ID EGR2_MOUSE Reviewed; 470 AA. AC P08152; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 3. DT 24-JAN-2024, entry version 211. DE RecName: Full=E3 SUMO-protein ligase EGR2; DE EC=2.3.2.- {ECO:0000250|UniProtKB:P11161}; DE AltName: Full=E3 SUMO-protein transferase ERG2 {ECO:0000305}; DE AltName: Full=Early growth response protein 2; DE Short=EGR-2; DE AltName: Full=Zinc finger protein Krox-20; GN Name=Egr2; Synonyms=Egr-2, Krox-20, Zfp-25; 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 [GENOMIC DNA] (ISOFORMS LONG AND SHORT). RX PubMed=2496302; DOI=10.1128/mcb.9.2.787-797.1989; RA Chavrier P., Janssen-Timmen U., Mattei M.-G., Zerial M., Bravo R., RA Charnay P.; RT "Structure, chromosome location, and expression of the mouse zinc finger RT gene Krox-20: multiple gene products and coregulation with the proto- RT oncogene c-fos."; RL Mol. Cell. Biol. 9:787-797(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND INDUCTION. RX PubMed=3129290; DOI=10.1002/j.1460-2075.1988.tb02780.x; RA Chavrier P., Zerial M., Lemaire P., Almendral J., Bravo R., Charnay P.; RT "A gene encoding a protein with zinc fingers is activated during G0/G1 RT transition in cultured cells."; RL EMBO J. 7:29-35(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 [GENOMIC DNA] OF 339-417. RX PubMed=2452975; DOI=10.1128/mcb.8.3.1319-1326.1988; RA Chavrier P., Lemaire P., Revelant O., Bravo R., Charnay P.; RT "Characterization of a mouse multigene family that encodes zinc finger RT structures."; RL Mol. Cell. Biol. 8:1319-1326(1988). RN [5] RP FUNCTION. RX PubMed=1969796; DOI=10.1002/j.1460-2075.1990.tb08228.x; RA Chavrier P., Vesque C., Galliot B., Vigneron M., Dolle P., Duboule D., RA Charnay P.; RT "The segment-specific gene Krox-20 encodes a transcription factor with RT binding sites in the promoter region of the Hox-1.4 gene."; RL EMBO J. 9:1209-1218(1990). RN [6] RP FUNCTION. RX PubMed=1674431; DOI=10.1016/0300-9084(91)90079-g; RA Gilardi P., Schneider-Maunoury S., Charnay P.; RT "Krox-20: a candidate gene for the regulation of pattern formation in the RT hindbrain."; RL Biochimie 73:85-91(1991). RN [7] RP DOMAINS. RX PubMed=1598206; DOI=10.1093/nar/20.10.2485; RA Vesque C., Charnay P.; RT "Mapping functional regions of the segment-specific transcription factor RT Krox-20."; RL Nucleic Acids Res. 20:2485-2492(1992). RN [8] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=8093858; DOI=10.1016/0092-8674(93)90659-e; RA Sham M.H., Vesque C., Nonchev S., Marshall H., Frain M., Gupta R.D., RA Whiting J., Wilkinson D., Charnay P., Krumlauf R.; RT "The zinc finger gene Krox20 regulates HoxB2 (Hox2.8) during hindbrain RT segmentation."; RL Cell 72:183-196(1993). RN [9] RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=7935840; DOI=10.1038/371796a0; RA Topilko P., Schneider-Maunoury S., Levi G., Baron-Van Evercooren A., RA Chennoufi A.B., Seitanidou T., Babinet C., Charnay P.; RT "Krox-20 controls myelination in the peripheral nervous system."; RL Nature 371:796-799(1994). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=10068633; DOI=10.1242/dev.126.7.1397; RA Zorick T.S., Syroid D.E., Brown A., Gridley T., Lemke G.; RT "Krox-20 controls SCIP expression, cell cycle exit and susceptibility to RT apoptosis in developing myelinating Schwann cells."; RL Development 126:1397-1406(1999). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=11509834; DOI=10.1159/000048703; RA Turman J.E. Jr., Chopiuk N.B., Shuler C.F.; RT "The Krox-20 null mutation differentially affects the development of RT masticatory muscles."; RL Dev. Neurosci. 23:113-121(2001). RN [12] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=11823429; DOI=10.1093/emboj/21.3.365; RA Manzanares M., Nardelli J., Gilardi-Hebenstreit P., Marshall H., RA Giudicelli F., Martinez-Pastor M.T., Krumlauf R., Charnay P.; RT "Krox20 and kreisler co-operate in the transcriptional control of segmental RT expression of Hoxb3 in the developing hindbrain."; RL EMBO J. 21:365-376(2002). RN [13] RP FUNCTION. RX PubMed=16054051; DOI=10.1016/j.cmet.2004.12.009; RA Chen Z., Torrens J.I., Anand A., Spiegelman B.M., Friedman J.M.; RT "Krox20 stimulates adipogenesis via C/EBPbeta-dependent and -independent RT mechanisms."; RL Cell Metab. 1:93-106(2005). RN [14] RP FUNCTION, INTERACTION WITH CITED1 AND SFN, MUTAGENESIS OF SER-377, RP DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX PubMed=17938205; DOI=10.1128/mcb.00866-07; RA Dillon R.L., Brown S.T., Ling C., Shioda T., Muller W.J.; RT "An EGR2/CITED1 transcription factor complex and the 14-3-3sigma tumor RT suppressor are involved in regulating ErbB2 expression in a transgenic- RT mouse model of human breast cancer."; RL Mol. Cell. Biol. 27:8648-8657(2007). RN [15] RP UBIQUITINATION, INTERACTION WITH WWP2, AND MUTAGENESIS OF TYR-174 AND RP TYR-208. RX PubMed=19651900; DOI=10.1128/mcb.00407-09; RA Chen A., Gao B., Zhang J., McEwen T., Ye S.Q., Zhang D., Fang D.; RT "The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced T-cell RT death by catalyzing EGR2 ubiquitination."; RL Mol. Cell. Biol. 29:5348-5356(2009). RN [16] RP ACETYLATION AT LYS-247, AND MUTAGENESIS OF LYS-247. RX PubMed=28576496; DOI=10.1016/j.bbrc.2017.05.170; RA Noritsugu K., Ito A., Nakao Y., Yoshida M.; RT "Identification of zinc finger transcription factor EGR2 as a novel RT acetylated protein."; RL Biochem. Biophys. Res. Commun. 489:455-459(2017). RN [17] RP FUNCTION, AND MUTAGENESIS OF ASP-408. RX PubMed=31852952; DOI=10.1038/s41598-019-55875-4; RA Grosz B.R., Golovchenko N.B., Ellis M., Kumar K., Nicholson G.A., RA Antonellis A., Kennerson M.L.; RT "A de novo EGR2 variant, c.1232A > G p.Asp411Gly, causes severe early-onset RT Charcot-Marie-Tooth Neuropathy Type 3 (Dejerine-Sottas Neuropathy)."; RL Sci. Rep. 9:19336-19336(2019). CC -!- FUNCTION: Sequence-specific DNA-binding transcription factor CC (PubMed:1969796, PubMed:1674431, PubMed:11823429, PubMed:31852952). CC Plays a role in hindbrain segmentation by regulating the expression of CC a subset of homeobox containing genes and in Schwann cell myelination CC by regulating the expression of genes involved in the formation and CC maintenance of myelin (PubMed:1969796, PubMed:1674431, PubMed:11823429, CC PubMed:31852952, PubMed:8093858). Binds to two EGR2-consensus sites CC EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in the HOXB3 CC enhancer and promotes HOXB3 transcriptional activation CC (PubMed:11823429). Binds to specific DNA sites located in the promoter CC region of HOXA4, HOXB2 and ERBB2 (PubMed:1969796, PubMed:8093858, CC PubMed:17938205). Regulates hindbrain segmentation by controlling the CC expression of Hox genes, such as HOXA4, HOXB3 and HOXB2, and thereby CC specifying odd and even rhombomeres (PubMed:11823429, PubMed:1674431). CC Promotes the expression of HOXB3 in the rhombomere r5 and of HOXB3 in CC r3 and r5 in the hindbrain (PubMed:11823429, PubMed:8093858). Regulates CC myelination in the peripheral nervous system after birth, possibly by CC regulating the expression of myelin proteins, such as MPZ, and by CC promoting the differentiation of Schwann cells (PubMed:7935840, CC PubMed:10068633). Involved in the development of the jaw openener CC musculature, probably by playing a role in its innervation through CC trigeminal motor neurons (PubMed:11509834). May play a role in CC adipogenesis, possibly by regulating the expression of CEBPB CC (PubMed:16054051). {ECO:0000269|PubMed:10068633, CC ECO:0000269|PubMed:11509834, ECO:0000269|PubMed:11823429, CC ECO:0000269|PubMed:16054051, ECO:0000269|PubMed:1674431, CC ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:1969796, CC ECO:0000269|PubMed:31852952, ECO:0000269|PubMed:7935840, CC ECO:0000269|PubMed:8093858}. CC -!- FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its CC coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2 CC transcriptional activity. {ECO:0000250|UniProtKB:P11161}. CC -!- PATHWAY: Protein modification; protein sumoylation. CC -!- SUBUNIT: Interacts with HCFC1 (By similarity). Interacts with WWP2 CC (PubMed:19651900). Interacts with UBC9 (By similarity). Interacts with CC CITED1 (PubMed:17938205). Interacts (via phosphorylated form) with SFN CC (PubMed:17938205). {ECO:0000250|UniProtKB:P11161, CC ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:19651900}. CC -!- INTERACTION: CC P08152; Q8C5D8-1: Pias2; NbExp=5; IntAct=EBI-7070449, EBI-8064899; CC P08152; P63280: Ube2i; NbExp=2; IntAct=EBI-7070449, EBI-80180; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17938205}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P08152-1; Sequence=Displayed; CC Name=Short; CC IsoId=P08152-2; Sequence=VSP_006864; CC -!- TISSUE SPECIFICITY: Expressed mainly in the thymus. CC {ECO:0000269|PubMed:17938205}. CC -!- DEVELOPMENTAL STAGE: Before 8 dpc, expressed in the future rhombomere CC r3 at 0-3 somites, followed by expression in rhombomere r5 in 4-7 CC somites at 8 dpc, and maintained until 12 somites (PubMed:8093858). CC Expressed in migrating neural crest cells from r5/r6 (PubMed:8093858). CC Expressed in boundary cap cells that surround nerve exit points from CC the central nervous system at 10.5 dpc (PubMed:7935840, CC PubMed:8093858). Up to 14.5 dpc, expressed in motor and sensory roots CC of cranial and spinal nerves (PubMed:7935840). After 15.5 dpc, CC expressed in the entire peripheral nervous system (PubMed:7935840). CC Expressed in the embryonic nervous system (PubMed:17938205). Expressed CC in myelinating Schwann cells 2 weeks after birth (PubMed:7935840). CC {ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:7935840, CC ECO:0000269|PubMed:8093858}. CC -!- INDUCTION: Activated during G0/G1 transition in cultured cells. CC {ECO:0000269|PubMed:3129290}. CC -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation. CC {ECO:0000269|PubMed:19651900}. CC -!- PTM: Acetylated at Lys-247. May be deacetylated by HDAC6, HDAC10 or CC SIRT1. {ECO:0000269|PubMed:28576496}. CC -!- DISRUPTION PHENOTYPE: Failure to promote expression of the Hoxb3 CC reporter in rhombomere r5 in the hindbrain (PubMed:11823429). Changed CC morphology of the sciatic nerves, with a higher density of Schwann CC cells, and a reduction in major components of compacted myelin, CC including lipidic components, as well as myelin proteins Mpz and Mbp CC (PubMed:7935840). Schwann cells in the sciatic nerves exhibit increased CC expression of Scip, reduced expression of Mpz, elevated mitotic CC activity and increased apoptosis at postnatal day P12 CC (PubMed:10068633). Total absence of myelin along the axons of sciatic CC nerves at postnatal day P15 (PubMed:7935840). Does not seem to affect CC the myelination in the central nervous system (PubMed:7935840). Signs CC of atrophy in the jaw openener anterior digastric (AD) and mylohoid CC (MY) muscles at 15 dpc with smaller diameter fibers, fibers with CC triangular shape, increased amount of connective tissue surrounding the CC fibers, suggesting a lack of neural innervation (PubMed:11509834). CC Reduced volume of the delineated trigeminal motor nucleus and CC restructuring of the brainstem at 15 dpc (PubMed:11509834). Reduced CC volume in both AD and MY musculature and reduced milk indigestion after CC birth (PubMed:11509834). {ECO:0000269|PubMed:10068633, CC ECO:0000269|PubMed:11509834, ECO:0000269|PubMed:11823429, CC ECO:0000269|PubMed:7935840}. CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M24377; AAA39379.1; -; Genomic_DNA. DR EMBL; M24376; AAA39379.1; JOINED; Genomic_DNA. DR EMBL; M24377; AAA39380.1; -; Genomic_DNA. DR EMBL; M24376; AAA39380.1; JOINED; Genomic_DNA. DR EMBL; X06746; CAA29921.1; -; mRNA. DR EMBL; BC009093; AAH09093.1; -; mRNA. DR EMBL; M20759; AAA39381.1; -; Genomic_DNA. DR CCDS; CCDS35927.2; -. [P08152-1] DR CCDS; CCDS83706.1; -. [P08152-2] DR PIR; A30136; A30136. DR PIR; S00256; S00256. DR RefSeq; NP_001334387.1; NM_001347458.1. [P08152-2] DR RefSeq; NP_034248.2; NM_010118.3. [P08152-1] DR RefSeq; XP_006513272.1; XM_006513209.2. DR RefSeq; XP_006513273.1; XM_006513210.2. DR RefSeq; XP_006513274.1; XM_006513211.2. DR RefSeq; XP_006513276.1; XM_006513213.3. DR RefSeq; XP_011241670.1; XM_011243368.2. DR AlphaFoldDB; P08152; -. DR SMR; P08152; -. DR BioGRID; 199405; 7. DR ELM; P08152; -. DR IntAct; P08152; 5. DR MINT; P08152; -. DR STRING; 10090.ENSMUSP00000041053; -. DR iPTMnet; P08152; -. DR PhosphoSitePlus; P08152; -. DR PaxDb; 10090-ENSMUSP00000041053; -. DR ProteomicsDB; 277805; -. [P08152-1] DR ProteomicsDB; 277806; -. [P08152-2] DR Antibodypedia; 14464; 583 antibodies from 43 providers. DR DNASU; 13654; -. DR Ensembl; ENSMUST00000048289.14; ENSMUSP00000041053.8; ENSMUSG00000037868.16. [P08152-1] DR Ensembl; ENSMUST00000105438.9; ENSMUSP00000101078.3; ENSMUSG00000037868.16. [P08152-2] DR GeneID; 13654; -. DR KEGG; mmu:13654; -. DR UCSC; uc007flx.1; mouse. [P08152-1] DR AGR; MGI:95296; -. DR CTD; 1959; -. DR MGI; MGI:95296; Egr2. DR VEuPathDB; HostDB:ENSMUSG00000037868; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000158394; -. DR InParanoid; P08152; -. DR OMA; QCQRELH; -. DR OrthoDB; 2912670at2759; -. DR PhylomeDB; P08152; -. DR TreeFam; TF318980; -. DR Reactome; R-MMU-9031628; NGF-stimulated transcription. DR UniPathway; UPA00886; -. DR BioGRID-ORCS; 13654; 0 hits in 76 CRISPR screens. DR ChiTaRS; Egr2; mouse. DR PRO; PR:P08152; -. DR Proteomes; UP000000589; Chromosome 10. DR RNAct; P08152; Protein. DR Bgee; ENSMUSG00000037868; Expressed in neurectoderm and 85 other cell types or tissues. DR ExpressionAtlas; P08152; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0071837; F:HMG box domain binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0061665; F:SUMO ligase activity; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0035904; P:aorta development; IMP:MGI. DR GO; GO:0035284; P:brain segmentation; IMP:MGI. DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI. DR GO; GO:0021612; P:facial nerve structural organization; IMP:UniProtKB. DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0007611; P:learning or memory; IEA:Ensembl. DR GO; GO:0008045; P:motor neuron axon guidance; IGI:MGI. DR GO; GO:0042552; P:myelination; IMP:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0031643; P:positive regulation of myelination; IMP:UniProtKB. DR GO; GO:0014040; P:positive regulation of Schwann cell differentiation; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB. DR GO; GO:0016925; P:protein sumoylation; IDA:ARUK-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:MGI. DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl. DR GO; GO:0030278; P:regulation of ossification; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0032868; P:response to insulin; ISO:MGI. DR GO; GO:0021569; P:rhombomere 3 development; IGI:MGI. DR GO; GO:0021660; P:rhombomere 3 formation; IMP:MGI. DR GO; GO:0021659; P:rhombomere 3 structural organization; IDA:UniProtKB. DR GO; GO:0021666; P:rhombomere 5 formation; IMP:MGI. DR GO; GO:0021665; P:rhombomere 5 structural organization; IDA:UniProtKB. DR GO; GO:0007622; P:rhythmic behavior; IDA:MGI. DR GO; GO:0014037; P:Schwann cell differentiation; IMP:UniProtKB. DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:UniProtKB. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR InterPro; IPR021849; EGR_N. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23235:SF54; E3 SUMO-PROTEIN LIGASE EGR2; 1. DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1. DR Pfam; PF11928; DUF3446; 1. DR Pfam; PF00096; zf-C2H2; 3. DR SMART; SM00355; ZnF_C2H2; 3. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. DR Genevisible; P08152; MM. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; DNA-binding; Metal-binding; KW Nucleus; Reference proteome; Repeat; Transcription; KW Transcription regulation; Transferase; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..470 FT /note="E3 SUMO-protein ligase EGR2" FT /id="PRO_0000047120" FT ZN_FING 337..361 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 367..389 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 395..417 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 126..153 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 159..178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 185..210 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 275..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 408..470 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 187..203 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 426..451 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 247 FT /note="N6-acetyllysine; by EP300" FT /evidence="ECO:0000269|PubMed:28576496" FT VAR_SEQ 1..50 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:3129290" FT /id="VSP_006864" FT MUTAGEN 174 FT /note="Y->F: Abolishes interaction with WWP2; if associated FT with F-208." FT /evidence="ECO:0000269|PubMed:19651900" FT MUTAGEN 208 FT /note="Y->F: Abolishes interaction with WWP2; if associated FT with F-174." FT /evidence="ECO:0000269|PubMed:19651900" FT MUTAGEN 247 FT /note="K->R: Abolishes acetylation." FT /evidence="ECO:0000269|PubMed:28576496" FT MUTAGEN 377 FT /note="S->A: Inhibits interaction with SFN." FT /evidence="ECO:0000269|PubMed:17938205" FT MUTAGEN 408 FT /note="D->G: Reduces transcriptional regulatory activity." FT /evidence="ECO:0000269|PubMed:31852952" SQ SEQUENCE 470 AA; 49819 MW; 67712733C77960F0 CRC64; MMTAKAVDKI PVTLSGFMHQ LPDSLYPVED LAASSVTIFP NGELGGPFDQ MNGVAGDGMI NIDMTGEKRP LDLPYPSSFA PISAPRNQTF TYMGKFSIDP QYPGASCYPE GIINIVSAGI LQGVTPPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPE LDHLYSPPPP PPPYSGCTGD LYQDPSAFLS PPSTTSTSSL AYQPPPSYPS PKPAMDPGLI PMIPDYPGFF PSPCQRDPHG AAGPDRKPFP CPLDSLRVPP PLTPLSTIRN FTLGGPGAGV TGPGASGGGE GPRLPGSGSA AVTATPYNPH HLPLRPILRP RKYPNRPSKT PVHERPYPCP AEGCDRRFSR SDELTRHIRI HTGHKPFQCR ICMRNFSRSD HLTTHIRTHT GEKPFACDYC GRKFARSDER KRHTKIHLRQ KERKSSAPSA PPSAQSSASG PGGSQAGGSL CGNSAIGGPL ASCTSRTRTP //