OZF_HUMAN
ID OZF_HUMAN Reviewed; 292 AA.
AC Q15072; Q2TB94;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Zinc finger protein OZF;
DE AltName: Full=Only zinc finger protein;
DE AltName: Full=Zinc finger protein 146;
GN Name=ZNF146; Synonyms=OZF;
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], TISSUE SPECIFICITY, AND VARIANT LYS-8.
RC TISSUE=Mammary gland;
RX PubMed=8107129; DOI=10.1006/jmbi.1994.1151;
RA le Chalony C., Prosperi M.-T., Haluza R., Apiou F., Dutrillaux B.,
RA Goubin G.;
RT "The OZF gene encodes a protein consisting essentially of zinc finger
RT motifs.";
RL J. Mol. Biol. 236:399-404(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-8.
RX PubMed=11306801; DOI=10.1159/000056873;
RA Pibouin L., Villaudy J., Prosperi M.-T., Goubin G.;
RT "Genomic organization and promoter identification of ZNF146, a gene
RT encoding a protein consisting solely of zinc finger domains.";
RL Cytogenet. Cell Genet. 92:80-84(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-8.
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 [5]
RP DNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8665923; DOI=10.1111/j.1432-1033.1996.00991.x;
RA Ferbus D., le Chalony C., Prosperi M.-T., Muleris M., Vincent-Salomon A.,
RA Goubin G.;
RT "Identification, nuclear localization, and binding activities of OZF, a
RT human protein solely composed of zinc-finger motifs.";
RL Eur. J. Biochem. 236:991-995(1996).
RN [6]
RP OVEREXPRESSION IN PANCREATIC CANCER.
RX PubMed=9935176;
RX DOI=10.1002/(sici)1097-0215(19990129)80:3<369::aid-ijc6>3.0.co;2-y;
RA Ferbus D., Flechon A., Muleris M., Li Y., Hanash S., Terris B., Hammel P.,
RA Pibouin L., Dutrillaux B., Goubin G.;
RT "Amplification and over-expression of OZF, a gene encoding a zinc finger
RT protein, in human pancreatic carcinomas.";
RL Int. J. Cancer 80:369-372(1999).
RN [7]
RP OVEREXPRESSION IN COLORECTAL CANCER.
RX PubMed=12754738; DOI=10.1002/path.1337;
RA Ferbus D., Bovin C., Validire P., Goubin G.;
RT "The zinc finger protein OZF (ZNF146) is overexpressed in colorectal
RT cancer.";
RL J. Pathol. 200:177-182(2003).
RN [8]
RP INTERACTION WITH TERF2IP.
RX PubMed=15838871; DOI=10.1002/jcb.20487;
RA Antoine K., Ferbus D., Kolahgar G., Prosperi M.-T., Goubin G.;
RT "Zinc finger protein overexpressed in colon carcinoma interacts with the
RT telomeric protein hRap1.";
RL J. Cell. Biochem. 95:763-768(2005).
RN [9]
RP INTERACTION WITH UBE2I, SUMOYLATION AT LYS-157 AND LYS-169, AND MUTAGENESIS
RP OF LYS-157 AND LYS-169.
RX PubMed=15881673; DOI=10.1007/s11010-005-6417-2;
RA Antoine K., Prosperi M.-T., Ferbus D., Boule C., Goubin G.;
RT "A Kruppel zinc finger of ZNF 146 interacts with the SUMO-1 conjugating
RT enzyme UBC9 and is sumoylated in vivo.";
RL Mol. Cell. Biochem. 271:215-223(2005).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-51; LYS-56 AND LYS-173,
RP AND IDENTIFICATION BY MASS 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 -!- SUBUNIT: Binds DNA. Interacts with SUMO conjugating enzyme UBC9/UBE2I.
CC Interacts with the telomeric protein TERF2IP.
CC {ECO:0000269|PubMed:15838871, ECO:0000269|PubMed:15881673}.
CC -!- INTERACTION:
CC Q15072; Q96Q77: CIB3; NbExp=3; IntAct=EBI-11914212, EBI-10292696;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8665923}.
CC -!- TISSUE SPECIFICITY: Liver, skeletal and heart muscle, mammary cells.
CC Very low levels in brain, lung, placenta and kidney. Strongly
CC overexpressed in many pancreas and colorectal cancers. Increased gene
CC copy numbers are detected in 3 of 12 tumor cell lines and 2 of 12
CC primary pancreatic carcinomas. Overexpressed in 80% of colorectal
CC cancers. {ECO:0000269|PubMed:8107129, ECO:0000269|PubMed:8665923}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15881673}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/OZFID267.html";
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DR EMBL; X70394; CAA49844.1; -; mRNA.
DR EMBL; AJ011806; CAB41967.1; -; Genomic_DNA.
DR EMBL; AC012617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110500; AAI10501.1; -; mRNA.
DR EMBL; BC110501; AAI10502.1; -; mRNA.
DR CCDS; CCDS12492.1; -.
DR PIR; S43826; S43826.
DR RefSeq; NP_001093108.1; NM_001099638.1.
DR RefSeq; NP_001093109.1; NM_001099639.1.
DR RefSeq; NP_009076.2; NM_007145.2.
DR RefSeq; XP_005259271.1; XM_005259214.2.
DR RefSeq; XP_016882733.1; XM_017027244.1.
DR RefSeq; XP_016882734.1; XM_017027245.1.
DR RefSeq; XP_016882735.1; XM_017027246.1.
DR RefSeq; XP_016882736.1; XM_017027247.1.
DR AlphaFoldDB; Q15072; -.
DR SMR; Q15072; -.
DR BioGRID; 113499; 71.
DR IntAct; Q15072; 21.
DR MINT; Q15072; -.
DR STRING; 9606.ENSP00000400391; -.
DR iPTMnet; Q15072; -.
DR PhosphoSitePlus; Q15072; -.
DR BioMuta; ZNF146; -.
DR DMDM; 134048495; -.
DR EPD; Q15072; -.
DR jPOST; Q15072; -.
DR MassIVE; Q15072; -.
DR MaxQB; Q15072; -.
DR PaxDb; Q15072; -.
DR PeptideAtlas; Q15072; -.
DR PRIDE; Q15072; -.
DR ProteomicsDB; 60426; -.
DR Antibodypedia; 929; 160 antibodies from 23 providers.
DR DNASU; 7705; -.
DR Ensembl; ENST00000443387.3; ENSP00000392095.1; ENSG00000167635.12.
DR Ensembl; ENST00000456324.5; ENSP00000400391.1; ENSG00000167635.12.
DR GeneID; 7705; -.
DR KEGG; hsa:7705; -.
DR MANE-Select; ENST00000443387.3; ENSP00000392095.1; NM_007145.3; NP_009076.2.
DR UCSC; uc002odq.5; human.
DR CTD; 7705; -.
DR DisGeNET; 7705; -.
DR GeneCards; ZNF146; -.
DR HGNC; HGNC:12931; ZNF146.
DR HPA; ENSG00000167635; Low tissue specificity.
DR MIM; 601505; gene.
DR neXtProt; NX_Q15072; -.
DR OpenTargets; ENSG00000167635; -.
DR PharmGKB; PA37518; -.
DR VEuPathDB; HostDB:ENSG00000167635; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162671; -.
DR HOGENOM; CLU_002678_2_1_1; -.
DR InParanoid; Q15072; -.
DR OMA; MDALDHW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q15072; -.
DR TreeFam; TF337055; -.
DR PathwayCommons; Q15072; -.
DR SignaLink; Q15072; -.
DR BioGRID-ORCS; 7705; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; ZNF146; human.
DR GeneWiki; ZNF146; -.
DR GenomeRNAi; 7705; -.
DR Pharos; Q15072; Tbio.
DR PRO; PR:Q15072; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q15072; protein.
DR Bgee; ENSG00000167635; Expressed in parietal pleura and 214 other tissues.
DR Genevisible; Q15072; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0008201; F:heparin binding; TAS:ProtInc.
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; TAS:ProtInc.
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; TAS:ProtInc.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..292
FT /note="Zinc finger protein OZF"
FT /id="PRO_0000047276"
FT ZN_FING 16..38
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 44..66
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 72..94
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 100..122
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 128..150
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 156..178
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 184..206
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 240..262
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..290
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 212..292
FT /note="Interaction with TERF2IP"
FT /evidence="ECO:0000269|PubMed:15838871"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 169
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 8
FT /note="R -> K (in dbSNP:rs2070132)"
FT /evidence="ECO:0000269|PubMed:11306801,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8107129"
FT /id="VAR_023746"
FT MUTAGEN 157
FT /note="K->R: Induces a decrease in sumoylation. Induces a
FT strong decrease but does not abolishes sumoylation; when
FT associated with R-169."
FT /evidence="ECO:0000269|PubMed:15881673"
FT MUTAGEN 169
FT /note="K->R: Induces a decrease in sumoylation. Induces a
FT strong decrease but does not abolishes sumoylation; when
FT associated with R-157."
FT /evidence="ECO:0000269|PubMed:15881673"
SQ SEQUENCE 292 AA; 33308 MW; D5062375D261B971 CRC64;
MSHLSQQRIY SGENPFACKV CGKVFSHKSN LTEHEHFHTR EKPFECNECG KAFSQKQYVI
KHQNTHTGEK LFECNECGKS FSQKENLLTH QKIHTGEKPF ECKDCGKAFI QKSNLIRHQR
THTGEKPFVC KECGKTFSGK SNLTEHEKIH IGEKPFKCSE CGTAFGQKKY LIKHQNIHTG
EKPYECNECG KAFSQRTSLI VHVRIHSGDK PYECNVCGKA FSQSSSLTVH VRSHTGEKPY
GCNECGKAFS QFSTLALHLR IHTGKKPYQC SECGKAFSQK SHHIRHQKIH TH
