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ZN296_HUMAN
ID   ZN296_HUMAN             Reviewed;         475 AA.
AC   Q8WUU4;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Zinc finger protein 296;
DE            Short=ZFP296;
DE   AltName: Full=Zinc finger protein 342;
GN   Name=ZNF296; Synonyms=ZNF342;
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].
RC   TISSUE=Lung;
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   [2]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35, 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 a transcriptional corepressor with KLF4.
CC       {ECO:0000250|UniProtKB:E9Q6W4}.
CC   -!- SUBUNIT: Interacts with KLF4. {ECO:0000250|UniProtKB:E9Q6W4}.
CC   -!- INTERACTION:
CC       Q8WUU4; P02489: CRYAA; NbExp=3; IntAct=EBI-8834821, EBI-6875961;
CC       Q8WUU4; P22607: FGFR3; NbExp=3; IntAct=EBI-8834821, EBI-348399;
CC       Q8WUU4; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-8834821, EBI-10226858;
CC       Q8WUU4; O14908-2: GIPC1; NbExp=3; IntAct=EBI-8834821, EBI-25913156;
CC       Q8WUU4; P28799: GRN; NbExp=3; IntAct=EBI-8834821, EBI-747754;
CC       Q8WUU4; P54652: HSPA2; NbExp=3; IntAct=EBI-8834821, EBI-356991;
CC       Q8WUU4; P60891: PRPS1; NbExp=3; IntAct=EBI-8834821, EBI-749195;
CC       Q8WUU4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-8834821, EBI-396669;
CC       Q8WUU4; P37840: SNCA; NbExp=3; IntAct=EBI-8834821, EBI-985879;
CC       Q8WUU4; Q5JTV8: TOR1AIP1; NbExp=3; IntAct=EBI-8834821, EBI-2559665;
CC       Q8WUU4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-8834821, EBI-741480;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:E9Q6W4}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; BC019352; AAH19352.1; -; mRNA.
DR   CCDS; CCDS12653.1; -.
DR   RefSeq; NP_660331.1; NM_145288.2.
DR   AlphaFoldDB; Q8WUU4; -.
DR   SMR; Q8WUU4; -.
DR   BioGRID; 127837; 27.
DR   IntAct; Q8WUU4; 16.
DR   STRING; 9606.ENSP00000302770; -.
DR   iPTMnet; Q8WUU4; -.
DR   PhosphoSitePlus; Q8WUU4; -.
DR   BioMuta; ZNF296; -.
DR   DMDM; 23396987; -.
DR   jPOST; Q8WUU4; -.
DR   MassIVE; Q8WUU4; -.
DR   MaxQB; Q8WUU4; -.
DR   PaxDb; Q8WUU4; -.
DR   PeptideAtlas; Q8WUU4; -.
DR   PRIDE; Q8WUU4; -.
DR   ProteomicsDB; 74710; -.
DR   Antibodypedia; 17828; 127 antibodies from 19 providers.
DR   DNASU; 162979; -.
DR   Ensembl; ENST00000303809.7; ENSP00000302770.1; ENSG00000170684.10.
DR   GeneID; 162979; -.
DR   KEGG; hsa:162979; -.
DR   MANE-Select; ENST00000303809.7; ENSP00000302770.1; NM_145288.3; NP_660331.1.
DR   UCSC; uc002pao.4; human.
DR   CTD; 162979; -.
DR   DisGeNET; 162979; -.
DR   GeneCards; ZNF296; -.
DR   HGNC; HGNC:15981; ZNF296.
DR   HPA; ENSG00000170684; Tissue enhanced (esophagus).
DR   MIM; 613226; gene.
DR   neXtProt; NX_Q8WUU4; -.
DR   OpenTargets; ENSG00000170684; -.
DR   PharmGKB; PA37660; -.
DR   VEuPathDB; HostDB:ENSG00000170684; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160667; -.
DR   InParanoid; Q8WUU4; -.
DR   OMA; LGARNPW; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q8WUU4; -.
DR   TreeFam; TF318131; -.
DR   PathwayCommons; Q8WUU4; -.
DR   SignaLink; Q8WUU4; -.
DR   BioGRID-ORCS; 162979; 18 hits in 1104 CRISPR screens.
DR   GenomeRNAi; 162979; -.
DR   Pharos; Q8WUU4; Tbio.
DR   PRO; PR:Q8WUU4; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8WUU4; protein.
DR   Bgee; ENSG00000170684; Expressed in granulocyte and 117 other tissues.
DR   ExpressionAtlas; Q8WUU4; baseline and differential.
DR   Genevisible; Q8WUU4; HS.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; 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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..475
FT                   /note="Zinc finger protein 296"
FT                   /id="PRO_0000047542"
FT   ZN_FING         157..180
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         231..253
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         259..281
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         386..408
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         414..436
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         445..468
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        35
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
SQ   SEQUENCE   475 AA;  50810 MW;  44C47A6C9C29BF93 CRC64;
     MSRRKAGSAP RRVEPAPAAN PDDEMEMQDL VIELKPEPDA QPQQAPRLGP FSPKEVSSAG
     RFGGEPHHSP GPMPAGAALL ALGPRNPWTL WTPLTPNYPD RQPWTDKHPD LLTCGRCLQT
     FPLEAITAFM DHKKLGCQLF RGPSRGQGSE REELKALSCL RCGKQFTVAW KLLRHAQWDH
     GLSIYQTESE APEAPLLGLA EVAAAVSAVV GPAAEAKSPR ASGSGLTRRS PTCPVCKKTL
     SSFSNLKVHM RSHTGERPYA CDQCPYACAQ SSKLNRHKKT HRQVPPQSPL MADTSQEQAS
     AAPPEPAVHA AAPTSTLPCS GGEGAGAAAT AGVQEPGAPG SGAQAGPGGD TWGAITTEQR
     TDPANSQKAS PKKMPKSGGK SRGPGGSCEF CGKHFTNSSN LTVHRRSHTG ERPYTCEFCN
     YACAQSSKLN RHRRMHGMTP GSTRFECPHC HVPFGLRATL DKHLRQKHPE AAGEA
 
 
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