PHF10_RAT
ID PHF10_RAT Reviewed; 497 AA.
AC Q4V7A6;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=PHD finger protein 10;
DE AltName: Full=BRG1-associated factor 45a;
DE Short=BAF45a;
GN Name=Phf10; Synonyms=Baf45a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-296; SER-300 AND
RP SER-326, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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=AAH98049.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC098049; AAH98049.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q4V7A6; -.
DR SMR; Q4V7A6; -.
DR STRING; 10116.ENSRNOP00000020865; -.
DR iPTMnet; Q4V7A6; -.
DR PhosphoSitePlus; Q4V7A6; -.
DR PaxDb; Q4V7A6; -.
DR PRIDE; Q4V7A6; -.
DR UCSC; RGD:1305266; rat.
DR RGD; 1305266; Phf10.
DR eggNOG; KOG1512; Eukaryota.
DR InParanoid; Q4V7A6; -.
DR PhylomeDB; Q4V7A6; -.
DR TreeFam; TF318971; -.
DR PRO; PR:Q4V7A6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
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:1990403; P:embryonic brain development; IEP:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 Isopeptide bond; Metal-binding; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..497
FT /note="PHD finger protein 10"
FT /id="PRO_0000391320"
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 /evidence="ECO:0000250"
FT REGION 284..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..333
FT /note="Essential to induce neural progenitor proliferation"
FT /evidence="ECO:0000250"
FT COMPBIAS 30..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..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:22673903"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8M7"
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"
SQ SEQUENCE 497 AA; 55884 MW; 88851011E8B24F82 CRC64;
MAAAGPGAAL SPRRCDSDPA SPGAQSPKDD NEDNSNDGGH PSKRRRMGSG 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 PPDSQEDTFQ GRQKSKDKMA TPRKDGSKRS
VLSKSVPGYK PKVIPNALCG ICLKGKESNK KGKAESLIHC SQCDNSGHPS CLDMTMELVS
MIKTYPWQCM ECKTCIICGQ PHHEEEMMFC DVCDRGYHTF CVGLGAIPSG RWICDCCQRA
PPTPRKVGRR GKNSKEG
