ZF64B_HUMAN
ID ZF64B_HUMAN Reviewed; 645 AA.
AC Q9NTW7; A2A2N4; Q53H69; Q53XQ1; Q5JWM0; Q5JWM1; Q8WU98; Q9H9P1; Q9NPA5;
AC Q9NTS7; Q9NVH4;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Zinc finger protein 64 {ECO:0000305};
DE Short=Zfp-64;
DE AltName: Full=Zinc finger protein 338 {ECO:0000312|HGNC:HGNC:15940};
GN Name=ZFP64 {ECO:0000312|HGNC:HGNC:15940};
GN Synonyms=ZNF338 {ECO:0000312|HGNC:HGNC:15940};
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND VARIANT
RP ASN-451 (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Colon;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ASN-451 (ISOFORM 1).
RC TISSUE=Lymph;
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 INTERACTION WITH NOTCH1.
RX PubMed=18430783; DOI=10.1242/jcs.023119;
RA Sakamoto K., Tamamura Y., Katsube K., Yamaguchi A.;
RT "Zfp64 participates in Notch signaling and regulates differentiation in
RT mesenchymal cells.";
RL J. Cell Sci. 121:1613-1623(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545 (ISOFORM 6), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [9]
RP INTERACTION WITH ZNF70, AND SUBCELLULAR LOCATION.
RX PubMed=27353377; DOI=10.1016/j.bbrc.2016.06.124;
RA Watanabe K., Nakayama K., Ohta S., Tago K., Boonvisut S., Millings E.J.,
RA Fischer S.G., LeDuc C.A., Leibel R.L., Iwamoto S.;
RT "ZNF70, a novel ILDR2-interacting protein, contributes to the regulation of
RT HES1 gene expression.";
RL Biochem. Biophys. Res. Commun. 477:712-716(2016).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-286 AND LYS-397 (ISOFORM 6), AND
RP IDENTIFICATION 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 ZINC FINGER (ISOFORMS 1 AND 2).
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C2H2 type zinc-binding domain of human zinc
RT finger protein 64, isoforms 1 and 2.";
RL Submitted (MAY-2005) to the PDB data bank.
RN [12]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-593 AND ASN-609.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in the regulation of mesenchymal cell
CC differentiation through transactivation of NOTCH1 target genes.
CC {ECO:0000250|UniProtKB:Q99KE8}.
CC -!- SUBUNIT: Interacts with ZNF70; this interaction promote the
CC transactivation of the HES1 gene (PubMed:27353377). Interacts with
CC NOTCH1 (PubMed:27353377). {ECO:0000269|PubMed:27353377}.
CC -!- INTERACTION:
CC Q9NTW7; Q8WTP8: AEN; NbExp=7; IntAct=EBI-711679, EBI-8637627;
CC Q9NTW7; Q13895: BYSL; NbExp=5; IntAct=EBI-711679, EBI-358049;
CC Q9NTW7; P50402: EMD; NbExp=3; IntAct=EBI-711679, EBI-489887;
CC Q9NTW7; Q86V42: FAM124A; NbExp=6; IntAct=EBI-711679, EBI-744506;
CC Q9NTW7; Q14192: FHL2; NbExp=8; IntAct=EBI-711679, EBI-701903;
CC Q9NTW7; P28799: GRN; NbExp=3; IntAct=EBI-711679, EBI-747754;
CC Q9NTW7; V9HWH0: HEL164; NbExp=6; IntAct=EBI-711679, EBI-10330301;
CC Q9NTW7; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-711679, EBI-739909;
CC Q9NTW7; P25791: LMO2; NbExp=3; IntAct=EBI-711679, EBI-739696;
CC Q9NTW7; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-711679, EBI-739832;
CC Q9NTW7; P55081: MFAP1; NbExp=3; IntAct=EBI-711679, EBI-1048159;
CC Q9NTW7; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-711679, EBI-1567797;
CC Q9NTW7; P98175: RBM10; NbExp=3; IntAct=EBI-711679, EBI-721525;
CC Q9NTW7; Q8WV44: TRIM41; NbExp=7; IntAct=EBI-711679, EBI-725997;
CC Q9NTW7; O76024: WFS1; NbExp=3; IntAct=EBI-711679, EBI-720609;
CC Q9NTW7-5; Q9NYJ8: TAB2; NbExp=3; IntAct=EBI-23201521, EBI-358708;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27353377}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=3;
CC IsoId=Q9NTW7-1; Sequence=Displayed;
CC Name=4; Synonyms=ZNF338;
CC IsoId=Q9NTW7-2; Sequence=VSP_007285, VSP_007286;
CC Name=5;
CC IsoId=Q9NTW7-3; Sequence=VSP_038213, VSP_038214;
CC Name=6;
CC IsoId=Q9NTW7-4; Sequence=VSP_046896, VSP_046897, VSP_046898;
CC Name=1;
CC IsoId=Q9NTW7-5; Sequence=VSP_046897, VSP_046898;
CC Name=2;
CC IsoId=Q9NTW7-6; Sequence=VSP_060092, VSP_046897, VSP_046898;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD96432.1; Type=Erroneous translation; Note=Translation C-terminally extended.; Evidence={ECO:0000305};
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DR EMBL; AK001596; BAA91777.1; -; mRNA.
DR EMBL; AK001744; BAA91876.1; -; mRNA.
DR EMBL; AK022690; BAB14182.1; -; mRNA.
DR EMBL; BT009760; AAP88762.1; -; mRNA.
DR EMBL; AK222712; BAD96432.1; ALT_SEQ; mRNA.
DR EMBL; AL109984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75591.1; -; Genomic_DNA.
DR EMBL; BC021087; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC012759; AAH12759.1; -; mRNA.
DR EMBL; BC041622; AAH41622.1; -; mRNA.
DR CCDS; CCDS13439.1; -. [Q9NTW7-1]
DR CCDS; CCDS13440.1; -. [Q9NTW7-5]
DR CCDS; CCDS13441.1; -. [Q9NTW7-6]
DR CCDS; CCDS13442.1; -. [Q9NTW7-4]
DR CCDS; CCDS82630.1; -. [Q9NTW7-2]
DR RefSeq; NP_001306075.1; NM_001319146.1. [Q9NTW7-2]
DR RefSeq; NP_060667.2; NM_018197.2. [Q9NTW7-5]
DR RefSeq; NP_071371.3; NM_022088.4. [Q9NTW7-6]
DR RefSeq; NP_955458.1; NM_199426.1. [Q9NTW7-4]
DR RefSeq; NP_955459.2; NM_199427.2. [Q9NTW7-1]
DR PDB; 1X5W; NMR; -; A=-.
DR PDB; 2DMD; NMR; -; A=174-235.
DR PDBsum; 1X5W; -.
DR PDBsum; 2DMD; -.
DR AlphaFoldDB; Q9NTW7; -.
DR SMR; Q9NTW7; -.
DR BioGRID; 120853; 42.
DR IntAct; Q9NTW7; 31.
DR MINT; Q9NTW7; -.
DR STRING; 9606.ENSP00000216923; -.
DR GlyGen; Q9NTW7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NTW7; -.
DR PhosphoSitePlus; Q9NTW7; -.
DR BioMuta; ZFP64; -.
DR DMDM; 30316391; -.
DR EPD; Q9NTW7; -.
DR jPOST; Q9NTW7; -.
DR MassIVE; Q9NTW7; -.
DR MaxQB; Q9NTW7; -.
DR PeptideAtlas; Q9NTW7; -.
DR PRIDE; Q9NTW7; -.
DR ProteomicsDB; 63393; -.
DR ProteomicsDB; 81951; -.
DR ProteomicsDB; 81952; -.
DR ProteomicsDB; 82633; -. [Q9NTW7-1]
DR ProteomicsDB; 82634; -. [Q9NTW7-2]
DR ProteomicsDB; 82635; -. [Q9NTW7-3]
DR Antibodypedia; 13873; 209 antibodies from 26 providers.
DR DNASU; 55734; -.
DR Ensembl; ENST00000216923.5; ENSP00000216923.4; ENSG00000020256.20. [Q9NTW7-5]
DR Ensembl; ENST00000346617.8; ENSP00000344615.4; ENSG00000020256.20. [Q9NTW7-6]
DR Ensembl; ENST00000361387.6; ENSP00000355179.2; ENSG00000020256.20. [Q9NTW7-1]
DR Ensembl; ENST00000371515.8; ENSP00000360570.4; ENSG00000020256.20. [Q9NTW7-4]
DR Ensembl; ENST00000371518.6; ENSP00000360573.2; ENSG00000020256.20. [Q9NTW7-3]
DR Ensembl; ENST00000371523.8; ENSP00000360578.4; ENSG00000020256.20. [Q9NTW7-2]
DR GeneID; 55734; -.
DR KEGG; hsa:55734; -.
DR MANE-Select; ENST00000216923.5; ENSP00000216923.4; NM_018197.3; NP_060667.2. [Q9NTW7-5]
DR UCSC; uc002xwj.4; human. [Q9NTW7-1]
DR CTD; 55734; -.
DR DisGeNET; 55734; -.
DR GeneCards; ZFP64; -.
DR HGNC; HGNC:15940; ZFP64.
DR HPA; ENSG00000020256; Low tissue specificity.
DR MIM; 618111; gene.
DR neXtProt; NX_Q9NTW7; -.
DR OpenTargets; ENSG00000020256; -.
DR PharmGKB; PA38060; -.
DR VEuPathDB; HostDB:ENSG00000020256; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156405; -.
DR HOGENOM; CLU_002678_71_1_1; -.
DR OMA; GCQFKTS; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF333046; -.
DR PathwayCommons; Q9NTW7; -.
DR SignaLink; Q9NTW7; -.
DR BioGRID-ORCS; 55734; 32 hits in 1103 CRISPR screens.
DR ChiTaRS; ZFP64; human.
DR GeneWiki; ZFP64; -.
DR GenomeRNAi; 55734; -.
DR Pharos; Q9NTW7; Tbio.
DR PRO; PR:Q9NTW7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR Bgee; ENSG00000020256; Expressed in germinal epithelium of ovary and 199 other tissues.
DR ExpressionAtlas; Q9NTW7; baseline and differential.
DR Genevisible; Q9NTW7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043076; C:megasporocyte nucleus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048762; P:mesenchymal cell differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..645
FT /note="Zinc finger protein 64"
FT /id="PRO_0000047308"
FT ZN_FING 175..197
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 203..225
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 231..253
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..324
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 330..352
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..380
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..465
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..546
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 580..602
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 543..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..219
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007285"
FT VAR_SEQ 16..18
FT /note="IPG -> S (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_046896"
FT VAR_SEQ 96..149
FT /note="Missing (in isoform 2)"
FT /id="VSP_060092"
FT VAR_SEQ 220..254
FT /note="KHLRIHSDERPFKCQICPYASRNSSQLTVHLRSHT -> MSRRKQAKPQHLN
FT SEEPRPARRECAEVAPQVAGEP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007286"
FT VAR_SEQ 236..390
FT /note="Missing (in isoform 6, isoform 1 and isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046897"
FT VAR_SEQ 411..415
FT /note="DTPFQ -> CCYVA (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038213"
FT VAR_SEQ 412..645
FT /note="TPFQCWLCSAKFKISSDLKRHMIVHSGEKPFKCEFCDVRCTMKANLKSHIRI
FT KHTFKCLHCAFQGRDRADLLEHSRLHQADHPEKCPECSYSCSSAAALRVHSRVHCKDRP
FT FKCDFCSFDTKRPSSLAKHVDKVHRDEAKTENRAPLGKEGLREGSSQHVAKIVTQRAFR
FT CETCGASFVRDDSLRCHKKQHSDQSENKNSDLVTFPPESGASGQLSTLVSVGQLEAPLE
FT PSQDL -> APFQCWLCSAKFKISSDLKRHMRVHSGEKPFKCEFCNVRCTMKGNLKSHI
FT RIKHSGNNFKCPHCDFLGDSKATLRKHSRVHQSEHPEKCSECSYSCSSKAALRIHERIH
FT CTDRPFKCNYCSFDTKQPSNLSKHMKKFHGDMVKTEALERKDTGRQSSRQVAKLDAKKS
FT FHCDICDASFMREDSLRSHKRQHSEYSESKNSDVTVLQFQIDPSKQPATPLTVGHLQVP
FT LQPSQVPQFSEGRVKIIVGHQVPQANTIVQAAAAAVNIVPPALVAQNPEELPGNSRLQI
FT LRQVSLIAPPQSSRCPSEAGAMTQPAVLLTTHEQTDGATLHQTLIPTASGGPQEGSGNQ
FT TFITSSGITCTDFEGLNALIQEGTAEVTVVSDGGQNIAVATTAPPVFSSSSQQELPKQT
FT YSIIQGAAHPALLCPADSIPD (in isoform 6, isoform 1 and isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046898"
FT VAR_SEQ 416..645
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038214"
FT VARIANT 68
FT /note="Q -> P (in dbSNP:rs7353222)"
FT /id="VAR_028019"
FT VARIANT 139
FT /note="P -> L (in dbSNP:rs6021773)"
FT /id="VAR_028020"
FT VARIANT 593
FT /note="D -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035564"
FT VARIANT 609
FT /note="K -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035565"
FT CONFLICT 240
FT /note="S -> G (in Ref. 3; BAD96432)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="R -> C (in Ref. 2; AAP88762 and 6; BC021087)"
FT /evidence="ECO:0000305"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2DMD"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:2DMD"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2DMD"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2DMD"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2DMD"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2DMD"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2DMD"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2DMD"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2DMD"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:2DMD"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:1X5W"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:1X5W"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:1X5W"
FT HELIX 507..514
FT /evidence="ECO:0007829|PDB:1X5W"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:1X5W"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:1X5W"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:1X5W"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:1X5W"
FT HELIX 535..546
FT /evidence="ECO:0007829|PDB:1X5W"
FT MOD_RES Q9NTW7-4:545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK Q9NTW7-4:286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9NTW7-4:397
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT Q9NTW7-5:425
FT /note="F -> Y (in dbSNP:rs16996517)"
FT /evidence="ECO:0000305"
FT /id="VAR_082942"
FT VARIANT Q9NTW7-5:451
FT /note="S -> N (in dbSNP:rs3746414)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_082943"
SQ SEQUENCE 645 AA; 72217 MW; D7D336A59C128CC0 CRC64;
MNASSEGESF AGSVQIPGGT TVLVELTPDI HICGICKQQF NNLDAFVAHK QSGCQLTGTS
AAAPSTVQFV SEETVPATQT QTTTRTITSE TQTITVSAPE FVFEHGYQTY LPTESNENQT
ATVISLPAKS RTKKPTTPPA QKRLNCCYPG CQFKTAYGMK DMERHLKIHT GDKPHKCEVC
GKCFSRKDKL KTHMRCHTGV KPYKCKTCDY AAADSSSLNK HLRIHSDERP FKCQICPYAS
RNSSQLTVHL RSHTASELDD DVPKANCLST ESTDTPKAPV ITLPSEAREQ MATLGERTFN
CCYPGCHFKT VHGMKDLDRH LRIHTGDKPH KCEFCDKCFS RKDNLTMHMR CHTSVKPHKC
HLCDYAAVDS SSLKKHLRIH SDERPYKCQL CPYASRNSSQ LTVHLRSHTG DTPFQCWLCS
AKFKISSDLK RHMIVHSGEK PFKCEFCDVR CTMKANLKSH IRIKHTFKCL HCAFQGRDRA
DLLEHSRLHQ ADHPEKCPEC SYSCSSAAAL RVHSRVHCKD RPFKCDFCSF DTKRPSSLAK
HVDKVHRDEA KTENRAPLGK EGLREGSSQH VAKIVTQRAF RCETCGASFV RDDSLRCHKK
QHSDQSENKN SDLVTFPPES GASGQLSTLV SVGQLEAPLE PSQDL
