ZKSC3_HUMAN
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 03-AUG-2022, entry version 185.
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}.
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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; 28.
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; Q9BRR0; -.
DR PeptideAtlas; Q9BRR0; -.
DR PRIDE; Q9BRR0; -.
DR ProteomicsDB; 43426; -.
DR ProteomicsDB; 78810; -. [Q9BRR0-1]
DR Antibodypedia; 11260; 166 antibodies from 27 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 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; QSAEDQM; -.
DR OrthoDB; 1318335at2759; -.
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 1100 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 sperm and 127 other tissues.
DR Genevisible; Q9BRR0; HS.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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; 1.10.4020.10; -; 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 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; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
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
