ZKSC2_HUMAN
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 03-AUG-2022, entry version 146.
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}.
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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 PRIDE; Q63HK3; -.
DR ProteomicsDB; 65876; -. [Q63HK3-1]
DR ProteomicsDB; 65877; -. [Q63HK3-2]
DR ABCD; Q63HK3; 5 sequenced antibodies.
DR Antibodypedia; 59128; 55 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 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; SSF109640; SSF109640; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
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
