TCF20_MOUSE
ID TCF20_MOUSE Reviewed; 1987 AA.
AC Q9EPQ8; B9EHJ7; Q60792;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transcription factor 20;
DE Short=TCF-20;
DE AltName: Full=Nuclear factor SPBP;
DE AltName: Full=Stromelysin-1 PDGF-responsive element-binding protein;
DE Short=SPRE-binding protein;
GN Name=Tcf20; Synonyms=Spbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10995766; DOI=10.1074/jbc.m006978200;
RA Rekdal C., Sjoettem E., Johansen T.;
RT "The nuclear factor SPBP contains different functional domains and
RT stimulates the activity of various transcriptional activators.";
RL J. Biol. Chem. 275:40288-40300(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 774-1965 (ISOFORM 2), AND FUNCTION.
RC TISSUE=Fibroblast;
RX PubMed=7760812; DOI=10.1128/mcb.15.6.3164;
RA Sanz L., Moscat J., Diaz-Meco M.T.;
RT "Molecular characterization of a novel transcription factor that controls
RT stromelysin expression.";
RL Mol. Cell. Biol. 15:3164-3170(1995).
RN [5]
RP INTERACTION WITH JUN.
RX PubMed=8663478; DOI=10.1074/jbc.271.30.18231;
RA Kirstein M., Sanz L., Moscat J., Diaz-Meco M.T., Saus J.;
RT "Cross-talk between different enhancer elements during mitogenic induction
RT of the human stromelysin-1 gene.";
RL J. Biol. Chem. 271:18231-18236(1996).
RN [6]
RP INTERACTION WITH RNF4, TISSUE SPECIFICITY, AND MUTAGENESIS.
RX PubMed=10849425; DOI=10.1074/jbc.m003405200;
RA Lyngsoe C., Bouteiller G., Damgaard C.K., Ryom D., Sanchez-Munoz S.,
RA Noerby P.L., Bonven B.J., Joergensen P.;
RT "Interaction between the transcription factor SPBP and the positive
RT cofactor RNF4. An interplay between protein binding zinc fingers.";
RL J. Biol. Chem. 275:26144-26149(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; THR-1790 AND THR-1792,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-631, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Transcriptional activator that binds to the regulatory region
CC of MMP3 and thereby controls stromelysin expression. It stimulates the
CC activity of various transcriptional activators such as JUN, SP1, PAX6
CC and ETS1, suggesting a function as a coactivator.
CC {ECO:0000269|PubMed:7760812}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with RNF4 and JUN. Binds to
CC the regulatory region of MMP3. {ECO:0000269|PubMed:10849425,
CC ECO:0000269|PubMed:8663478, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:7760812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EPQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EPQ8-2; Sequence=VSP_003986;
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, liver, kidney and testes.
CC {ECO:0000269|PubMed:10849425}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is exclusively expressed at 7-11 days of
CC development. Isoform 1 is found only at low levels in 15-17 days
CC embryos.
CC -!- DOMAIN: The atypical PHD domain functions as a negative modulator of
CC cofactor binding.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA86495.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY007594; AAG28929.1; -; mRNA.
DR EMBL; AC087902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138038; AAI38039.1; -; mRNA.
DR EMBL; U20284; AAA86495.1; ALT_FRAME; mRNA.
DR CCDS; CCDS27693.1; -. [Q9EPQ8-2]
DR CCDS; CCDS49681.1; -. [Q9EPQ8-1]
DR RefSeq; NP_001107612.1; NM_001114140.1. [Q9EPQ8-1]
DR RefSeq; XP_006520795.1; XM_006520732.2. [Q9EPQ8-1]
DR RefSeq; XP_006520796.1; XM_006520733.1. [Q9EPQ8-1]
DR RefSeq; XP_011243853.1; XM_011245551.2. [Q9EPQ8-1]
DR RefSeq; XP_011243855.1; XM_011245553.2. [Q9EPQ8-2]
DR AlphaFoldDB; Q9EPQ8; -.
DR SMR; Q9EPQ8; -.
DR BioGRID; 204004; 6.
DR IntAct; Q9EPQ8; 2.
DR MINT; Q9EPQ8; -.
DR STRING; 10090.ENSMUSP00000105136; -.
DR iPTMnet; Q9EPQ8; -.
DR PhosphoSitePlus; Q9EPQ8; -.
DR EPD; Q9EPQ8; -.
DR jPOST; Q9EPQ8; -.
DR MaxQB; Q9EPQ8; -.
DR PaxDb; Q9EPQ8; -.
DR PeptideAtlas; Q9EPQ8; -.
DR PRIDE; Q9EPQ8; -.
DR ProteomicsDB; 263146; -. [Q9EPQ8-1]
DR ProteomicsDB; 263147; -. [Q9EPQ8-2]
DR DNASU; 21411; -.
DR Ensembl; ENSMUST00000048966; ENSMUSP00000048486; ENSMUSG00000041852. [Q9EPQ8-2]
DR Ensembl; ENSMUST00000109510; ENSMUSP00000105136; ENSMUSG00000041852. [Q9EPQ8-1]
DR GeneID; 21411; -.
DR KEGG; mmu:21411; -.
DR UCSC; uc007wzo.3; mouse. [Q9EPQ8-1]
DR UCSC; uc007wzp.3; mouse. [Q9EPQ8-2]
DR CTD; 6942; -.
DR MGI; MGI:108399; Tcf20.
DR VEuPathDB; HostDB:ENSMUSG00000041852; -.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000157896; -.
DR HOGENOM; CLU_234705_0_0_1; -.
DR InParanoid; Q9EPQ8; -.
DR OMA; LNRQHQM; -.
DR PhylomeDB; Q9EPQ8; -.
DR TreeFam; TF331317; -.
DR BioGRID-ORCS; 21411; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Tcf20; mouse.
DR PRO; PR:Q9EPQ8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9EPQ8; protein.
DR Bgee; ENSMUSG00000041852; Expressed in rostral migratory stream and 243 other tissues.
DR ExpressionAtlas; Q9EPQ8; baseline and differential.
DR Genevisible; Q9EPQ8; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15699; ePHD_TCF20; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR041972; TCF-20_ePHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 1.
DR PROSITE; PS51805; EPHD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1987
FT /note="Transcription factor 20"
FT /id="PRO_0000072449"
FT DNA_BIND 1565..1579
FT /note="A.T hook"
FT ZN_FING 1856..1892
FT /note="C2HC pre-PHD-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 1912..1960
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1219
FT /note="Leucine-zipper"
FT REGION 1415..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1760..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1966..1987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1282..1295
FT /note="Nuclear localization signal"
FT MOTIF 1604..1628
FT /note="Nuclear localization signal"
FT MOTIF 1812..1819
FT /note="Nuclear localization signal"
FT COMPBIAS 1..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1623
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1692..1710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1773..1803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1842..1858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 994
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1052
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1699
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT MOD_RES 1790
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1792
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 739
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 762
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 777
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 852
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 861
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 873
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 949
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 951
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 958
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 958
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 985
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1043
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1206
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1538
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1552
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT CROSSLNK 1641
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UGU0"
FT VAR_SEQ 1961..1987
FT /note="PPLPCPLPPLQNKTAKGSLSTEQSERG -> VRLWR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10995766,
FT ECO:0000303|PubMed:7760812"
FT /id="VSP_003986"
FT MUTAGEN 1629
FT /note="A->T: Loss of interaction with RNF4; when associated
FT with S-1702; R-1736 and V-1737."
FT /evidence="ECO:0000269|PubMed:10849425"
FT MUTAGEN 1702
FT /note="P->S: Loss of interaction with RNF4; when associated
FT with T-1629; R-1736 and V-1737."
FT /evidence="ECO:0000269|PubMed:10849425"
FT MUTAGEN 1736..1737
FT /note="CG->RV: Loss of interaction with RNF4; when
FT associated with T-1629 and S-1702."
FT /evidence="ECO:0000269|PubMed:10849425"
FT MUTAGEN 1926
FT /note="C->A: Reduces the inhibitory effect of the atypical
FT PHD domain."
FT /evidence="ECO:0000269|PubMed:10849425"
FT MUTAGEN 1931
FT /note="C->A: Reduces the inhibitory effect of the atypical
FT PHD domain."
FT /evidence="ECO:0000269|PubMed:10849425"
FT MUTAGEN 1936
FT /note="H->L: Reduces the inhibitory effect of the atypical
FT PHD domain."
FT /evidence="ECO:0000269|PubMed:10849425"
FT MUTAGEN 1939
FT /note="C->A: Reduces the inhibitory effect of the atypical
FT PHD domain."
FT /evidence="ECO:0000269|PubMed:10849425"
FT CONFLICT 355
FT /note="H -> R (in Ref. 1; AAG28929)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="M -> I (in Ref. 1; AAG28929)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="M -> L (in Ref. 1; AAG28929)"
FT /evidence="ECO:0000305"
FT CONFLICT 954
FT /note="S -> G (in Ref. 1; AAG28929)"
FT /evidence="ECO:0000305"
FT CONFLICT 1022
FT /note="R -> I (in Ref. 4; AAA86495)"
FT /evidence="ECO:0000305"
FT CONFLICT 1082
FT /note="P -> R (in Ref. 4; AAA86495)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="R -> G (in Ref. 4; AAA86495)"
FT /evidence="ECO:0000305"
FT CONFLICT 1201
FT /note="K -> Q (in Ref. 1; AAG28929)"
FT /evidence="ECO:0000305"
FT CONFLICT 1216
FT /note="C -> R (in Ref. 1; AAG28929)"
FT /evidence="ECO:0000305"
FT CONFLICT 1297
FT /note="Q -> R (in Ref. 4; AAA86495)"
FT /evidence="ECO:0000305"
FT CONFLICT 1418
FT /note="S -> G (in Ref. 4; AAA86495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1987 AA; 215683 MW; DB6EE205C311DB59 CRC64;
MQSFREQSSY HGNQQSYPQE VHSSSRIEEF SPRQAQMFQN FGGAGGGSSG TGSSSSGRRG
TAAAAAAMAS ETSGHQGYQG FRKEAGDFYY MAGNKDTVAA GTPQPPQRRP SGPVQSYGPP
QGSSFGNQYA SEGHVSQFQA QHSALGGVSH YQQDYTGPFS PGSAQYQQQA SSQQQQQQQQ
QQQQQQQQQQ QQVQQLRQQL YQSHQPLPQT TGQPASGSSH LQPMQRPSTL PSSAGYQLRV
GQFGQHYQSS ASSSSSSSFP SPQRFSQSGQ SYDGSYSVNA GSQYEGHNVG SNAQAYGTQS
NYSYQPQSMK NFEQAKIPPG NQQGQQQQQQ QPQPQQQQPQ QQQQQQQQQQ HPPQHVMQYT
NAATKMPLQS QVGQYNQPEV PVRSPMQFHQ NFSPISNPSP AASVVQSPSC SSTPSPLMQS
GENLQCGQGN VPMSSRNRIL QLMPQLSPTP SMMPSPNSHA AGFKGFGLEG VPEKRLTDPG
LSSLSALSSQ VANLPNTVQH MLLSDALTPQ KKTSKRPSSS SKKADSCTNS EGSSQPEEQL
KSPMAESLDG GCSSSSEDQG ERVRQLSGQS TSSDTTYKCG ASEKAGSSPT QGAQNEAPRL
STSPATRDEA ASPGAKDTSL SSEGNTKVNE KTVGVIVSRE AMTGRVEKSG GQDKGSQEDD
PAASQRPPSN SGVKEISHTS LPQPDPPGGG SKGNKNGDNN SSNHNGEGNG PSSHSAVGPS
FTGRTEPSKS PGSLRYSYKE SFGSAVPRNV SGYPQYPSGQ EKGDFGSHGE RKGRNEKFPS
LLQEVLQGYH HHPDRRYPRS AQEHQGMASG LEGTARPNIL VSQTNELASR GLLNKSIGSL
LENPHWGPWE RKSSSTAPEM KQINLSDYPI PRKFEIEPPS SAHEPGGSLS ERRSVICDIS
PLRQIVRDPG AHSLGHMGTD ARIGRNERLN PSLSQSVILP GGLVSMETKL KSQSGQIKEE
DFEQSKSQAS FNKKSGDHCH PTSIKHETYR GNASPGAAAH DSISDYGPQD SRSTPMRRVP
GRVGSRETMR GRSSSQYHDF AEKLKMSPGR SRGPGGDPHH MNPHMTFSER ANRSSLHAPF
SPNSESLASA YHTNTRAHAY GDPNTGLNSQ LHYKRQMYQQ QQEEYKDWAS SSAQGVIAAA
QHRQEGPRKS PRQQQFLDRV RSPLKNDKDG MMYGPPVGTY HDPSTQEAGR CLMSSDGLPA
KSMELKHSSQ KLQESCWDLS RQTSPAKSSG PPGMSNQKRY GPPHEPDGHG LAESAQSSKP
SNVMLRLPGQ EDHSSQNPLI MRRRVRSFIS PIPSKRQSQD VKNSNADDKG RLLHPSKEGA
DKAYNSYSHL SHSQDIKSIP KRDSSKDLPN PDNRNCPAVT LTSPAKTKIL PPRKGRGLKL
EAIVQKITSP NIRRSASANS AEAGGDTVTL DDILSLKSGP PEGGTVATQE AEMEKRKCEV
VSDLVSVTNQ ESNVEKPLPG PSEEWRGSGD DKVKTEAHVE TASTGKEPSG TMTSTASQKP
GGNQGRPDGS LGGAAPLIFP DSKNVAPVGI LAPEANPKAE EKENDTVMIS PKQESFPPKG
YFPSGKKKGR PIGSVNKQKK QQQQPPPPPQ PPQMPEGSAD GEPKPKKQRQ RRERRKPGAQ
PRKRKTKQAV PIVEPQEPEI KLKYATQPLD KTDAKNKSFF PYIHVVNKCE LGAVCTIINA
EEEEQTKLVR SRKGQRSLTP PPSSTESKVL PASSFMLQGP VVTESSVMGH LVCCLCGKWA
SYRNMGDLFG PFYPQDYAAT LPKNPPPKRS SEMQSKVKVR HKSASNGSKT DTEEEEEQQQ
QKEQRSLAAH PRFKRRHRSE DCGGGPRSLS RGLPCKKAAT EGSSEKTVSD TKPSVPTTSE
GGPELELQIP ELPLDSNEFW VHEGCILWAN GIYLVCGRLY GLQEALEIAR EMKCSHCQEA
GATLGCYNKG CSFRYHYPCA IDADCLLHEE NFSVRCPKHK PPLPCPLPPL QNKTAKGSLS
TEQSERG
