ZFP90_HUMAN
ID ZFP90_HUMAN Reviewed; 636 AA.
AC Q8TF47; B2RU00; B3KVE7; L7S2P3; Q49AD1; Q96MQ6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein 90 homolog;
DE Short=Zfp-90;
DE AltName: Full=Zinc finger protein 756;
GN Name=ZFP90; Synonyms=KIAA1954, ZNF756;
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 2), FUNCTION, AND INTERACTION WITH
RP FOXP3 AND TRIM28.
RX PubMed=23543754; DOI=10.4049/jimmunol.1203561;
RA Huang C., Martin S., Pfleger C., Du J., Buckner J.H., Bluestone J.A.,
RA Riley J.L., Ziegler S.F.;
RT "Cutting Edge: a novel, human-specific interacting protein couples FOXP3 to
RT a chromatin-remodeling complex that contains KAP1/TRIM28.";
RL J. Immunol. 190:4470-4473(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-636 (ISOFORM 1).
RC TISSUE=Melanoma, and Testis;
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 1-372 (ISOFORM 1).
RA Lincoln S.E., Altus C.M., Dufour G.E., Chalup M.S., Hillman J.L., Jones A.,
RA Yu J.Y., Wright R.J., Gietzen D., Liu T.F., Yap P., Dahl C.R., Momiyama M.,
RA Bradley D., Rohatgi S., Harris B., Roseberry A.M., Gerstin E.H.,
RA Peralta C.H., David M., Panzer S., Flores V., Daffo A., Marwaha R.,
RA Chen A., Chang S.C., Inman R.R.;
RT "Molecules for diagnostics and therapeutics.";
RL Patent number WO0220754, 14-MAR-2002.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-636 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [8]
RP FUNCTION, INTERACTION WITH REST, AND TISSUE SPECIFICITY.
RX PubMed=21284946; DOI=10.1016/j.yjmcc.2011.01.017;
RA Hata L., Murakami M., Kuwahara K., Nakagawa Y., Kinoshita H., Usami S.,
RA Yasuno S., Fujiwara M., Kuwabara Y., Minami T., Yamada Y., Yamada C.,
RA Nakao K., Ueshima K., Nishikimi T., Nakao K.;
RT "Zinc-finger protein 90 negatively regulates neuron-restrictive silencer
RT factor-mediated transcriptional repression of fetal cardiac genes.";
RL J. Mol. Cell. Cardiol. 50:972-981(2011).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-448, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Inhibits the transcriptional repressor activity of REST by
CC inhibiting its binding to DNA, thereby derepressing transcription of
CC REST target genes. {ECO:0000269|PubMed:21284946}.
CC -!- FUNCTION: [Isoform 2]: Acts as a bridge between FOXP3 and the
CC corepressor TRIM28, and is required for the transcriptional repressor
CC activity of FOXP3 in regulatory T-cells (Treg).
CC {ECO:0000269|PubMed:23543754}.
CC -!- SUBUNIT: Interacts (via N- and C-termini) with REST (via zinc-finger
CC DNA-binding domain); the interaction inhibits REST repressor activity
CC (PubMed:21284946). {ECO:0000269|PubMed:21284946}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with FOXP3 and TRIM28
CC (PubMed:23543754). {ECO:0000269|PubMed:23543754}.
CC -!- INTERACTION:
CC Q8TF47; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-11419867, EBI-11096309;
CC Q8TF47; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-11419867, EBI-1166928;
CC Q8TF47; A0A087WZT3: BOLA2B; NbExp=3; IntAct=EBI-11419867, EBI-12006120;
CC Q8TF47; P24863: CCNC; NbExp=3; IntAct=EBI-11419867, EBI-395261;
CC Q8TF47; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-11419867, EBI-12012272;
CC Q8TF47; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-11419867, EBI-744099;
CC Q8TF47; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-11419867, EBI-371876;
CC Q8TF47; O43559: FRS3; NbExp=3; IntAct=EBI-11419867, EBI-725515;
CC Q8TF47; Q96CN9: GCC1; NbExp=3; IntAct=EBI-11419867, EBI-746252;
CC Q8TF47; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-11419867, EBI-748515;
CC Q8TF47; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-11419867, EBI-740290;
CC Q8TF47; P31273: HOXC8; NbExp=3; IntAct=EBI-11419867, EBI-1752118;
CC Q8TF47; P25800: LMO1; NbExp=3; IntAct=EBI-11419867, EBI-8639312;
CC Q8TF47; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-11419867, EBI-2341787;
CC Q8TF47; Q96EH3: MALSU1; NbExp=3; IntAct=EBI-11419867, EBI-2339737;
CC Q8TF47; P40692: MLH1; NbExp=3; IntAct=EBI-11419867, EBI-744248;
CC Q8TF47; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-11419867, EBI-11750983;
CC Q8TF47; Q16512: PKN1; NbExp=3; IntAct=EBI-11419867, EBI-602382;
CC Q8TF47; O43741: PRKAB2; NbExp=3; IntAct=EBI-11419867, EBI-1053424;
CC Q8TF47; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-11419867, EBI-11984663;
CC Q8TF47; P51687: SUOX; NbExp=3; IntAct=EBI-11419867, EBI-3921347;
CC Q8TF47; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-11419867, EBI-8787464;
CC Q8TF47; Q9Y2W6: TDRKH; NbExp=3; IntAct=EBI-11419867, EBI-12842466;
CC Q8TF47; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-11419867, EBI-750487;
CC Q8TF47; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-11419867, EBI-8451480;
CC Q8TF47-3; Q9BZS1: FOXP3; NbExp=4; IntAct=EBI-11419904, EBI-983719;
CC Q8TF47-3; Q13263: TRIM28; NbExp=2; IntAct=EBI-11419904, EBI-78139;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61967}.
CC Note=Colocalizes with REST in the nucleus.
CC {ECO:0000250|UniProtKB:Q61967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TF47-1; Sequence=Displayed;
CC Name=2; Synonyms=FOXP3-interacting KRAB-domain containing protein, FIK
CC {ECO:0000303|PubMed:23543754};
CC IsoId=Q8TF47-3; Sequence=VSP_057516, VSP_057517;
CC -!- TISSUE SPECIFICITY: Expressed in heart (PubMed:21284946). Isoform 2:
CC Highly expressed in regulatory T-cells (Treg) (PubMed:23543754).
CC {ECO:0000269|PubMed:21284946, ECO:0000269|PubMed:23543754}.
CC -!- MISCELLANEOUS: [Isoform 2]: Interacts (via 75-113 AA) with FOXP3.
CC Interacts (via KRAB domain) with TRIM28. {ECO:0000269|PubMed:23543754}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AX721106; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB71228.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG53759.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; KC249978; AGC13464.1; -; mRNA.
DR EMBL; AK056596; BAB71228.1; ALT_INIT; mRNA.
DR EMBL; AK122847; BAG53759.1; ALT_SEQ; mRNA.
DR EMBL; AK304152; BAG65042.1; -; mRNA.
DR EMBL; AK316251; BAH14622.1; -; mRNA.
DR EMBL; AC009162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83234.1; -; Genomic_DNA.
DR EMBL; BC033165; AAH33165.2; -; mRNA.
DR EMBL; BC140886; AAI40887.1; -; mRNA.
DR EMBL; BC140887; AAI40888.1; -; mRNA.
DR EMBL; AX721106; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB075834; BAB85540.1; -; mRNA.
DR CCDS; CCDS42183.1; -. [Q8TF47-1]
DR CCDS; CCDS76892.1; -. [Q8TF47-3]
DR RefSeq; NP_001292132.1; NM_001305203.1. [Q8TF47-1]
DR RefSeq; NP_001292133.1; NM_001305204.1. [Q8TF47-3]
DR RefSeq; NP_597715.2; NM_133458.3. [Q8TF47-1]
DR RefSeq; XP_005255861.1; XM_005255804.2. [Q8TF47-1]
DR AlphaFoldDB; Q8TF47; -.
DR SMR; Q8TF47; -.
DR BioGRID; 126969; 28.
DR CORUM; Q8TF47; -.
DR IntAct; Q8TF47; 27.
DR STRING; 9606.ENSP00000460547; -.
DR iPTMnet; Q8TF47; -.
DR PhosphoSitePlus; Q8TF47; -.
DR BioMuta; ZFP90; -.
DR DMDM; 94730444; -.
DR EPD; Q8TF47; -.
DR jPOST; Q8TF47; -.
DR MassIVE; Q8TF47; -.
DR MaxQB; Q8TF47; -.
DR PaxDb; Q8TF47; -.
DR PeptideAtlas; Q8TF47; -.
DR PRIDE; Q8TF47; -.
DR ProteomicsDB; 74559; -.
DR Antibodypedia; 29788; 76 antibodies from 18 providers.
DR DNASU; 146198; -.
DR Ensembl; ENST00000398253.6; ENSP00000381304.2; ENSG00000184939.16. [Q8TF47-1]
DR Ensembl; ENST00000563169.7; ENSP00000454418.2; ENSG00000184939.16. [Q8TF47-1]
DR Ensembl; ENST00000570495.5; ENSP00000460547.1; ENSG00000184939.16. [Q8TF47-1]
DR Ensembl; ENST00000611381.4; ENSP00000480309.1; ENSG00000184939.16. [Q8TF47-3]
DR GeneID; 146198; -.
DR KEGG; hsa:146198; -.
DR MANE-Select; ENST00000563169.7; ENSP00000454418.2; NM_001305203.2; NP_001292132.1.
DR UCSC; uc002ewd.4; human. [Q8TF47-1]
DR UCSC; uc031qws.2; human.
DR CTD; 146198; -.
DR DisGeNET; 146198; -.
DR GeneCards; ZFP90; -.
DR HGNC; HGNC:23329; ZFP90.
DR HPA; ENSG00000184939; Low tissue specificity.
DR MIM; 609451; gene.
DR neXtProt; NX_Q8TF47; -.
DR OpenTargets; ENSG00000184939; -.
DR PharmGKB; PA134967487; -.
DR VEuPathDB; HostDB:ENSG00000184939; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162132; -.
DR HOGENOM; CLU_002678_57_1_1; -.
DR InParanoid; Q8TF47; -.
DR OMA; TLEDTWD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8TF47; -.
DR TreeFam; TF350822; -.
DR PathwayCommons; Q8TF47; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q8TF47; -.
DR BioGRID-ORCS; 146198; 212 hits in 1043 CRISPR screens.
DR ChiTaRS; ZFP90; human.
DR GenomeRNAi; 146198; -.
DR Pharos; Q8TF47; Tbio.
DR PRO; PR:Q8TF47; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8TF47; protein.
DR Bgee; ENSG00000184939; Expressed in ganglionic eminence and 193 other tissues.
DR ExpressionAtlas; Q8TF47; baseline and differential.
DR Genevisible; Q8TF47; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..636
FT /note="Zinc finger protein 90 homolog"
FT /id="PRO_0000047310"
FT DOMAIN 14..85
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 211..233
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 254..276
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..304
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 338..360
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 394..416
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 450..472
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..547
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..575
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..603
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 609..631
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 448
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 86..113
FT /note="DWKTRPEVKSSHLQQDVSEVSHCTHDLL -> GFVCLLPLSLPSGSKGERRQ
FT KLPRKNPE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:23543754"
FT /id="VSP_057516"
FT VAR_SEQ 114..636
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:23543754"
FT /id="VSP_057517"
FT CONFLICT 550
FT /note="E -> V (in Ref. 2; BAB71228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 73031 MW; 2D645DD5F5EFD8A6 CRC64;
MAPRPPTAAP QESVTFKDVS VDFTQEEWYH VDPAQRSLYR DVMLENYSHL VSLGYQVSKP
EVIFKLEQGE EPWISEGEIQ RPFYPDWKTR PEVKSSHLQQ DVSEVSHCTH DLLHATLEDS
WDVSSQLDRQ QENWKRHLGS EASTQKKIIT PQENFEQNKF GENSRLNTNL VTQLNIPARI
RPSECETLGS NLGHNADLLN ENNILAKKKP YKCDKCRKAF IHRSSLTKHE KTHKGEGAFP
NGTDQGIYPG KKHHECTDCG KTFLWKTQLT EHQRIHTGEK PFECNVCGKA FRHSSSLGQH
ENAHTGEKPY QCSLCGKAFQ RSSSLVQHQR IHTGEKPYRC NLCGRSFRHG TSLTQHEVTH
SGEKPFQCKE CGKAFSRCSS LVQHERTHTG EKPFECSICG RAFGQSPSLY KHMRIHKRGK
PYQSSNYSID FKHSTSLTQD ESTLTEVKSY HCNDCGEDFS HITDFTDHQR IHTAENPYDC
EQAFSQQAIS HPGEKPYQCN VCGKAFKRST SFIEHHRIHT GEKPYECNEC GEAFSRRSSL
TQHERTHTGE KPYECIDCGK AFSQSSSLIQ HERTHTGEKP YECNECGRAF RKKTNLHDHQ
RIHTGEKPYS CKECGKNFSR SSALTKHQRI HTRNKL
