COIL_HUMAN
ID COIL_HUMAN Reviewed; 576 AA.
AC P38432; B2R931;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Coilin;
DE AltName: Full=p80-coilin;
GN Name=COIL; Synonyms=CLN80;
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].
RC TISSUE=Liver;
RX PubMed=7971277; DOI=10.1093/nar/22.21.4462;
RA Chan E.K.L., Takano S., Andrade L.E.C., Hamel J.C., Matera A.G.;
RT "Structure, expression and chromosomal localization of human p80-coilin
RT gene.";
RL Nucleic Acids Res. 22:4462-4469(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 172-576.
RC TISSUE=Liver;
RX PubMed=2033369; DOI=10.1084/jem.173.6.1407;
RA Andrade L.E.C., Chan E.K.L., Raska I., Peebles C.L., Roos G., Tan E.M.;
RT "Human autoantibody to a novel protein of the nuclear coiled body:
RT immunological characterization and cDNA cloning of p80-coilin.";
RL J. Exp. Med. 173:1407-1419(1991).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=7679389; DOI=10.1083/jcb.120.4.841;
RA Carmo-Fonseca M., Ferreira J., Lamond A.I.;
RT "Assembly of snRNP-containing coiled bodies is regulated in interphase and
RT mitosis -- evidence that the coiled body is a kinetic nuclear structure.";
RL J. Cell Biol. 120:841-852(1993).
RN [8]
RP INTERACTION WITH SMN, AND MUTAGENESIS OF 413-ARG--ARG-419.
RX PubMed=11641277; DOI=10.1101/gad.908401;
RA Hebert M.D., Szymczyk P.W., Shpargel K.B., Matera A.G.;
RT "Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular
RT atrophy protein.";
RL Genes Dev. 15:2720-2729(2001).
RN [9]
RP METHYLATION OF RG REPEATS.
RX PubMed=12361597; DOI=10.1016/s1534-5807(02)00222-8;
RA Hebert M.D., Shpargel K.B., Ospina J.K., Tucker K.E., Matera A.G.;
RT "Coilin methylation regulates nuclear body formation.";
RL Dev. Cell 3:329-337(2002).
RN [10]
RP INTERACTION WITH ANKS1B.
RX PubMed=15862129; DOI=10.1186/1471-2121-6-23;
RA Xu H., Hebert M.D.;
RT "A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body
RT protein coilin.";
RL BMC Cell Biol. 6:23-23(2005).
RN [11]
RP INTERACTION WITH AK6.
RX PubMed=16079131; DOI=10.1074/jbc.m501982200;
RA Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K., Lamond A.I.;
RT "Characterization of hCINAP, a novel coilin-interacting protein encoded by
RT a transcript from the transcription factor TAFIID32 locus.";
RL J. Biol. Chem. 280:36429-36441(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122 AND SER-489, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-290; SER-301;
RP THR-303 AND SER-489, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [15]
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 [16]
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 [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH WRAP53.
RX PubMed=21072240; DOI=10.1371/journal.pbio.1000521;
RA Mahmoudi S., Henriksson S., Weibrecht I., Smith S., Soederberg O.,
RA Stroemblad S., Wiman K.G., Farnebo M.;
RT "WRAP53 is essential for Cajal body formation and for targeting the
RT survival of motor neuron complex to Cajal bodies.";
RL PLoS Biol. 8:E1000521-E1000521(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-122; SER-271;
RP SER-272; THR-456; SER-489 AND SER-566, 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 [19]
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 [20]
RP PHOSPHORYLATION AT SER-184 BY VRK1 AND VRK2.
RX PubMed=21920476; DOI=10.1016/j.jprot.2011.08.019;
RA Sanz-Garcia M., Vazquez-Cedeira M., Kellerman E., Renbaum P.,
RA Levy-Lahad E., Lazo P.A.;
RT "Substrate profiling of human vaccinia-related kinases identifies coilin, a
RT Cajal body nuclear protein, as a phosphorylation target with neurological
RT implications.";
RL J. Proteomics 75:548-560(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-271 AND SER-566, 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 [22]
RP SUBCELLULAR LOCATION.
RX PubMed=22547674; DOI=10.1128/mcb.00379-12;
RA Stern J.L., Zyner K.G., Pickett H.A., Cohen S.B., Bryan T.M.;
RT "Telomerase recruitment requires both TCAB1 and Cajal bodies
RT independently.";
RL Mol. Cell. Biol. 32:2384-2395(2012).
RN [23]
RP INTERACTION WITH HMBOX1.
RX PubMed=23685356; DOI=10.1038/emboj.2013.105;
RA Kappei D., Butter F., Benda C., Scheibe M., Draskovic I., Stevense M.,
RA Novo C.L., Basquin C., Araki M., Araki K., Krastev D.B., Kittler R.,
RA Jessberger R., Londono-Vallejo J.A., Mann M., Buchholz F.;
RT "HOT1 is a mammalian direct telomere repeat-binding protein contributing to
RT telomerase recruitment.";
RL EMBO J. 32:1681-1701(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-271; SER-301;
RP THR-303; SER-403; THR-456; SER-487; SER-489 AND SER-566, AND IDENTIFICATION
RP 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP 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).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127; LYS-204 AND LYS-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127; LYS-151; LYS-160; LYS-204;
RP LYS-209; LYS-274; LYS-281; LYS-293; LYS-297; LYS-444 AND LYS-496, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [28]
RP INTERACTION WITH PSME3.
RX PubMed=29934401; DOI=10.1073/pnas.1722299115;
RA Jonik-Nowak B., Menneteau T., Fesquet D., Baldin V., Bonne-Andrea C.,
RA Mechali F., Fabre B., Boisguerin P., de Rossi S., Henriquet C.,
RA Pugniere M., Ducoux-Petit M., Burlet-Schiltz O., Lamond A.I., Fort P.,
RA Boulon S., Bousquet M.P., Coux O.;
RT "PIP30/FAM192A is a novel regulator of the nuclear proteasome activator
RT PA28gamma.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E6477-E6486(2018).
RN [29]
RP STRUCTURE BY NMR OF 460-576, AND DOMAIN TUDOR.
RX PubMed=20875822; DOI=10.1016/j.febslet.2010.09.034;
RA Shanbhag R., Kurabi A., Kwan J.J., Donaldson L.W.;
RT "Solution structure of the carboxy-terminal Tudor domain from human
RT Coilin.";
RL FEBS Lett. 584:4351-4356(2010).
CC -!- FUNCTION: Component of nuclear coiled bodies, also known as Cajal
CC bodies or CBs, which are involved in the modification and assembly of
CC nucleoplasmic snRNPs. {ECO:0000269|PubMed:7679389}.
CC -!- SUBUNIT: Interacts with ANKS1B (PubMed:15862129). Interacts with SMN1
CC (via Tudor domain) (PubMed:11641277). Interacts (via C-terminus) with
CC AK6 (PubMed:16079131). Interacts with WRAP53/TCAB1 (PubMed:21072240).
CC Interacts with HMBOX1 (PubMed:23685356). Interacts with PSME3; the
CC interaction is inhibited by PSME3IP1 (PubMed:29934401).
CC {ECO:0000269|PubMed:11641277, ECO:0000269|PubMed:15862129,
CC ECO:0000269|PubMed:16079131, ECO:0000269|PubMed:21072240,
CC ECO:0000269|PubMed:23685356, ECO:0000269|PubMed:29934401}.
CC -!- INTERACTION:
CC P38432; P58397-3: ADAMTS12; NbExp=3; IntAct=EBI-945751, EBI-12048761;
CC P38432; Q9Y3D8: AK6; NbExp=5; IntAct=EBI-945751, EBI-2896123;
CC P38432; Q7Z6G8-1: ANKS1B; NbExp=3; IntAct=EBI-945751, EBI-20771343;
CC P38432; Q7Z6G8-2: ANKS1B; NbExp=3; IntAct=EBI-945751, EBI-20771303;
CC P38432; Q9P291: ARMCX1; NbExp=3; IntAct=EBI-945751, EBI-2843626;
CC P38432; P54253: ATXN1; NbExp=9; IntAct=EBI-945751, EBI-930964;
CC P38432; P54253-1: ATXN1; NbExp=6; IntAct=EBI-945751, EBI-930975;
CC P38432; Q13895: BYSL; NbExp=11; IntAct=EBI-945751, EBI-358049;
CC P38432; Q96LT7: C9orf72; NbExp=3; IntAct=EBI-945751, EBI-2961725;
CC P38432; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-945751, EBI-10961624;
CC P38432; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-945751, EBI-396137;
CC P38432; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-945751, EBI-739624;
CC P38432; P38432: COIL; NbExp=3; IntAct=EBI-945751, EBI-945751;
CC P38432; Q9Y295: DRG1; NbExp=3; IntAct=EBI-945751, EBI-719554;
CC P38432; Q96EX3: DYNC2I2; NbExp=3; IntAct=EBI-945751, EBI-2556091;
CC P38432; P61328: FGF12; NbExp=3; IntAct=EBI-945751, EBI-6657662;
CC P38432; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-945751, EBI-14103818;
CC P38432; O75031: HSF2BP; NbExp=3; IntAct=EBI-945751, EBI-7116203;
CC P38432; O60341: KDM1A; NbExp=3; IntAct=EBI-945751, EBI-710124;
CC P38432; Q8TBB1: LNX1; NbExp=2; IntAct=EBI-945751, EBI-739832;
CC P38432; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-945751, EBI-348259;
CC P38432; P55081: MFAP1; NbExp=3; IntAct=EBI-945751, EBI-1048159;
CC P38432; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-945751, EBI-725252;
CC P38432; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-945751, EBI-3920396;
CC P38432; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-945751, EBI-741158;
CC P38432; Q08499: PDE4D; NbExp=3; IntAct=EBI-945751, EBI-1642831;
CC P38432; Q08499-8: PDE4D; NbExp=3; IntAct=EBI-945751, EBI-9090666;
CC P38432; Q96HC4: PDLIM5; NbExp=4; IntAct=EBI-945751, EBI-751267;
CC P38432; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-945751, EBI-79165;
CC P38432; O60568: PLOD3; NbExp=3; IntAct=EBI-945751, EBI-741582;
CC P38432; P62875: POLR2L; NbExp=3; IntAct=EBI-945751, EBI-359527;
CC P38432; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-945751, EBI-5452779;
CC P38432; P61289: PSME3; NbExp=6; IntAct=EBI-945751, EBI-355546;
CC P38432; Q03393: PTS; NbExp=3; IntAct=EBI-945751, EBI-712344;
CC P38432; Q16637: SMN2; NbExp=4; IntAct=EBI-945751, EBI-395421;
CC P38432; P62306: SNRPF; NbExp=6; IntAct=EBI-945751, EBI-356900;
CC P38432; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-945751, EBI-12023934;
CC P38432; P78362: SRPK2; NbExp=3; IntAct=EBI-945751, EBI-593303;
CC P38432; Q99986: VRK1; NbExp=9; IntAct=EBI-945751, EBI-1769146;
CC P38432; Q9BUR4: WRAP53; NbExp=4; IntAct=EBI-945751, EBI-2563542;
CC P38432; P13010: XRCC5; NbExp=6; IntAct=EBI-945751, EBI-357997;
CC P38432; P12956: XRCC6; NbExp=3; IntAct=EBI-945751, EBI-353208;
CC P38432; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-945751, EBI-597063;
CC P38432; G5E9M4: ZNF277; NbExp=3; IntAct=EBI-945751, EBI-11995620;
CC P38432; Q8WWA6: ZNF277; NbExp=3; IntAct=EBI-945751, EBI-10192794;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7679389}. Nucleus,
CC Cajal body {ECO:0000269|PubMed:16079131, ECO:0000269|PubMed:22547674,
CC ECO:0000269|PubMed:7679389}.
CC -!- TISSUE SPECIFICITY: Found in all the cell types examined.
CC -!- DOMAIN: The atypical Tudor domain at the C-terminus contains two large
CC unstructured loops, and does not bind methylated residues.
CC {ECO:0000269|PubMed:20875822}.
CC -!- PTM: Symmetrical dimethylation of arginine residues within the RG
CC repeat region enhances affinity for SMN, and thus localization of SMN
CC complexes to CBs.
CC -!- PTM: Phosphorylation during mitosis is associated with disassembly of
CC CBs. {ECO:0000269|PubMed:21920476, ECO:0000269|PubMed:7679389}.
CC -!- SIMILARITY: Belongs to the coilin family. {ECO:0000305}.
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DR EMBL; M58411; AAA36412.1; -; mRNA.
DR EMBL; AK313616; BAG36378.1; -; mRNA.
DR EMBL; AC004584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94522.1; -; Genomic_DNA.
DR EMBL; BC010385; AAH10385.1; -; mRNA.
DR EMBL; U06632; AAB81550.1; -; mRNA.
DR CCDS; CCDS11592.1; -.
DR PIR; S50113; S50113.
DR RefSeq; NP_004636.1; NM_004645.2.
DR AlphaFoldDB; P38432; -.
DR BMRB; P38432; -.
DR BioGRID; 113815; 545.
DR CORUM; P38432; -.
DR DIP; DIP-38503N; -.
DR IntAct; P38432; 110.
DR MINT; P38432; -.
DR STRING; 9606.ENSP00000240316; -.
DR GlyGen; P38432; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P38432; -.
DR PhosphoSitePlus; P38432; -.
DR SwissPalm; P38432; -.
DR BioMuta; COIL; -.
DR DMDM; 585632; -.
DR EPD; P38432; -.
DR jPOST; P38432; -.
DR MassIVE; P38432; -.
DR MaxQB; P38432; -.
DR PaxDb; P38432; -.
DR PeptideAtlas; P38432; -.
DR PRIDE; P38432; -.
DR ProteomicsDB; 55295; -.
DR Antibodypedia; 4307; 330 antibodies from 37 providers.
DR DNASU; 8161; -.
DR Ensembl; ENST00000240316.5; ENSP00000240316.4; ENSG00000121058.5.
DR GeneID; 8161; -.
DR KEGG; hsa:8161; -.
DR MANE-Select; ENST00000240316.5; ENSP00000240316.4; NM_004645.3; NP_004636.1.
DR UCSC; uc002iuu.4; human.
DR CTD; 8161; -.
DR DisGeNET; 8161; -.
DR GeneCards; COIL; -.
DR HGNC; HGNC:2184; COIL.
DR HPA; ENSG00000121058; Tissue enriched (testis).
DR MIM; 600272; gene.
DR neXtProt; NX_P38432; -.
DR OpenTargets; ENSG00000121058; -.
DR PharmGKB; PA26700; -.
DR VEuPathDB; HostDB:ENSG00000121058; -.
DR eggNOG; ENOG502QVWV; Eukaryota.
DR GeneTree; ENSGT00390000004832; -.
DR HOGENOM; CLU_034553_0_0_1; -.
DR InParanoid; P38432; -.
DR OMA; RKITVFW; -.
DR OrthoDB; 1068620at2759; -.
DR PhylomeDB; P38432; -.
DR TreeFam; TF331811; -.
DR PathwayCommons; P38432; -.
DR SignaLink; P38432; -.
DR SIGNOR; P38432; -.
DR BioGRID-ORCS; 8161; 108 hits in 1077 CRISPR screens.
DR ChiTaRS; COIL; human.
DR GeneWiki; Coilin; -.
DR GenomeRNAi; 8161; -.
DR Pharos; P38432; Tbio.
DR PRO; PR:P38432; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P38432; protein.
DR Bgee; ENSG00000121058; Expressed in sperm and 206 other tissues.
DR ExpressionAtlas; P38432; baseline and differential.
DR Genevisible; P38432; HS.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR InterPro; IPR024822; Coilin.
DR InterPro; IPR031722; Coilin_N.
DR PANTHER; PTHR15197; PTHR15197; 1.
DR Pfam; PF15862; Coilin_N; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..576
FT /note="Coilin"
FT /id="PRO_0000058146"
FT REPEAT 223..226
FT /note="1-1"
FT REPEAT 268..271
FT /note="1-2"
FT REPEAT 386..389
FT /note="2-1"
FT REPEAT 413..414
FT /note="3-1"
FT REPEAT 415..416
FT /note="3-2"
FT REPEAT 417..418
FT /note="3-3"
FT REPEAT 419..420
FT /note="3-4"
FT DOMAIN 460..559
FT /note="Tudor; atypical"
FT REPEAT 517..520
FT /note="2-2"
FT REGION 125..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..271
FT /note="2 X 4 AA repeats of A-R-N-S"
FT REGION 352..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..520
FT /note="2 X 4 AA repeats of S-L-P-A"
FT REGION 392..420
FT /note="Required for interaction with SMN"
FT /evidence="ECO:0000269|PubMed:11641277"
FT REGION 413..420
FT /note="4 X 2 AA tandem repeats of R-G"
FT COMPBIAS 125..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 184
FT /note="Phosphoserine; by VRK1 and VRK2"
FT /evidence="ECO:0000269|PubMed:21920476"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SU73"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SU73"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SU73"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 456
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 413..419
FT /note="RGRGRGR->GGGGGGG: Impaired interaction with SMN."
FT /evidence="ECO:0000269|PubMed:11641277"
SQ SEQUENCE 576 AA; 62608 MW; 879702B590F16849 CRC64;
MAASETVRLR LQFDYPPPAT PHCTAFWLLV DLNRCRVVTD LISLIRQRFG FSSGAFLGLY
LEGGLLPPAE SARLVRDNDC LRVKLEERGV AENSVVISNG DINLSLRKAK KRAFQLEEGE
ETEPDCKYSK KHWKSRENNN NNEKVLDLEP KAVTDQTVSK KNKRKNKATC GTVGDDNEEA
KRKSPKKKEK CEYKKKAKNP KSPKVQAVKD WANQRCSSPK GSARNSLVKA KRKGSVSVCS
KESPSSSSES ESCDESISDG PSKVTLEARN SSEKLPTELS KEEPSTKNTT ADKLAIKLGF
SLTPSKGKTS GTTSSSSDSS AESDDQCLMS SSTPECAAGF LKTVGLFAGR GRPGPGLSSQ
TAGAAGWRRS GSNGGGQAPG ASPSVSLPAS LGRGWGREEN LFSWKGAKGR GMRGRGRGRG
HPVSCVVNRS TDNQRQQQLN DVVKNSSTII QNPVETPKKD YSLLPLLAAA PQVGEKIAFK
LLELTSSYSP DVSDYKEGRI LSHNPETQQV DIEILSSLPA LREPGKFDLV YHNENGAEVV
EYAVTQESKI TVFWKELIDP RLIIESPSNT SSTEPA
