TCRG1_HUMAN
ID TCRG1_HUMAN Reviewed; 1098 AA.
AC O14776; Q2NKN2; Q59EA1;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Transcription elongation regulator 1;
DE AltName: Full=TATA box-binding protein-associated factor 2S;
DE AltName: Full=Transcription factor CA150;
GN Name=TCERG1; Synonyms=CA150, TAF2S;
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), PROTEIN SEQUENCE OF 610-620;
RP 745-753; 928-939 AND 945-955, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RNA POLYMERASE II.
RC TISSUE=Cervix carcinoma;
RX PubMed=9315662; DOI=10.1128/mcb.17.10.6029;
RA Sune C., Hayashi T., Liu Y., Lane W.S., Young R.A., Garcia-Blanco M.A.;
RT "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme,
RT is involved in Tat-activated human immunodeficiency virus type 1
RT transcription.";
RL Mol. Cell. Biol. 17:6029-6039(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Aortic endothelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION
RP WITH RNA POLYMERASE II.
RX PubMed=10908677; DOI=10.1073/pnas.160266597;
RA Carty S.M., Goldstrohm A.C., Sune C., Garcia-Blanco M.A., Greenleaf A.L.;
RT "Protein-interaction modules that organize nuclear function: FF domains of
RT CA150 bind the phosphoCTD of RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9015-9020(2000).
RN [5]
RP FUNCTION, MUTAGENESIS OF 148-TYR--TYR-150; 446-TYR--TYR-448 AND
RP 545-PHE--TYR-547, AND INTERACTION WITH RNA POLYMERASE II AND SF1.
RX PubMed=11604498; DOI=10.1128/mcb.21.22.7617-7628.2001;
RA Goldstrohm A.C., Albrecht T.R., Sune C., Bedford M.T., Garcia-Blanco M.A.;
RT "The transcription elongation factor CA150 interacts with RNA polymerase II
RT and the pre-mRNA splicing factor SF1.";
RL Mol. Cell. Biol. 21:7617-7628(2001).
RN [6]
RP INTERACTION WITH HD, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11172033; DOI=10.1073/pnas.98.4.1811;
RA Holbert S., Denghien I., Kiechle T., Rosenblatt A., Wellington C.,
RA Hayden M.R., Margolis R.L., Ross C.A., Dausset J., Ferrante R.J., Neri C.;
RT "The Gln-Ala repeat transcriptional activator CA150 interacts with
RT huntingtin: neuropathologic and genetic evidence for a role in Huntington's
RT disease pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1811-1816(2001).
RN [7]
RP INTERACTION WITH HTATSF1, AND SUBCELLULAR LOCATION.
RX PubMed=15485897; DOI=10.1128/mcb.24.21.9274-9285.2004;
RA Smith M.J., Kulkarni S., Pawson T.;
RT "FF domains of CA150 bind transcription and splicing factors through
RT multiple weak interactions.";
RL Mol. Cell. Biol. 24:9274-9285(2004).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-638; SER-834 AND
RP SER-933, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-20; ARG-28; ARG-30; ARG-41 AND
RP ARG-48, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-503, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-503, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-503, AND IDENTIFICATION BY MASS
RP 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-503; LYS-507 AND LYS-608, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP STRUCTURE BY NMR OF 428-464.
RX PubMed=17060612; DOI=10.1073/pnas.0607815103;
RA Ferguson N., Becker J., Tidow H., Tremmel S., Sharpe T.D., Krause G.,
RA Flinders J., Petrovich M., Berriman J., Oschkinat H., Fersht A.R.;
RT "General structural motifs of amyloid protofilaments.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16248-16253(2006).
RN [16]
RP STRUCTURE BY NMR OF 520-959.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of WW domain and FF domains in transcription elongation
RT regulator 1.";
RL Submitted (APR-2007) to the PDB data bank.
CC -!- FUNCTION: Transcription factor that binds RNA polymerase II and
CC inhibits the elongation of transcripts from target promoters. Regulates
CC transcription elongation in a TATA box-dependent manner. Necessary for
CC TAT-dependent activation of the human immunodeficiency virus type 1
CC (HIV-1) promoter. {ECO:0000269|PubMed:11604498,
CC ECO:0000269|PubMed:9315662}.
CC -!- SUBUNIT: Binds formin (By similarity). Interacts (via the second WW
CC domain) with TREX1 (via proline-rich region) (By similarity). Binds RNA
CC polymerase II, HD and SF1. {ECO:0000250, ECO:0000269|PubMed:10908677,
CC ECO:0000269|PubMed:11172033, ECO:0000269|PubMed:11604498,
CC ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:9315662}.
CC -!- INTERACTION:
CC O14776; Q99728: BARD1; NbExp=2; IntAct=EBI-473271, EBI-473181;
CC O14776; P42858: HTT; NbExp=9; IntAct=EBI-473271, EBI-466029;
CC O14776; O14776: TCERG1; NbExp=4; IntAct=EBI-473271, EBI-473271;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10908677,
CC ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:9315662}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14776-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14776-2; Sequence=VSP_026933;
CC -!- TISSUE SPECIFICITY: Detected in brain neurons.
CC {ECO:0000269|PubMed:11172033}.
CC -!- INDUCTION: Up-regulated in brain tissue from patients with Huntington
CC disease. {ECO:0000269|PubMed:11172033}.
CC -!- DOMAIN: The FF domains bind the phosphorylated C-terminus of the
CC largest subunit of RNA polymerase II, probably mediate interaction with
CC HTATSF1 and preferentially bind peptides with the consensus sequence
CC [DE](2-5)-[FWY]-[DE](2-5).
CC -!- DOMAIN: The WW domains bind Pro-rich domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93147.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF017789; AAB80727.1; -; mRNA.
DR EMBL; AB209910; BAD93147.1; ALT_INIT; mRNA.
DR EMBL; BC111727; AAI11728.1; -; mRNA.
DR CCDS; CCDS4282.1; -. [O14776-1]
DR CCDS; CCDS43379.1; -. [O14776-2]
DR PIR; T08599; T08599.
DR RefSeq; NP_001035095.1; NM_001040006.1. [O14776-2]
DR RefSeq; NP_006697.2; NM_006706.3. [O14776-1]
DR PDB; 2DK7; NMR; -; A=520-579.
DR PDB; 2DOD; NMR; -; A=651-719.
DR PDB; 2DOE; NMR; -; A=784-853.
DR PDB; 2DOF; NMR; -; A=888-959.
DR PDB; 2E71; NMR; -; A=717-786.
DR PDB; 2KIQ; NMR; -; A=724-782.
DR PDB; 2KIS; NMR; -; A=659-724.
DR PDB; 2MW9; NMR; -; A=428-464.
DR PDB; 2MWA; NMR; -; A=428-464.
DR PDB; 2MWB; NMR; -; A=428-464.
DR PDB; 2MWD; NMR; -; A=433-460.
DR PDB; 2MWE; NMR; -; A=433-460.
DR PDB; 2MWF; NMR; -; A=433-464.
DR PDB; 2N4R; NMR; -; A=428-464.
DR PDB; 2N4S; NMR; -; A=428-464.
DR PDB; 2N4T; NMR; -; A=428-464.
DR PDB; 2N4U; NMR; -; A=428-464.
DR PDB; 2N4V; NMR; -; A=428-464.
DR PDB; 2N4W; NMR; -; A=428-464.
DR PDB; 2NNT; NMR; -; A/B/C/D=428-464.
DR PDB; 3HFH; X-ray; 2.70 A; A/B=661-845.
DR PDB; 3Q1I; X-ray; 1.40 A; E=99-107.
DR PDB; 4FQG; X-ray; 2.00 A; A/B=895-1081.
DR PDB; 7ABF; EM; 3.90 A; A4=1-1098.
DR PDB; 7ABG; EM; 7.80 A; A4=1-1098.
DR PDBsum; 2DK7; -.
DR PDBsum; 2DOD; -.
DR PDBsum; 2DOE; -.
DR PDBsum; 2DOF; -.
DR PDBsum; 2E71; -.
DR PDBsum; 2KIQ; -.
DR PDBsum; 2KIS; -.
DR PDBsum; 2MW9; -.
DR PDBsum; 2MWA; -.
DR PDBsum; 2MWB; -.
DR PDBsum; 2MWD; -.
DR PDBsum; 2MWE; -.
DR PDBsum; 2MWF; -.
DR PDBsum; 2N4R; -.
DR PDBsum; 2N4S; -.
DR PDBsum; 2N4T; -.
DR PDBsum; 2N4U; -.
DR PDBsum; 2N4V; -.
DR PDBsum; 2N4W; -.
DR PDBsum; 2NNT; -.
DR PDBsum; 3HFH; -.
DR PDBsum; 3Q1I; -.
DR PDBsum; 4FQG; -.
DR PDBsum; 7ABF; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; O14776; -.
DR SMR; O14776; -.
DR BioGRID; 116120; 133.
DR CORUM; O14776; -.
DR DIP; DIP-32504N; -.
DR IntAct; O14776; 36.
DR MINT; O14776; -.
DR STRING; 9606.ENSP00000296702; -.
DR CarbonylDB; O14776; -.
DR GlyGen; O14776; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14776; -.
DR MetOSite; O14776; -.
DR PhosphoSitePlus; O14776; -.
DR SwissPalm; O14776; -.
DR BioMuta; TCERG1; -.
DR EPD; O14776; -.
DR jPOST; O14776; -.
DR MassIVE; O14776; -.
DR MaxQB; O14776; -.
DR PaxDb; O14776; -.
DR PeptideAtlas; O14776; -.
DR PRIDE; O14776; -.
DR ProteomicsDB; 48229; -. [O14776-1]
DR ProteomicsDB; 48230; -. [O14776-2]
DR Antibodypedia; 15805; 194 antibodies from 27 providers.
DR DNASU; 10915; -.
DR Ensembl; ENST00000296702.9; ENSP00000296702.5; ENSG00000113649.13. [O14776-1]
DR Ensembl; ENST00000394421.7; ENSP00000377943.2; ENSG00000113649.13. [O14776-2]
DR GeneID; 10915; -.
DR KEGG; hsa:10915; -.
DR UCSC; uc003lob.4; human. [O14776-1]
DR CTD; 10915; -.
DR DisGeNET; 10915; -.
DR GeneCards; TCERG1; -.
DR HGNC; HGNC:15630; TCERG1.
DR HPA; ENSG00000113649; Low tissue specificity.
DR MalaCards; TCERG1; -.
DR MIM; 605409; gene.
DR neXtProt; NX_O14776; -.
DR OpenTargets; ENSG00000113649; -.
DR PharmGKB; PA38007; -.
DR VEuPathDB; HostDB:ENSG00000113649; -.
DR eggNOG; KOG0155; Eukaryota.
DR GeneTree; ENSGT00940000157770; -.
DR HOGENOM; CLU_008684_0_0_1; -.
DR InParanoid; O14776; -.
DR OMA; KPPGYKG; -.
DR OrthoDB; 1388955at2759; -.
DR PhylomeDB; O14776; -.
DR TreeFam; TF317748; -.
DR PathwayCommons; O14776; -.
DR SignaLink; O14776; -.
DR BioGRID-ORCS; 10915; 289 hits in 1094 CRISPR screens.
DR ChiTaRS; TCERG1; human.
DR EvolutionaryTrace; O14776; -.
DR GeneWiki; Transcription_elongation_regulator_1; -.
DR GenomeRNAi; 10915; -.
DR Pharos; O14776; Tbio.
DR PRO; PR:O14776; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O14776; protein.
DR Bgee; ENSG00000113649; Expressed in right hemisphere of cerebellum and 134 other tissues.
DR ExpressionAtlas; O14776; baseline and differential.
DR Genevisible; O14776; HS.
DR GO; GO:0016607; C:nuclear speck; TAS:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
DR GO; GO:0003711; F:transcription elongation regulator activity; TAS:ARUK-UCL.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:ARUK-UCL.
DR GO; GO:0006397; P:mRNA processing; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; TAS:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; TAS:ARUK-UCL.
DR GO; GO:0008380; P:RNA splicing; IDA:ARUK-UCL.
DR CDD; cd00201; WW; 3.
DR DisProt; DP01893; -.
DR Gene3D; 1.10.10.440; -; 6.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR045148; TCRG1-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR15377; PTHR15377; 2.
DR Pfam; PF01846; FF; 6.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00441; FF; 6.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF51045; SSF51045; 3.
DR SUPFAM; SSF81698; SSF81698; 5.
DR PROSITE; PS51676; FF; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Coiled coil;
KW Direct protein sequencing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1098
FT /note="Transcription elongation regulator 1"
FT /id="PRO_0000076063"
FT DOMAIN 131..164
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 429..462
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 528..561
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 659..712
FT /note="FF 1"
FT DOMAIN 725..779
FT /note="FF 2"
FT DOMAIN 791..846
FT /note="FF 3"
FT DOMAIN 896..952
FT /note="FF 4"
FT DOMAIN 954..1010
FT /note="FF 5"
FT DOMAIN 1012..1077
FT /note="FF 6"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..244
FT /evidence="ECO:0000255"
FT COILED 606..655
FT /evidence="ECO:0000255"
FT COILED 844..906
FT /evidence="ECO:0000255"
FT MOTIF 626..630
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 36..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 20
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 28
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 30
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 41
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 48
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 503
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 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 608
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 379..399
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_026933"
FT MUTAGEN 148..150
FT /note="YYY->AAA: Reduces repression of transcription by
FT 35%. Reduces repression of transcription by 63%; when
FT associated with 446-AAA-448."
FT /evidence="ECO:0000269|PubMed:11604498"
FT MUTAGEN 446..448
FT /note="YYY->AAA: Loss of interaction with SF1. Reduces
FT repression of transcription by 35%. Reduces repression of
FT transcription by 63%; when associated with 148-AAA-150."
FT /evidence="ECO:0000269|PubMed:11604498"
FT MUTAGEN 545..547
FT /note="FFY->AAA: No effect."
FT /evidence="ECO:0000269|PubMed:11604498"
FT CONFLICT 324
FT /note="P -> R (in Ref. 1; AAB80727)"
FT /evidence="ECO:0000305"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3Q1I"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:2MW9"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:2MW9"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:2MW9"
FT TURN 450..453
FT /evidence="ECO:0007829|PDB:2MW9"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:2MW9"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:2MW9"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:2DK7"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:2DK7"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:2DK7"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:2DK7"
FT TURN 549..552
FT /evidence="ECO:0007829|PDB:2DK7"
FT TURN 560..564
FT /evidence="ECO:0007829|PDB:2DK7"
FT HELIX 567..573
FT /evidence="ECO:0007829|PDB:2DK7"
FT TURN 576..578
FT /evidence="ECO:0007829|PDB:2DK7"
FT STRAND 652..656
FT /evidence="ECO:0007829|PDB:2DOD"
FT TURN 661..663
FT /evidence="ECO:0007829|PDB:3HFH"
FT HELIX 669..672
FT /evidence="ECO:0007829|PDB:3HFH"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:3HFH"
FT HELIX 681..689
FT /evidence="ECO:0007829|PDB:2DOD"
FT HELIX 692..696
FT /evidence="ECO:0007829|PDB:3HFH"
FT HELIX 705..710
FT /evidence="ECO:0007829|PDB:3HFH"
FT HELIX 713..720
FT /evidence="ECO:0007829|PDB:3HFH"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:2E71"
FT TURN 726..728
FT /evidence="ECO:0007829|PDB:3HFH"
FT HELIX 747..752
FT /evidence="ECO:0007829|PDB:3HFH"
FT HELIX 758..762
FT /evidence="ECO:0007829|PDB:2E71"
FT HELIX 773..780
FT /evidence="ECO:0007829|PDB:3HFH"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:2E71"
FT HELIX 798..804
FT /evidence="ECO:0007829|PDB:3HFH"
FT HELIX 814..821
FT /evidence="ECO:0007829|PDB:2DOE"
FT TURN 825..827
FT /evidence="ECO:0007829|PDB:3HFH"
FT HELIX 833..840
FT /evidence="ECO:0007829|PDB:3HFH"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:2DOF"
FT HELIX 895..910
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 918..925
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 929..934
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 939..966
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 977..984
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 988..991
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 997..1025
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 1033..1039
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 1042..1051
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 1055..1058
FT /evidence="ECO:0007829|PDB:4FQG"
FT TURN 1059..1062
FT /evidence="ECO:0007829|PDB:4FQG"
FT HELIX 1064..1076
FT /evidence="ECO:0007829|PDB:4FQG"
SQ SEQUENCE 1098 AA; 123901 MW; 5F0A0C3A07EBF00F CRC64;
MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP PPFGMMRGPP
PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM PPPMSSMPPP PGMMFPPGMP
PVTAPGTPAL PPTEEIWVEN KTPDGKVYYY NARTRESAWT KPDGVKVIQQ SELTPMLAAQ
AQVQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ
AQVQAQVQAQ VQAQAVGAST PTTSSPAPAV STSTSSSTPS STTSTTTTAT SVAQTVSTPT
TQDQTPSSAV SVATPTVSVS TPAPTATPVQ TVPQPHPQTL PPAVPHSVPQ PTTAIPAFPP
VMVPPFRVPL PGMPIPLPGV AMMQIVSCPY VKTVATTKTG VLPGMAPPIV PMIHPQVAIA
ASPATLAGAT AVSEWTEYKT ADGKTYYYNN RTLESTWEKP QELKEKEKLE EKIKEPIKEP
SEEPLPMETE EEDPKEEPIK EIKEEPKEEE MTEEEKAAQK AKPVATAPIP GTPWCVVWTG
DERVFFYNPT TRLSMWDRPD DLIGRADVDK IIQEPPHKKG MEELKKLRHP TPTMLSIQKW
QFSMSAIKEE QELMEEINED EPVKAKKRKR DDNKDIDSEK EAAMEAEIKA ARERAIVPLE
ARMKQFKDML LERGVSAFST WEKELHKIVF DPRYLLLNPK ERKQVFDQYV KTRAEEERRE
KKNKIMQAKE DFKKMMEEAK FNPRATFSEF AAKHAKDSRF KAIEKMKDRE ALFNEFVAAA
RKKEKEDSKT RGEKIKSDFF ELLSNHHLDS QSRWSKVKDK VESDPRYKAV DSSSMREDLF
KQYIEKIAKN LDSEKEKELE RQARIEASLR EREREVQKAR SEQTKEIDRE REQHKREEAI
QNFKALLSDM VRSSDVSWSD TRRTLRKDHR WESGSLLERE EKEKLFNEHI EALTKKKREH
FRQLLDETSA ITLTSTWKEV KKIIKEDPRC IKFSSSDRKK QREFEEYIRD KYITAKADFR
TLLKETKFIT YRSKKLIQES DQHLKDVEKI LQNDKRYLVL DCVPEERRKL IVAYVDDLDR
RGPPPPPTAS EPTRRSTK
