VPS72_PONAB
ID VPS72_PONAB Reviewed; 364 AA.
AC Q5R5V9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Vacuolar protein sorting-associated protein 72 homolog;
DE AltName: Full=Transcription factor-like 1;
GN Name=VPS72; Synonyms=TCFL1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deposition-and-exchange histone chaperone specific for H2AZ1,
CC specifically chaperones H2AZ1 and deposits it into nucleosomes. As
CC component of the SRCAP complex, mediates the ATP-dependent exchange of
CC histone H2AZ1/H2B dimers for nucleosomal H2A/H2B, leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC {ECO:0000250|UniProtKB:Q15906}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41 and VPS72/YL1. Component of a NuA4-related complex which
CC contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41.
CC Also part of a multiprotein complex which contains SRCAP and which
CC binds to H2AZ1/H2AZ. Interacts (via N-terminal domain) with H2AZ1.
CC {ECO:0000250|UniProtKB:Q15906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15906}.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family. {ECO:0000305}.
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DR EMBL; CR860743; CAH92857.1; -; mRNA.
DR RefSeq; NP_001126671.1; NM_001133199.1.
DR AlphaFoldDB; Q5R5V9; -.
DR SMR; Q5R5V9; -.
DR STRING; 9601.ENSPPYP00000001020; -.
DR PRIDE; Q5R5V9; -.
DR Ensembl; ENSPPYT00000001054; ENSPPYP00000001020; ENSPPYG00000000873.
DR GeneID; 100173671; -.
DR KEGG; pon:100173671; -.
DR CTD; 6944; -.
DR eggNOG; KOG2897; Eukaryota.
DR GeneTree; ENSGT00390000017503; -.
DR HOGENOM; CLU_040862_0_0_1; -.
DR InParanoid; Q5R5V9; -.
DR OrthoDB; 1468037at2759; -.
DR TreeFam; TF314532; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IEA:InterPro.
DR GO; GO:0043968; P:histone H2A acetylation; IEA:Ensembl.
DR GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR InterPro; IPR008895; Vps72/YL1.
DR InterPro; IPR013272; Vps72/YL1_C.
DR PANTHER; PTHR13275; PTHR13275; 1.
DR Pfam; PF05764; YL1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR SMART; SM00993; YL1_C; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..364
FT /note="Vacuolar protein sorting-associated protein 72
FT homolog"
FT /id="PRO_0000239004"
FT DNA_BIND 156..206
FT /evidence="ECO:0000255"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15906"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15906"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15906"
SQ SEQUENCE 364 AA; 40539 MW; 27E38F521B2BCE77 CRC64;
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD
FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK VSTPAGSSQK AREEKALLPL
ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE ELLREAKITE
ELNLRSLETY ERLEADKKKQ VHKKRKCPGP IITYHSVTVP LVGEPGPKEE NVDIEGLDPA
PSASALTPHA GTGPVNPPAR CSRTFITFSD DATFEEWFPQ GRPPKVPVRE VCPVTHRPAL
YRDPVTDIPY ATARAFKIIR EAYKKYITAH GLPPTASALG PGPPPPEPLP GSGPRALRQK
IVIK