ZN120_MOUSE
ID ZN120_MOUSE Reviewed; 436 AA.
AC Q8BZW4; Q78JR8; Q9EQK4; Q9JIB8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Zinc finger protein 120 {ECO:0000312|EMBL:AAI41129.1};
DE AltName: Full=Zinc finger protein 31 {ECO:0000303|PubMed:10360839};
DE Short=mZF31;
GN Name=Zfp120 {ECO:0000312|MGI:MGI:1345179};
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] {ECO:0000305, ECO:0000312|EMBL:AAF79951.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Monocyte {ECO:0000269|PubMed:10360839};
RX PubMed=10360839; DOI=10.1089/104454999315277;
RA Mark C., Abrink M., Hellman L.;
RT "Comparative analysis of KRAB zinc finger proteins in rodents and man:
RT evidence for several evolutionarily distinct subfamilies of KRAB zinc
RT finger genes.";
RL DNA Cell Biol. 18:381-396(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG43564.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue {ECO:0000312|EMBL:AAG43564.1};
RA Bi S., Tartaglia L.A., Reitman M.L.;
RT "Isolation of a cDNA clone for a novel Kruppel-related zinc finger protein
RT from mouse adipose tissue.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC28268.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28268.1};
RC TISSUE=Embryonic head {ECO:0000312|EMBL:BAE21102.1}, and
RC Embryonic lung {ECO:0000312|EMBL:BAC28268.1};
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAG43564.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAI41129.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH13500.2};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAI41129.1}, and
RC Kidney {ECO:0000312|EMBL:AAH13500.2};
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).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|Ref.2};
CC IsoId=Q8BZW4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10360839};
CC IsoId=Q8BZW4-2; Sequence=VSP_053088;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in kidney,
CC brain, and liver, and the lowest levels in spleen.
CC {ECO:0000269|PubMed:10360839}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79951.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG43564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH13500.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EDL28560.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF242378; AAF79951.1; ALT_FRAME; mRNA.
DR EMBL; AF211867; AAG43564.1; ALT_INIT; mRNA.
DR EMBL; AK033399; BAC28268.1; -; mRNA.
DR EMBL; AK132318; BAE21102.1; -; mRNA.
DR EMBL; AL831742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28560.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC013500; AAH13500.2; ALT_INIT; mRNA.
DR EMBL; BC141128; AAI41129.1; -; mRNA.
DR CCDS; CCDS38263.1; -. [Q8BZW4-1]
DR RefSeq; NP_075755.4; NM_023266.4.
DR RefSeq; NP_851783.2; NM_181266.2. [Q8BZW4-1]
DR AlphaFoldDB; Q8BZW4; -.
DR SMR; Q8BZW4; -.
DR BioGRID; 222567; 17.
DR STRING; 10090.ENSMUSP00000086615; -.
DR iPTMnet; Q8BZW4; -.
DR PhosphoSitePlus; Q8BZW4; -.
DR MaxQB; Q8BZW4; -.
DR PaxDb; Q8BZW4; -.
DR PRIDE; Q8BZW4; -.
DR ProteomicsDB; 302071; -. [Q8BZW4-1]
DR ProteomicsDB; 302072; -. [Q8BZW4-2]
DR DNASU; 104348; -.
DR Ensembl; ENSMUST00000089207; ENSMUSP00000086615; ENSMUSG00000068134. [Q8BZW4-1]
DR GeneID; 104348; -.
DR KEGG; mmu:104348; -.
DR UCSC; uc008mtx.1; mouse. [Q8BZW4-1]
DR CTD; 104348; -.
DR MGI; MGI:1345179; Zfp120.
DR VEuPathDB; HostDB:ENSMUSG00000068134; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153805; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q8BZW4; -.
DR OMA; FNCQSAL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BZW4; -.
DR TreeFam; TF338854; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 104348; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q8BZW4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BZW4; protein.
DR Bgee; ENSMUSG00000068134; Expressed in metanephric loop of Henle and 239 other tissues.
DR ExpressionAtlas; Q8BZW4; baseline and differential.
DR Genevisible; Q8BZW4; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..436
FT /note="Zinc finger protein 120"
FT /id="PRO_0000374052"
FT DOMAIN 28..115
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 156..178
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 184..206
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 240..262
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..290
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 296..318
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 324..346
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 352..374
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 380..402
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 408..430
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 69..135
FT /note="YYWKGHNISEGHFQNSRRNGRHERSDTEEKLSEFTQYDKDFAYQSHPQRHER
FT IYSGEKPYEGVQYFE -> MKEVILKRNFLNLLNMIKTLHIRAILKGMKEFILERNPMK
FT VSNILK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10360839"
FT /id="VSP_053088"
SQ SEQUENCE 436 AA; 51252 MW; 05079C12AD528C0F CRC64;
MFLLDVFCVP LLGAGTSGKP RSSDMDIVTY DDVHVNFTWE EWALLDPSQK DLYRDVMLET
YRNLAAIGYY WKGHNISEGH FQNSRRNGRH ERSDTEEKLS EFTQYDKDFA YQSHPQRHER
IYSGEKPYEG VQYFEDFAHH SSLQIQRRTH VVEKPYECNQ CGKAFAYHSY LQRHERSHTG
EKPYECNQCG KAFGRHSHLQ RHERIHTGEK SYDCNQCGKT FVHHSHLQIH KRTHIGEKPF
ECNQCGKAFA RNSHLLIHKR IHTGEKPYEC KQCGKAFAYQ SGLLYHKRRY TVEKLYECNQ
CGKAFACHNS LQVHKRTHTG EKPYKCNQCG KAFGRYSSLQ RHERIHTGEK PYECKQCGKA
FGRHSSLQRH ERIHTGQKPD ECSQCCKDCG CYNSLQIHKR PHTGEKYFEC NQCGKGFSQN
CYLEIHKRAH TVEKHY
