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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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