OZF_MOUSE
ID OZF_MOUSE Reviewed; 292 AA.
AC Q8BQN6; A0JNX3; Q9Z0Q5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
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, Zfp146;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10449921; DOI=10.1159/000015316;
RA Blottiere L., Apiou F., Ferbus D., Guenzi C., Dutrillaux B.,
RA Prosperi M.-T., Goubin G.;
RT "Cloning, characterization, and chromosome assignment of Zfp146 the mouse
RT ortholog of human ZNF146, a gene amplified and overexpressed in pancreatic
RT cancer, and Zfp260 a closely related gene.";
RL Cytogenet. Cell Genet. 85:297-300(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12437081; DOI=10.1023/a:1020347123109;
RA Besnar N., Persuy M.-A., Stinnakre M.-G., Lepourry L., Da Silva J.C.,
RA Goubin G., Vilotte J.-L.;
RT "Targeted expression of the only zinc finger gene in transgenic mice is
RT associated with impaired mammary development.";
RL Transgenic Res. 11:505-513(2002).
CC -!- SUBUNIT: Binds DNA. Interacts with SUMO conjugating enzyme UBC9/UBE2I.
CC Interacts with the telomeric protein TERF2IP (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, lung, skeletal
CC muscle and kidney, and at much lower level in spleen and testicle.
CC Expressed in lactating mammary gland. {ECO:0000269|PubMed:10449921,
CC ECO:0000269|PubMed:12437081}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Zfp146 in mammary gland display
CC impaired mammary gland development. They cannot sustain full growth of
CC their pups. This phenotype is associated with an impaired mammary gland
CC development noticeable only after mid-gestation.
CC {ECO:0000269|PubMed:12437081}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33129.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ224763; CAB38320.1; -; mRNA.
DR EMBL; AK047696; BAC33129.1; ALT_INIT; mRNA.
DR EMBL; BC127038; AAI27039.1; -; mRNA.
DR EMBL; BC127039; AAI27040.1; -; mRNA.
DR CCDS; CCDS21079.1; -.
DR RefSeq; NP_036110.1; NM_011980.3.
DR RefSeq; XP_006540071.1; XM_006540008.2.
DR RefSeq; XP_006540072.1; XM_006540009.2.
DR AlphaFoldDB; Q8BQN6; -.
DR SMR; Q8BQN6; -.
DR STRING; 10090.ENSMUSP00000058588; -.
DR iPTMnet; Q8BQN6; -.
DR PhosphoSitePlus; Q8BQN6; -.
DR EPD; Q8BQN6; -.
DR MaxQB; Q8BQN6; -.
DR PaxDb; Q8BQN6; -.
DR PeptideAtlas; Q8BQN6; -.
DR PRIDE; Q8BQN6; -.
DR ProteomicsDB; 294086; -.
DR Antibodypedia; 929; 160 antibodies from 23 providers.
DR DNASU; 26465; -.
DR Ensembl; ENSMUST00000062181; ENSMUSP00000058588; ENSMUSG00000037029.
DR GeneID; 26465; -.
DR KEGG; mmu:26465; -.
DR UCSC; uc009gdn.1; mouse.
DR CTD; 26465; -.
DR MGI; MGI:1347092; Zfp146.
DR VEuPathDB; HostDB:ENSMUSG00000037029; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162671; -.
DR HOGENOM; CLU_002678_2_1_1; -.
DR InParanoid; Q8BQN6; -.
DR OMA; MDALDHW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BQN6; -.
DR TreeFam; TF337055; -.
DR BioGRID-ORCS; 26465; 0 hits in 74 CRISPR screens.
DR PRO; PR:Q8BQN6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BQN6; protein.
DR Bgee; ENSMUSG00000037029; Expressed in ventricular zone and 150 other tissues.
DR Genevisible; Q8BQN6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative 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 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; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 2: Evidence at transcript 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_0000047277"
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:0000250"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15072"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15072"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15072"
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:0000250|UniProtKB:Q15072"
SQ SEQUENCE 292 AA; 33093 MW; A0F985ABBEE7CADD CRC64;
MSQLSQQRIL SGGSPFACKV CGKLFSHKSN LTEHEHFHSR EKPFECNECG KAFSQKQYVI
KHQSTHSGEK LFECSDCGKA FSQKENLLTH QKIHTGEKPF ECKDCGKAFI QKSNLIRHQR
THTGEKPFIC KECGKTFSGK SNLTEHEKIH IGEKPFKCNE CGTAFGQKKY LIKHQNIHTG
EKPYECNECG KAFSQRTSLI VHVRIHSGDK PYECNVCGKA FSQSSSLTVH VRSHTGEKPY
GCNECGKAFS QFSTLALHLR IHTGKKPYQC SECGKAFSQK SHHIRHQKIH TH
