ZN239_HUMAN
ID ZN239_HUMAN Reviewed; 458 AA.
AC Q16600; Q5T1G9; Q8TAS5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Zinc finger protein 239;
DE AltName: Full=Zinc finger protein HOK-2;
DE AltName: Full=Zinc finger protein MOK-2;
GN Name=ZNF239; Synonyms=HOK2, MOK2;
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], AND VARIANTS GLY-172; GLY-209 AND
RP GLU-266.
RX PubMed=8587123; DOI=10.1007/bf00173158;
RA Ernoult-Lange M., Arranz V., le Coniat M., Berger R., Kress M.;
RT "Human and mouse Kruppel-like (MOK2) orthologue genes encode two different
RT zinc finger proteins.";
RL J. Mol. Evol. 41:784-794(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, 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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-108, 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 Q16600; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-8787052, EBI-3866279;
CC Q16600; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-8787052, EBI-739624;
CC Q16600; P28799: GRN; NbExp=3; IntAct=EBI-8787052, EBI-747754;
CC Q16600; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-8787052, EBI-12012928;
CC Q16600; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-8787052, EBI-11522433;
CC Q16600; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-8787052, EBI-5235340;
CC Q16600; O76024: WFS1; NbExp=3; IntAct=EBI-8787052, EBI-720609;
CC Q16600; Q15007: WTAP; NbExp=3; IntAct=EBI-8787052, EBI-751647;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; X82125; CAA57637.1; -; mRNA.
DR EMBL; X82126; CAA57638.1; -; Genomic_DNA.
DR EMBL; AL450326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026030; AAH26030.1; -; mRNA.
DR CCDS; CCDS41502.1; -.
DR RefSeq; NP_001092752.1; NM_001099282.1.
DR RefSeq; NP_001092753.1; NM_001099283.1.
DR RefSeq; NP_001092754.1; NM_001099284.1.
DR RefSeq; NP_001311276.1; NM_001324347.1.
DR RefSeq; NP_001311277.1; NM_001324348.1.
DR RefSeq; NP_001311278.1; NM_001324349.1.
DR RefSeq; NP_001311279.1; NM_001324350.1.
DR RefSeq; NP_001311280.1; NM_001324351.1.
DR RefSeq; NP_005665.2; NM_005674.2.
DR RefSeq; XP_005271889.1; XM_005271832.2.
DR RefSeq; XP_006718066.1; XM_006718003.3.
DR RefSeq; XP_011538540.1; XM_011540238.2.
DR AlphaFoldDB; Q16600; -.
DR SMR; Q16600; -.
DR BioGRID; 113831; 7.
DR IntAct; Q16600; 10.
DR STRING; 9606.ENSP00000307774; -.
DR iPTMnet; Q16600; -.
DR PhosphoSitePlus; Q16600; -.
DR BioMuta; ZNF239; -.
DR DMDM; 251757424; -.
DR EPD; Q16600; -.
DR jPOST; Q16600; -.
DR MassIVE; Q16600; -.
DR MaxQB; Q16600; -.
DR PaxDb; Q16600; -.
DR PeptideAtlas; Q16600; -.
DR PRIDE; Q16600; -.
DR ProteomicsDB; 60941; -.
DR Antibodypedia; 6019; 108 antibodies from 19 providers.
DR DNASU; 8187; -.
DR Ensembl; ENST00000306006.10; ENSP00000307774.6; ENSG00000196793.14.
DR Ensembl; ENST00000374446.7; ENSP00000363569.1; ENSG00000196793.14.
DR Ensembl; ENST00000426961.1; ENSP00000398202.1; ENSG00000196793.14.
DR Ensembl; ENST00000535642.5; ENSP00000443907.1; ENSG00000196793.14.
DR GeneID; 8187; -.
DR KEGG; hsa:8187; -.
DR MANE-Select; ENST00000374446.7; ENSP00000363569.1; NM_001099282.2; NP_001092752.1.
DR UCSC; uc001jaw.5; human.
DR CTD; 8187; -.
DR DisGeNET; 8187; -.
DR GeneCards; ZNF239; -.
DR HGNC; HGNC:13031; ZNF239.
DR HPA; ENSG00000196793; Low tissue specificity.
DR MIM; 601069; gene.
DR neXtProt; NX_Q16600; -.
DR OpenTargets; ENSG00000196793; -.
DR PharmGKB; PA37609; -.
DR VEuPathDB; HostDB:ENSG00000196793; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163366; -.
DR HOGENOM; CLU_002678_12_0_1; -.
DR InParanoid; Q16600; -.
DR OMA; LLIHHSV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q16600; -.
DR TreeFam; TF350845; -.
DR PathwayCommons; Q16600; -.
DR SignaLink; Q16600; -.
DR SIGNOR; Q16600; -.
DR BioGRID-ORCS; 8187; 11 hits in 1101 CRISPR screens.
DR ChiTaRS; ZNF239; human.
DR GeneWiki; ZNF239; -.
DR GenomeRNAi; 8187; -.
DR Pharos; Q16600; Tbio.
DR PRO; PR:Q16600; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q16600; protein.
DR Bgee; ENSG00000196793; Expressed in endothelial cell and 112 other tissues.
DR Genevisible; Q16600; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..458
FT /note="Zinc finger protein 239"
FT /id="PRO_0000047480"
FT ZN_FING 207..229
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 235..257
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 263..285
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 291..313
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..369
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 375..397
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 172
FT /note="A -> G (in dbSNP:rs2230660)"
FT /evidence="ECO:0000269|PubMed:8587123"
FT /id="VAR_024205"
FT VARIANT 209
FT /note="C -> G (in dbSNP:rs2230661)"
FT /evidence="ECO:0000269|PubMed:8587123"
FT /id="VAR_024206"
FT VARIANT 266
FT /note="D -> E (in dbSNP:rs1128865)"
FT /evidence="ECO:0000269|PubMed:8587123"
FT /id="VAR_025536"
FT CONFLICT 340
FT /note="V -> D (in Ref. 1; CAA57637/CAA57638)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="I -> S (in Ref. 1; CAA57637/CAA57638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 51591 MW; 94753A790CB5F559 CRC64;
MASTITGSQD CIVNHRGEVD GEPELDISPC QQWGEASSPI SRNRDSVMTL QSGCFENIES
ETYLPLKVSS QIDTQDSSVK FCKNEPQDHQ ESRRLFVMEE STERKVIKGE SCSENLQVKL
VSDGQELASP LLNGEATCQN GQLKESLDPI DCNCKDIHGW KSQVVSCSQQ RAHTEEKPCD
HNNCGKILNT SPDGHPYEKI HTAEKQYECS QCGKNFSQSS ELLLHQRDHT EEKPYKCEQC
GKGFTRSSSL LIHQAVHTDE KPYKCDKCGK GFTRSSSLLI HHAVHTGEKP YKCDKCGKGF
SQSSKLHIHQ RVHTGEKPYE CEECGMSFSQ RSNLHIHQRV HTGERPYKCG ECGKGFSQSS
NLHIHRCIHT GEKPYQCYEC GKGFSQSSDL RIHLRVHTGE KPYHCGKCGK GFSQSSKLLI
HQRVHTGEKP YECSKCGKGF SQSSNLHIHQ RVHKKDPR
