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Database: UniProt
Entry: P43268
LinkDB: P43268
Original site: P43268 
ID   ETV4_HUMAN              Reviewed;         484 AA.
AC   P43268; A8K314; B7Z5J3; B7Z9J6; Q96AW9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 3.
DT   29-SEP-2021, entry version 179.
DE   RecName: Full=ETS translocation variant 4;
DE   AltName: Full=Adenovirus E1A enhancer-binding protein;
DE   AltName: Full=E1A-F;
DE   AltName: Full=Polyomavirus enhancer activator 3 homolog;
DE            Short=Protein PEA3;
GN   Name=ETV4; Synonyms=E1AF, PEA3;
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).
RX   PubMed=7774926; DOI=10.1016/0888-7543(95)80133-7;
RA   Friedman L.S., Ostermeyer E.A., Lynch E.D., Szabo C.I., Meza J.E.,
RA   Anderson L.A., Dowd P., Lee M.K., Rowell S.E., Ellison J., Boyd J.,
RA   King M.-C.;
RT   "22 genes from chromosome 17q21: cloning, sequencing, and characterization
RT   of mutations in breast cancer families and tumors.";
RL   Genomics 25:256-263(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10564827; DOI=10.1016/s0378-1119(99)00400-x;
RA   Coutte L., Monte D., Baert J.-L., de Launoit Y.;
RT   "Genomic organization of the human e1af gene, a member of Ets transcription
RT   factors.";
RL   Gene 240:201-207(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ILE-195.
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Colon;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 23-484 (ISOFORM 1), AND FUNCTION.
RX   PubMed=8441666; DOI=10.1093/nar/21.3.547;
RA   Higashino F., Yoshida K., Fujinaga K., Kamio K., Fujinaga K.;
RT   "Isolation of a cDNA encoding the adenovirus E1A enhancer binding protein:
RT   a new human member of the ets oncogene family.";
RL   Nucleic Acids Res. 21:547-553(1993).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   FUNCTION, SUMOYLATION AT LYS-96; LYS-226 AND LYS-260, DESUMOYLATION BY
RP   SENP1, PHOSPHORYLATION AT SER-101, UBIQUITINATION BY RNF4, DEUBIQUITINATION
RP   BY UPS2, AND MUTAGENESIS OF LYS-96; GLU-98; SER-101; PRO-102; LYS-226;
RP   GLU-228; LYS-260; GLU-262; GLU-324 AND GLU-443.
RX   PubMed=19307308; DOI=10.1128/mcb.01128-08;
RA   Guo B., Sharrocks A.D.;
RT   "Extracellular signal-regulated kinase mitogen-activated protein kinase
RT   signaling initiates a dynamic interplay between sumoylation and
RT   ubiquitination to regulate the activity of the transcriptional activator
RT   PEA3.";
RL   Mol. Cell. Biol. 29:3204-3218(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-149, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-322, 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   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-139, AND IDENTIFICATION
RP   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   [12]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=31552090; DOI=10.3389/fgene.2019.00775;
RA   Finnegan A., Cho R.J., Luu A., Harirchian P., Lee J., Cheng J.B.,
RA   Song J.S.;
RT   "Single-Cell Transcriptomics Reveals Spatial and Temporal Turnover of
RT   Keratinocyte Differentiation Regulators.";
RL   Front. Genet. 10:775-775(2019).
CC   -!- FUNCTION: Transcriptional activator (PubMed:19307308, PubMed:31552090).
CC       May play a role in keratinocyte differentiation (PubMed:31552090).
CC       {ECO:0000269|PubMed:19307308, ECO:0000269|PubMed:31552090}.
CC   -!- FUNCTION: (Microbial infection) Binds to the enhancer of the adenovirus
CC       E1A gene and acts as a transcriptional activator; the core-binding
CC       sequence is 5'-[AC]GGA[AT]GT-3'. {ECO:0000269|PubMed:8441666}.
CC   -!- INTERACTION:
CC       P43268; Q16236: NFE2L2; NbExp=6; IntAct=EBI-6447147, EBI-2007911;
CC       P43268; P14079: tax; Xeno; NbExp=3; IntAct=EBI-6447147, EBI-9675698;
CC       P43268-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12130722, EBI-16439278;
CC       P43268-3; Q13485: SMAD4; NbExp=3; IntAct=EBI-12130722, EBI-347263;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P43268-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P43268-2; Sequence=VSP_046036;
CC       Name=3;
CC         IsoId=P43268-3; Sequence=VSP_055314;
CC   -!- TISSUE SPECIFICITY: Expressed in keratinocytes.
CC       {ECO:0000269|PubMed:31552090}.
CC   -!- PTM: Sumoylated; enhanced upon ERK/MAP kinase pathway activation, it
CC       positively regulates the transcriptional activator capacity.
CC       Sumoylation at Lys-96 probably requires phosphorylation at Ser-101.
CC       Transiently polysumoylated and desumoylated by SENP1. Sumoylation is a
CC       prerequisite to polyubiquitination which in turn increases proteasomal-
CC       mediated degradation. Probably polyubiquitinated by RNF4 and
CC       deubiquitinated by USP2. {ECO:0000269|PubMed:19307308}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA95991.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ETV4ID133ch17q21.html";
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DR   EMBL; U18018; AAA95991.1; ALT_INIT; mRNA.
DR   EMBL; AF095890; AAD09186.1; -; Genomic_DNA.
DR   EMBL; AF095887; AAD09186.1; JOINED; Genomic_DNA.
DR   EMBL; AF095888; AAD09186.1; JOINED; Genomic_DNA.
DR   EMBL; AF095889; AAD09186.1; JOINED; Genomic_DNA.
DR   EMBL; AK290429; BAF83118.1; -; mRNA.
DR   EMBL; AK299019; BAH12929.1; -; mRNA.
DR   EMBL; AK315961; BAH14332.1; -; mRNA.
DR   EMBL; AC068675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007242; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC016623; AAH16623.1; -; mRNA.
DR   EMBL; D12765; BAA02234.1; -; mRNA.
DR   CCDS; CCDS11465.1; -. [P43268-1]
DR   CCDS; CCDS58553.1; -. [P43268-2]
DR   CCDS; CCDS59292.1; -. [P43268-3]
DR   PIR; S35534; S35534.
DR   RefSeq; NP_001073143.1; NM_001079675.2. [P43268-1]
DR   RefSeq; NP_001248366.1; NM_001261437.1. [P43268-2]
DR   RefSeq; NP_001248367.1; NM_001261438.1. [P43268-2]
DR   RefSeq; NP_001248368.1; NM_001261439.1. [P43268-3]
DR   RefSeq; NP_001977.1; NM_001986.2. [P43268-1]
DR   PDB; 4CO8; X-ray; 1.05 A; A=338-470.
DR   PDB; 4UUV; X-ray; 2.80 A; A/D/G/J/M/P/S/V=338-435.
DR   PDB; 5ILU; X-ray; 1.10 A; A=340-436.
DR   PDBsum; 4CO8; -.
DR   PDBsum; 4UUV; -.
DR   PDBsum; 5ILU; -.
DR   SMR; P43268; -.
DR   BioGRID; 108419; 17.
DR   DIP; DIP-748N; -.
DR   IntAct; P43268; 9.
DR   STRING; 9606.ENSP00000321835; -.
DR   iPTMnet; P43268; -.
DR   PhosphoSitePlus; P43268; -.
DR   BioMuta; ETV4; -.
DR   DMDM; 62512145; -.
DR   EPD; P43268; -.
DR   jPOST; P43268; -.
DR   MassIVE; P43268; -.
DR   MaxQB; P43268; -.
DR   PaxDb; P43268; -.
DR   PeptideAtlas; P43268; -.
DR   PRIDE; P43268; -.
DR   ProteomicsDB; 55606; -. [P43268-1]
DR   ProteomicsDB; 6696; -.
DR   Antibodypedia; 890; 300 antibodies.
DR   DNASU; 2118; -.
DR   Ensembl; ENST00000319349; ENSP00000321835; ENSG00000175832. [P43268-1]
DR   Ensembl; ENST00000393664; ENSP00000377273; ENSG00000175832. [P43268-1]
DR   Ensembl; ENST00000538265; ENSP00000443846; ENSG00000175832. [P43268-2]
DR   Ensembl; ENST00000545954; ENSP00000440023; ENSG00000175832. [P43268-2]
DR   Ensembl; ENST00000586826; ENSP00000468636; ENSG00000175832. [P43268-3]
DR   Ensembl; ENST00000591713; ENSP00000465718; ENSG00000175832. [P43268-1]
DR   GeneID; 2118; -.
DR   KEGG; hsa:2118; -.
DR   UCSC; uc002idv.5; human. [P43268-1]
DR   CTD; 2118; -.
DR   DisGeNET; 2118; -.
DR   GeneCards; ETV4; -.
DR   HGNC; HGNC:3493; ETV4.
DR   HPA; ENSG00000175832; Tissue enhanced (gallbladder).
DR   MalaCards; ETV4; -.
DR   MIM; 600711; gene.
DR   neXtProt; NX_P43268; -.
DR   OpenTargets; ENSG00000175832; -.
DR   Orphanet; 319; Skeletal Ewing sarcoma.
DR   PharmGKB; PA27907; -.
DR   VEuPathDB; HostDB:ENSG00000175832; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000158142; -.
DR   HOGENOM; CLU_030025_1_0_1; -.
DR   InParanoid; P43268; -.
DR   OMA; PLDVCHS; -.
DR   OrthoDB; 536648at2759; -.
DR   PhylomeDB; P43268; -.
DR   TreeFam; TF316214; -.
DR   PathwayCommons; P43268; -.
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   SignaLink; P43268; -.
DR   SIGNOR; P43268; -.
DR   BioGRID-ORCS; 2118; 11 hits in 1051 CRISPR screens.
DR   ChiTaRS; ETV4; human.
DR   GeneWiki; ETV4; -.
DR   GenomeRNAi; 2118; -.
DR   Pharos; P43268; Tbio.
DR   PRO; PR:P43268; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P43268; protein.
DR   Bgee; ENSG00000175832; Expressed in cingulate cortex and 171 other tissues.
DR   ExpressionAtlas; P43268; baseline and differential.
DR   Genevisible; P43268; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005694; C:chromosome; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
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   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR006715; ETS_PEA3_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF04621; ETS_PEA3_N; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; DNA-binding;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..484
FT                   /note="ETS translocation variant 4"
FT                   /id="PRO_0000204116"
FT   DNA_BIND        341..421
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          90..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50549"
FT   CROSSLNK        6
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        96
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   CROSSLNK        139
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        226
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   CROSSLNK        260
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   CROSSLNK        322
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297"
FT   VAR_SEQ         1..277
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055314"
FT   VAR_SEQ         1..39
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046036"
FT   VARIANT         195
FT                   /note="F -> I (in dbSNP:rs150119757)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_069110"
FT   VARIANT         437
FT                   /note="R -> C (in dbSNP:rs34260468)"
FT                   /id="VAR_048950"
FT   MUTAGEN         96
FT                   /note="K->R: Altered sumoylation pattern. Loss of
FT                   sumoylation, ubiquitination and transcriptional activator
FT                   function; when associated with R-226 and R-260."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         98
FT                   /note="E->A: Loss of polysumoylation and ubiquitination;
FT                   when associated with A-228; A-262; A-324 and A-443."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         101
FT                   /note="S->A: Loss of sumoylation at K-96."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         101
FT                   /note="S->E: Normal sumoylation at K-96."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         102
FT                   /note="P->A: Loss of sumoylation at K-96."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         226
FT                   /note="K->R: Altered sumoylation pattern. Loss of
FT                   sumoylation, ubiquitination and transcriptional activator
FT                   function; when associated with R-96 and R-260."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         228
FT                   /note="E->A: Loss of polysumoylation and ubiquitination;
FT                   when associated with A-98; A-262; A-324 and A-443."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         260
FT                   /note="K->R: Altered sumoylation pattern. Loss of
FT                   sumoylation, ubiquitination and transcriptional activator
FT                   function; when associated with R-96 and R-226."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         262
FT                   /note="E->A: Loss of polysumoylation and ubiquitination;
FT                   when associated with A-98; A-228; A-324 and A-443."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         324
FT                   /note="E->A: Loss of polysumoylation and ubiquitination;
FT                   when associated with A-98; A-228; A-262 and A-443."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   MUTAGEN         443
FT                   /note="E->A: Loss of polysumoylation and ubiquitination;
FT                   when associated with A-98; A-228; A-262 and A-324."
FT                   /evidence="ECO:0000269|PubMed:19307308"
FT   CONFLICT        24..27
FT                   /note="GNGS -> EMSD (in Ref. 6; BAA02234)"
FT                   /evidence="ECO:0000305"
FT   HELIX           343..352
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   HELIX           354..356
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   TURN            357..359
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   STRAND          368..373
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   HELIX           374..385
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   HELIX           392..404
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   STRAND          407..410
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   STRAND          415..420
FT                   /evidence="ECO:0007829|PDB:4CO8"
FT   HELIX           424..431
FT                   /evidence="ECO:0007829|PDB:4CO8"
SQ   SEQUENCE   484 AA;  53938 MW;  BA9864F3C690A8C1 CRC64;
     MERRMKAGYL DQQVPYTFSS KSPGNGSLRE ALIGPLGKLM DPGSLPPLDS EDLFQDLSHF
     QETWLAEAQV PDSDEQFVPD FHSENLAFHS PTTRIKKEPQ SPRTDPALSC SRKPPLPYHH
     GEQCLYSSAY DPPRQIAIKS PAPGALGQSP LQPFPRAEQR NFLRSSGTSQ PHPGHGYLGE
     HSSVFQQPLD ICHSFTSQGG GREPLPAPYQ HQLSEPCPPY PQQSFKQEYH DPLYEQAGQP
     AVDQGGVNGH RYPGAGVVIK QEQTDFAYDS DVTGCASMYL HTEGFSGPSP GDGAMGYGYE
     KPLRPFPDDV CVVPEKFEGD IKQEGVGAFR EGPPYQRRGA LQLWQFLVAL LDDPTNAHFI
     AWTGRGMEFK LIEPEEVARL WGIQKNRPAM NYDKLSRSLR YYYEKGIMQK VAGERYVYKF
     VCEPEALFSL AFPDNQRPAL KAEFDRPVSE EDTVPLSHLD ESPAYLPELA GPAQPFGPKG
     GYSY
//
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