RU1C_HUMAN
ID RU1C_HUMAN Reviewed; 159 AA.
AC P09234; Q5TAL3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=U1 small nuclear ribonucleoprotein C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1 snRNP C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1-C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1C {ECO:0000255|HAMAP-Rule:MF_03153};
GN Name=SNRPC {ECO:0000255|HAMAP-Rule:MF_03153};
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=2971157; DOI=10.1093/nar/16.17.8307;
RA Sillekens P.T.G., Beijer R.P., Habets W.J., van Venrooij W.J.;
RT "Human U1 snRNP-specific C protein: complete cDNA and protein sequence and
RT identification of a multigene family in mammals.";
RL Nucleic Acids Res. 16:8307-8321(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-131.
RX PubMed=2961811;
RA Yamamoto K., Miura H., Moroi Y., Yoshinoya S., Goto M., Nishioka K.,
RA Miyamoto T.;
RT "Isolation and characterization of a complementary DNA expressing human U1
RT small nuclear ribonucleoprotein C polypeptide.";
RL J. Immunol. 140:311-317(1988).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=2136774; DOI=10.1126/science.2136774;
RA Heinrichs V., Bach M., Winkelmann G., Luehrmann R.;
RT "U1-specific protein C needed for efficient complex formation of U1 snRNP
RT with a 5' splice site.";
RL Science 247:69-72(1990).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF CYS-6; CYS-9; HIS-24; CYS-25 AND HIS-30.
RX PubMed=1826349; DOI=10.1093/nar/19.3.449;
RA Nelissen R.L.H., Heinrichs V., Habets W.J., Simons F., Luehrmann R.,
RA van Venrooij W.J.;
RT "Zinc finger-like structure in U1-specific protein C is essential for
RT specific binding to U1 snRNP.";
RL Nucleic Acids Res. 19:449-454(1991).
RN [6]
RP FUNCTION.
RX PubMed=8798632; DOI=10.1074/jbc.271.39.23985;
RA Rossi F., Forne T., Antoine E., Tazi J., Brunel C., Cathala G.;
RT "Involvement of U1 small nuclear ribonucleoproteins (snRNP) in 5' splice
RT site-U1 snRNP interaction.";
RL J. Biol. Chem. 271:23985-23991(1996).
RN [7]
RP INTERACTION WITH TIA1.
RX PubMed=12486009; DOI=10.1093/emboj/cdf668;
RA Foerch P., Puig O., Martinez C., Seraphin B., Valcarcel J.;
RT "The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP
RT recruitment to 5' splice sites.";
RL EMBO J. 21:6882-6892(2002).
RN [8]
RP IDENTIFICATION IN THE U1 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15525645; DOI=10.1074/jbc.m409587200;
RA Hochleitner E.O., Kastner B., Froehlich T., Schmidt A., Luehrmann R.,
RA Arnold G., Lottspeich F.;
RT "Protein stoichiometry of a multiprotein complex, the human spliceosomal U1
RT small nuclear ribonucleoprotein: absolute quantification using isotope-
RT coded tags and mass spectrometry.";
RL J. Biol. Chem. 280:2536-2542(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [15]
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).
RN [16]
RP STRUCTURE BY NMR OF 1-61, SUBUNIT, AND DOMAIN ZINC-FINGER.
RX PubMed=15312772; DOI=10.1016/j.jmb.2004.04.078;
RA Muto Y., Pomeranz Krummel D., Oubridge C., Hernandez H., Robinson C.V.,
RA Neuhaus D., Nagai K.;
RT "The structure and biochemical properties of the human spliceosomal protein
RT U1C.";
RL J. Mol. Biol. 341:185-198(2004).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-77 IN SPLICEOSOMAL U1 SNRNP,
RP SUBUNIT, AND FUNCTION.
RX PubMed=19325628; DOI=10.1038/nature07851;
RA Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.;
RT "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution.";
RL Nature 458:475-480(2009).
RN [18] {ECO:0007744|PDB:4PJO}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-61 IN COMPLEX WITH ZINC, AND
RP SUBUNIT.
RX PubMed=25555158; DOI=10.7554/elife.04986;
RA Kondo Y., Oubridge C., van Roon A.M., Nagai K.;
RT "Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein
RT particle, reveals the mechanism of 5' splice site recognition.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Component of the spliceosomal U1 snRNP, which is essential
CC for recognition of the pre-mRNA 5' splice-site and the subsequent
CC assembly of the spliceosome. SNRPC/U1-C is directly involved in initial
CC 5' splice-site recognition for both constitutive and regulated
CC alternative splicing. The interaction with the 5' splice-site seems to
CC precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates
CC commitment or early (E) complex formation by stabilizing the base
CC pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
CC {ECO:0000255|HAMAP-Rule:MF_03153, ECO:0000269|PubMed:1826349,
CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:2136774,
CC ECO:0000269|PubMed:8798632}.
CC -!- SUBUNIT: Component of the U1 snRNP (PubMed:2136774). The U1 snRNP is
CC composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1,
CC SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric
CC protein ring on the Sm site of the small nuclear RNA to form the core
CC snRNP, and at least 3 U1 snRNP-specific proteins SNRNP70/U1-70K,
CC SNRPA/U1-A and SNRPC/U1-C. SNRPC/U1-C interacts with U1 snRNA and the
CC 5' splice-site region of the pre-mRNA. Interacts (via N-terminus) with
CC TIA1 (via C-terminus); thereby promoting spliceosomal U1 snRNP
CC recruitment to 5' splice sites (PubMed:12486009). {ECO:0000255|HAMAP-
CC Rule:MF_03153, ECO:0000269|PubMed:12486009,
CC ECO:0000269|PubMed:15312772, ECO:0000269|PubMed:15525645,
CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:2136774,
CC ECO:0000269|PubMed:25555158}.
CC -!- INTERACTION:
CC P09234; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-766589, EBI-357530;
CC P09234; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-766589, EBI-12102070;
CC P09234; Q9BRR9: ARHGAP9; NbExp=3; IntAct=EBI-766589, EBI-750254;
CC P09234; O95429: BAG4; NbExp=3; IntAct=EBI-766589, EBI-2949658;
CC P09234; O75934: BCAS2; NbExp=3; IntAct=EBI-766589, EBI-1050106;
CC P09234; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-766589, EBI-11983447;
CC P09234; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-766589, EBI-11976299;
CC P09234; Q03060-25: CREM; NbExp=3; IntAct=EBI-766589, EBI-12884642;
CC P09234; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-766589, EBI-3867333;
CC P09234; Q15038: DAZAP2; NbExp=3; IntAct=EBI-766589, EBI-724310;
CC P09234; Q16610: ECM1; NbExp=3; IntAct=EBI-766589, EBI-947964;
CC P09234; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-766589, EBI-371922;
CC P09234; O00167-2: EYA2; NbExp=3; IntAct=EBI-766589, EBI-12807776;
CC P09234; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-766589, EBI-12193763;
CC P09234; Q13643: FHL3; NbExp=3; IntAct=EBI-766589, EBI-741101;
CC P09234; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-766589, EBI-12121668;
CC P09234; O75420: GIGYF1; NbExp=3; IntAct=EBI-766589, EBI-947774;
CC P09234; O14979: HNRNPDL; NbExp=3; IntAct=EBI-766589, EBI-299727;
CC P09234; P31943: HNRNPH1; NbExp=3; IntAct=EBI-766589, EBI-351590;
CC P09234; P49639: HOXA1; NbExp=5; IntAct=EBI-766589, EBI-740785;
CC P09234; Q9BPX1: HSD17B14; NbExp=3; IntAct=EBI-766589, EBI-742664;
CC P09234; Q5TA45: INTS11; NbExp=3; IntAct=EBI-766589, EBI-748258;
CC P09234; P0C870: JMJD7; NbExp=5; IntAct=EBI-766589, EBI-9090173;
CC P09234; Q13351: KLF1; NbExp=3; IntAct=EBI-766589, EBI-8284732;
CC P09234; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-766589, EBI-1052037;
CC P09234; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-766589, EBI-11953846;
CC P09234; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-766589, EBI-12196745;
CC P09234; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-766589, EBI-1048945;
CC P09234; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-766589, EBI-12805508;
CC P09234; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-766589, EBI-18395721;
CC P09234; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-766589, EBI-11962084;
CC P09234; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-766589, EBI-18394498;
CC P09234; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-766589, EBI-10261141;
CC P09234; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-766589, EBI-716006;
CC P09234; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-766589, EBI-8487781;
CC P09234; Q13064: MKRN3; NbExp=3; IntAct=EBI-766589, EBI-2340269;
CC P09234; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-766589, EBI-10963850;
CC P09234; A1E959: ODAM; NbExp=3; IntAct=EBI-766589, EBI-5774125;
CC P09234; O15496: PLA2G10; NbExp=3; IntAct=EBI-766589, EBI-726466;
CC P09234; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-766589, EBI-3957793;
CC P09234; P86480: PRR20D; NbExp=3; IntAct=EBI-766589, EBI-12754095;
CC P09234; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-766589, EBI-744023;
CC P09234; P98175: RBM10; NbExp=2; IntAct=EBI-766589, EBI-721525;
CC P09234; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-766589, EBI-740343;
CC P09234; Q9P2R6: RERE; NbExp=3; IntAct=EBI-766589, EBI-948076;
CC P09234; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-766589, EBI-12001422;
CC P09234; Q15437: SEC23B; NbExp=3; IntAct=EBI-766589, EBI-742673;
CC P09234; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-766589, EBI-11959123;
CC P09234; Q8IWL8: STH; NbExp=3; IntAct=EBI-766589, EBI-12843506;
CC P09234; P31483: TIA1; NbExp=6; IntAct=EBI-766589, EBI-1387216;
CC P09234; Q08117-2: TLE5; NbExp=3; IntAct=EBI-766589, EBI-11741437;
CC P09234; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-766589, EBI-492476;
CC P09234; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-766589, EBI-12068150;
CC P09234; Q9BRX9: WDR83; NbExp=2; IntAct=EBI-766589, EBI-7705033;
CC P09234; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-766589, EBI-12040603;
CC P09234; O00308: WWP2; NbExp=3; IntAct=EBI-766589, EBI-743923;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153,
CC ECO:0000269|PubMed:2136774}.
CC -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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DR EMBL; X12517; CAA31037.1; -; mRNA.
DR EMBL; AL139100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M18465; AAA36618.1; -; mRNA.
DR CCDS; CCDS34436.1; -.
DR PIR; S01387; S01387.
DR RefSeq; NP_003084.1; NM_003093.2.
DR PDB; 2VRD; NMR; -; A=1-61.
DR PDB; 3CW1; X-ray; 5.49 A; 0/9/L/l=1-77.
DR PDB; 4PJO; X-ray; 3.30 A; L/M/l/m=1-61.
DR PDB; 6ELD; X-ray; 2.48 A; A=30-61.
DR PDB; 6QX9; EM; 3.28 A; 1C=1-159.
DR PDBsum; 2VRD; -.
DR PDBsum; 3CW1; -.
DR PDBsum; 4PJO; -.
DR PDBsum; 6ELD; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; P09234; -.
DR SMR; P09234; -.
DR BioGRID; 112515; 232.
DR ComplexPortal; CPX-2392; U1 small nuclear ribonucleoprotein complex.
DR CORUM; P09234; -.
DR DIP; DIP-34235N; -.
DR IntAct; P09234; 113.
DR MINT; P09234; -.
DR STRING; 9606.ENSP00000244520; -.
DR GlyGen; P09234; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09234; -.
DR PhosphoSitePlus; P09234; -.
DR SwissPalm; P09234; -.
DR BioMuta; SNRPC; -.
DR DMDM; 134093; -.
DR CPTAC; CPTAC-947; -.
DR EPD; P09234; -.
DR jPOST; P09234; -.
DR MassIVE; P09234; -.
DR PaxDb; P09234; -.
DR PeptideAtlas; P09234; -.
DR PRIDE; P09234; -.
DR ProteomicsDB; 52209; -.
DR Antibodypedia; 45711; 71 antibodies from 21 providers.
DR DNASU; 6631; -.
DR Ensembl; ENST00000244520.10; ENSP00000244520.5; ENSG00000124562.10.
DR GeneID; 6631; -.
DR KEGG; hsa:6631; -.
DR MANE-Select; ENST00000244520.10; ENSP00000244520.5; NM_003093.3; NP_003084.1.
DR CTD; 6631; -.
DR DisGeNET; 6631; -.
DR GeneCards; SNRPC; -.
DR HGNC; HGNC:11157; SNRPC.
DR HPA; ENSG00000124562; Low tissue specificity.
DR MIM; 603522; gene.
DR neXtProt; NX_P09234; -.
DR OpenTargets; ENSG00000124562; -.
DR PharmGKB; PA35998; -.
DR VEuPathDB; HostDB:ENSG00000124562; -.
DR eggNOG; KOG3454; Eukaryota.
DR GeneTree; ENSGT00730000110997; -.
DR HOGENOM; CLU_079697_3_0_1; -.
DR InParanoid; P09234; -.
DR OMA; FLTHDST; -.
DR OrthoDB; 1594407at2759; -.
DR TreeFam; TF313578; -.
DR PathwayCommons; P09234; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P09234; -.
DR BioGRID-ORCS; 6631; 573 hits in 1085 CRISPR screens.
DR ChiTaRS; SNRPC; human.
DR EvolutionaryTrace; P09234; -.
DR GeneWiki; Small_nuclear_ribonucleoprotein_polypeptide_C; -.
DR GenomeRNAi; 6631; -.
DR Pharos; P09234; Tbio.
DR PRO; PR:P09234; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P09234; protein.
DR Bgee; ENSG00000124562; Expressed in apex of heart and 208 other tissues.
DR ExpressionAtlas; P09234; baseline and differential.
DR Genevisible; P09234; HS.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0005685; C:U1 snRNP; IDA:UniProtKB.
DR GO; GO:0071004; C:U2-type prespliceosome; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030627; F:pre-mRNA 5'-splice site binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR HAMAP; MF_03153; U1_C; 1.
DR IDEAL; IID00139; -.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR013085; U1-CZ_Znf_C2H2.
DR InterPro; IPR017340; U1_snRNP-C.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR31148; PTHR31148; 1.
DR Pfam; PF06220; zf-U1; 1.
DR PIRSF; PIRSF037969; U1_snRNP-C; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..159
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000097525"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 62..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 6
FT /note="C->S: Abolishes the binding to U1 snRNP."
FT /evidence="ECO:0000269|PubMed:1826349"
FT MUTAGEN 9
FT /note="C->S: Abolishes the binding to U1 snRNP."
FT /evidence="ECO:0000269|PubMed:1826349"
FT MUTAGEN 24
FT /note="H->Q: Abolishes the binding to U1 snRNP."
FT /evidence="ECO:0000269|PubMed:1826349"
FT MUTAGEN 25
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:1826349"
FT MUTAGEN 30
FT /note="H->Q: Abolishes the binding to U1 snRNP."
FT /evidence="ECO:0000269|PubMed:1826349"
FT CONFLICT 25..27
FT /note="CSG -> RSR (in Ref. 3; AAA36618)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..98
FT /note="APHMG -> TPIW (in Ref. 3; AAA36618)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="P -> S (in Ref. 3; AAA36618)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..131
FT /note="HMP -> ICQ (in Ref. 3; AAA36618)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4PJO"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:4PJO"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:4PJO"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:4PJO"
FT HELIX 36..58
FT /evidence="ECO:0007829|PDB:6ELD"
SQ SEQUENCE 159 AA; 17394 MW; EC313A57DEC79D95 CRC64;
MPKFYCDYCD TYLTHDSPSV RKTHCSGRKH KENVKDYYQK WMEEQAQSLI DKTTAAFQQG
KIPPTPFSAP PPAGAMIPPP PSLPGPPRPG MMPAPHMGGP PMMPMMGPPP PGMMPVGPAP
GMRPPMGGHM PMMPGPPMMR PPARPMMVPT RPGMTRPDR
