ZMYM5_HUMAN
ID ZMYM5_HUMAN Reviewed; 669 AA.
AC Q9UJ78; B2R6V1; Q5T6E1; Q5T6E2; Q5T6E4; Q96IY6; Q9NZY5; Q9UBW0; Q9UJ77;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 4.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger MYM-type protein 5;
DE AltName: Full=Zinc finger protein 198-like 1;
DE AltName: Full=Zinc finger protein 237;
GN Name=ZMYM5; Synonyms=ZNF198L1, ZNF237; ORFNames=HSPC050;
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] (ISOFORMS 1; 2 AND 3).
RX PubMed=10894931; DOI=10.1159/000015584;
RA Sohal J., Reiter A., Goldman J.M., Cross N.C.;
RT "Cloning of ZNF237, a novel member of the MYM gene family that maps to
RT human chromosome 13q11-->q12.";
RL Cytogenet. Cell Genet. 89:24-28(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS VAL-125
RP AND PHE-137.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS VAL-125
RP AND PHE-137.
RC TISSUE=Urinary bladder;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-346.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-455, 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-88; LYS-91; LYS-134; LYS-149;
RP LYS-166; LYS-225; LYS-443; LYS-455; LYS-462 AND LYS-552, 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 [11]
RP STRUCTURE BY NMR OF 229-277.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of TRASH domain of zinc finger MYM-type protein 5.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [12]
RP INTERACTION WITH ETV5, FUNCTION, AND MUTAGENESIS OF ASN-112; SER-114;
RP THR-116 AND ASP-120.
RX PubMed=17126306; DOI=10.1016/j.brainres.2006.10.056;
RA Pastorcic M., Das H.K.;
RT "Analysis of transcriptional modulation of the presenilin 1 gene promoter
RT by ZNF237, a candidate binding partner of the Ets transcription factor
RT ERM.";
RL Brain Res. 1128:21-32(2007).
CC -!- FUNCTION: Functions as a transcriptional regulator.
CC {ECO:0000269|PubMed:17126306}.
CC -!- SUBUNIT: Interacts (via N-terminal 120 amino acid region) with ETV5
CC (via C-terminal). {ECO:0000269|PubMed:17126306}.
CC -!- INTERACTION:
CC Q9UJ78; P63165: SUMO1; NbExp=4; IntAct=EBI-7228860, EBI-80140;
CC Q9UJ78-2; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-17634549, EBI-11523526;
CC Q9UJ78-2; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-17634549, EBI-11530605;
CC Q9UJ78-2; P35520: CBS; NbExp=3; IntAct=EBI-17634549, EBI-740135;
CC Q9UJ78-2; P17661: DES; NbExp=3; IntAct=EBI-17634549, EBI-1055572;
CC Q9UJ78-2; Q13158: FADD; NbExp=3; IntAct=EBI-17634549, EBI-494804;
CC Q9UJ78-2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-17634549, EBI-2549423;
CC Q9UJ78-2; Q86YM7: HOMER1; NbExp=3; IntAct=EBI-17634549, EBI-746815;
CC Q9UJ78-2; Q5TA77: LCE3B; NbExp=3; IntAct=EBI-17634549, EBI-11974495;
CC Q9UJ78-2; Q02548: PAX5; NbExp=3; IntAct=EBI-17634549, EBI-296331;
CC Q9UJ78-2; Q92734: TFG; NbExp=3; IntAct=EBI-17634549, EBI-357061;
CC Q9UJ78-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-17634549, EBI-355744;
CC Q9UJ78-2; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-17634549, EBI-3650647;
CC Q9UJ78-2; Q15645: TRIP13; NbExp=3; IntAct=EBI-17634549, EBI-358993;
CC Q9UJ78-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-17634549, EBI-741480;
CC Q9UJ78-2; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-17634549, EBI-3918996;
CC Q9UJ78-2; O60232: ZNRD2; NbExp=3; IntAct=EBI-17634549, EBI-741415;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=4;
CC IsoId=Q9UJ78-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9UJ78-1; Sequence=VSP_034646, VSP_034647;
CC Name=2;
CC IsoId=Q9UJ78-2; Sequence=VSP_011443, VSP_011444;
CC Name=3;
CC IsoId=Q9UJ78-3; Sequence=VSP_011442, VSP_011445;
CC Name=5;
CC IsoId=Q9UJ78-5; Sequence=VSP_034645;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29022.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ133352; CAB57262.1; -; mRNA.
DR EMBL; AJ133353; CAB57263.1; -; mRNA.
DR EMBL; AJ133355; CAB57265.1; -; mRNA.
DR EMBL; AJ133354; CAB57264.1; -; mRNA.
DR EMBL; BT006687; AAP35333.1; -; mRNA.
DR EMBL; AK312724; BAG35598.1; -; mRNA.
DR EMBL; AL354808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08238.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08240.1; -; Genomic_DNA.
DR EMBL; BC007048; AAH07048.1; -; mRNA.
DR EMBL; AF161535; AAF29022.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31942.1; -. [Q9UJ78-1]
DR CCDS; CCDS31943.1; -. [Q9UJ78-2]
DR RefSeq; NP_001034738.1; NM_001039649.2. [Q9UJ78-2]
DR RefSeq; NP_001034739.1; NM_001039650.2. [Q9UJ78-1]
DR RefSeq; NP_001136156.1; NM_001142684.1. [Q9UJ78-4]
DR RefSeq; XP_005266650.1; XM_005266593.3. [Q9UJ78-4]
DR RefSeq; XP_005266651.1; XM_005266594.2. [Q9UJ78-4]
DR RefSeq; XP_006719957.1; XM_006719894.2. [Q9UJ78-4]
DR PDB; 2DAS; NMR; -; A=229-277.
DR PDBsum; 2DAS; -.
DR AlphaFoldDB; Q9UJ78; -.
DR SMR; Q9UJ78; -.
DR BioGRID; 114639; 31.
DR IntAct; Q9UJ78; 27.
DR MINT; Q9UJ78; -.
DR STRING; 9606.ENSP00000372361; -.
DR iPTMnet; Q9UJ78; -.
DR PhosphoSitePlus; Q9UJ78; -.
DR BioMuta; ZMYM5; -.
DR DMDM; 212288108; -.
DR EPD; Q9UJ78; -.
DR jPOST; Q9UJ78; -.
DR MassIVE; Q9UJ78; -.
DR MaxQB; Q9UJ78; -.
DR PaxDb; Q9UJ78; -.
DR PeptideAtlas; Q9UJ78; -.
DR PRIDE; Q9UJ78; -.
DR ProteomicsDB; 84596; -. [Q9UJ78-4]
DR ProteomicsDB; 84597; -. [Q9UJ78-1]
DR ProteomicsDB; 84598; -. [Q9UJ78-2]
DR ProteomicsDB; 84599; -. [Q9UJ78-3]
DR ProteomicsDB; 84600; -. [Q9UJ78-5]
DR Antibodypedia; 22270; 37 antibodies from 13 providers.
DR DNASU; 9205; -.
DR Ensembl; ENST00000337963.9; ENSP00000337034.4; ENSG00000132950.19. [Q9UJ78-4]
DR Ensembl; ENST00000382905.8; ENSP00000372361.4; ENSG00000132950.19. [Q9UJ78-1]
DR Ensembl; ENST00000382907.8; ENSP00000372364.4; ENSG00000132950.19. [Q9UJ78-2]
DR GeneID; 9205; -.
DR KEGG; hsa:9205; -.
DR MANE-Select; ENST00000337963.9; ENSP00000337034.4; NM_001142684.2; NP_001136156.1.
DR UCSC; uc001umn.4; human. [Q9UJ78-4]
DR CTD; 9205; -.
DR DisGeNET; 9205; -.
DR GeneCards; ZMYM5; -.
DR HGNC; HGNC:13029; ZMYM5.
DR HPA; ENSG00000132950; Low tissue specificity.
DR MIM; 616443; gene.
DR neXtProt; NX_Q9UJ78; -.
DR OpenTargets; ENSG00000132950; -.
DR PharmGKB; PA37607; -.
DR VEuPathDB; HostDB:ENSG00000132950; -.
DR eggNOG; ENOG502S9U9; Eukaryota.
DR GeneTree; ENSGT00940000162379; -.
DR HOGENOM; CLU_026638_0_1_1; -.
DR InParanoid; Q9UJ78; -.
DR OMA; EHCGEYM; -.
DR OrthoDB; 537563at2759; -.
DR PhylomeDB; Q9UJ78; -.
DR PathwayCommons; Q9UJ78; -.
DR SignaLink; Q9UJ78; -.
DR BioGRID-ORCS; 9205; 10 hits in 1083 CRISPR screens.
DR ChiTaRS; ZMYM5; human.
DR EvolutionaryTrace; Q9UJ78; -.
DR GenomeRNAi; 9205; -.
DR Pharos; Q9UJ78; Tdark.
DR PRO; PR:Q9UJ78; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9UJ78; protein.
DR Bgee; ENSG00000132950; Expressed in buccal mucosa cell and 180 other tissues.
DR Genevisible; Q9UJ78; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR010507; Znf_MYM.
DR Pfam; PF06467; zf-FCS; 3.
DR SMART; SM00746; TRASH; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..669
FT /note="Zinc finger MYM-type protein 5"
FT /id="PRO_0000191380"
FT ZN_FING 265..299
FT /note="MYM-type 1"
FT ZN_FING 311..351
FT /note="MYM-type 2"
FT ZN_FING 358..393
FT /note="MYM-type 3"
FT ZN_FING 404..431
FT /note="MYM-type 4"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 552
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..176
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_034645"
FT VAR_SEQ 165..213
FT /note="TKTGVRPFNPGRMNVAGDLFQNGEFATHHSPDSWISQSASFPSNQKQPG ->
FT VNAGMGNSGITTELTLKYIITNVTTLETGISSVNAGQDVNIIITYKTSL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10894931,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_011442"
FT VAR_SEQ 196..208
FT /note="DSWISQSASFPSN -> EMHLQRRLMSFFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10894931,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_011443"
FT VAR_SEQ 209..669
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10894931,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_011444"
FT VAR_SEQ 214..669
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10894931,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_011445"
FT VAR_SEQ 347..382
FT /note="IRHEVSVNNVTHKLCSNHCFNKYRLANGLIMNCCEH -> VWIFIPKLLFRL
FT TVIILTFKCYYVLFHLHNARVLDV (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10894931"
FT /id="VSP_034646"
FT VAR_SEQ 383..669
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10894931"
FT /id="VSP_034647"
FT VARIANT 125
FT /note="I -> V (in dbSNP:rs9579718)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_025508"
FT VARIANT 137
FT /note="C -> F (in dbSNP:rs9579717)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_025509"
FT VARIANT 231
FT /note="T -> A (in dbSNP:rs41292167)"
FT /id="VAR_062160"
FT MUTAGEN 112
FT /note="N->H: Abolishes interaction with ETV5. Abolished
FT repression activity."
FT /evidence="ECO:0000269|PubMed:17126306"
FT MUTAGEN 114
FT /note="S->G: Abolishes interaction with ETV5. No effect on
FT repression activity."
FT /evidence="ECO:0000269|PubMed:17126306"
FT MUTAGEN 116
FT /note="T->A: No effect on repression activity."
FT /evidence="ECO:0000269|PubMed:17126306"
FT MUTAGEN 120
FT /note="D->G: Increases repression activity."
FT /evidence="ECO:0000269|PubMed:17126306"
FT CONFLICT 210
FT /note="K -> R (in Ref. 7; AAF29022)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="V -> M (in Ref. 7; AAF29022)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="S -> A (in Ref. 7; AAF29022)"
FT /evidence="ECO:0000305"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2DAS"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:2DAS"
FT HELIX 270..276
FT /evidence="ECO:0007829|PDB:2DAS"
SQ SEQUENCE 669 AA; 74817 MW; 3365CE4EFB8D73A9 CRC64;
MEKCSVGGLE LTEQTPALLG NMAMATSLMD IGDSFGHPAC PLVSRSRNSP VEDDDDDDDV
VFIESIQPPS ISAPAIADQR NFIFASSKNE KPQGNYSVIP PSSRDLASQK GNISETIVID
DEEDIETNGG AEKKSSCFIE WGLPGTKNKT NDLDFSTSSL SRSKTKTGVR PFNPGRMNVA
GDLFQNGEFA THHSPDSWIS QSASFPSNQK QPGVDSLSPV ALLRKQNFQP TAQQQLTKPA
KITCANCKKP LQKGQTAYQR KGSAHLFCST TCLSSFSHKR TQNTRSIICK KDASTKKANV
ILPVESSKSF QEFYSTSCLS PCENNWNLKK GVFNKSRCTI CSKLAEIRHE VSVNNVTHKL
CSNHCFNKYR LANGLIMNCC EHCGEYMPSK STGNNILVIG GQQKRFCCQS CINEYKQMME
TKSKKLTASE NRKRNAFREE NEKQLYGSSN TLLKKIEGIP EKKEKTSQLQ LSVECGTDTL
LIQENVNLPP SSTSTIADTF QEQLEEKNFE DSIVPVVLSA DPGTWPRILN IKQRDTLVEN
VPPQVRNFNF PKDNTGRKFS ETYYTRILPN GEKTTRSWLL YSTSKDSVFC LYCKLFGEGK
NQLKNENGCK DWQHLSHILS KHEESEMHVN NSVKYSKLKS DLKKNKAIDA AEHRLYENEK
NDGVLLLYT
