KLF12_MOUSE
ID KLF12_MOUSE Reviewed; 402 AA.
AC O35738; Q6NWV9;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Krueppel-like factor 12;
DE AltName: Full=Transcriptional repressor AP-2rep;
GN Name=Klf12; Synonyms=Ap2rep;
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].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9858544; DOI=10.1128/mcb.19.1.194;
RA Imhof A., Schuierer M., Werner O., Moser M., Roth C., Bauer R.,
RA Buettner R.;
RT "Transcriptional regulation of the AP-2alpha promoter by BTEB-1 and AP-
RT 2rep, a novel wt-1/egr-related zinc finger repressor.";
RL Mol. Cell. Biol. 19:194-204(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Confers strong transcriptional repression to the AP-2-alpha
CC gene. Binds to a regulatory element (A32) in the AP-2-alpha gene
CC promoter.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors. In KLF12, the motif
CC is inactive. {ECO:0000250|UniProtKB:Q9Y4X4}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; Y14295; CAA74670.1; -; mRNA.
DR EMBL; BC067408; AAH67408.1; -; mRNA.
DR CCDS; CCDS36998.1; -.
DR RefSeq; NP_034766.2; NM_010636.3.
DR RefSeq; XP_006518686.1; XM_006518623.3.
DR RefSeq; XP_006518687.1; XM_006518624.3.
DR RefSeq; XP_011243270.1; XM_011244968.2.
DR RefSeq; XP_011243271.1; XM_011244969.2.
DR AlphaFoldDB; O35738; -.
DR SMR; O35738; -.
DR BioGRID; 200963; 9.
DR STRING; 10090.ENSMUSP00000094844; -.
DR iPTMnet; O35738; -.
DR PhosphoSitePlus; O35738; -.
DR MaxQB; O35738; -.
DR PaxDb; O35738; -.
DR PeptideAtlas; O35738; -.
DR PRIDE; O35738; -.
DR ProteomicsDB; 263618; -.
DR Antibodypedia; 24434; 287 antibodies from 29 providers.
DR DNASU; 16597; -.
DR Ensembl; ENSMUST00000097079; ENSMUSP00000094844; ENSMUSG00000072294.
DR Ensembl; ENSMUST00000228216; ENSMUSP00000153901; ENSMUSG00000072294.
DR GeneID; 16597; -.
DR KEGG; mmu:16597; -.
DR UCSC; uc007uvh.2; mouse.
DR CTD; 11278; -.
DR MGI; MGI:1333796; Klf12.
DR VEuPathDB; HostDB:ENSMUSG00000072294; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158108; -.
DR HOGENOM; CLU_002678_33_0_1; -.
DR InParanoid; O35738; -.
DR OMA; NIPMKRK; -.
DR OrthoDB; 845652at2759; -.
DR PhylomeDB; O35738; -.
DR TreeFam; TF350556; -.
DR BioGRID-ORCS; 16597; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Klf12; mouse.
DR PRO; PR:O35738; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O35738; protein.
DR Bgee; ENSMUSG00000072294; Expressed in rostral migratory stream and 207 other tissues.
DR ExpressionAtlas; O35738; baseline and differential.
DR Genevisible; O35738; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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; IDA:NTNU_SB.
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; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
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; IDA:MGI.
DR InterPro; IPR030447; KLF12.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF56; PTHR23235:SF56; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..402
FT /note="Krueppel-like factor 12"
FT /id="PRO_0000047183"
FT ZN_FING 317..341
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..371
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 81..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 80..88
FT /note="9aaTAD; inactive"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4X4"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 313
FT /note="N6-methylated lysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4X4"
FT CONFLICT 105
FT /note="A -> G (in Ref. 1; CAA74670)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="S -> R (in Ref. 1; CAA74670)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="A -> G (in Ref. 1; CAA74670)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> R (in Ref. 1; CAA74670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 44105 MW; B80D73C2123F1FF5 CRC64;
MNIHMKRKTI KNLSALENRM LMLDGMPAVR VKTELVESEQ GSPNVHNYPD MEAVPLLLNN
VKGEPPEDSL PVDHFQTQTE PVDLSINKAR TSPTAASSSP VSMTASASSP SSTSTSSSSS
SRPASSPTVI TSVSSASSSS TVLSPGPLVA SASGVGGQQF LHIIHPVPPS SPMNLQSNKL
SHVHRIPVVV QSVPVVYTAV RSPGNVNNTI VVPLLEDGRS HGKAQMEPRG LSPRQSKSDS
DDDDLPNVTL DSVNETGSTA LSIARAVQEV HPSPVSRVRG NRMNNQKFAC SISPFSIEST
RRQRRSESPD SRKRRIHRCD FEGCNKVYTK SSHLKAHRRT HTGEKPYKCT WEGCTWKFAR
SDELTRHYRK HTGVKPFKCA DCDRSFSRSD HLALHRRRHM LV
