ZKSC7_HUMAN
ID ZKSC7_HUMAN Reviewed; 754 AA.
AC Q9P0L1; A0PJV3; A8K5H0; Q6WL09; Q96FQ2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 7;
DE AltName: Full=Zinc finger protein 167;
DE AltName: Full=Zinc finger protein 448;
DE AltName: Full=Zinc finger protein 64;
GN Name=ZKSCAN7; Synonyms=ZNF167, ZNF448, ZNF64;
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 [MRNA] (ISOFORM 1), AND VARIANT ILE-483.
RA Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.;
RT "Cloning and isolating human ZFP cDNA.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Luo K.T., Yu L.;
RT "Cloning and characterization of a human novel znf gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-483.
RC TISSUE=Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-28, 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 Q9P0L1; P57086: SCAND1; NbExp=4; IntAct=EBI-743851, EBI-745846;
CC Q9P0L1; Q969J2: ZKSCAN4; NbExp=4; IntAct=EBI-743851, EBI-2818641;
CC Q9P0L1; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-743851, EBI-740232;
CC Q9P0L1; O43309: ZSCAN12; NbExp=3; IntAct=EBI-743851, EBI-1210440;
CC Q9P0L1; Q9Y5A6: ZSCAN21; NbExp=3; IntAct=EBI-743851, EBI-10281938;
CC Q9P0L1-2; Q96JS3: PGBD1; NbExp=3; IntAct=EBI-10698225, EBI-10290053;
CC Q9P0L1-2; P57086: SCAND1; NbExp=6; IntAct=EBI-10698225, EBI-745846;
CC Q9P0L1-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-10698225, EBI-11955057;
CC Q9P0L1-2; A0A0S2Z6X0: ZKSCAN4; NbExp=3; IntAct=EBI-10698225, EBI-16431094;
CC Q9P0L1-2; Q969J2: ZKSCAN4; NbExp=6; IntAct=EBI-10698225, EBI-2818641;
CC Q9P0L1-2; Q9Y5A6: ZSCAN21; NbExp=3; IntAct=EBI-10698225, EBI-10281938;
CC Q9P0L1-2; P10073: ZSCAN22; NbExp=3; IntAct=EBI-10698225, EBI-10178224;
CC Q9P0L1-2; Q3MJ62: ZSCAN23; NbExp=3; IntAct=EBI-10698225, EBI-5667532;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P0L1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0L1-2; Sequence=VSP_011955, VSP_011956;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF154846; AAF72104.1; -; mRNA.
DR EMBL; AY280798; AAQ16302.1; -; mRNA.
DR EMBL; AK291285; BAF83974.1; -; mRNA.
DR EMBL; BC010555; AAH10555.1; -; mRNA.
DR EMBL; BC063020; AAH63020.1; -; mRNA.
DR EMBL; BC127640; AAI27641.1; -; mRNA.
DR CCDS; CCDS2714.1; -. [Q9P0L1-2]
DR CCDS; CCDS2715.1; -. [Q9P0L1-1]
DR PIR; G45193; G45193.
DR RefSeq; NP_001275519.1; NM_001288590.1. [Q9P0L1-1]
DR RefSeq; NP_001275520.1; NM_001288591.1. [Q9P0L1-2]
DR RefSeq; NP_001275521.1; NM_001288592.1.
DR RefSeq; NP_061121.2; NM_018651.3. [Q9P0L1-1]
DR RefSeq; NP_079445.1; NM_025169.2. [Q9P0L1-2]
DR AlphaFoldDB; Q9P0L1; -.
DR SMR; Q9P0L1; -.
DR BioGRID; 120978; 18.
DR IntAct; Q9P0L1; 16.
DR STRING; 9606.ENSP00000273320; -.
DR iPTMnet; Q9P0L1; -.
DR PhosphoSitePlus; Q9P0L1; -.
DR BioMuta; ZKSCAN7; -.
DR DMDM; 124078992; -.
DR jPOST; Q9P0L1; -.
DR MassIVE; Q9P0L1; -.
DR MaxQB; Q9P0L1; -.
DR PaxDb; Q9P0L1; -.
DR PeptideAtlas; Q9P0L1; -.
DR PRIDE; Q9P0L1; -.
DR ProteomicsDB; 83569; -. [Q9P0L1-1]
DR Antibodypedia; 12496; 88 antibodies from 21 providers.
DR DNASU; 55888; -.
DR Ensembl; ENST00000273320.7; ENSP00000273320.3; ENSG00000196345.13. [Q9P0L1-1]
DR Ensembl; ENST00000341840.7; ENSP00000345404.3; ENSG00000196345.13. [Q9P0L1-2]
DR Ensembl; ENST00000426540.6; ENSP00000395524.1; ENSG00000196345.13. [Q9P0L1-1]
DR Ensembl; ENST00000431636.5; ENSP00000416681.1; ENSG00000196345.13. [Q9P0L1-2]
DR Ensembl; ENST00000625422.2; ENSP00000486331.1; ENSG00000281894.3. [Q9P0L1-2]
DR Ensembl; ENST00000626497.2; ENSP00000485942.1; ENSG00000281894.3. [Q9P0L1-1]
DR Ensembl; ENST00000629379.3; ENSP00000485948.1; ENSG00000281894.3. [Q9P0L1-1]
DR Ensembl; ENST00000629459.2; ENSP00000486642.1; ENSG00000281894.3. [Q9P0L1-2]
DR GeneID; 55888; -.
DR KEGG; hsa:55888; -.
DR MANE-Select; ENST00000426540.6; ENSP00000395524.1; NM_001288590.2; NP_001275519.1.
DR UCSC; uc003cni.5; human. [Q9P0L1-1]
DR CTD; 55888; -.
DR DisGeNET; 55888; -.
DR GeneCards; ZKSCAN7; -.
DR HGNC; HGNC:12955; ZKSCAN7.
DR HPA; ENSG00000196345; Low tissue specificity.
DR neXtProt; NX_Q9P0L1; -.
DR OpenTargets; ENSG00000196345; -.
DR PharmGKB; PA37537; -.
DR VEuPathDB; HostDB:ENSG00000196345; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162985; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; Q9P0L1; -.
DR OMA; EPASQTW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9P0L1; -.
DR TreeFam; TF350837; -.
DR PathwayCommons; Q9P0L1; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9P0L1; -.
DR BioGRID-ORCS; 55888; 7 hits in 1087 CRISPR screens.
DR ChiTaRS; ZKSCAN7; human.
DR GenomeRNAi; 55888; -.
DR Pharos; Q9P0L1; Tbio.
DR PRO; PR:Q9P0L1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9P0L1; protein.
DR Bgee; ENSG00000196345; Expressed in ganglionic eminence and 101 other tissues.
DR ExpressionAtlas; Q9P0L1; baseline and differential.
DR Genevisible; Q9P0L1; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; 13.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..754
FT /note="Zinc finger protein with KRAB and SCAN domains 7"
FT /id="PRO_0000047437"
FT DOMAIN 54..136
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 231..306
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 383..405
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..433
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 439..461
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..545
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 551..573
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 579..601
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 607..629
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 635..657
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 663..685
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 691..713
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 719..741
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 157..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 271..276
FT /note="AGENMM -> GWSTMA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011955"
FT VAR_SEQ 277..754
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011956"
FT VARIANT 24
FT /note="R -> C (in dbSNP:rs35696191)"
FT /id="VAR_052782"
FT VARIANT 153
FT /note="F -> S (in dbSNP:rs13081859)"
FT /id="VAR_052783"
FT VARIANT 342
FT /note="T -> I (in dbSNP:rs34396823)"
FT /id="VAR_052784"
FT VARIANT 359
FT /note="E -> K (in dbSNP:rs34181686)"
FT /id="VAR_052785"
FT VARIANT 432
FT /note="T -> A (in dbSNP:rs9835485)"
FT /id="VAR_052786"
FT VARIANT 483
FT /note="T -> I (in dbSNP:rs9873604)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT /id="VAR_052787"
FT VARIANT 746
FT /note="S -> F (in dbSNP:rs34437520)"
FT /id="VAR_052788"
FT CONFLICT 665
FT /note="C -> Y (in Ref. 1; AAF72104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 85033 MW; B568F187A3ED2D1B CRC64;
MTTAGRGNLG LIPRSTAFQK QEGRLTVKQE PANQTWGQGS SLQKNYPPVC EIFRLHFRQL
CYHEMSGPQE ALSRLRELCR WWLMPEVHTK EQILELLVLE QFLSILPGEL RTWVQLHHPE
SGEEAVAVVE DFQRHLSGSE EVSAPAQKQE MHFEETTALG TTKESPPTSP LSGGSAPGAH
LEPPYDPGTH HLPSGDFAQC TSPVPTLPQV GNSGDQAGAT VLRMVRPQDT VAYEDLSVDY
TQKKWKSLTL SQRALQWNMM PENHHSMASL AGENMMKGSE LTPKQEFFKG SESSNRTSGG
LFGVVPGAAE TGDVCEDTFK ELEGQTSDEE GSRLENDFLE ITDEDKKKST KDRYDKYKEV
GEHPPLSSSP VEHEGVLKGQ KSYRCDECGK AFNRSSHLIG HQRIHTGEKP YECNECGKTF
RQTSQLIVHL RTHTGEKPYE CSECGKAYRH SSHLIQHQRL HNGEKPYKCN ECAKAFTQSS
RLTDHQRTHT GEKPYECNEC GEAFIRSKSL ARHQVLHTGK KPYKCNECGR AFCSNRNLID
HQRIHTGEKP YECSECGKAF SRSKCLIRHQ SLHTGEKPYK CSECGKAFNQ NSQLIEHERI
HTGEKPFECS ECGKAFGLSK CLIRHQRLHT GEKPYKCNEC GKSFNQNSHL IIHQRIHTGE
KPYECNECGK VFSYSSSLMV HQRTHTGEKP YKCNDCGKAF SDSSQLIVHQ RVHTGEKPYE
CSECGKAFSQ RSTFNHHQRT HTGEKSSGLA WSVS
