ID ZKSC2_HUMAN Reviewed; 967 AA. AC Q63HK3; A1L3B4; Q6ZN77; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 14-DEC-2022, entry version 148. DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 2; DE AltName: Full=Zinc finger protein 694; GN Name=ZKSCAN2; Synonyms=ZNF694; 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 2). RC TISSUE=Thymus; 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 1). RC TISSUE=Uterine endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-615. RC TISSUE=Brain; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 AND SER-600, AND RP IDENTIFICATION BY 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 [6] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-242; LYS-259; LYS-277; RP LYS-337; LYS-482; LYS-529; LYS-734; LYS-745 AND LYS-752, AND IDENTIFICATION RP 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). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q63HK3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q63HK3-2; Sequence=VSP_018189, VSP_018190; 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; AK131342; BAD18498.1; -; mRNA. DR EMBL; BX648785; CAH56131.1; -; mRNA. DR EMBL; AC008741; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC130007; AAI30008.1; -; mRNA. DR EMBL; BC151139; AAI51140.1; -; mRNA. DR CCDS; CCDS32410.1; -. [Q63HK3-1] DR RefSeq; NP_001012999.3; NM_001012981.4. [Q63HK3-1] DR AlphaFoldDB; Q63HK3; -. DR SMR; Q63HK3; -. DR BioGRID; 131170; 7. DR STRING; 9606.ENSP00000331626; -. DR iPTMnet; Q63HK3; -. DR PhosphoSitePlus; Q63HK3; -. DR BioMuta; ZKSCAN2; -. DR DMDM; 296453036; -. DR jPOST; Q63HK3; -. DR MassIVE; Q63HK3; -. DR MaxQB; Q63HK3; -. DR PaxDb; Q63HK3; -. DR PeptideAtlas; Q63HK3; -. DR ProteomicsDB; 65876; -. [Q63HK3-1] DR ProteomicsDB; 65877; -. [Q63HK3-2] DR ABCD; Q63HK3; 5 sequenced antibodies. DR Antibodypedia; 59128; 57 antibodies from 12 providers. DR DNASU; 342357; -. DR Ensembl; ENST00000328086.12; ENSP00000331626.7; ENSG00000155592.16. [Q63HK3-1] DR GeneID; 342357; -. DR KEGG; hsa:342357; -. DR MANE-Select; ENST00000328086.12; ENSP00000331626.7; NM_001012981.5; NP_001012999.3. DR UCSC; uc002dod.5; human. [Q63HK3-1] DR AGR; HGNC:25677; -. DR CTD; 342357; -. DR GeneCards; ZKSCAN2; -. DR HGNC; HGNC:25677; ZKSCAN2. DR HPA; ENSG00000155592; Low tissue specificity. DR neXtProt; NX_Q63HK3; -. DR PharmGKB; PA162409748; -. DR VEuPathDB; HostDB:ENSG00000155592; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000161884; -. DR HOGENOM; CLU_002678_88_0_1; -. DR InParanoid; Q63HK3; -. DR OMA; NGHMLEP; -. DR OrthoDB; 1318335at2759; -. DR PhylomeDB; Q63HK3; -. DR TreeFam; TF336839; -. DR PathwayCommons; Q63HK3; -. DR BioGRID-ORCS; 342357; 16 hits in 1106 CRISPR screens. DR GenomeRNAi; 342357; -. DR Pharos; Q63HK3; Tdark. DR PRO; PR:Q63HK3; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q63HK3; protein. DR Bgee; ENSG00000155592; Expressed in cortical plate and 150 other tissues. DR ExpressionAtlas; Q63HK3; baseline and differential. DR Genevisible; Q63HK3; 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; IPR044822; Myb_DNA-bind_4. DR InterPro; IPR038765; Papain-like_cys_pep_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; PF13837; Myb_DNA-bind_4; 2. DR Pfam; PF02023; SCAN; 1. DR Pfam; PF00096; zf-C2H2; 4. DR SMART; SM00349; KRAB; 1. DR SMART; SM00431; SCAN; 1. DR SMART; SM00355; ZnF_C2H2; 6. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS50804; SCAN_BOX; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. 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..967 FT /note="Zinc finger protein with KRAB and SCAN domains 2" FT /id="PRO_0000234016" FT DOMAIN 45..127 FT /note="SCAN box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187" FT DOMAIN 229..300 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 775..797 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 803..825 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 831..853 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 859..881 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 887..909 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 915..937 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 150..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 586..626 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 941..967 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 172..189 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 591 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 600 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 242 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 259 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 277 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 337 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 482 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 529 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 734 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 745 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 752 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 498..505 FT /note="VHWGYEET -> KNCALFLW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_018189" FT VAR_SEQ 506..967 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_018190" FT VARIANT 253 FT /note="L -> F (in dbSNP:rs2112811)" FT /id="VAR_033597" FT VARIANT 615 FT /note="E -> D (in dbSNP:rs8059494)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_033598" FT VARIANT 947 FT /note="P -> S (in dbSNP:rs7197424)" FT /id="VAR_057460" FT CONFLICT 667 FT /note="S -> G (in Ref. 2; CAH56131)" FT /evidence="ECO:0000305" SQ SEQUENCE 967 AA; 110941 MW; 6742FECD4D5D5300 CRC64; MAVALDSQID APLEVEGCLI MKVEKDPEWA SEPILEGSDS SETFRKCFRQ FCYEDVTGPH EAFSKLWELC CRWLKPEMRS KEQILELLVI EQFLTILPEK IQAWAQKQCP QSGEEAVALV VHLEKETGRL RQQVSSPVHR EKHSPLGAAW EVADFQPEQV ETQPRAVSRE EPGSLHSGHQ EQLNRKRERR PLPKNARPSP WVPALADEWN TLDQEVTTTR LPAGSQEPVK DVHVARGFSY RKSVHQIPAQ RDLYRDFRKE NVGNVVSLGS AVSTSNKITR LEQRKEPWTL GLHSSNKRSI LRSNYVKEKS VHAIQVPARS AGKTWREQQQ WGLEDEKIAG VHWSYEETKT FLAILKESRF YETLQACPRN SQVYGAVAEW LRECGFLRTP EQCRTKFKSL QKSYRKVRNG HMLEPCAFFE DMDALLNPAA RAPSTDKPKE MIPVPRLKRI AISAKEHISL VEEEEAAEDS DDDEIGIEFI RKSEIHGAPV LFQNLSGVHW GYEETKTFLD ILRETRFYEA LQACHRKSKL YGAVAEQLRE CGFLRTPEQC RTKFKSLQKS YRKVKNGHVL ESCAFYKEMD ALINSRASAP SPSTPEEVPS PSRQERGGIE VEPQEPTGWE PEETSQEAVI EDSCSERMSE EEIVQEPEFQ GPPGLLQSPN DFEIGSSIKE DPTQIVYKDM EQHRALIEKS KRVVSQSTDP SKYRKRECIS GRQWENLQGI RQGKPMSQPR DLGKAVVHQR PFVGKRPYRL LKYGESFGRS TRLMCRMTHH KENPYKCGVC GKCFGRSRSL IRHQRIHTGE KPFKCLDCGK SFNDSSNFGA HQRIHTGEKP YRCGECGKCF SQSSSLIIHQ RTHTGEKPYQ CGECGKSFTN SSHFSAHRRV HTGENPYKCV DCEKSFNNCT RFREHRRIHT GEKPYGCAQC GKRFSKSSVL TKHREVHVRE KPLPHPPSLY CPENPHKGKT DEFRKTF //