ZKSC8_HUMAN
ID ZKSC8_HUMAN Reviewed; 578 AA.
AC Q15776; A1L3D4; B4DYF1; Q4VAR1; Q4VAR2; Q4VAR3; Q9H4T1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 8;
DE AltName: Full=LD5-1;
DE AltName: Full=Zinc finger protein 192;
GN Name=ZKSCAN8; Synonyms=ZNF192;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT LEU-163.
RC TISSUE=Ovary;
RX PubMed=9244436; DOI=10.1006/geno.1997.4806;
RA Lee P.L., Gelbart T., West C., Adams M., Blackstone R., Beutler E.;
RT "Three genes encoding zinc finger proteins on human chromosome 6p21.3:
RT members of a new subclass of the Kruppel gene family containing the
RT conserved SCAN box domain.";
RL Genomics 43:191-201(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=8673473; DOI=10.1006/bcmd.1995.0024;
RA Beutler E., Gelbart T., West C., Kuhl W., Lee P.;
RT "A strategy for cloning the hereditary hemochromatosis gene.";
RL Blood Cells Mol. Dis. 21:207-216(1995).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-572, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-572, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26; LYS-176; LYS-199; LYS-272;
RP LYS-288; LYS-374; LYS-441; LYS-502 AND LYS-572, 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: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q15776; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2602314, EBI-10976677;
CC Q15776; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-2602314, EBI-21603100;
CC Q15776; P28799: GRN; NbExp=3; IntAct=EBI-2602314, EBI-747754;
CC Q15776; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-2602314, EBI-8561769;
CC Q15776; P42858: HTT; NbExp=9; IntAct=EBI-2602314, EBI-466029;
CC Q15776; Q92993: KAT5; NbExp=3; IntAct=EBI-2602314, EBI-399080;
CC Q15776; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2602314, EBI-10975473;
CC Q15776; P02545: LMNA; NbExp=3; IntAct=EBI-2602314, EBI-351935;
CC Q15776; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2602314, EBI-11742507;
CC Q15776; P61326: MAGOH; NbExp=3; IntAct=EBI-2602314, EBI-299134;
CC Q15776; P07196: NEFL; NbExp=3; IntAct=EBI-2602314, EBI-475646;
CC Q15776; P35240: NF2; NbExp=3; IntAct=EBI-2602314, EBI-1014472;
CC Q15776; P62937-2: PPIA; NbExp=3; IntAct=EBI-2602314, EBI-25884072;
CC Q15776; P60891: PRPS1; NbExp=3; IntAct=EBI-2602314, EBI-749195;
CC Q15776; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2602314, EBI-396669;
CC Q15776; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2602314, EBI-9090795;
CC Q15776; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2602314, EBI-5235340;
CC Q15776; Q15560: TCEA2; NbExp=3; IntAct=EBI-2602314, EBI-710310;
CC Q15776; O76024: WFS1; NbExp=3; IntAct=EBI-2602314, EBI-720609;
CC Q15776; P61981: YWHAG; NbExp=3; IntAct=EBI-2602314, EBI-359832;
CC Q15776; Q8N0Y2-2: ZNF444; NbExp=4; IntAct=EBI-2602314, EBI-12010736;
CC Q15776; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-2602314, EBI-6427977;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15776-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15776-2; Sequence=VSP_056437, VSP_056438;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U57796; AAB02260.1; -; mRNA.
DR EMBL; U88080; AAC51656.1; -; Genomic_DNA.
DR EMBL; U88079; AAC51656.1; JOINED; Genomic_DNA.
DR EMBL; AK302402; BAG63713.1; -; mRNA.
DR EMBL; AL358933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03135.1; -; Genomic_DNA.
DR EMBL; BC096282; AAH96282.1; -; mRNA.
DR EMBL; BC096283; AAH96283.1; -; mRNA.
DR EMBL; BC096284; AAH96284.1; -; mRNA.
DR EMBL; BC113961; AAI13962.1; -; mRNA.
DR EMBL; BC130032; AAI30033.1; -; mRNA.
DR EMBL; BC152378; AAI52379.1; -; mRNA.
DR CCDS; CCDS4645.1; -. [Q15776-1]
DR RefSeq; NP_001265048.1; NM_001278119.1. [Q15776-1]
DR RefSeq; NP_001265050.1; NM_001278121.1.
DR RefSeq; NP_006289.2; NM_006298.3. [Q15776-1]
DR RefSeq; XP_011513172.1; XM_011514870.2. [Q15776-1]
DR RefSeq; XP_016866755.1; XM_017011266.1. [Q15776-1]
DR AlphaFoldDB; Q15776; -.
DR SMR; Q15776; -.
DR BioGRID; 113529; 136.
DR IntAct; Q15776; 51.
DR STRING; 9606.ENSP00000332750; -.
DR iPTMnet; Q15776; -.
DR PhosphoSitePlus; Q15776; -.
DR BioMuta; ZKSCAN8; -.
DR DMDM; 116242856; -.
DR EPD; Q15776; -.
DR jPOST; Q15776; -.
DR MassIVE; Q15776; -.
DR MaxQB; Q15776; -.
DR PaxDb; Q15776; -.
DR PeptideAtlas; Q15776; -.
DR PRIDE; Q15776; -.
DR ProteomicsDB; 5520; -.
DR ProteomicsDB; 60756; -. [Q15776-1]
DR TopDownProteomics; Q15776-1; -. [Q15776-1]
DR ABCD; Q15776; 4 sequenced antibodies.
DR Antibodypedia; 830; 189 antibodies from 27 providers.
DR DNASU; 7745; -.
DR Ensembl; ENST00000330236.7; ENSP00000332750.5; ENSG00000198315.11. [Q15776-1]
DR Ensembl; ENST00000457389.6; ENSP00000402948.2; ENSG00000198315.11. [Q15776-1]
DR Ensembl; ENST00000536028.2; ENSP00000439117.1; ENSG00000198315.11. [Q15776-2]
DR Ensembl; ENST00000606198.5; ENSP00000475589.1; ENSG00000198315.11. [Q15776-2]
DR GeneID; 7745; -.
DR KEGG; hsa:7745; -.
DR MANE-Select; ENST00000330236.7; ENSP00000332750.5; NM_006298.4; NP_006289.2.
DR UCSC; uc003nkn.3; human. [Q15776-1]
DR CTD; 7745; -.
DR DisGeNET; 7745; -.
DR GeneCards; ZKSCAN8; -.
DR HGNC; HGNC:12983; ZKSCAN8.
DR HPA; ENSG00000198315; Low tissue specificity.
DR MIM; 602240; gene.
DR neXtProt; NX_Q15776; -.
DR OpenTargets; ENSG00000198315; -.
DR PharmGKB; PA37563; -.
DR VEuPathDB; HostDB:ENSG00000198315; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161576; -.
DR HOGENOM; CLU_002678_53_4_1; -.
DR InParanoid; Q15776; -.
DR OMA; AARCNGD; -.
DR PhylomeDB; Q15776; -.
DR TreeFam; TF338146; -.
DR PathwayCommons; Q15776; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q15776; -.
DR BioGRID-ORCS; 7745; 6 hits in 1095 CRISPR screens.
DR ChiTaRS; ZKSCAN8; human.
DR GenomeRNAi; 7745; -.
DR Pharos; Q15776; Tbio.
DR PRO; PR:Q15776; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q15776; protein.
DR Bgee; ENSG00000198315; Expressed in ganglionic eminence and 168 other tissues.
DR ExpressionAtlas; Q15776; baseline and differential.
DR Genevisible; Q15776; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..578
FT /note="Zinc finger protein with KRAB and SCAN domains 8"
FT /id="PRO_0000047445"
FT DOMAIN 51..133
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 220..316
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 322..344
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..400
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 406..428
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..456
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 462..484
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 490..512
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 518..540
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..568
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 288
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 502
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 142..158
FT /note="ARVHGHRVLWEEVVHSA -> RRRSQLAYMDIGYSGRR (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056437"
FT VAR_SEQ 159..578
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056438"
FT VARIANT 163
FT /note="P -> L (in dbSNP:rs62620225)"
FT /evidence="ECO:0000269|PubMed:9244436"
FT /id="VAR_009877"
FT CONFLICT 34
FT /note="D -> A (in Ref. 1; AAB02260/AAC51656)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="E -> D (in Ref. 1; AAB02260/AAC51656)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="E -> G (in Ref. 5; AAH96283)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="Q -> R (in Ref. 5; AAH96284)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="L -> F (in Ref. 5; AAH96283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 65816 MW; 0A4FCA610DFF31F2 CRC64;
MAEESRKPSA PSPPDQTPEE DLVIVKVEED HGWDQESSLH ESNPLGQEVF RLRFRQLRYQ
ETLGPREALI QLRALCHQWL RPDLNTKEQI LELLVLEQFL TILPEELQTL VKEHQLENGE
EVVTLLEDLE RQIDILGRPV SARVHGHRVL WEEVVHSASA PEPPNTQLQS EATQHKSPVP
QESQERAMST SQSPTRSQKG SSGDQEMTAT LLTAGFQTLE KIEDMAVSLI REEWLLDPSQ
KDLCRDNRPE NFRNMFSLGG ETRSENRELA SKQVISTGIQ PHGETAAKCN GDVIRGLEHE
EARDLLGRLE RQRGNPTQER RHKCDECGKS FAQSSGLVRH WRIHTGEKPY QCNVCGKAFS
YRSALLSHQD IHNKVKRYHC KECGKAFSQN TGLILHQRIH TGEKPYQCNQ CGKAFSQSAG
LILHQRIHSG ERPYECNECG KAFSHSSHLI GHQRIHTGEK PYECDECGKT FRRSSHLIGH
QRSHTGEKPY KCNECGRAFS QKSGLIEHQR IHTGERPYKC KECGKAFNGN TGLIQHLRIH
TGEKPYQCNE CGKAFIQRSS LIRHQRIHSG EKSESISV
