ZNF12_MOUSE
ID ZNF12_MOUSE Reviewed; 686 AA.
AC Q7TSI0; Q8C7Q7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger protein 12;
GN Name=Znf12; Synonyms=Zfp12;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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: Transcriptional repressor which suppresses activation protein
CC 1 (AP-1)- and serum response element (SRE)-mediated transcriptional
CC activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TSI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSI0-2; Sequence=VSP_040336;
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; AK049650; BAC33859.1; -; mRNA.
DR EMBL; CH466529; EDL19061.1; -; Genomic_DNA.
DR EMBL; CH466529; EDL19062.1; -; Genomic_DNA.
DR EMBL; BC053080; AAH53080.1; -; mRNA.
DR CCDS; CCDS19837.1; -. [Q7TSI0-2]
DR CCDS; CCDS71702.1; -. [Q7TSI0-1]
DR RefSeq; NP_001276518.1; NM_001289589.1. [Q7TSI0-1]
DR RefSeq; NP_001276519.1; NM_001289590.1.
DR RefSeq; NP_808349.1; NM_177681.4. [Q7TSI0-2]
DR RefSeq; XP_017176364.1; XM_017320875.1. [Q7TSI0-1]
DR AlphaFoldDB; Q7TSI0; -.
DR SMR; Q7TSI0; -.
DR BioGRID; 231183; 1.
DR IntAct; Q7TSI0; 1.
DR iPTMnet; Q7TSI0; -.
DR PhosphoSitePlus; Q7TSI0; -.
DR EPD; Q7TSI0; -.
DR PaxDb; Q7TSI0; -.
DR PRIDE; Q7TSI0; -.
DR ProteomicsDB; 275096; -. [Q7TSI0-1]
DR ProteomicsDB; 275097; -. [Q7TSI0-2]
DR Antibodypedia; 6020; 93 antibodies from 20 providers.
DR DNASU; 231866; -.
DR Ensembl; ENSMUST00000032591; ENSMUSP00000032591; ENSMUSG00000029587. [Q7TSI0-1]
DR Ensembl; ENSMUST00000077485; ENSMUSP00000076693; ENSMUSG00000029587. [Q7TSI0-2]
DR GeneID; 231866; -.
DR KEGG; mmu:231866; -.
DR UCSC; uc009ajt.2; mouse. [Q7TSI0-2]
DR UCSC; uc009aju.2; mouse. [Q7TSI0-1]
DR CTD; 231866; -.
DR MGI; MGI:99157; Zfp12.
DR VEuPathDB; HostDB:ENSMUSG00000029587; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154303; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; Q7TSI0; -.
DR OMA; DYHCYQM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q7TSI0; -.
DR TreeFam; TF350803; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 231866; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q7TSI0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q7TSI0; protein.
DR Bgee; ENSMUSG00000029587; Expressed in ear vesicle and 226 other tissues.
DR ExpressionAtlas; Q7TSI0; baseline and differential.
DR Genevisible; Q7TSI0; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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 InterPro; IPR017455; Znf_FYVE-rel.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 2: Evidence at transcript level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..686
FT /note="Zinc finger protein 12"
FT /id="PRO_0000402833"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 263..285
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 291..313
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..369
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 375..397
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..537
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 543..565
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 571..593
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 599..621
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 627..649
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 655..677
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 90..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17014"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17014"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17014"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17014"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17014"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT VAR_SEQ 48..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040336"
SQ SEQUENCE 686 AA; 78617 MW; A391CBF8D69FE3E4 CRC64;
MNTSLGPLSF KDVAVAFSQE EWQQLDPEER TTYRDVMLET YSNLVSVGYD IIKPDVIIKL
EQGEEPWIVE GAFSPQSYPD EIRHMSRLME EDQGGEENQS SSAVFSYRSR ADASSKATDG
ETKPFPSQKA LPQCNSCEKS LMCVSAFIRS DGSYAKLRPN VCAGCGKPLP CSKPEETHPG
GESYEFSGDG DEDPLGEEGV YQKGHFLEEP FEYVECQKSF PKGTVFLNHL EEEPCDWNDA
EVAFLQTSDL SAHQDSLMEM KPYECQQCGK SFCKKSKFVI HQRTHTGEKP FKCSQCGKSF
CQKGTLTVHQ RTHTGEKPYE CTECGKTFYQ KLHLIQHQRT HSGEKPYKCG YCGKSFCQKT
HLTQHQRTHS GERPYVCHDC GKTFSQKSAL NDHQKIHTGV KLYKCSECGK CFCRKSTLTT
HMRTHTGEKP YECNECGKFF SRLSYLTVHY RTHSGEKPYE CAECGKSFYL NSALMRHQRV
HTGEKPYECN ECGKLFSQLS YLTVHHRTHS GVKPYECSEC GKTFYQNSAL CRHRRIHRGE
KPYECYICGK FFSQMSYLTI HHRIHSGEKP YECRECGKSF CQNSALNRHQ RTHTGEKAYE
CYECGKCFSQ MSYLTIHHRI HSGEKPFECN ECGKAFSRMS YLTVHHRTHS GEKPYECTEC
GKKFYHKSAF NSHQRTHRRG SGNGVD
