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 27-MAR-2024, entry version 172. 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}; 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; 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 PDB; 7VDV; EM; 3.40 A; R=1-498. DR PDB; 7Y8R; EM; 4.40 A; R=1-498. DR PDBsum; 7VDV; -. DR PDBsum; 7Y8R; -. DR AlphaFoldDB; Q8WUB8; -. DR EMDB; EMD-31926; -. DR EMDB; EMD-33684; -. DR SMR; Q8WUB8; -. DR BioGRID; 120562; 140. 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; 65. 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; 9606-ENSP00000341805; -. DR PeptideAtlas; Q8WUB8; -. DR ProteomicsDB; 74654; -. [Q8WUB8-1] DR ProteomicsDB; 74655; -. [Q8WUB8-2] DR ProteomicsDB; 74656; -. [Q8WUB8-3] DR Pumba; Q8WUB8; -. DR Antibodypedia; 33573; 102 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 AGR; HGNC:18250; -. 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; ECKRCTI; -. DR OrthoDB; 5490909at2759; -. DR PhylomeDB; Q8WUB8; -. DR TreeFam; TF318971; -. DR PathwayCommons; Q8WUB8; -. DR SignaLink; Q8WUB8; -. DR SIGNOR; Q8WUB8; -. DR BioGRID-ORCS; 55274; 31 hits in 1156 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 203 other cell types or tissues. DR ExpressionAtlas; Q8WUB8; baseline and differential. DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal. DR GO; GO:0000776; C:kinetochore; NAS:ComplexPortal. DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0016586; C:RSC-type complex; NAS:ComplexPortal. DR GO; GO:0016514; C:SWI/SNF complex; NAS:ComplexPortal. DR GO; GO:0004402; F:histone acetyltransferase activity; 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; NAS:ComplexPortal. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS: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; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR CDD; cd15528; PHD1_PHF10; 1. DR CDD; cd15529; PHD2_PHF10; 1. DR CDD; cd21085; WH_NTD_PHF10; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR038045; PHF10_PHD_finger_1. 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; PTHR45888; HL01030P-RELATED; 1. DR PANTHER; PTHR45888:SF8; PHD FINGER PROTEIN 10; 1. DR Pfam; PF00628; PHD; 2. DR SMART; SM00249; PHD; 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 2. DR Genevisible; Q8WUB8; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond; KW Metal-binding; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; 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" FT HELIX 198..218 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 223..226 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 233..236 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:7VDV" FT TURN 245..248 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 257..261 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 271..276 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:7VDV" 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 //