TF3C1_HUMAN
ID TF3C1_HUMAN Reviewed; 2109 AA.
AC Q12789; B2RP21; Q12838; Q6DKN9; Q9Y4W9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=General transcription factor 3C polypeptide 1;
DE AltName: Full=TF3C-alpha;
DE AltName: Full=TFIIIC box B-binding subunit;
DE AltName: Full=Transcription factor IIIC 220 kDa subunit;
DE Short=TFIIIC 220 kDa subunit;
DE Short=TFIIIC220;
DE AltName: Full=Transcription factor IIIC subunit alpha;
GN Name=GTF3C1;
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 1), AND PROTEIN SEQUENCE OF 1103-1121.
RX PubMed=8127861; DOI=10.1073/pnas.91.5.1652;
RA L'Etoile N.D., Fahnestock M.L., Shen Y., Aebersold R., Berk A.J.;
RT "Human transcription factor IIIC box B binding subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1652-1656(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1107-2109 (ISOFORM 2).
RC TISSUE=Brain, and Cervix;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-728 (ISOFORM 1).
RX PubMed=8164661; DOI=10.1128/mcb.14.5.3053-3064.1994;
RA Lagna G., Kovelman R., Sukegawa J., Roeder R.G.;
RT "Cloning and characterization of an evolutionarily divergent DNA-binding
RT subunit of mammalian TFIIIC.";
RL Mol. Cell. Biol. 14:3053-3064(1994).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1068, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1653, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1969, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739; SER-1062; SER-1632;
RP SER-1653; SER-1856; SER-1865 AND SER-1868, AND IDENTIFICATION BY MASS
RP 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 INTERACTION WITH MAF1.
RX PubMed=18377933; DOI=10.1016/j.jmb.2008.02.060;
RA Goodfellow S.J., Graham E.L., Kantidakis T., Marshall L., Coppins B.A.,
RA Oficjalska-Pham D., Gerard M., Lefebvre O., White R.J.;
RT "Regulation of RNA polymerase III transcription by Maf1 in mammalian
RT cells.";
RL J. Mol. Biol. 378:481-491(2008).
RN [12]
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 [13]
RP INTERACTION WITH IGHMBP2.
RX PubMed=19299493; DOI=10.1093/hmg/ddp134;
RA de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A.,
RA Mourelatos Z.;
RT "Biochemical and genetic evidence for a role of IGHMBP2 in the
RT translational machinery.";
RL Hum. Mol. Genet. 18:2115-2126(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1068; SER-1865 AND SER-1868,
RP AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1062; SER-1068; SER-1632;
RP SER-1653; SER-1865 AND SER-1868, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-739; SER-1062 AND
RP SER-1068, AND 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739; SER-1068; SER-1253;
RP SER-1611; SER-1632; SER-1653; SER-1865 AND SER-1868, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1911, 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-833 AND LYS-1142, 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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-529; LYS-770; LYS-833 AND
RP LYS-1142, AND 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).
CC -!- FUNCTION: Required for RNA polymerase III-mediated transcription.
CC Component of TFIIIC that initiates transcription complex assembly on
CC tRNA and is required for transcription of 5S rRNA and other stable
CC nuclear and cytoplasmic RNAs. Binds to the box B promoter element.
CC -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6
CC (PubMed:19299493). Interacts with IGHMBP2. Interacts with MAF1
CC (PubMed:18377933). {ECO:0000269|PubMed:18377933,
CC ECO:0000269|PubMed:19299493}.
CC -!- INTERACTION:
CC Q12789; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-357956, EBI-741181;
CC Q12789; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-357956, EBI-2548702;
CC Q12789; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-357956, EBI-10194128;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12789-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12789-3; Sequence=VSP_021819;
CC -!- SIMILARITY: Belongs to the TFIIIC subunit 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17985.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA85638.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential vector sequence at the N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U02619; AAA17985.1; ALT_FRAME; mRNA.
DR EMBL; AC002303; AAB67637.1; -; Genomic_DNA.
DR EMBL; AC025275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002551; AAC05811.1; -; Genomic_DNA.
DR EMBL; BC044857; AAH44857.1; -; mRNA.
DR EMBL; BC137229; AAI37230.1; -; mRNA.
DR EMBL; U06485; AAA85638.1; ALT_SEQ; mRNA.
DR CCDS; CCDS32414.1; -. [Q12789-2]
DR CCDS; CCDS66988.1; -. [Q12789-3]
DR PIR; B56011; B56011.
DR PIR; I38414; I38414.
DR RefSeq; NP_001273171.1; NM_001286242.1. [Q12789-3]
DR RefSeq; NP_001511.2; NM_001520.3. [Q12789-2]
DR AlphaFoldDB; Q12789; -.
DR BioGRID; 109230; 219.
DR CORUM; Q12789; -.
DR DIP; DIP-38212N; -.
DR IntAct; Q12789; 86.
DR MINT; Q12789; -.
DR STRING; 9606.ENSP00000348510; -.
DR GlyGen; Q12789; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12789; -.
DR MetOSite; Q12789; -.
DR PhosphoSitePlus; Q12789; -.
DR BioMuta; GTF3C1; -.
DR DMDM; 215274233; -.
DR EPD; Q12789; -.
DR jPOST; Q12789; -.
DR MassIVE; Q12789; -.
DR MaxQB; Q12789; -.
DR PaxDb; Q12789; -.
DR PeptideAtlas; Q12789; -.
DR PRIDE; Q12789; -.
DR ProteomicsDB; 58924; -. [Q12789-2]
DR ProteomicsDB; 58925; -. [Q12789-3]
DR Antibodypedia; 26269; 40 antibodies from 11 providers.
DR DNASU; 2975; -.
DR Ensembl; ENST00000356183.9; ENSP00000348510.4; ENSG00000077235.18. [Q12789-2]
DR Ensembl; ENST00000561623.5; ENSP00000455417.1; ENSG00000077235.18. [Q12789-3]
DR GeneID; 2975; -.
DR KEGG; hsa:2975; -.
DR MANE-Select; ENST00000356183.9; ENSP00000348510.4; NM_001520.4; NP_001511.2.
DR UCSC; uc002dou.4; human. [Q12789-2]
DR CTD; 2975; -.
DR DisGeNET; 2975; -.
DR GeneCards; GTF3C1; -.
DR HGNC; HGNC:4664; GTF3C1.
DR HPA; ENSG00000077235; Low tissue specificity.
DR MIM; 603246; gene.
DR neXtProt; NX_Q12789; -.
DR OpenTargets; ENSG00000077235; -.
DR PharmGKB; PA29052; -.
DR VEuPathDB; HostDB:ENSG00000077235; -.
DR eggNOG; KOG4560; Eukaryota.
DR GeneTree; ENSGT00390000008664; -.
DR HOGENOM; CLU_001556_1_0_1; -.
DR InParanoid; Q12789; -.
DR OMA; PHKVHVE; -.
DR OrthoDB; 143012at2759; -.
DR PhylomeDB; Q12789; -.
DR TreeFam; TF351624; -.
DR PathwayCommons; Q12789; -.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR SignaLink; Q12789; -.
DR SIGNOR; Q12789; -.
DR BioGRID-ORCS; 2975; 662 hits in 1071 CRISPR screens.
DR ChiTaRS; GTF3C1; human.
DR GeneWiki; GTF3C1; -.
DR GenomeRNAi; 2975; -.
DR Pharos; Q12789; Tbio.
DR PRO; PR:Q12789; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q12789; protein.
DR Bgee; ENSG00000077235; Expressed in lower esophagus mucosa and 203 other tissues.
DR ExpressionAtlas; Q12789; baseline and differential.
DR Genevisible; Q12789; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:GO_Central.
DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IBA:GO_Central.
DR GO; GO:0009303; P:rRNA transcription; TAS:ProtInc.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IC:HGNC-UCL.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IBA:GO_Central.
DR GO; GO:0009304; P:tRNA transcription; TAS:ProtInc.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IC:HGNC-UCL.
DR CDD; cd16169; Tau138_eWH; 1.
DR InterPro; IPR044210; Tfc3-like.
DR InterPro; IPR035625; Tfc3_eWH.
DR InterPro; IPR007309; TFIIIC_Bblock-bd.
DR PANTHER; PTHR15180; PTHR15180; 1.
DR Pfam; PF04182; B-block_TFIIIC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Ubl conjugation.
FT CHAIN 1..2109
FT /note="General transcription factor 3C polypeptide 1"
FT /id="PRO_0000209710"
FT REGION 467..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1823..1961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1229
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1653
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 1856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1865
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K284"
FT MOD_RES 1911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 529
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 770
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 833
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 1142
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 VAR_SEQ 1933..1957
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021819"
FT VARIANT 1889
FT /note="Q -> E (in dbSNP:rs35233306)"
FT /id="VAR_047534"
FT VARIANT 1959
FT /note="F -> S (in dbSNP:rs12919017)"
FT /id="VAR_047535"
FT VARIANT 2077
FT /note="E -> K (in dbSNP:rs2228248)"
FT /id="VAR_047536"
FT CONFLICT 141
FT /note="A -> P (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="A -> P (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> P (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> P (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="G -> A (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="L -> V (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1015..1018
FT /note="ARSS -> GRRR (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1256
FT /note="Q -> H (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1316
FT /note="V -> L (in Ref. 1; AAA17985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2109 AA; 238875 MW; 37A03135EFE695FC CRC64;
MDALESLLDE VALEGLDGLC LPALWSRLET RVPPFPLPLE PCTQEFLWRA LATHPGISFY
EEPRERPDLQ LQDRYEEIDL ETGILESRRD PVALEDVYPI HMILENKDGI QGSCRYFKER
KNITNDIRTK SLQPRCTMVE AFDRWGKKLI IVASQAMRYR ALIGQEGDPD LKLPDFSYCI
LERLGRSRWQ GELQRDLHTT AFKVDAGKLH YHRKILNKNG LITMQSHVIR LPTGAQQHSI
LLLLNRFHVD RRSKYDILME KLSVMLSTRT NHIETLGKLR EELGLCERTF KRLYQYMLNA
GLAKVVSLRL QEIHPECGPC KTKKGTDVMV RCLKLLKEFK RNDHDDDEDE EVISKTVPPV
DIVFERDMLT QTYDLIERRG TKGISQAEIR VAMNVGKLEA RMLCRLLQRF KVVKGFMEDE
GRQRTTKYIS CVFAEESDLS RQYQREKARS ELLTTVSLAS MQEESLLPEG EDTFLSESDS
EEERSSSKRR GRGSQKDTRA SANLRPKTQP HHSTPTKGGW KVVNLHPLKK QPPSFPGAAE
ERACQSLASR DSLLDTSSVS EPNVSFVSHC ADSNSGDIAV IEEVRMENPK ESSSSLKTGR
HSSGQDKPHE TYRLLKRRNL IIEAVTNLRL IESLFTIQKM IMDQEKQEGV STKCCKKSIV
RLVRNLSEEG LLRLYRTTVI QDGIKKKVDL VVHPSMDQND PLVRSAIEQV RFRISNSSTA
NRVKTSQPPV PQGEAEEDSQ GKEGPSGSGD SQLSASSRSE SGRMKKSDNK MGITPLRNYH
PIVVPGLGRS LGFLPKMPRL RVVHMFLWYL IYGHPASNTV EKPSFISERR TIKQESGRAG
VRPSSSGSAW EACSEAPSKG SQDGVTWEAE VELATETVYV DDASWMRYIP PIPVHRDFGF
GWALVSDILL CLPLSIFIQI VQVSYKVDNL EEFLNDPLKK HTLIRFLPRP IRQQLLYKRR
YIFSVVENLQ RLCYMGLLQF GPTEKFQDKD QVFIFLKKNA VIVDTTICDP HYNLARSSRP
FERRLYVLNS MQDVENYWFD LQCVCLNTPL GVVRCPRVRK NSSTDQGSDE EGSLQKEQES
AMDKHNLERK CAMLEYTTGS REVVDEGLIP GDGLGAAGLD SSFYGHLKRN WIWTSYIINQ
AKKENTAAEN GLTVRLQTFL SKRPMPLSAR GNSRLNIWGE ARVGSELCAG WEEQFEVDRE
PSLDRNRRVR GGKSQKRKRL KKDPGKKIKR KKKGEFPGEK SKRLRYHDEA DQSALQRMTR
LRVTWSMQED GLLVLCRIAS NVLNTKVKGP FVTWQVVRDI LHATFEESLD KTSHSVGRRA
RYIVKNPQAY LNYKVCLAEV YQDKALVGDF MNRRGDYDDP KVCANEFKEF VEKLKEKFSS
ALRNSNLEIP DTLQELFARY RVLAIGDEKD QTRKEDELNS VDDIHFLVLQ NLIQSTLALS
DSQMKSYQSF QTFRLYREYK DHVLVKAFME CQKRSLVNRR RVNHTLGPKK NRALPFVPMS
YQLSQTYYRI FTWRFPSTIC TESFQFLDRM RAAGKLDQPD RFSFKDQDNN EPTNDMVAFS
LDGPGGNCVA VLTLFSLGLI SVDVRIPEQI IVVDSSMVEN EVIKSLGKDG SLEDDEDEED
DLDEGVGGKR RSMEVKPAQA SHTNYLLMRG YYSPGIVSTR NLNPNDSIVV NSCQMKFQLR
CTPVPARLRP AAAPLEELTM GTSCLPDTFT KLINPQENTC SLEEFVLQLE LSGYSPEDLT
AALEILEAII ATGCFGIDKE ELRRRFSALE KAGGGRTRTF ADCIQALLEQ HQVLEVGGNT
ARLVAMGSAW PWLLHSVRLK DREDADIQRE DPQARPLEGS SSEDSPPEGQ APPSHSPRGT
KRRASWASEN GETDAEGTQM TPAKRPALQD SNLAPSLGPG AEDGAEAQAP SPPPALEDTA
AAGAAQEDQE GVGEFSSPGQ EQLSGQAQPP EGSEDPRGFT ESFGAANISQ AARERDCESV
CFIGRPWRVV DGHLNLPVCK GMMEAMLYHI MTRPGIPESS LLRHYQGVLQ PVAVLELLQG
LESLGCIRKR WLRKPRPVSL FSTPVVEEVE VPSSLDESPM AFYEPTLDCT LRLGRVFPHE
VNWNKWIHL
