PHF12_MOUSE
ID PHF12_MOUSE Reviewed; 1003 AA.
AC Q5SPL2; Q5SPL3; Q6ZPN8; Q80W50;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=PHD finger protein 12;
DE AltName: Full=PHD factor 1;
DE Short=Pf1;
GN Name=Phf12 {ECO:0000312|EMBL:CAI25224.1}; Synonyms=Kiaa1523;
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 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 [2] {ECO:0000305, ECO:0000312|EMBL:AAH43080.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH43080.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH43080.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC98193.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-1003 (ISOFORM 1).
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC98193.2};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAI25224.1}
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11390640; DOI=10.1128/mcb.21.13.4110-4118.2001;
RA Yochum G.S., Ayer D.E.;
RT "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the
RT mSin3A-histone deacetylase complex.";
RL Mol. Cell. Biol. 21:4110-4118(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND THR-670, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, 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: Acts as a transcriptional repressor. Involved in recruitment
CC of functional SIN3A complexes to DNA. Represses transcription at least
CC in part through the activity of an associated histone deacetylase
CC (HDAC). May also repress transcription in a SIN3A-independent manner
CC through recruitment of functional TLE5 complexes to DNA (By
CC similarity). {ECO:0000250|UniProtKB:Q96QT6}.
CC -!- SUBUNIT: Interacts with SIN3A in a complex composed of HDAC1, SAP30 and
CC SIN3A. Interacts with TLE5 (By similarity).
CC {ECO:0000250|UniProtKB:Q96QT6}.
CC -!- INTERACTION:
CC Q5SPL2; Q9UBU8-2: MORF4L1; Xeno; NbExp=2; IntAct=EBI-15963335, EBI-10288852;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SPL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SPL2-2; Sequence=VSP_051773, VSP_051774;
CC -!- TISSUE SPECIFICITY: Expressed mainly in heart, brain, lung, liver and
CC testis. {ECO:0000269|PubMed:11390640}.
CC -!- DEVELOPMENTAL STAGE: Expression is low in day 7 embryos, peaks at day
CC 11 and declines through to day 17. {ECO:0000269|PubMed:11390640}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43080.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL669840; CAI25700.1; -; Genomic_DNA.
DR EMBL; AL845484; CAI25700.1; JOINED; Genomic_DNA.
DR EMBL; AL669840; CAI25701.1; -; Genomic_DNA.
DR EMBL; AL845484; CAI25701.1; JOINED; Genomic_DNA.
DR EMBL; AL845484; CAI25223.1; -; Genomic_DNA.
DR EMBL; AL669840; CAI25223.1; JOINED; Genomic_DNA.
DR EMBL; AL845484; CAI25224.1; -; Genomic_DNA.
DR EMBL; AL669840; CAI25224.1; JOINED; Genomic_DNA.
DR EMBL; BC043080; AAH43080.1; ALT_INIT; mRNA.
DR EMBL; AK129383; BAC98193.2; -; Transcribed_RNA.
DR CCDS; CCDS48855.1; -. [Q5SPL2-1]
DR RefSeq; NP_777277.2; NM_174852.3. [Q5SPL2-1]
DR AlphaFoldDB; Q5SPL2; -.
DR BMRB; Q5SPL2; -.
DR SMR; Q5SPL2; -.
DR BioGRID; 234499; 4.
DR DIP; DIP-59633N; -.
DR IntAct; Q5SPL2; 1.
DR STRING; 10090.ENSMUSP00000044990; -.
DR iPTMnet; Q5SPL2; -.
DR PhosphoSitePlus; Q5SPL2; -.
DR EPD; Q5SPL2; -.
DR jPOST; Q5SPL2; -.
DR MaxQB; Q5SPL2; -.
DR PaxDb; Q5SPL2; -.
DR PRIDE; Q5SPL2; -.
DR ProteomicsDB; 301809; -. [Q5SPL2-1]
DR ProteomicsDB; 301810; -. [Q5SPL2-2]
DR Antibodypedia; 14939; 84 antibodies from 20 providers.
DR DNASU; 268448; -.
DR Ensembl; ENSMUST00000049167; ENSMUSP00000044990; ENSMUSG00000037791. [Q5SPL2-1]
DR Ensembl; ENSMUST00000108360; ENSMUSP00000103997; ENSMUSG00000037791. [Q5SPL2-2]
DR GeneID; 268448; -.
DR KEGG; mmu:268448; -.
DR UCSC; uc007kht.2; mouse. [Q5SPL2-1]
DR CTD; 57649; -.
DR MGI; MGI:1924057; Phf12.
DR VEuPathDB; HostDB:ENSMUSG00000037791; -.
DR eggNOG; KOG4299; Eukaryota.
DR GeneTree; ENSGT00940000155713; -.
DR HOGENOM; CLU_015009_0_0_1; -.
DR InParanoid; Q5SPL2; -.
DR OMA; NYGHCNF; -.
DR PhylomeDB; Q5SPL2; -.
DR TreeFam; TF336193; -.
DR BioGRID-ORCS; 268448; 13 hits in 80 CRISPR screens.
DR ChiTaRS; Phf12; mouse.
DR PRO; PR:Q5SPL2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SPL2; protein.
DR Bgee; ENSMUSG00000037791; Expressed in undifferentiated genital tubercle and 252 other tissues.
DR ExpressionAtlas; Q5SPL2; baseline and differential.
DR Genevisible; Q5SPL2; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; ISO:MGI.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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; cd00060; FHA; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 6.10.20.60; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR042163; PHF12.
DR InterPro; IPR031966; PHF12_MRG-bd.
DR InterPro; IPR038098; PHF12_MRG-bd_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46309; PTHR46309; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF16737; PHF12_MRG_bd; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1003
FT /note="PHD finger protein 12"
FT /id="PRO_0000059303"
FT DOMAIN 814..868
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT ZN_FING 56..105
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 271..321
FT /note="PHD-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 29..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT MOD_RES 670
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT CROSSLNK 899
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT CROSSLNK 972
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT CROSSLNK 986
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT CROSSLNK 990
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QT6"
FT VAR_SEQ 739..788
FT /note="IEINMLDEKLIKFLALQRVHQLFPSRVQASPGNVGTHPLASGGHHPEVQR
FT -> STSAFPFPGPSFTGQCWDTSAGFWRAPPRRCARVHMPATTPSALLSDVCE (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_051773"
FT VAR_SEQ 789..1003
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_051774"
SQ SEQUENCE 1003 AA; 109509 MW; 915622923FA3EBF7 CRC64;
MWEKMETKTI VYDLDTSGGL MEQIQALLAP PKTDEAEKRS RKPEKESRRS GRATNHDSCD
SCKEGGDLLC CDHCPAAFHL QCCNPPLSEE MLPPGEWMCH RCTVRRKKRE QKKELGHVNG
LVDKSSKRTT SPSSDTDLLD RPASKTELKA IAHARILERR ASRPGTPTSN ASTETPTSEH
NDVDEDIVDV DEEPVAAEPD YVQPQLRRPF ELLIAAAMER NPTQFQLPNE LTCTTALPGS
SKRRRKEETT GKNVKRTQHE LDHNGLVPLP VKVCFTCNRS CRVAPLIQCD YCPLLFHMDC
LEPPLTAMPL GRWMCPNHIE HVVLNQKNLT LSNRCQVFDR FQDTISQHVV KVDFLNRIHK
KHPPNRRVLQ SVKRRSLKVP DAIKSQYQFP PPLIAPAAIR DGELICSGVP EESQTHLLNS
EHLATQAEQQ EWLCSVVALQ CSILKHLSAK QMPSPWDSEQ TEKADIKPVI VTDSSITTSL
QTADKAPLPS HYPLSCPSAV STQNSLGCSP PHQPPTLEDI SCSSCVEKSK KAPCGTANGP
VNTEIKANGP HLYSSPTDST DPRRLPGANT PLPGLTHRQG WPRPLTPPSA GGLQNHVGII
VKTENATGPS SCPQRSLVPV PSLPPSIPSS CASIENTSTL HRKTVQSQIG PSSTESRPLG
SPPNATRVLT PPQAAGDSIL ATGANQRFCS PAPSSDGKVS PGTLSIGSAL TVPSFPANST
AMVDLTNSLR AFMDVNGEIE INMLDEKLIK FLALQRVHQL FPSRVQASPG NVGTHPLASG
GHHPEVQRKE VQARAVFCPL LGLGGAVNMC YRTLYIGTGA DMDVCLTNYG HCNYVSGKHA
CIFYDENTKH YELLNYSEHG TTVDNVLYSC DFSEKTPPTP PSSIVAKVQS VIRRRRHQKQ
DEEPSEEAAM MSSQAQGPQR RPCNCKASSS SLIGGSGAGW EGTALLHHGS YIKLGCLQFV
FSITEFATKQ PKGDASLLQD GVLAEKLSLK PHQGPVLRSN SVP
