PHF12_HUMAN
ID PHF12_HUMAN Reviewed; 1004 AA.
AC Q96QT6; Q0VAI5; Q2TAK2; Q6ZML2; Q9BV34; Q9H7U9; Q9P205;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=PHD finger protein 12;
DE AltName: Full=PHD factor 1;
DE Short=Pf1;
GN Name=PHF12 {ECO:0000312|HGNC:HGNC:20816};
GN Synonyms=KIAA1523 {ECO:0000312|EMBL:BAA96047.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK38349.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH TLE5 AND
RP SIN3A, AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal liver {ECO:0000269|PubMed:11390640};
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 [2] {ECO:0000305, ECO:0000312|EMBL:BAD18713.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 80-1004 (ISOFORM 3).
RC TISSUE=Spleen {ECO:0000312|EMBL:BAD18713.1}, and
RC Teratocarcinoma {ECO:0000312|EMBL:BAB14875.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 86-1004 (ISOFORM 1).
RC TISSUE=Eye {ECO:0000312|EMBL:AAH01657.1}, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1004 (ISOFORM 1).
RC TISSUE=Brain {ECO:0000269|PubMed:10819331};
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [7]
RP PHOSPHOINOSITIDE-BINDING.
RX PubMed=16893883; DOI=10.1074/jbc.m605624200;
RA Kaadige M.R., Ayer D.E.;
RT "The polybasic region that follows the plant homeodomain zinc finger 1 of
RT Pf1 is necessary and sufficient for specific phosphoinositide binding.";
RL J. Biol. Chem. 281:28831-28836(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-134 AND THR-671, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND THR-671, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-134, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-555; THR-557;
RP THR-570 AND THR-671, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-671, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-467, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-467, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-467, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-467; LYS-900; LYS-973; LYS-987
RP AND LYS-991, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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.
CC {ECO:0000269|PubMed:11390640, ECO:0000303|PubMed:11390640}.
CC -!- SUBUNIT: Isoform 2 interacts with SIN3A in a complex composed of HDAC1,
CC SAP30 and SIN3A. Interacts with TLE5. {ECO:0000269|PubMed:11390640}.
CC -!- INTERACTION:
CC Q96QT6; Q9UBU8-2: MORF4L1; NbExp=6; IntAct=EBI-2803760, EBI-10288852;
CC Q96QT6-2; Q8N8Y2: ATP6V0D2; NbExp=3; IntAct=EBI-10293106, EBI-3923949;
CC Q96QT6-2; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-10293106, EBI-10288852;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11390640}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000305};
CC IsoId=Q96QT6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11390640};
CC IsoId=Q96QT6-2; Sequence=VSP_051769, VSP_051770;
CC Name=3 {ECO:0000305};
CC IsoId=Q96QT6-3; Sequence=VSP_051768, VSP_051771, VSP_051772;
CC Name=4 {ECO:0000305};
CC IsoId=Q96QT6-4; Sequence=VSP_051767;
CC Name=5;
CC IsoId=Q96QT6-5; Sequence=VSP_051771, VSP_051772;
CC -!- DOMAIN: The polybasic region (PBR) is responsive to the binding to
CC phosphoinositides (PtdInsPs).
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
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DR EMBL; AY030283; AAK38349.1; -; mRNA.
DR EMBL; AK024290; BAB14875.1; -; mRNA.
DR EMBL; AK160370; BAD18713.1; -; mRNA.
DR EMBL; AC024267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471159; EAW51166.1; -; Genomic_DNA.
DR EMBL; BC001657; AAH01657.1; ALT_SEQ; mRNA.
DR EMBL; BC110882; AAI10883.1; -; mRNA.
DR EMBL; BC121044; AAI21045.1; -; mRNA.
DR EMBL; AB040956; BAA96047.1; -; mRNA.
DR CCDS; CCDS11247.1; -. [Q96QT6-2]
DR CCDS; CCDS32598.1; -. [Q96QT6-1]
DR CCDS; CCDS76981.1; -. [Q96QT6-5]
DR RefSeq; NP_001028733.1; NM_001033561.1. [Q96QT6-1]
DR RefSeq; NP_001277060.1; NM_001290131.1. [Q96QT6-5]
DR RefSeq; NP_065940.1; NM_020889.2. [Q96QT6-2]
DR PDB; 2L9S; NMR; -; A=200-241.
DR PDB; 2LKM; NMR; -; A=200-241.
DR PDBsum; 2L9S; -.
DR PDBsum; 2LKM; -.
DR AlphaFoldDB; Q96QT6; -.
DR BMRB; Q96QT6; -.
DR SMR; Q96QT6; -.
DR BioGRID; 121686; 98.
DR DIP; DIP-59632N; -.
DR IntAct; Q96QT6; 42.
DR MINT; Q96QT6; -.
DR STRING; 9606.ENSP00000329933; -.
DR GlyGen; Q96QT6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96QT6; -.
DR PhosphoSitePlus; Q96QT6; -.
DR BioMuta; PHF12; -.
DR DMDM; 71153050; -.
DR EPD; Q96QT6; -.
DR jPOST; Q96QT6; -.
DR MassIVE; Q96QT6; -.
DR MaxQB; Q96QT6; -.
DR PaxDb; Q96QT6; -.
DR PeptideAtlas; Q96QT6; -.
DR PRIDE; Q96QT6; -.
DR ProteomicsDB; 77899; -. [Q96QT6-1]
DR ProteomicsDB; 77900; -. [Q96QT6-2]
DR ProteomicsDB; 77901; -. [Q96QT6-3]
DR ProteomicsDB; 77902; -. [Q96QT6-4]
DR Antibodypedia; 14939; 84 antibodies from 20 providers.
DR DNASU; 57649; -.
DR Ensembl; ENST00000268756.7; ENSP00000268756.3; ENSG00000109118.14. [Q96QT6-2]
DR Ensembl; ENST00000332830.9; ENSP00000329933.4; ENSG00000109118.14. [Q96QT6-1]
DR Ensembl; ENST00000577226.5; ENSP00000465161.1; ENSG00000109118.14. [Q96QT6-5]
DR GeneID; 57649; -.
DR KEGG; hsa:57649; -.
DR MANE-Select; ENST00000332830.9; ENSP00000329933.4; NM_001033561.2; NP_001028733.1.
DR UCSC; uc002hdg.2; human. [Q96QT6-1]
DR CTD; 57649; -.
DR DisGeNET; 57649; -.
DR GeneCards; PHF12; -.
DR HGNC; HGNC:20816; PHF12.
DR HPA; ENSG00000109118; Low tissue specificity.
DR MIM; 618645; gene.
DR neXtProt; NX_Q96QT6; -.
DR OpenTargets; ENSG00000109118; -.
DR PharmGKB; PA134954478; -.
DR VEuPathDB; HostDB:ENSG00000109118; -.
DR eggNOG; KOG4299; Eukaryota.
DR GeneTree; ENSGT00940000155713; -.
DR HOGENOM; CLU_015009_0_0_1; -.
DR InParanoid; Q96QT6; -.
DR OMA; NYGHCNF; -.
DR OrthoDB; 1203363at2759; -.
DR PhylomeDB; Q96QT6; -.
DR TreeFam; TF336193; -.
DR PathwayCommons; Q96QT6; -.
DR SignaLink; Q96QT6; -.
DR SIGNOR; Q96QT6; -.
DR BioGRID-ORCS; 57649; 325 hits in 1097 CRISPR screens.
DR ChiTaRS; PHF12; human.
DR EvolutionaryTrace; Q96QT6; -.
DR GeneWiki; PHF12; -.
DR GenomeRNAi; 57649; -.
DR Pharos; Q96QT6; Tbio.
DR PRO; PR:Q96QT6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96QT6; protein.
DR Bgee; ENSG00000109118; Expressed in sural nerve and 143 other tissues.
DR ExpressionAtlas; Q96QT6; baseline and differential.
DR Genevisible; Q96QT6; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; IDA:MGI.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA: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 IDEAL; IID00326; -.
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 3D-structure; Alternative splicing; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1004
FT /note="PHD finger protein 12"
FT /id="PRO_0000059302"
FT DOMAIN 815..869
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 28..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..273
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000269|PubMed:11390640"
FT REGION 105..128
FT /note="PBR"
FT REGION 113..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..704
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000269|PubMed:11390640"
FT REGION 530..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..923
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 124..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 671
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 900
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 973
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 987
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 991
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..414
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051767"
FT VAR_SEQ 80..107
FT /note="LQCCNPPLSEEMLPPGEWMCHRCTVRRK -> LVVYQDFVAPISLFHGTFHD
FT GPTCSFAQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051768"
FT VAR_SEQ 697..704
FT /note="DGKVSPGT -> GECCSALG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11390640,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051769"
FT VAR_SEQ 705..1004
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11390640,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051770"
FT VAR_SEQ 787..849
FT /note="VQRKEVQARAVFYPLLGLGGAVNMCYRTLYIGTGADMDVCLTNYGHCNYVSG
FT KHACIFYDENT -> GAHVHTCHHIIRSPLYVCEWSPCLHGESELPVSQTSLCAFHGLN
FT KAPWFFSEESRNKMATTAF (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051771"
FT VAR_SEQ 850..1004
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051772"
FT CONFLICT 762
FT /note="F -> Y (in Ref. 2; BAB14875)"
FT /evidence="ECO:0000305"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:2L9S"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2LKM"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2L9S"
SQ SEQUENCE 1004 AA; 109698 MW; 239223BE9EAF619B CRC64;
MWEKMETKTI VYDLDTSGGL MEQIQALLAP PKTDEAEKRS RKPEKEPRRS GRATNHDSCD
SCKEGGDLLC CDHCPAAFHL QCCNPPLSEE MLPPGEWMCH RCTVRRKKRE QKKELGHVNG
LVDKSGKRTT SPSSDTDLLD RSASKTELKA IAHARILERR ASRPGTPTSS ASTETPTSEQ
NDVDEDIIDV DEEPVAAEPD YVQPQLRRPF ELLIAAAMER NPTQFQLPNE LTCTTALPGS
SKRRRKEETT GKNVKKTQHE LDHNGLVPLP VKVCFTCNRS CRVAPLIQCD YCPLLFHMDC
LEPPLTAMPL GRWMCPNHIE HVVLNQKNMT LSNRCQVFDR FQDTVSQHVV KVDFLNRIHK
KHPPNRRVLQ SVKRRSLKVP DAIKSQYQFP PPLIAPAAIR DGELICNGIP EESQMHLLNS
EHLATQAEQQ EWLCSVVALQ CSILKHLSAK QMPSHWDSEQ TEKADIKPVI VTDSSVTTSL
QTADKTPTPS HYPLSCPSGI STQNSLSCSP PHQSPALEDI GCSSCAEKSK KTPCGTANGP
VNTEVKANGP HLYSSPTDST DPRRLPGANT PLPGLSHRQG WPRPLTPPAA GGLQNHTVGI
IVKTENATGP SSCPQRSLVP VPSLPPSIPS SCASIENTST LQRKTVQSQI GPPLTDSRPL
GSPPNATRVL TPPQAAGDGI LATTANQRFS SPAPSSDGKV SPGTLSIGSA LTVPSFPANS
TAMVDLTNSL RAFMDVNGEI EINMLDEKLI KFLALQRIHQ LFPSRVQPSP GSVGTHQLAS
GGHHIEVQRK EVQARAVFYP LLGLGGAVNM CYRTLYIGTG ADMDVCLTNY GHCNYVSGKH
ACIFYDENTK HYELLNYSEH GTTVDNVLYS CDFSEKTPPT PPSSIVAKVQ SVIRRRRHQK
QDEEPSEEAA MMSSQAQGPQ RRPCNCKASS SSLIGGSGAG WEGTALLHHG SYIKLGCLQF
VFSITEFATK QPKGDASLLQ DGVLAEKLSL KPHQGPVLRS NSVP
