ID   PHF10_MOUSE             Reviewed;         497 AA.
AC   Q9D8M7; E9QLI2; Q99LV5;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=PHD finger protein 10;
DE   AltName: Full=BRG1-associated factor 45a;
DE            Short=BAF45a;
GN   Name=Phf10; Synonyms=Baf45a;
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 MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 66-497 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION IN THE
RP   NPBAF COMPLEX, INTERACTION WITH ACTL6A; SMARCA2; SMARCA4 AND PBRM1,
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA   Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-296; SER-300;
RP   SER-326 AND SER-330, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=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: 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. {ECO:0000269|PubMed:17640523}.
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. {ECO:0000269|PubMed:17640523}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D8M7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D8M7-2; Sequence=VSP_013441;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed selectively in neural
CC       stem and progenitor cells (at protein level).
CC       {ECO:0000269|PubMed:17640523}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in neural cells at 10.5-11.5 dpc. At
CC       10.5 to 16.5 dpc, in the developing spinal cord, specifically expressed
CC       in proliferating neural progenitors of the ventricular zone. In the
CC       developing forebrain and cerebellar primordium, expression is
CC       restricted to proliferating neuroepithelial progenitors and cerebellar
CC       granule precursors. {ECO:0000269|PubMed:17640523}.
CC   -!- SIMILARITY: Belongs to the SAYP family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-88 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH02206.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB25323.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK007873; BAB25323.1; ALT_INIT; mRNA.
DR   EMBL; AC154411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC182749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002206; AAH02206.1; ALT_INIT; mRNA.
DR   CCDS; CCDS28407.2; -. [Q9D8M7-1]
DR   RefSeq; NP_077212.3; NM_024250.4.
DR   AlphaFoldDB; Q9D8M7; -.
DR   SMR; Q9D8M7; -.
DR   BioGRID; 215123; 7.
DR   ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR   ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR   ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR   ComplexPortal; CPX-1252; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1254; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   IntAct; Q9D8M7; 2.
DR   MINT; Q9D8M7; -.
DR   STRING; 10090.ENSMUSP00000024657; -.
DR   GlyGen; Q9D8M7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9D8M7; -.
DR   PhosphoSitePlus; Q9D8M7; -.
DR   EPD; Q9D8M7; -.
DR   jPOST; Q9D8M7; -.
DR   MaxQB; Q9D8M7; -.
DR   PaxDb; 10090-ENSMUSP00000024657; -.
DR   ProteomicsDB; 289491; -. [Q9D8M7-1]
DR   ProteomicsDB; 289492; -. [Q9D8M7-2]
DR   Pumba; Q9D8M7; -.
DR   DNASU; 72057; -.
DR   GeneID; 72057; -.
DR   KEGG; mmu:72057; -.
DR   UCSC; uc008anj.2; mouse. [Q9D8M7-2]
DR   AGR; MGI:1919307; -.
DR   CTD; 55274; -.
DR   MGI; MGI:1919307; Phf10.
DR   eggNOG; KOG1512; Eukaryota.
DR   InParanoid; Q9D8M7; -.
DR   OrthoDB; 5490909at2759; -.
DR   BioGRID-ORCS; 72057; 3 hits in 82 CRISPR screens.
DR   PRO; PR:Q9D8M7; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9D8M7; Protein.
DR   GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR   GO; GO:0000776; C:kinetochore; NAS:ComplexPortal.
DR   GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IMP:UniProtKB.
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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Isopeptide bond; Metal-binding; Neurogenesis;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..497
FT                   /note="PHD finger protein 10"
FT                   /id="PRO_0000059298"
FT   ZN_FING         378..435
FT                   /note="PHD-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         437..480
FT                   /note="PHD-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..294
FT                   /note="SAY"
FT   REGION          88..184
FT                   /note="Essential to induce neural progenitor proliferation"
FT   REGION          284..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..333
FT                   /note="Essential to induce neural progenitor proliferation"
FT   COMPBIAS        30..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT   MOD_RES         269
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT   CROSSLNK        384
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT   VAR_SEQ         108..109
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013441"
FT   CONFLICT        2
FT                   /note="T -> A (in Ref. 1; BAB25323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10
FT                   /note="P -> L (in Ref. 1; BAB25323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="S -> Y (in Ref. 1; BAB25323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349
FT                   /note="M -> V (in Ref. 1; BAB25323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="M -> V (in Ref. 1; BAB25323)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   497 AA;  55840 MW;  A1F27CB9F616A271 CRC64;
     MTAAGPGAAP SPGRCDSDPA SPGAQSPKDD NEDNSNDGTH PCKRRRMGSG DSSRSCETSS
     QDLSFSYYPA ENLIEYKWPP DETGEYYMLQ EQVSEYLGVT SFKRKYPDLE RRDLSHKEKL
     YLRELNVITE TQCTLGLTAL RSDEVIDLMI KEYPAKHAEY SVILQEKERQ RITDHYKEYS
     QMQQQSTQKV EASKVPEYIK KAAKKAAEFN SNLNRERMEE RRAYFDLQTH VIQVPQGKYK
     VLPTDRTKVS SYPVALIPGQ FQEYYKRYSP DELRYLPLNT ALYEPPLDPE LPALDSDGDS
     DDGEDGGGDE KRKNKGTSDS SSGNVSEGDS PPDSQEDTFH GRQKSKDKMA TPRKDGSKRS
     VLSKSAPGYK PKVIPNALCG ICLKGKESNK KGKAESLIHC SQCDNSGHPS CLDMTMELVS
     MIKTYPWQCM ECKTCIICGQ PHHEEEMMFC DVCDRGYHTF CVGLGAIPSG RWICDCCQRA
     PPTPRKVGRR GKNSKEG
//