ID ZKSC3_HUMAN Reviewed; 538 AA. AC Q9BRR0; B2R8W2; B3KVC0; H7BXX1; Q5VXH3; Q92972; Q9H4T3; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 194. DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 3; DE AltName: Full=Zinc finger and SCAN domain-containing protein 13; DE AltName: Full=Zinc finger protein 306; DE AltName: Full=Zinc finger protein 309; DE AltName: Full=Zinc finger protein 47 homolog; DE Short=Zf47; DE Short=Zfp-47; GN Name=ZKSCAN3; Synonyms=ZFP47, ZNF306, ZNF309, ZSCAN13; 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] (ISOFORM 1), AND VARIANTS MET-189 RP AND ALA-200. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP ALA-200 AND GLU-200. RC TISSUE=Testis; 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=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-200. RC TISSUE=Placenta; 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 206-538 (ISOFORM 1/2). RX PubMed=10520746; DOI=10.3109/10425179809072191; RA Petroni D., Bartolini E., Chiaramonte R., Ottolenghi S., Comi P.; RT "Computer sequence analysis of human highly conserved zinc finger RT modules."; RL DNA Seq. 9:163-169(1998). RN [7] RP TISSUE SPECIFICITY. RX PubMed=18519692; DOI=10.1158/0008-5472.can-08-0407; RA Yang L., Hamilton S.R., Sood A., Kuwai T., Ellis L., Sanguino A., RA Lopez-Berestein G., Boyd D.D.; RT "The previously undescribed ZKSCAN3 (ZNF306) is a novel 'driver' of RT colorectal cancer progression."; RL Cancer Res. 68:4321-4330(2008). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND INDUCTION. RX PubMed=18940803; DOI=10.1074/jbc.m806965200; RA Yang L., Zhang L., Wu Q., Boyd D.D.; RT "Unbiased screening for transcriptional targets of ZKSCAN3 identifies RT integrin beta 4 and vascular endothelial growth factor as downstream RT targets."; RL J. Biol. Chem. 283:35295-35304(2008). RN [9] RP FUNCTION, AND INDUCTION. RX PubMed=21057542; DOI=10.1038/onc.2010.515; RA Yang L., Wang H., Kornblau S.M., Graber D.A., Zhang N., Matthews J.A., RA Wang M., Weber D.M., Thomas S.K., Shah J.J., Zhang L., Lu G., Zhao M., RA Muddasani R., Yoo S.Y., Baggerly K.A., Orlowski R.Z.; RT "Evidence of a role for the novel zinc-finger transcription factor ZKSCAN3 RT in modulating Cyclin D2 expression in multiple myeloma."; RL Oncogene 30:1329-1340(2011). RN [10] RP FUNCTION, AND INDUCTION. RX PubMed=22531714; DOI=10.1016/j.biocel.2012.04.005; RA Zhang X., Jing Y., Qin Y., Hunsucker S., Meng H., Sui J., Jiang Y., Gao L., RA An G., Yang N., Orlowski R.Z., Yang L.; RT "The zinc finger transcription factor ZKSCAN3 promotes prostate cancer cell RT migration."; RL Int. J. Biochem. Cell Biol. 44:1166-1173(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207 AND THR-449, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [12] RP FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=23434374; DOI=10.1016/j.molcel.2013.01.024; RA Chauhan S., Goodwin J.G., Chauhan S., Manyam G., Wang J., Kamat A.M., RA Boyd D.D.; RT "ZKSCAN3 is a master transcriptional repressor of autophagy."; RL Mol. Cell 50:16-28(2013). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-171, 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: Transcriptional factor that binds to the consensus sequence CC 5'-[GT][AG][AGT]GGGG-3' and acts as a repressor of autophagy. CC Specifically represses expression of genes involved in autophagy and CC lysosome biogenesis/function such as MAP1LC3B, ULK1 or WIPI2. CC Associates with chromatin at the ITGB4 and VEGF promoters. Also acts as CC a transcription activator and promotes cancer cell progression and/or CC migration in various tumors and myelomas. {ECO:0000269|PubMed:18940803, CC ECO:0000269|PubMed:21057542, ECO:0000269|PubMed:22531714, CC ECO:0000269|PubMed:23434374}. CC -!- INTERACTION: CC Q9BRR0; P41091: EIF2S3; NbExp=3; IntAct=EBI-1965777, EBI-1054228; CC Q9BRR0; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-1965777, EBI-10226858; CC Q9BRR0; P14136: GFAP; NbExp=3; IntAct=EBI-1965777, EBI-744302; CC Q9BRR0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1965777, EBI-5916454; CC Q9BRR0; P54652: HSPA2; NbExp=3; IntAct=EBI-1965777, EBI-356991; CC Q9BRR0; P42858: HTT; NbExp=3; IntAct=EBI-1965777, EBI-466029; CC Q9BRR0; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-1965777, EBI-8638439; CC Q9BRR0; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1965777, EBI-1055254; CC Q9BRR0; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-1965777, EBI-741037; CC Q9BRR0; O15151: MDM4; NbExp=3; IntAct=EBI-1965777, EBI-398437; CC Q9BRR0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1965777, EBI-16439278; CC Q9BRR0; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-1965777, EBI-9640281; CC Q9BRR0; D3DTS7: PMP22; NbExp=3; IntAct=EBI-1965777, EBI-25882629; CC Q9BRR0; P49591: SARS1; NbExp=3; IntAct=EBI-1965777, EBI-1053431; CC Q9BRR0; P57086: SCAND1; NbExp=3; IntAct=EBI-1965777, EBI-745846; CC Q9BRR0; Q12933: TRAF2; NbExp=3; IntAct=EBI-1965777, EBI-355744; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly localizes in the CC nucleus. Under starvation conditions translocates to the cytoplasm, CC allowing expression of target genes involved in autophagy and lysosome CC biogenesis/function. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BRR0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BRR0-2; Sequence=VSP_045908; CC -!- INDUCTION: Overexpressed in various tumors, such as multiple myeloma, CC colorectal and prostate cancers (at protein level). CC {ECO:0000269|PubMed:18940803, ECO:0000269|PubMed:21057542, CC ECO:0000269|PubMed:22531714}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {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; BT007427; AAP36095.1; -; mRNA. DR EMBL; AK122790; BAG53732.1; -; mRNA. DR EMBL; AK313532; BAG36309.1; -; mRNA. DR EMBL; AL358785; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL021997; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03157.1; -; Genomic_DNA. DR EMBL; BC006118; AAH06118.1; -; mRNA. DR EMBL; U71601; AAB16813.1; -; mRNA. DR CCDS; CCDS4650.1; -. [Q9BRR0-1] DR CCDS; CCDS56408.1; -. [Q9BRR0-2] DR RefSeq; NP_001229823.1; NM_001242894.1. [Q9BRR0-1] DR RefSeq; NP_001229824.1; NM_001242895.1. [Q9BRR0-2] DR RefSeq; NP_077819.2; NM_024493.3. [Q9BRR0-1] DR RefSeq; XP_006715278.1; XM_006715215.2. [Q9BRR0-1] DR RefSeq; XP_006715281.1; XM_006715218.3. [Q9BRR0-2] DR AlphaFoldDB; Q9BRR0; -. DR SMR; Q9BRR0; -. DR BioGRID; 123230; 29. DR IntAct; Q9BRR0; 33. DR STRING; 9606.ENSP00000366465; -. DR iPTMnet; Q9BRR0; -. DR PhosphoSitePlus; Q9BRR0; -. DR BioMuta; ZKSCAN3; -. DR DMDM; 116242859; -. DR EPD; Q9BRR0; -. DR jPOST; Q9BRR0; -. DR MassIVE; Q9BRR0; -. DR MaxQB; Q9BRR0; -. DR PaxDb; 9606-ENSP00000366465; -. DR PeptideAtlas; Q9BRR0; -. DR ProteomicsDB; 43426; -. DR ProteomicsDB; 78810; -. [Q9BRR0-1] DR Pumba; Q9BRR0; -. DR Antibodypedia; 11260; 179 antibodies from 26 providers. DR DNASU; 80317; -. DR Ensembl; ENST00000252211.7; ENSP00000252211.2; ENSG00000189298.14. [Q9BRR0-1] DR Ensembl; ENST00000341464.9; ENSP00000341883.5; ENSG00000189298.14. [Q9BRR0-2] DR Ensembl; ENST00000377255.3; ENSP00000366465.1; ENSG00000189298.14. [Q9BRR0-1] DR GeneID; 80317; -. DR KEGG; hsa:80317; -. DR MANE-Select; ENST00000252211.7; ENSP00000252211.2; NM_024493.4; NP_077819.2. DR UCSC; uc003nle.4; human. [Q9BRR0-1] DR AGR; HGNC:13853; -. DR CTD; 80317; -. DR DisGeNET; 80317; -. DR GeneCards; ZKSCAN3; -. DR HGNC; HGNC:13853; ZKSCAN3. DR HPA; ENSG00000189298; Low tissue specificity. DR MIM; 612791; gene. DR neXtProt; NX_Q9BRR0; -. DR OpenTargets; ENSG00000189298; -. DR PharmGKB; PA37821; -. DR VEuPathDB; HostDB:ENSG00000189298; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000163682; -. DR HOGENOM; CLU_002678_49_4_1; -. DR InParanoid; Q9BRR0; -. DR OMA; QELPCCK; -. DR OrthoDB; 5255661at2759; -. DR PhylomeDB; Q9BRR0; -. DR TreeFam; TF350830; -. DR PathwayCommons; Q9BRR0; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q9BRR0; -. DR BioGRID-ORCS; 80317; 12 hits in 1178 CRISPR screens. DR ChiTaRS; ZKSCAN3; human. DR GenomeRNAi; 80317; -. DR Pharos; Q9BRR0; Tbio. DR PRO; PR:Q9BRR0; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9BRR0; Protein. DR Bgee; ENSG00000189298; Expressed in primordial germ cell in gonad and 128 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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:UniProtKB. 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; IBA:GO_Central. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB. 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:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0007040; P:lysosome organization; IMP:UniProtKB. DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB. DR GO; GO:2000773; P:negative regulation of cellular senescence; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR CDD; cd07936; SCAN; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 7. DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR003309; SCAN_dom. DR InterPro; IPR038269; SCAN_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1. DR PANTHER; PTHR16515:SF55; ZINC FINGER PROTEIN 711; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF02023; SCAN; 1. DR Pfam; PF00096; zf-C2H2; 7. DR SMART; SM00349; KRAB; 1. DR SMART; SM00431; SCAN; 1. DR SMART; SM00355; ZnF_C2H2; 7. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1. DR PROSITE; PS50804; SCAN_BOX; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7. DR Genevisible; Q9BRR0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Autophagy; Cytoplasm; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..538 FT /note="Zinc finger protein with KRAB and SCAN domains 3" FT /id="PRO_0000047524" FT DOMAIN 46..128 FT /note="SCAN box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187" FT DOMAIN 214..274 FT /note="KRAB" FT ZN_FING 314..336 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 342..364 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 370..392 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 398..420 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 426..448 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 480..502 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 508..530 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 226..274 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 237..274 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 42 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91VW9" FT MOD_RES 207 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 449 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 171 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..148 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045908" FT VARIANT 3 FT /note="R -> T (in dbSNP:rs733743)" FT /id="VAR_024208" FT VARIANT 33 FT /note="G -> V (in dbSNP:rs3857554)" FT /id="VAR_028313" FT VARIANT 34 FT /note="F -> L (in dbSNP:rs3857555)" FT /id="VAR_028314" FT VARIANT 189 FT /note="V -> M (in dbSNP:rs17856167)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_028315" FT VARIANT 200 FT /note="K -> A (requires 2 nucleotide substitutions; FT dbSNP:rs371085669)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1" FT /id="VAR_059950" FT VARIANT 200 FT /note="K -> E (in dbSNP:rs13201752)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_028316" FT VARIANT 200 FT /note="K -> T (in dbSNP:rs13201753)" FT /id="VAR_028317" FT VARIANT 246 FT /note="H -> Q (in dbSNP:rs213227)" FT /id="VAR_028318" FT CONFLICT 206..207 FT /note="LT -> IP (in Ref. 6; AAB16813)" FT /evidence="ECO:0000305" FT CONFLICT 348..350 FT /note="GKA -> AKP (in Ref. 6; AAB16813)" FT /evidence="ECO:0000305" FT CONFLICT 437 FT /note="R -> D (in Ref. 6; AAB16813)" FT /evidence="ECO:0000305" FT CONFLICT 459..479 FT /note="QGEAWKSRMESQLENVETPMS -> TGRGWKVGWKASWKMLKLPCP (in FT Ref. 6; AAB16813)" FT /evidence="ECO:0000305" SQ SEQUENCE 538 AA; 60641 MW; 0D8F706F1B2F888F CRC64; MARELSESTA LDAQSTEDQM ELLVIKVEEE EAGFPSSPDL GSEGSRERFR GFRYPEAAGP REALSRLREL CRQWLQPEMH SKEQILELLV LEQFLTILPG NLQSWVREQH PESGEEVVVL LEYLERQLDE PAPQVSGVDQ GQELLCCKMA LLTPAPGSQS SQFQLMKALL KHESVGSQPL QDRVLQVPVL AHGGCCREDK VVASRLTPES QGLLKVEDVA LTLTPEWTQQ DSSQGNLCRD EKQENHGSLV SLGDEKQTKS RDLPPAEELP EKEHGKISCH LREDIAQIPT CAEAGEQEGR LQRKQKNATG GRRHICHECG KSFAQSSGLS KHRRIHTGEK PYECEECGKA FIGSSALVIH QRVHTGEKPY ECEECGKAFS HSSDLIKHQR THTGEKPYEC DDCGKTFSQS CSLLEHHRIH TGEKPYQCSM CGKAFRRSSH LLRHQRIHTG DKNVQEPEQG EAWKSRMESQ LENVETPMSY KCNECERSFT QNTGLIEHQK IHTGEKPYQC NACGKGFTRI SYLVQHQRSH VGKNILSQ //