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   27-MAR-2024, entry version 199.
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; 47.
DR   IntAct; Q9NTW7; 34.
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   PaxDb; 9606-ENSP00000216923; -.
DR   PeptideAtlas; 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   Pumba; Q9NTW7; -.
DR   Antibodypedia; 13873; 235 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   AGR; HGNC:15940; -.
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   InParanoid; Q9NTW7; -.
DR   OMA; DAPFQCR; -.
DR   OrthoDB; 4036417at2759; -.
DR   TreeFam; TF333046; -.
DR   PathwayCommons; Q9NTW7; -.
DR   SignaLink; Q9NTW7; -.
DR   BioGRID-ORCS; 55734; 32 hits in 1181 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 201 other cell types or tissues.
DR   ExpressionAtlas; Q9NTW7; baseline and differential.
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   Gene3D; 3.30.160.60; Classic Zinc Finger; 11.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR24403:SF108; ZINC FINGER PROTEIN 64; 1.
DR   Pfam; PF00096; zf-C2H2; 8.
DR   SMART; SM00355; ZnF_C2H2; 15.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 8.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
DR   Genevisible; Q9NTW7; HS.
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
//