ICLN_HUMAN
ID ICLN_HUMAN Reviewed; 237 AA.
AC P54105; B2RCS9; Q0VDK6; Q9NRD2; Q9NRD3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Methylosome subunit pICln;
DE AltName: Full=Chloride channel, nucleotide sensitive 1A;
DE AltName: Full=Chloride conductance regulatory protein ICln;
DE Short=I(Cln);
DE AltName: Full=Chloride ion current inducer protein;
DE Short=ClCI;
DE AltName: Full=Reticulocyte pICln;
GN Name=CLNS1A; Synonyms=CLCI, ICLN;
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].
RX PubMed=8579598; DOI=10.1006/bbrc.1996.0146;
RA Buyse G., de Greef C., Raeymaekers L., Droogmans G., Nilius B.,
RA Eggermont J.;
RT "The ubiquitously expressed pICln protein forms homomeric complexes in
RT vitro.";
RL Biochem. Biophys. Res. Commun. 218:822-827(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ocular ciliary epithelium;
RX PubMed=7887970; DOI=10.1006/bbrc.1995.1309;
RA Anquita J., Chalfant M.L., Civan M.M., Coca-Prados M.;
RT "Molecular cloning of the human volume-sensitive chloride conductance
RT regulatory protein, pICln, from ocular ciliary epithelium.";
RL Biochem. Biophys. Res. Commun. 208:89-95(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lamb F.S., Mathews K., Mills K., Barna T., Pruessner J., Kresnicka L.S.,
RA Schutte B.C.;
RT "Colocalization of CLCI and CLCN3 to human 4q32 and mouse 8: the candidate
RT region for tottering (tg).";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9359436; DOI=10.1042/bj3270609;
RA Schwartz R.S., Rybicki A.C., Nagel R.L.;
RT "Molecular cloning and expression of a chloride channel-associated protein
RT pI(Cln) in human young red blood cells: association with actin.";
RL Biochem. J. 327:609-616(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RT "Chloride ion current inducer protein in human lens epithelium.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-20 AND THR-218.
RC TISSUE=Colon cancer, and Kidney;
RX PubMed=10825435; DOI=10.1016/s0005-2736(00)00177-2;
RA Hubert M.D., Levitan I., Hoffman M.M., Zraggen M., Hofreiter M.E.,
RA Garber S.S.;
RT "Modulation of volume regulated anion current by I(Cln).";
RL Biochim. Biophys. Acta 1466:105-114(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [10]
RP PROTEIN SEQUENCE OF 2-43; 86-113 AND 188-237, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Colon carcinoma;
RA Bienvenut W.V., Calvo F., Zebisch A., Kolch W.;
RL Submitted (OCT-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 19-113 AND 188-237, PHOSPHORYLATION AT SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [12]
RP FUNCTION IN SNRNP BIOGENESIS.
RX PubMed=10330151; DOI=10.1128/mcb.19.6.4113;
RA Pu W.T., Krapivinsky G.B., Krapivinsky L., Clapham D.E.;
RT "pICln inhibits snRNP biogenesis by binding core spliceosomal proteins.";
RL Mol. Cell. Biol. 19:4113-4120(1999).
RN [13]
RP IDENTIFICATION IN THE METHYLOSOME COMPLEX.
RX PubMed=11747828; DOI=10.1016/s0960-9822(01)00592-9;
RA Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.;
RT "Methylation of Sm proteins by a complex containing PRMT5 and the putative
RT U snRNP assembly factor pICln.";
RL Curr. Biol. 11:1990-1994(2001).
RN [14]
RP FUNCTION IN METHYLOSOME.
RX PubMed=11713266; DOI=10.1128/mcb.21.24.8289-8300.2001;
RA Friesen W.J., Paushkin S., Wyce A., Massenet S., Pesiridis G.S.,
RA Van Duyne G., Rappsilber J., Mann M., Dreyfuss G.;
RT "The methylosome, a 20S complex containing JBP1 and pICln, produces
RT dimethylarginine-modified Sm proteins.";
RL Mol. Cell. Biol. 21:8289-8300(2001).
RN [15]
RP INTERACTION WITH LSM10; LSM11 AND SNRPB.
RX PubMed=16087681; DOI=10.1074/jbc.m505077200;
RA Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
RA Fischer U., Schuemperli D.;
RT "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm
RT proteins with PRMT5 and SMN complexes.";
RL J. Biol. Chem. 280:34435-34440(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [18]
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 [19]
RP FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN THE METHYLOSOME COMPLEX,
RP IDENTIFICATION IN 6S PICLN-SM COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
RA Englbrecht C., Sickmann A., Stark H., Fischer U.;
RT "An assembly chaperone collaborates with the SMN complex to generate
RT spliceosomal SnRNPs.";
RL Cell 135:497-509(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND THR-223, AND
RP 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP 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 [27]
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 [28]
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH PRTM5, IDENTIFICATION IN
RP THE METHYLOSOME COMPLEX, AND FUNCTION.
RX PubMed=21081503; DOI=10.1074/jbc.m110.148486;
RA Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K.,
RA Fischer U., Grimmler M.;
RT "RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5),
RT competes with pICln for binding and modulates PRMT5 complex composition and
RT substrate specificity.";
RL J. Biol. Chem. 286:1976-1986(2011).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP 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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-193; SER-195;
RP SER-198; SER-210 AND THR-223, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, 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).
CC -!- FUNCTION: Involved in both the assembly of spliceosomal snRNPs and the
CC methylation of Sm proteins (PubMed:21081503, PubMed:18984161,
CC PubMed:10330151, PubMed:11713266). Chaperone that regulates the
CC assembly of spliceosomal U1, U2, U4 and U5 small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs (PubMed:18984161, PubMed:10330151). Most spliceosomal snRNPs
CC contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on
CC the Sm site of the small nuclear RNA to form the core snRNP (Sm core)
CC (PubMed:10330151). In the cytosol, the Sm proteins SNRPD1, SNRPD2,
CC SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex
CC by the chaperone CLNS1A that controls the assembly of the core snRNP
CC (PubMed:10330151, PubMed:18984161). Dissociation by the SMN complex of
CC CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm
CC complex triggers the assembly of core snRNPs and their transport to the
CC nucleus (PubMed:10330151, PubMed:18984161).
CC {ECO:0000269|PubMed:10330151, ECO:0000269|PubMed:11713266,
CC ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:21081503}.
CC -!- SUBUNIT: Component of the methylosome, a 20S complex containing at
CC least PRMT5/SKB1, WDR77/MEP50 and CLNS1A/pICln (PubMed:21081503,
CC PubMed:11747828, PubMed:18984161). May mediate SNRPD1 and SNRPD3
CC methylation. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln,
CC SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where
CC CLNS1A/pICln mimics additional Sm proteins and which is unable to
CC assemble into the core snRNP (PubMed:18984161). Interacts with LSM10
CC and LSM11 (PubMed:16087681). {ECO:0000269|PubMed:11747828,
CC ECO:0000269|PubMed:16087681, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:21081503}.
CC -!- INTERACTION:
CC P54105; P11171-2: EPB41; NbExp=3; IntAct=EBI-724693, EBI-10197451;
CC P54105; Q6ZUT3: FRMD7; NbExp=3; IntAct=EBI-724693, EBI-12325851;
CC P54105; Q9Y333: LSM2; NbExp=7; IntAct=EBI-724693, EBI-347416;
CC P54105; P62310: LSM3; NbExp=7; IntAct=EBI-724693, EBI-348239;
CC P54105; P62312: LSM6; NbExp=8; IntAct=EBI-724693, EBI-373310;
CC P54105; O14744: PRMT5; NbExp=8; IntAct=EBI-724693, EBI-351098;
CC P54105; P14678: SNRPB; NbExp=3; IntAct=EBI-724693, EBI-372458;
CC P54105; P14678-2: SNRPB; NbExp=3; IntAct=EBI-724693, EBI-372475;
CC P54105; P62314: SNRPD1; NbExp=12; IntAct=EBI-724693, EBI-372177;
CC P54105; P62316: SNRPD2; NbExp=11; IntAct=EBI-724693, EBI-297993;
CC P54105; P62318: SNRPD3; NbExp=9; IntAct=EBI-724693, EBI-372789;
CC P54105; P62306: SNRPF; NbExp=5; IntAct=EBI-724693, EBI-356900;
CC P54105; P62308: SNRPG; NbExp=9; IntAct=EBI-724693, EBI-624585;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:21081503}. Nucleus {ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:21081503}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18984161}. Note=A small fraction is also associated
CC with the cytoskeleton (PubMed:18984161).
CC -!- SIMILARITY: Belongs to the pICln (TC 1.A.47) family. {ECO:0000305}.
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DR EMBL; X91788; CAA62902.1; -; mRNA.
DR EMBL; U17899; AAC50111.1; -; mRNA.
DR EMBL; U53454; AAB03316.1; -; mRNA.
DR EMBL; AF005422; AAB61444.1; -; mRNA.
DR EMBL; AF026003; AAB88806.1; -; mRNA.
DR EMBL; AF232708; AAF76861.1; -; Genomic_DNA.
DR EMBL; AF232224; AAF76858.1; -; Genomic_DNA.
DR EMBL; AF232225; AAF76859.1; -; Genomic_DNA.
DR EMBL; AK315259; BAG37676.1; -; mRNA.
DR EMBL; BT019907; AAV38710.1; -; mRNA.
DR EMBL; BC119634; AAI19635.1; -; mRNA.
DR EMBL; BC119635; AAI19636.1; -; mRNA.
DR CCDS; CCDS8252.1; -.
DR PIR; JC4135; JC4135.
DR RefSeq; NP_001284.1; NM_001293.2.
DR RefSeq; NP_001298128.1; NM_001311199.1.
DR RefSeq; NP_001298129.1; NM_001311200.1.
DR RefSeq; NP_001298130.1; NM_001311201.1.
DR RefSeq; NP_001298131.1; NM_001311202.1.
DR PDB; 6V0O; X-ray; 2.86 A; D=225-237.
DR PDBsum; 6V0O; -.
DR AlphaFoldDB; P54105; -.
DR SMR; P54105; -.
DR BioGRID; 107617; 147.
DR ComplexPortal; CPX-696; PRMT5 methylosome complex.
DR CORUM; P54105; -.
DR DIP; DIP-44185N; -.
DR IntAct; P54105; 53.
DR MINT; P54105; -.
DR STRING; 9606.ENSP00000433919; -.
DR TCDB; 1.A.47.1.1; the nucleotide-sensitive anion-selective channel, icln (icln) family.
DR GlyGen; P54105; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P54105; -.
DR PhosphoSitePlus; P54105; -.
DR BioMuta; CLNS1A; -.
DR EPD; P54105; -.
DR jPOST; P54105; -.
DR MassIVE; P54105; -.
DR MaxQB; P54105; -.
DR PaxDb; P54105; -.
DR PeptideAtlas; P54105; -.
DR PRIDE; P54105; -.
DR ProteomicsDB; 56643; -.
DR Antibodypedia; 4508; 194 antibodies from 31 providers.
DR DNASU; 1207; -.
DR Ensembl; ENST00000525428.6; ENSP00000433919.1; ENSG00000074201.9.
DR Ensembl; ENST00000528364.1; ENSP00000434311.1; ENSG00000074201.9.
DR GeneID; 1207; -.
DR KEGG; hsa:1207; -.
DR MANE-Select; ENST00000525428.6; ENSP00000433919.1; NM_001293.3; NP_001284.1.
DR UCSC; uc001oyk.4; human.
DR CTD; 1207; -.
DR DisGeNET; 1207; -.
DR GeneCards; CLNS1A; -.
DR HGNC; HGNC:2080; CLNS1A.
DR HPA; ENSG00000074201; Low tissue specificity.
DR MIM; 602158; gene.
DR neXtProt; NX_P54105; -.
DR OpenTargets; ENSG00000074201; -.
DR PharmGKB; PA26607; -.
DR VEuPathDB; HostDB:ENSG00000074201; -.
DR eggNOG; KOG3238; Eukaryota.
DR GeneTree; ENSGT00390000010063; -.
DR InParanoid; P54105; -.
DR OMA; SAFPWEH; -.
DR OrthoDB; 1508796at2759; -.
DR PhylomeDB; P54105; -.
DR TreeFam; TF315155; -.
DR PathwayCommons; P54105; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR SignaLink; P54105; -.
DR BioGRID-ORCS; 1207; 717 hits in 1048 CRISPR screens.
DR ChiTaRS; CLNS1A; human.
DR GeneWiki; CLNS1A; -.
DR GenomeRNAi; 1207; -.
DR Pharos; P54105; Tbio.
DR PRO; PR:P54105; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P54105; protein.
DR Bgee; ENSG00000074201; Expressed in ventricular zone and 208 other tissues.
DR ExpressionAtlas; P54105; baseline and differential.
DR Genevisible; P54105; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0034709; C:methylosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034715; C:pICln-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; IEA:InterPro.
DR GO; GO:0006821; P:chloride transport; IEA:InterPro.
DR GO; GO:0043985; P:histone H4-R3 methylation; IC:ComplexPortal.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR003521; ICln.
DR InterPro; IPR039924; ICln/Lot5/Saf5.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR21399; PTHR21399; 1.
DR Pfam; PF03517; Voldacs; 1.
DR PRINTS; PR01348; ICLNCHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:22814378"
FT CHAIN 2..237
FT /note="Methylosome subunit pICln"
FT /id="PRO_0000185155"
FT REGION 135..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..153
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:22814378"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.10, ECO:0000269|Ref.11,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17487921,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 20
FT /note="Q -> H"
FT /evidence="ECO:0000269|PubMed:10825435"
FT /id="VAR_015736"
FT VARIANT 218
FT /note="M -> T"
FT /evidence="ECO:0000269|PubMed:10825435"
FT /id="VAR_015737"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:6V0O"
SQ SEQUENCE 237 AA; 26215 MW; AE9C09884A6FF158 CRC64;
MSFLKSFPPP GPAEGLLRQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT
ISLHALSRDR SDCLGEHLYV MVNAKFEEES KEPVADEEEE DSDDDVEPIT EFRFVPSDKS
ALEAMFTAMC ECQALHPDPE DEDSDDYDGE EYDVEAHEQG QGDIPTFYTY EEGLSHLTAE
GQATLERLEG MLSQSVSSQY NMAGVRTEDS IRDYEDGMEV DTTPTVAGQF EDADVDH
