HNRPC_HUMAN
ID HNRPC_HUMAN Reviewed; 306 AA.
AC P07910; D3DS19; D3DS22; P22628; Q53EX2; Q59FD3; Q5FWE8; Q86SF8; Q86U45;
AC Q96HK7; Q96HM4; Q96IY5; Q9BTS3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 4.
DT 03-AUG-2022, entry version 253.
DE RecName: Full=Heterogeneous nuclear ribonucleoproteins C1/C2;
DE Short=hnRNP C1/C2;
GN Name=HNRNPC; Synonyms=HNRPC;
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] (ISOFORM C2).
RX PubMed=2557628; DOI=10.1073/pnas.86.24.9788;
RA Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G.;
RT "Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1,
RT and C2 proteins: a diversity of RNA binding proteins is generated by small
RT peptide inserts.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C1).
RX PubMed=3110598; DOI=10.1128/mcb.7.5.1731-1739.1987;
RA Swanson M.S., Nakagawa T.Y., Levan K., Dreyfuss G.;
RT "Primary structure of human nuclear ribonucleoprotein particle C proteins:
RT conservation of sequence and domain structures in heterogeneous nuclear
RT RNA, mRNA, and pre-rRNA-binding proteins.";
RL Mol. Cell. Biol. 7:1731-1739(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1 AND 3).
RC TISSUE=Neuroblastoma, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1; C2 AND 4).
RC TISSUE=Bone marrow, Brain, Chondrosarcoma, Eye, and Placenta;
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 [7]
RP PROTEIN SEQUENCE OF 2-12; 18-39; 43-61; 74-89; 143-151; 188-198 AND
RP 205-216, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Cooper W.N., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 18-39; 51-61; 74-89 AND 207-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, AND CHARACTERIZATION.
RX PubMed=2587210; DOI=10.1093/nar/17.21.8441;
RA Merrill B.M., Barnett S.F., Lestourgeon W.M., Williams K.R.;
RT "Primary structure differences between proteins C1 and C2 of HeLa 40S
RT nuclear ribonucleoprotein particles.";
RL Nucleic Acids Res. 17:8441-8449(1989).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8264621; DOI=10.1128/mcb.14.1.518-533.1994;
RA Huang M., Rech J.E., Northington S.J., Flicker P.F., Mayeda A.,
RA Krainer A.R., LeStourgeon W.M.;
RT "The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and
RT nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein
RT particles.";
RL Mol. Cell. Biol. 14:518-533(1994).
RN [11]
RP FUNCTION.
RX PubMed=7567451; DOI=10.1093/nar/23.17.3419;
RA Sebillon P., Beldjord C., Kaplan J.-C., Brody E., Marie J.;
RT "A T to G mutation in the polypyrimidine tract of the second intron of the
RT human beta-globin gene reduces in vitro splicing efficiency: evidence for
RT an increased hnRNP C interaction.";
RL Nucleic Acids Res. 23:3419-3425(1995).
RN [12]
RP INTERACTION WITH DHX9.
RX PubMed=11687588; DOI=10.1074/jbc.m109393200;
RA Zhang S., Buder K., Burkhardt C., Schlott B., Goerlach M., Grosse F.;
RT "Nuclear DNA helicase II/RNA helicase A binds to filamentous actin.";
RL J. Biol. Chem. 277:843-853(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [14]
RP PHOSPHORYLATION AT SER-253; SER-260 AND SER-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12564933; DOI=10.1021/bi0268091;
RA Stone J.R., Maki J.L., Collins T.;
RT "Basal and hydrogen peroxide stimulated sites of phosphorylation in
RT heterogeneous nuclear ribonucleoprotein C1/C2.";
RL Biochemistry 42:1301-1308(2003).
RN [15]
RP FUNCTION.
RX PubMed=12509468; DOI=10.1128/mcb.23.2.708-720.2003;
RA Kim J.H., Paek K.Y., Choi K., Kim T.-D., Hahm B., Kim K.-T., Jang S.K.;
RT "Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc
RT mRNA in a cell cycle phase-dependent manner.";
RL Mol. Cell. Biol. 23:708-720(2003).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [17]
RP MUTAGENESIS OF LYS-197 AND LYS-250, AND SUMOYLATION AT LYS-250.
RX PubMed=15082759; DOI=10.1128/mcb.24.9.3623-3632.2004;
RA Vassileva M.T., Matunis M.J.;
RT "SUMO modification of heterogeneous nuclear ribonucleoproteins.";
RL Mol. Cell. Biol. 24:3623-3632(2004).
RN [18]
RP FUNCTION.
RX PubMed=16010978; DOI=10.1007/s11010-005-7644-2;
RA Shetty S.;
RT "Regulation of urokinase receptor mRNA stability by hnRNP C in lung
RT epithelial cells.";
RL Mol. Cell. Biochem. 272:107-118(2005).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-233; SER-253 AND
RP SER-260, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [22]
RP INTERACTION WITH IGF2BP1.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-260, AND
RP IDENTIFICATION BY 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-233; SER-241 AND
RP SER-299, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-108
RP (ISOFORMS 4 AND C1), 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-253; SER-260;
RP SER-299 AND SER-306, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [27]
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109; SER-113; SER-115;
RP SER-233; SER-253 AND SER-260, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-260 AND SER-299, AND
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 [30]
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-233; SER-241;
RP SER-253; SER-260; SER-299 AND SER-306, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-107 (ISOFORMS 4 AND C1), AND IDENTIFICATION BY MASS
RP 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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-238; SER-241;
RP SER-253 AND SER-260, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-233; SER-238;
RP SER-239; SER-253 AND SER-260, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-89; LYS-176; LYS-229;
RP LYS-232 AND LYS-243, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-229 AND LYS-232, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [37]
RP INTERACTION WITH PPIA.
RX PubMed=25678563; DOI=10.1093/brain/awv005;
RA Lauranzano E., Pozzi S., Pasetto L., Stucchi R., Massignan T., Paolella K.,
RA Mombrini M., Nardo G., Lunetta C., Corbo M., Mora G., Bendotti C.,
RA Bonetto V.;
RT "Peptidylprolyl isomerase A governs TARDBP function and assembly in
RT heterogeneous nuclear ribonucleoprotein complexes.";
RL Brain 138:974-991(2015).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-94; LYS-229; LYS-232;
RP LYS-243 AND LYS-244, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-176; LYS-223; LYS-229;
RP LYS-232; LYS-243 AND LYS-244, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [40]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=25719671; DOI=10.1038/nature14234;
RA Liu N., Dai Q., Zheng G., He C., Parisien M., Pan T.;
RT "N(6)-methyladenosine-dependent RNA structural switches regulate RNA-
RT protein interactions.";
RL Nature 518:560-564(2015).
RN [41]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [42]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-50; LYS-89; LYS-176;
RP LYS-223; LYS-229; LYS-232; LYS-243 AND LYS-250, AND IDENTIFICATION BY MASS
RP 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 [43]
RP STRUCTURE BY NMR OF 1-94.
RX PubMed=1385725; DOI=10.1021/bi00142a013;
RA Witteking M., Goerlach M., Friedrichs M., Dreyfuss G., Mueller L.;
RT "1H, 13C, and 15N NMR assignments and global folding pattern of the RNA-
RT binding domain of the human hnRNP C proteins.";
RL Biochemistry 31:6254-6265(1992).
RN [44]
RP STRUCTURE BY NMR OF 1-94.
RX PubMed=1380452; DOI=10.1002/j.1460-2075.1992.tb05407.x;
RA Goerlach M., Witteking M., Beckman R.A., Mueller L., Dreyfuss G.;
RT "Interaction of the RNA-binding domain of the hnRNP C proteins with RNA.";
RL EMBO J. 11:3289-3295(1992).
RN [45]
RP STRUCTURE BY NMR OF 193-220, AND SUBUNIT.
RX PubMed=11162094; DOI=10.1006/jmbi.2000.4331;
RA Shahied L., Braswell E.H., LeStourgeon W.M., Krezel A.M.;
RT "An antiparallel four-helix bundle orients the high-affinity RNA binding
RT sites in hnRNP C: a mechanism for RNA chaperonin activity.";
RL J. Mol. Biol. 305:817-828(2001).
RN [46]
RP STRUCTURE BY NMR OF 8-92.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in HNRPC protein.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [47]
RP STRUCTURE BY NMR OF 193-220, AND SUBUNIT.
RX PubMed=15936032; DOI=10.1016/j.jmb.2005.05.002;
RA Whitson S.R., LeStourgeon W.M., Krezel A.M.;
RT "Solution structure of the symmetric coiled coil tetramer formed by the
RT oligomerization domain of hnRNP C: implications for biological function.";
RL J. Mol. Biol. 350:319-337(2005).
CC -!- FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP
CC particles (PubMed:8264621). Interacts with poly-U tracts in the 3'-UTR
CC or 5'-UTR of mRNA and modulates the stability and the level of
CC translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978,
CC PubMed:7567451, PubMed:8264621). Single HNRNPC tetramers bind 230-240
CC nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides
CC (PubMed:8264621). May play a role in the early steps of spliceosome
CC assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown
CC to alter the local structure in mRNAs and long non-coding RNAs
CC (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of
CC HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671).
CC {ECO:0000269|PubMed:12509468, ECO:0000269|PubMed:16010978,
CC ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:7567451,
CC ECO:0000269|PubMed:8264621}.
CC -!- SUBUNIT: Tetramer composed of 3 copies of isoform C1 and 1 copy of
CC isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a
CC 19S complex that interacts with HNRNPA2B1 tetramers. Component of the
CC 40S hnRNP particle. Identified in the spliceosome C complex. Interacts
CC with IGF2BP1. Interacts with DHX9; this interaction is direct, enhanced
CC probably by their concomitant binding to RNA and mediates the
CC attachment to actin filaments (PubMed:11687588). Interacts with
CC PPIA/CYPA (PubMed:25678563). {ECO:0000269|PubMed:11162094,
CC ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:15936032, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:8264621}.
CC -!- INTERACTION:
CC P07910; Q99459: CDC5L; NbExp=2; IntAct=EBI-357966, EBI-374880;
CC P07910; Q9NR30: DDX21; NbExp=3; IntAct=EBI-357966, EBI-357942;
CC P07910; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-357966, EBI-11988027;
CC P07910; Q12929: EPS8; NbExp=3; IntAct=EBI-357966, EBI-375576;
CC P07910; P09651: HNRNPA1; NbExp=3; IntAct=EBI-357966, EBI-352662;
CC P07910; P07910: HNRNPC; NbExp=8; IntAct=EBI-357966, EBI-357966;
CC P07910; O60812: HNRNPCL1; NbExp=3; IntAct=EBI-357966, EBI-1046507;
CC P07910; B2RXH8: HNRNPCL2; NbExp=3; IntAct=EBI-357966, EBI-9512317;
CC P07910; P42858: HTT; NbExp=7; IntAct=EBI-357966, EBI-466029;
CC P07910; Q9NQR1: KMT5A; NbExp=2; IntAct=EBI-357966, EBI-1268946;
CC P07910; P52292: KPNA2; NbExp=4; IntAct=EBI-357966, EBI-349938;
CC P07910; O00505: KPNA3; NbExp=5; IntAct=EBI-357966, EBI-358297;
CC P07910; O00629: KPNA4; NbExp=9; IntAct=EBI-357966, EBI-396343;
CC P07910; P25791: LMO2; NbExp=3; IntAct=EBI-357966, EBI-739696;
CC P07910; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-357966, EBI-16439278;
CC P07910; P26367: PAX6; NbExp=3; IntAct=EBI-357966, EBI-747278;
CC P07910; Q53GL6: RALY; NbExp=3; IntAct=EBI-357966, EBI-9512693;
CC P07910; Q9UKM9: RALY; NbExp=2; IntAct=EBI-357966, EBI-714796;
CC P07910; Q86SE5: RALYL; NbExp=7; IntAct=EBI-357966, EBI-741520;
CC P07910; Q86SE5-3: RALYL; NbExp=3; IntAct=EBI-357966, EBI-11526555;
CC P07910; Q96IZ5: RBM41; NbExp=5; IntAct=EBI-357966, EBI-740773;
CC P07910; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-357966, EBI-11987469;
CC P07910; P78317: RNF4; NbExp=3; IntAct=EBI-357966, EBI-2340927;
CC P07910; O00560: SDCBP; NbExp=6; IntAct=EBI-357966, EBI-727004;
CC P07910; Q9BYB0: SHANK3; NbExp=2; IntAct=EBI-357966, EBI-1752330;
CC P07910; P78362: SRPK2; NbExp=2; IntAct=EBI-357966, EBI-593303;
CC P07910; P63165: SUMO1; NbExp=6; IntAct=EBI-357966, EBI-80140;
CC P07910; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-357966, EBI-10175576;
CC P07910; Q13148: TARDBP; NbExp=3; IntAct=EBI-357966, EBI-372899;
CC P07910; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-357966, EBI-10180829;
CC P07910; P63104: YWHAZ; NbExp=2; IntAct=EBI-357966, EBI-347088;
CC P07910; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-357966, EBI-8656416;
CC P07910-2; P42858: HTT; NbExp=9; IntAct=EBI-5280084, EBI-466029;
CC P07910-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-5280084, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Component of ribonucleosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=C2;
CC IsoId=P07910-1; Sequence=Displayed;
CC Name=C1;
CC IsoId=P07910-2; Sequence=VSP_005831;
CC Name=3;
CC IsoId=P07910-3; Sequence=VSP_019225;
CC Name=4;
CC IsoId=P07910-4; Sequence=VSP_005831, VSP_019226;
CC -!- PTM: Phosphorylated on Ser-260 and Ser-299 in resting cells.
CC Phosphorylated on Ser-253 and on 1 serine residue in the poly-Ser
CC stretch at position 238 in response to hydrogen peroxide.
CC {ECO:0000269|PubMed:12564933}.
CC -!- PTM: Sumoylated. Sumoylation reduces affinity for mRNA.
CC {ECO:0000269|PubMed:15082759}.
CC -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92764.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M29063; AAA36576.1; -; mRNA.
DR EMBL; M16342; AAA52680.1; -; mRNA.
DR EMBL; BX161480; CAD61934.1; -; mRNA.
DR EMBL; BX247961; CAD62300.1; -; mRNA.
DR EMBL; BX247992; CAD62326.1; -; mRNA.
DR EMBL; AB209527; BAD92764.1; ALT_INIT; mRNA.
DR EMBL; AK223517; BAD97237.1; -; mRNA.
DR EMBL; CH471078; EAW66392.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66393.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66394.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66395.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66396.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66399.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66400.1; -; Genomic_DNA.
DR EMBL; BC003394; AAH03394.1; -; mRNA.
DR EMBL; BC007052; AAH07052.1; -; mRNA.
DR EMBL; BC008364; AAH08364.1; -; mRNA.
DR EMBL; BC008423; AAH08423.1; -; mRNA.
DR EMBL; BC066932; AAH66932.1; -; mRNA.
DR EMBL; BC089438; AAH89438.1; -; mRNA.
DR EMBL; BC108658; AAI08659.1; -; mRNA.
DR EMBL; BC103758; AAI03759.1; -; mRNA.
DR CCDS; CCDS41915.1; -. [P07910-1]
DR CCDS; CCDS45079.1; -. [P07910-2]
DR PIR; A26885; A26885.
DR PIR; C34504; C34504.
DR RefSeq; NP_001070910.1; NM_001077442.1. [P07910-1]
DR RefSeq; NP_001070911.1; NM_001077443.1. [P07910-2]
DR RefSeq; NP_004491.2; NM_004500.3. [P07910-2]
DR RefSeq; NP_112604.2; NM_031314.2. [P07910-1]
DR RefSeq; XP_006720188.1; XM_006720125.2. [P07910-2]
DR RefSeq; XP_011535010.1; XM_011536708.1. [P07910-1]
DR RefSeq; XP_011535011.1; XM_011536709.2. [P07910-1]
DR RefSeq; XP_011535012.1; XM_011536710.2. [P07910-1]
DR RefSeq; XP_011535013.1; XM_011536711.2. [P07910-1]
DR RefSeq; XP_011535014.1; XM_011536712.1. [P07910-2]
DR RefSeq; XP_016876741.1; XM_017021252.1. [P07910-2]
DR RefSeq; XP_016876742.1; XM_017021253.1. [P07910-2]
DR PDB; 1TXP; NMR; -; A/B/C/D=194-220.
DR PDB; 1WF2; NMR; -; A=8-92.
DR PDB; 2MXY; NMR; -; A=2-106.
DR PDB; 2MZ1; NMR; -; A=2-106.
DR PDB; 3LN4; X-ray; 1.30 A; C=102-117.
DR PDBsum; 1TXP; -.
DR PDBsum; 1WF2; -.
DR PDBsum; 2MXY; -.
DR PDBsum; 2MZ1; -.
DR PDBsum; 3LN4; -.
DR AlphaFoldDB; P07910; -.
DR BMRB; P07910; -.
DR SMR; P07910; -.
DR BioGRID; 109424; 506.
DR CORUM; P07910; -.
DR DIP; DIP-29854N; -.
DR IntAct; P07910; 210.
DR MINT; P07910; -.
DR STRING; 9606.ENSP00000451291; -.
DR ChEMBL; CHEMBL2216742; -.
DR GlyGen; P07910; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07910; -.
DR MetOSite; P07910; -.
DR PhosphoSitePlus; P07910; -.
DR SwissPalm; P07910; -.
DR BioMuta; HNRNPC; -.
DR DMDM; 108935845; -.
DR SWISS-2DPAGE; P07910; -.
DR EPD; P07910; -.
DR jPOST; P07910; -.
DR MassIVE; P07910; -.
DR MaxQB; P07910; -.
DR PaxDb; P07910; -.
DR PeptideAtlas; P07910; -.
DR PRIDE; P07910; -.
DR ProteomicsDB; 52034; -. [P07910-1]
DR ProteomicsDB; 52035; -. [P07910-2]
DR ProteomicsDB; 52036; -. [P07910-3]
DR ProteomicsDB; 52037; -. [P07910-4]
DR TopDownProteomics; P07910-1; -. [P07910-1]
DR TopDownProteomics; P07910-2; -. [P07910-2]
DR Antibodypedia; 3927; 488 antibodies from 38 providers.
DR DNASU; 3183; -.
DR Ensembl; ENST00000420743.6; ENSP00000404848.2; ENSG00000092199.19. [P07910-1]
DR Ensembl; ENST00000430246.6; ENSP00000442816.1; ENSG00000092199.19. [P07910-2]
DR Ensembl; ENST00000553300.6; ENSP00000450544.1; ENSG00000092199.19. [P07910-2]
DR Ensembl; ENST00000554455.5; ENSP00000451291.1; ENSG00000092199.19. [P07910-1]
DR Ensembl; ENST00000554969.5; ENSP00000450725.1; ENSG00000092199.19. [P07910-2]
DR Ensembl; ENST00000555883.5; ENSP00000450629.1; ENSG00000092199.19. [P07910-4]
DR Ensembl; ENST00000556628.5; ENSP00000451652.1; ENSG00000092199.19. [P07910-3]
DR Ensembl; ENST00000556897.5; ENSP00000451176.1; ENSG00000092199.19. [P07910-2]
DR Ensembl; ENST00000557201.5; ENSP00000452276.1; ENSG00000092199.19. [P07910-1]
DR GeneID; 3183; -.
DR KEGG; hsa:3183; -.
DR MANE-Select; ENST00000553300.6; ENSP00000450544.1; NM_004500.4; NP_004491.2. [P07910-2]
DR UCSC; uc001vzw.5; human. [P07910-1]
DR CTD; 3183; -.
DR DisGeNET; 3183; -.
DR GeneCards; HNRNPC; -.
DR HGNC; HGNC:5035; HNRNPC.
DR HPA; ENSG00000092199; Low tissue specificity.
DR MIM; 164020; gene.
DR neXtProt; NX_P07910; -.
DR OpenTargets; ENSG00000092199; -.
DR PharmGKB; PA162391217; -.
DR VEuPathDB; HostDB:ENSG00000092199; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153402; -.
DR InParanoid; P07910; -.
DR OrthoDB; 1211602at2759; -.
DR PhylomeDB; P07910; -.
DR TreeFam; TF330974; -.
DR PathwayCommons; P07910; -.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; P07910; -.
DR SIGNOR; P07910; -.
DR BioGRID-ORCS; 3183; 734 hits in 1025 CRISPR screens.
DR ChiTaRS; HNRNPC; human.
DR EvolutionaryTrace; P07910; -.
DR GeneWiki; HNRNPC; -.
DR GenomeRNAi; 3183; -.
DR Pharos; P07910; Tbio.
DR PRO; PR:P07910; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P07910; protein.
DR Bgee; ENSG00000092199; Expressed in ventricular zone and 178 other tissues.
DR ExpressionAtlas; P07910; baseline and differential.
DR Genevisible; P07910; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0031492; F:nucleosomal DNA binding; HDA:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IPI:BHF-UCL.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; HDA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017347; hnRNP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Direct protein sequencing; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT CHAIN 2..306
FT /note="Heterogeneous nuclear ribonucleoproteins C1/C2"
FT /id="PRO_0000081844"
FT DOMAIN 16..87
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 139..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..238
FT /evidence="ECO:0000255"
FT MOTIF 155..161
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 158..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z204"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 176
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z204"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12564933,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12564933,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12564933,
FT ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 223
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 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 39..119
FT /note="KYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKV
FT NRGKAGVKRSAAEMYGSVTEHPSPSPLLS -> N (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019225"
FT VAR_SEQ 108..120
FT /note="Missing (in isoform C1 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3110598, ECO:0000303|Ref.3"
FT /id="VSP_005831"
FT VAR_SEQ 153..195
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019226"
FT MUTAGEN 197
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:15082759"
FT MUTAGEN 250
FT /note="K->R: Loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:15082759"
FT CONFLICT 110
FT /note="E -> G (in Ref. 6; AAH08423)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="I -> M (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="Q -> R (in Ref. 6; AAH08364)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="K -> R (in Ref. 6; AAH08364)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="E -> G (in Ref. 6; AAH07052)"
FT /evidence="ECO:0000305"
FT CONFLICT 303..306
FT /note="EDDS -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:2MXY"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1WF2"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1WF2"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:1WF2"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2MZ1"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1WF2"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:1WF2"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:1WF2"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:1WF2"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1WF2"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2MXY"
FT HELIX 194..216
FT /evidence="ECO:0007829|PDB:1TXP"
FT MOD_RES P07910-2:107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES P07910-2:108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P07910-4:107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES P07910-4:108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 306 AA; 33670 MW; 17BBC78690C69C5C CRC64;
MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE
RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVTE HPSPSPLLSS
SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR
GSSKSGKLKG DDLQAIKKEL TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS
SVKKDETNVK MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA
NGEDDS
