ETV4_HUMAN
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 03-AUG-2022, entry version 182.
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 AlphaFoldDB; P43268; -.
DR SMR; P43268; -.
DR BioGRID; 108419; 67.
DR DIP; DIP-748N; -.
DR IntAct; P43268; 54.
DR MINT; P43268; -.
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; 317 antibodies from 37 providers.
DR DNASU; 2118; -.
DR Ensembl; ENST00000319349.10; ENSP00000321835.4; ENSG00000175832.13. [P43268-1]
DR Ensembl; ENST00000393664.6; ENSP00000377273.1; ENSG00000175832.13. [P43268-1]
DR Ensembl; ENST00000538265.5; ENSP00000443846.1; ENSG00000175832.13. [P43268-2]
DR Ensembl; ENST00000545954.5; ENSP00000440023.1; ENSG00000175832.13. [P43268-2]
DR Ensembl; ENST00000586826.1; ENSP00000468636.1; ENSG00000175832.13. [P43268-3]
DR Ensembl; ENST00000591713.5; ENSP00000465718.1; ENSG00000175832.13. [P43268-1]
DR GeneID; 2118; -.
DR KEGG; hsa:2118; -.
DR MANE-Select; ENST00000319349.10; ENSP00000321835.4; NM_001079675.5; NP_001073143.1.
DR UCSC; uc002idv.5; human. [P43268-1]
DR CTD; 2118; -.
DR DisGeNET; 2118; -.
DR GeneCards; ETV4; -.
DR HGNC; HGNC:3493; ETV4.
DR HPA; ENSG00000175832; Low tissue specificity.
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; DPCVPYL; -.
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; 17 hits in 1111 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 lower esophagus mucosa and 133 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; IPR046328; ETS_fam.
DR InterPro; IPR006715; ETS_PEA3_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
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
