ZKSC5_HUMAN
ID ZKSC5_HUMAN Reviewed; 839 AA.
AC Q9Y2L8; A4D280; D6W5S9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 5;
DE AltName: Full=Zinc finger protein 95 homolog;
DE Short=Zfp-95;
GN Name=ZKSCAN5; Synonyms=KIAA1015, ZFP95;
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].
RX PubMed=10585779; DOI=10.1006/geno.1999.5981;
RA Dreyer S.D., Zheng Q., Zabel B., Winterpacht A., Lee B.;
RT "Isolation, characterization, and mapping of a zinc finger gene, ZFP95,
RT containing both a SCAN box and an alternatively spliced KRAB A domain.";
RL Genomics 62:119-122(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-216; LYS-248; LYS-270; LYS-303;
RP LYS-317; LYS-509; LYS-513; LYS-709 AND LYS-785, 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).
RN [7]
RP STRUCTURE BY NMR OF 369-828.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C2H2 type zinc finger region of human zinc
RT finger protein 95 homolog.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9Y2L8; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-2876965, EBI-702390;
CC Q9Y2L8; P14136: GFAP; NbExp=3; IntAct=EBI-2876965, EBI-744302;
CC Q9Y2L8; Q53GS7: GLE1; NbExp=3; IntAct=EBI-2876965, EBI-1955541;
CC Q9Y2L8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2876965, EBI-5235340;
CC Q9Y2L8; O43463: SUV39H1; NbExp=2; IntAct=EBI-2876965, EBI-349968;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76859.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF170025; AAF24219.1; -; mRNA.
DR EMBL; AB023232; BAA76859.2; ALT_INIT; mRNA.
DR EMBL; CH236956; EAL23873.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76654.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76655.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76656.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76657.1; -; Genomic_DNA.
DR CCDS; CCDS5667.1; -.
DR RefSeq; NP_001305011.1; NM_001318082.1.
DR RefSeq; NP_001305012.1; NM_001318083.1.
DR RefSeq; NP_001305013.1; NM_001318084.1.
DR RefSeq; NP_055384.1; NM_014569.3.
DR RefSeq; NP_659570.1; NM_145102.3.
DR RefSeq; XP_016867407.1; XM_017011918.1.
DR RefSeq; XP_016867408.1; XM_017011919.1.
DR PDB; 2EM5; NMR; -; A=768-800.
DR PDB; 2EMM; NMR; -; A=544-576.
DR PDB; 2EMZ; NMR; -; A=628-660.
DR PDB; 2EN3; NMR; -; A=796-828.
DR PDB; 2EOM; NMR; -; A=341-373.
DR PDB; 2EON; NMR; -; A=397-429.
DR PDB; 2EOO; NMR; -; A=425-457.
DR PDB; 2YSO; NMR; -; A=656-688.
DR PDB; 2YTG; NMR; -; A=369-401.
DR PDBsum; 2EM5; -.
DR PDBsum; 2EMM; -.
DR PDBsum; 2EMZ; -.
DR PDBsum; 2EN3; -.
DR PDBsum; 2EOM; -.
DR PDBsum; 2EON; -.
DR PDBsum; 2EOO; -.
DR PDBsum; 2YSO; -.
DR PDBsum; 2YTG; -.
DR AlphaFoldDB; Q9Y2L8; -.
DR SMR; Q9Y2L8; -.
DR BioGRID; 117182; 13.
DR IntAct; Q9Y2L8; 13.
DR MINT; Q9Y2L8; -.
DR STRING; 9606.ENSP00000377725; -.
DR iPTMnet; Q9Y2L8; -.
DR PhosphoSitePlus; Q9Y2L8; -.
DR BioMuta; ZKSCAN5; -.
DR DMDM; 11136143; -.
DR jPOST; Q9Y2L8; -.
DR MassIVE; Q9Y2L8; -.
DR MaxQB; Q9Y2L8; -.
DR PaxDb; Q9Y2L8; -.
DR PeptideAtlas; Q9Y2L8; -.
DR PRIDE; Q9Y2L8; -.
DR ProteomicsDB; 85838; -.
DR ABCD; Q9Y2L8; 4 sequenced antibodies.
DR Antibodypedia; 30392; 125 antibodies from 21 providers.
DR DNASU; 23660; -.
DR Ensembl; ENST00000326775.10; ENSP00000322872.5; ENSG00000196652.12.
DR Ensembl; ENST00000394170.6; ENSP00000377725.2; ENSG00000196652.12.
DR Ensembl; ENST00000451158.5; ENSP00000392104.1; ENSG00000196652.12.
DR GeneID; 23660; -.
DR KEGG; hsa:23660; -.
DR MANE-Select; ENST00000326775.10; ENSP00000322872.5; NM_145102.4; NP_659570.1.
DR UCSC; uc003uqv.4; human.
DR CTD; 23660; -.
DR DisGeNET; 23660; -.
DR GeneCards; ZKSCAN5; -.
DR HGNC; HGNC:12867; ZKSCAN5.
DR HPA; ENSG00000196652; Low tissue specificity.
DR MIM; 611272; gene.
DR neXtProt; NX_Q9Y2L8; -.
DR OpenTargets; ENSG00000196652; -.
DR PharmGKB; PA162409785; -.
DR VEuPathDB; HostDB:ENSG00000196652; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162299; -.
DR HOGENOM; CLU_002678_23_3_1; -.
DR InParanoid; Q9Y2L8; -.
DR OMA; TKSHQCN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Y2L8; -.
DR TreeFam; TF338146; -.
DR PathwayCommons; Q9Y2L8; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9Y2L8; -.
DR BioGRID-ORCS; 23660; 20 hits in 1101 CRISPR screens.
DR ChiTaRS; ZKSCAN5; human.
DR EvolutionaryTrace; Q9Y2L8; -.
DR GeneWiki; ZKSCAN5; -.
DR GenomeRNAi; 23660; -.
DR Pharos; Q9Y2L8; Tdark.
DR PRO; PR:Q9Y2L8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y2L8; protein.
DR Bgee; ENSG00000196652; Expressed in tendon of biceps brachii and 152 other tissues.
DR ExpressionAtlas; Q9Y2L8; baseline and differential.
DR Genevisible; Q9Y2L8; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
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; 10.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
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; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..839
FT /note="Zinc finger protein with KRAB and SCAN domains 5"
FT /id="PRO_0000047315"
FT DOMAIN 51..132
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 218..291
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 346..368
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 402..424
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..452
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 549..571
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 577..599
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 605..627
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..655
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 661..683
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 717..739
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 745..763
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 773..795
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 801..823
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 785
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2EOM"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:2EOM"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:2YTG"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:2YTG"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:2YTG"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:2YTG"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:2YTG"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2EON"
FT HELIX 414..420
FT /evidence="ECO:0007829|PDB:2EON"
FT TURN 421..425
FT /evidence="ECO:0007829|PDB:2EON"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:2EOO"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:2EOO"
FT HELIX 442..453
FT /evidence="ECO:0007829|PDB:2EOO"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:2EMM"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:2EMM"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:2EMM"
FT HELIX 561..571
FT /evidence="ECO:0007829|PDB:2EMM"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:2EMZ"
FT HELIX 645..657
FT /evidence="ECO:0007829|PDB:2EMZ"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:2YSO"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:2YSO"
FT HELIX 673..683
FT /evidence="ECO:0007829|PDB:2YSO"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:2EM5"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:2EM5"
FT STRAND 781..784
FT /evidence="ECO:0007829|PDB:2EM5"
FT HELIX 785..792
FT /evidence="ECO:0007829|PDB:2EM5"
FT TURN 793..795
FT /evidence="ECO:0007829|PDB:2EM5"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:2EN3"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:2EN3"
FT STRAND 809..813
FT /evidence="ECO:0007829|PDB:2EN3"
FT HELIX 814..825
FT /evidence="ECO:0007829|PDB:2EN3"
SQ SEQUENCE 839 AA; 96903 MW; F2E082CF6610806D CRC64;
MIMTESREVI DLDPPAETSQ EQEDLFIVKV EEEDCTWMQE YNPPTFETFY QRFRHFQYHE
ASGPREALSQ LRVLCCEWLR PELHTKEQIL ELLVLEQFLT ILPEEFQPWV REHHPESGEE
AVAVIENIQR ELEERRQQIV ACPDVLPRKM ATPGAVQESC SPHPLTVDTQ PEQAPQKPRL
LEENALPVLQ VPSLPLKDSQ ELTASLLSTG SQKLVKIEEV ADVAVSFILE EWGHLDQSQK
SLYRDDRKEN YGSITSMGYE SRDNMELIVK QISDDSESHW VAPEHTERSV PQDPDFAEVS
DLKGMVQRWQ VNPTVGKSRQ NPSQKRDLDA ITDISPKQST HGERGHRCSD CGKFFLQASN
FIQHRRIHTG EKPFKCGECG KSYNQRVHLT QHQRVHTGEK PYKCQVCGKA FRVSSHLVQH
HSVHSGERPY GCNECGKNFG RHSHLIEHLK RHFREKSQRC SDKRSKNTKL SVKKKISEYS
EADMELSGKT QRNVSQVQDF GEGCEFQGKL DRKQGIPMKE ILGQPSSKRM NYSEVPYVHK
KSSTGERPHK CNECGKSFIQ SAHLIQHQRI HTGEKPFRCE ECGKSYNQRV HLTQHQRVHT
GEKPYTCPLC GKAFRVRSHL VQHQSVHSGE RPFKCNECGK GFGRRSHLAG HLRLHSREKS
HQCRECGEIF FQYVSLIEHQ VLHMGQKNEK NGICEEAYSW NLTVIEDKKI ELQEQPYQCD
ICGKAFGYSS DLIQHYRTHT AEKPYQCDIC RENVGQCSHT KQHQKIYSST KSHQCHECGR
GFTLKSHLNQ HQRIHTGEKP FQCKECGMNF SWSCSLFKHL RSHERTDPIN TLSVEGSLL
