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   27-MAR-2024, entry version 193.
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; 8.
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; 9606-ENSP00000307774; -.
DR   PeptideAtlas; Q16600; -.
DR   ProteomicsDB; 60941; -.
DR   Pumba; Q16600; -.
DR   Antibodypedia; 6019; 129 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   AGR; HGNC:13031; -.
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; 3831299at2759; -.
DR   PhylomeDB; Q16600; -.
DR   TreeFam; TF350845; -.
DR   PathwayCommons; Q16600; -.
DR   SignaLink; Q16600; -.
DR   SIGNOR; Q16600; -.
DR   BioGRID-ORCS; 8187; 11 hits in 1177 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 primordial germ cell in gonad and 114 other cell types or tissues.
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   Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24393; ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR24393:SF88; ZINC FINGER PROTEIN 485; 1.
DR   Pfam; PF00096; zf-C2H2; 9.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
DR   Genevisible; Q16600; HS.
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
//