PHF10_HUMAN
ID PHF10_HUMAN Reviewed; 498 AA.
AC Q8WUB8; Q2YDA3; Q53HG8; Q9BXD2; Q9NV26;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=PHD finger protein 10;
DE AltName: Full=BRG1-associated factor 45a;
DE Short=BAF45a;
DE AltName: Full=XAP135;
GN Name=PHF10; Synonyms=BAF45A;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=20068294; DOI=10.1159/000251960;
RA Banga S.S., Peng L., Dasgupta T., Palejwala V., Ozer H.L.;
RT "PHF10 is required for cell proliferation in normal and SV40-immortalized
RT human fibroblast cells.";
RL Cytogenet. Genome Res. 126:227-242(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-498 (ISOFORM 1), AND ALTERNATIVE
RP SPLICING.
RX PubMed=11827455; DOI=10.1006/geno.2001.6680;
RA Aradhya S., Woffendin H., Bonnen P., Heiss N.S., Yamagata T., Esposito T.,
RA Bardaro T., Poustka A., D'Urso M., Kenwrick S., Nelson D.L.;
RT "Physical and genetic characterization reveals a pseudogene, an
RT evolutionary junction, and unstable loci in distal Xq28.";
RL Genomics 79:31-40(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-498 (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-498 (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-498 (ISOFORM 1).
RC TISSUE=Artery smooth muscle;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-297 AND SER-301, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-301 AND SER-327, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-12; SER-270; SER-297 AND SER-301, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-50; SER-297; SER-301
RP AND SER-327, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-327, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-301, AND
RP IDENTIFICATION BY 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-241, 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-385, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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: Involved in transcription activity regulation by chromatin
CC remodeling. Belongs to the neural progenitors-specific chromatin
CC remodeling complex (npBAF complex) and is required for the
CC proliferation of neural progenitors. During neural development a switch
CC from a stem/progenitor to a post-mitotic chromatin remodeling mechanism
CC occurs as neurons exit the cell cycle and become committed to their
CC adult state. The transition from proliferating neural stem/progenitor
CC cells to post-mitotic neurons requires a switch in subunit composition
CC of the npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and PHF10/BAF45A, are exchanged for homologous alternative
CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC specific complexes (nBAF). The npBAF complex is essential for the self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role regulating the activity
CC of genes essential for dendrite growth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of neural progenitors-specific chromatin remodeling
CC complex (npBAF complex) composed of at least, ARID1A/BAF250A or
CC ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57,
CC SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Interacts with
CC ACTL6A/BAF53A, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A and
CC PBRM1/BAF180 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8WUB8-2; P05067: APP; NbExp=3; IntAct=EBI-10276329, EBI-77613;
CC Q8WUB8-2; Q969R5: L3MBTL2; NbExp=6; IntAct=EBI-10276329, EBI-739909;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WUB8-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q8WUB8-2; Sequence=VSP_013440;
CC Name=3;
CC IsoId=Q8WUB8-3; Sequence=VSP_039090;
CC -!- SIMILARITY: Belongs to the SAYP family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-89 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20954.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI10324.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK27451.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA91934.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD96332.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAG33554.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL513547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020954; AAH20954.1; ALT_INIT; mRNA.
DR EMBL; BC110323; AAI10324.1; ALT_INIT; mRNA.
DR EMBL; AF338735; AAK27451.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK001837; BAA91934.1; ALT_INIT; mRNA.
DR EMBL; CR457273; CAG33554.1; ALT_INIT; mRNA.
DR EMBL; AK222612; BAD96332.1; ALT_INIT; mRNA.
DR CCDS; CCDS5308.2; -. [Q8WUB8-1]
DR CCDS; CCDS5309.2; -. [Q8WUB8-2]
DR RefSeq; NP_060758.2; NM_018288.3. [Q8WUB8-1]
DR RefSeq; NP_579866.2; NM_133325.2. [Q8WUB8-2]
DR AlphaFoldDB; Q8WUB8; -.
DR SMR; Q8WUB8; -.
DR BioGRID; 120562; 120.
DR ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR CORUM; Q8WUB8; -.
DR IntAct; Q8WUB8; 64.
DR MINT; Q8WUB8; -.
DR STRING; 9606.ENSP00000341805; -.
DR iPTMnet; Q8WUB8; -.
DR MetOSite; Q8WUB8; -.
DR PhosphoSitePlus; Q8WUB8; -.
DR BioMuta; PHF10; -.
DR DMDM; 296439276; -.
DR EPD; Q8WUB8; -.
DR jPOST; Q8WUB8; -.
DR MassIVE; Q8WUB8; -.
DR MaxQB; Q8WUB8; -.
DR PaxDb; Q8WUB8; -.
DR PeptideAtlas; Q8WUB8; -.
DR PRIDE; Q8WUB8; -.
DR ProteomicsDB; 74654; -. [Q8WUB8-1]
DR ProteomicsDB; 74655; -. [Q8WUB8-2]
DR ProteomicsDB; 74656; -. [Q8WUB8-3]
DR Antibodypedia; 33573; 91 antibodies from 20 providers.
DR DNASU; 55274; -.
DR Ensembl; ENST00000339209.9; ENSP00000341805.4; ENSG00000130024.15. [Q8WUB8-1]
DR Ensembl; ENST00000366780.8; ENSP00000355743.4; ENSG00000130024.15. [Q8WUB8-2]
DR Ensembl; ENST00000621772.4; ENSP00000484117.1; ENSG00000130024.15. [Q8WUB8-3]
DR GeneID; 55274; -.
DR KEGG; hsa:55274; -.
DR MANE-Select; ENST00000339209.9; ENSP00000341805.4; NM_018288.4; NP_060758.2.
DR UCSC; uc011egy.3; human. [Q8WUB8-1]
DR CTD; 55274; -.
DR DisGeNET; 55274; -.
DR GeneCards; PHF10; -.
DR HGNC; HGNC:18250; PHF10.
DR HPA; ENSG00000130024; Low tissue specificity.
DR MIM; 613069; gene.
DR neXtProt; NX_Q8WUB8; -.
DR OpenTargets; ENSG00000130024; -.
DR PharmGKB; PA134972675; -.
DR VEuPathDB; HostDB:ENSG00000130024; -.
DR eggNOG; KOG1512; Eukaryota.
DR GeneTree; ENSGT00940000155172; -.
DR HOGENOM; CLU_028634_2_0_1; -.
DR InParanoid; Q8WUB8; -.
DR OMA; PKDDTEE; -.
DR OrthoDB; 708781at2759; -.
DR PhylomeDB; Q8WUB8; -.
DR TreeFam; TF318971; -.
DR PathwayCommons; Q8WUB8; -.
DR SignaLink; Q8WUB8; -.
DR BioGRID-ORCS; 55274; 29 hits in 1077 CRISPR screens.
DR ChiTaRS; PHF10; human.
DR GeneWiki; PHF10; -.
DR GenomeRNAi; 55274; -.
DR Pharos; Q8WUB8; Tbio.
DR PRO; PR:Q8WUB8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8WUB8; protein.
DR Bgee; ENSG00000130024; Expressed in adrenal tissue and 201 other tissues.
DR ExpressionAtlas; Q8WUB8; baseline and differential.
DR Genevisible; Q8WUB8; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IC:ComplexPortal.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038045; PHF10.
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; PTHR10615:SF174; PTHR10615:SF174; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Metal-binding;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..498
FT /note="PHD finger protein 10"
FT /id="PRO_0000059297"
FT ZN_FING 379..436
FT /note="PHD-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 438..481
FT /note="PHD-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..295
FT /note="SAY"
FT REGION 89..185
FT /note="Essential to induce neural progenitor proliferation"
FT /evidence="ECO:0000250"
FT REGION 285..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..334
FT /note="Essential to induce neural progenitor proliferation"
FT /evidence="ECO:0000250"
FT COMPBIAS 42..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8M7"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:20068294"
FT /id="VSP_039090"
FT VAR_SEQ 109..110
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013440"
FT CONFLICT 126
FT /note="L -> P (in Ref. 4; AAK27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="E -> G (in Ref. 4; AAK27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="R -> W (in Ref. 4; AAK27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="PP -> AT (in Ref. 4; AAK27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="N -> K (in Ref. 4; AAK27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="P -> S (in Ref. 4; AAK27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="G -> A (in Ref. 4; AAK27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="K -> N (in Ref. 4; AAK27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="M -> T (in Ref. 7; BAD96332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 56051 MW; 05EFDABD2000C2B7 CRC64;
MAAAAGPGAA LSPRPCDSDP ATPGAQSPKD DNEDNSNDGT QPSKRRRMGS GDSSRSCETS
SQDLGFSYYP AENLIEYKWP PDETGEYYML QEQVSEYLGV TSFKRKYPDL ERRDLSHKEK
LYLRELNVIT ETQCTLGLTA LRSDEVIDLM IKEYPAKHAE YSVILQEKER QRITDHYKEY
SQMQQQNTQK VEASKVPEYI KKAAKKAAEF NSNLNRERME ERRAYFDLQT HVIQVPQGKY
KVLPTERTKV SSYPVALIPG QFQEYYKRYS PDELRYLPLN TALYEPPLDP ELPALDSDGD
SDDGEDGRGD EKRKNKGTSD SSSGNVSEGE SPPDSQEDSF QGRQKSKDKA ATPRKDGPKR
SVLSKSVPGY KPKVIPNAIC GICLKGKESN KKGKAESLIH CSQCENSGHP SCLDMTMELV
SMIKTYPWQC MECKTCIICG QPHHEEEMMF CDMCDRGYHT FCVGLGAIPS GRWICDCCQR
APPTPRKVGR RGKNSKEG
