cells, colocalizes with CYTH2 in both
CC neurite shaft and growth cone areas (PubMed:25326380). Partially
CC colocalizes with endosomes along neurites in differentiating
CC neuroblastoma cells (PubMed:25326380). {ECO:0000269|PubMed:25326380,
CC ECO:0000269|PubMed:28422092}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96HB5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HB5-2; Sequence=VSP_042859;
CC Name=3;
CC IsoId=Q96HB5-3; Sequence=VSP_047104;
CC Name=4;
CC IsoId=Q96HB5-4; Sequence=VSP_054527, VSP_047104;
CC Name=5;
CC IsoId=Q96HB5-5; Sequence=VSP_042859, VSP_047104;
CC -!- PTM: Ubiquitinated; interaction with CYTH2 may prevent ubiquitination.
CC {ECO:0000269|PubMed:25326380}.
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DR EMBL; DQ896186; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK293898; BAG57285.1; -; mRNA.
DR EMBL; AK294024; BAG57382.1; -; mRNA.
DR EMBL; AK291370; BAF84059.1; -; mRNA.
DR EMBL; AK300366; BAG62104.1; -; mRNA.
DR EMBL; AK315837; BAF98728.1; -; mRNA.
DR EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50708.1; -; Genomic_DNA.
DR EMBL; BC008769; AAH08769.1; -; mRNA.
DR CCDS; CCDS14316.1; -. [Q96HB5-1]
DR CCDS; CCDS55413.1; -. [Q96HB5-2]
DR CCDS; CCDS55414.2; -. [Q96HB5-4]
DR RefSeq; NP_001156793.2; NM_001163321.2. [Q96HB5-4]
DR RefSeq; NP_001156794.1; NM_001163322.2. [Q96HB5-5]
DR RefSeq; NP_001156795.1; NM_001163323.2. [Q96HB5-2]
DR RefSeq; NP_001258764.1; NM_001271835.1. [Q96HB5-1]
DR RefSeq; NP_001258765.1; NM_001271836.1. [Q96HB5-1]
DR RefSeq; NP_296375.1; NM_033626.3. [Q96HB5-1]
DR AlphaFoldDB; Q96HB5; -.
DR SMR; Q96HB5; -.
DR BioGRID; 124658; 169.
DR IntAct; Q96HB5; 161.
DR MINT; Q96HB5; -.
DR STRING; 9606.ENSP00000474071; -.
DR iPTMnet; Q96HB5; -.
DR PhosphoSitePlus; Q96HB5; -.
DR BioMuta; CCDC120; -.
DR DMDM; 74731908; -.
DR EPD; Q96HB5; -.
DR jPOST; Q96HB5; -.
DR MassIVE; Q96HB5; -.
DR MaxQB; Q96HB5; -.
DR PaxDb; Q96HB5; -.
DR PeptideAtlas; Q96HB5; -.
DR PRIDE; Q96HB5; -.
DR ProteomicsDB; 25131; -.
DR ProteomicsDB; 76728; -. [Q96HB5-1]
DR ProteomicsDB; 76729; -. [Q96HB5-2]
DR Antibodypedia; 347; 118 antibodies from 21 providers.
DR DNASU; 90060; -.
DR Ensembl; ENST00000496529.6; ENSP00000474761.1; ENSG00000147144.13. [Q96HB5-1]
DR Ensembl; ENST00000536628.3; ENSP00000443351.1; ENSG00000147144.13. [Q96HB5-2]
DR Ensembl; ENST00000597275.5; ENSP00000470294.1; ENSG00000147144.13. [Q96HB5-1]
DR Ensembl; ENST00000603986.6; ENSP00000474071.1; ENSG00000147144.13. [Q96HB5-4]
DR Ensembl; ENST00000606812.5; ENSP00000475676.1; ENSG00000147144.13. [Q96HB5-1]
DR GeneID; 90060; -.
DR KEGG; hsa:90060; -.
DR MANE-Select; ENST00000603986.6; ENSP00000474071.1; NM_001163321.4; NP_001156793.2. [Q96HB5-4]
DR UCSC; uc064zdh.1; human. [Q96HB5-1]
DR CTD; 90060; -.
DR GeneCards; CCDC120; -.
DR HGNC; HGNC:28910; CCDC120.
DR HPA; ENSG00000147144; Tissue enhanced (esophagus, skin).
DR MIM; 300947; gene.
DR neXtProt; NX_Q96HB5; -.
DR OpenTargets; ENSG00000147144; -.
DR PharmGKB; PA145149329; -.
DR VEuPathDB; HostDB:ENSG00000147144; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00940000154102; -.
DR HOGENOM; CLU_029533_0_0_1; -.
DR InParanoid; Q96HB5; -.
DR OMA; PDVQGCQ; -.
DR OrthoDB; 595503at2759; -.
DR PhylomeDB; Q96HB5; -.
DR TreeFam; TF328984; -.
DR PathwayCommons; Q96HB5; -.
DR SignaLink; Q96HB5; -.
DR BioGRID-ORCS; 90060; 5 hits in 711 CRISPR screens.
DR ChiTaRS; CCDC120; human.
DR GenomeRNAi; 90060; -.
DR Pharos; Q96HB5; Tbio.
DR PRO; PR:Q96HB5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96HB5; protein.
DR Bgee; ENSG00000147144; Expressed in lower esophagus mucosa and 97 other tissues.
DR ExpressionAtlas; Q96HB5; baseline and differential.
DR Genevisible; Q96HB5; HS.
DR GO; GO:0120103; C:centriolar subdistal appendage; IDA:GO_Central.
DR GO; GO:0005814; C:centriole; IDA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:GO_Central.
DR InterPro; IPR039108; CCDC120.
DR InterPro; IPR043447; CCDC120/INAVA.
DR InterPro; IPR021774; DUF3338.
DR PANTHER; PTHR16093; PTHR16093; 1.
DR PANTHER; PTHR16093:SF5; PTHR16093:SF5; 1.
DR Pfam; PF11819; CUPID; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Endosome; Methylation; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..630
FT /note="Coiled-coil domain-containing protein 120"
FT /id="PRO_0000254141"
FT REGION 31..70
FT /note="Involved in CYTH2-binding"
FT /evidence="ECO:0000269|PubMed:25326380"
FT REGION 212..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..173
FT /evidence="ECO:0000255"
FT COMPBIAS 278..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 435
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:A2AEV7"
FT VAR_SEQ 1
FT /note="M -> MRREPRYQGQVGPDIHTDSERTLSSHQPRPLDSTKM (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054527"
FT VAR_SEQ 5..16
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042859"
FT VAR_SEQ 626..630
FT /note="GGCFY -> YADFLYPPELSARLSDLTLEGEQSSSSDTQTPGTLV (in
FT isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047104"
SQ SEQUENCE 630 AA; 67567 MW; E652C8AFD738BF6E CRC64;
MEVKGQLISS PTFNAPAALF GEAAPQVKSE RLRGLLDRQR TLQEALSLKL QELRKVCLQE
AELTGQLPPE CPLEPGERPQ LVRRRPPTAR AYPPPHPNQA HHSLCPAEEL ALEALEREVS
VQQQIAAAAR RLALAPDLST EQRRRRRQVQ ADALRRLHEL EEQLRDVRAR LGLPVLPLPQ
PLPLSTGSVI TTQGVCLGMR LAQLSQEDVV LHSESSSLSE SGASHDNEEP HGCFSLAERP
SPPKAWDQLR AVSGGSPERR TPWKPPPSDL YGDLKSRRNS VASPTSPTRS LPRSASSFEG
RSVPATPVLT RGAGPQLCKP EGLHSRQWSG SQDSQMGFPR ADPASDRASL FVARTRRSNS
SEALLVDRAA GGGAGSPPAP LAPSASGPPV CKSSEVLYER PQPTPAFSSR TAGPPDPPRA
ARPSSAAPAS RGAPRLPPVC GDFLLDYSLD RGLPRSGGGT GWGELPPAAE VPGPLSRRDG
LLTMLPGPPP VYAADSNSPL LRTKDPHTRA TRTKPCGLPP EAAEGPEVHP NPLLWMPPPT
RIPSAGERSG HKNLALEGLR DWYIRNSGLA AGPQRRPVLP SVGPPHPPFL HARCYEVGQA
LYGAPSQAPL PHSRSFTAPP VSGRYGGCFY
