VPS72_MOUSE
ID VPS72_MOUSE Reviewed; 368 AA.
AC Q62481; Q3U2N4; Q810A9; Q99K81;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Vacuolar protein sorting-associated protein 72 homolog;
DE AltName: Full=Protein YL-1;
DE AltName: Full=Transcription factor-like 1;
GN Name=Vps72; Synonyms=Tcfl1, Yl1;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7702631; DOI=10.1006/bbrc.1995.1433;
RA Horikawa I., Tanaka H., Yuasa Y., Suzuki M., Oshimura M.;
RT "Molecular cloning of a novel human cDNA on chromosome 1q21 and its mouse
RT homolog encoding a nuclear protein with DNA-binding ability.";
RL Biochem. Biophys. Res. Commun. 208:999-1007(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, and Dendritic cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary gland;
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).
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 -!- TISSUE SPECIFICITY: In all tissues examined, most abundantly in brain
CC and thymus.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family. {ECO:0000305}.
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DR EMBL; D43643; BAA07758.1; -; mRNA.
DR EMBL; AK140284; BAE24317.1; -; mRNA.
DR EMBL; AK155191; BAE33106.1; -; mRNA.
DR EMBL; BC004834; AAH04834.1; -; mRNA.
DR EMBL; BC043029; AAH43029.2; -; mRNA.
DR CCDS; CCDS38543.1; -.
DR PIR; JC4141; JC4141.
DR RefSeq; NP_033362.2; NM_009336.2.
DR AlphaFoldDB; Q62481; -.
DR SMR; Q62481; -.
DR BioGRID; 204018; 3.
DR ComplexPortal; CPX-976; SRCAP chromatin remodeling complex.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q62481; 5.
DR MINT; Q62481; -.
DR STRING; 10090.ENSMUSP00000009102; -.
DR iPTMnet; Q62481; -.
DR PhosphoSitePlus; Q62481; -.
DR EPD; Q62481; -.
DR MaxQB; Q62481; -.
DR PaxDb; Q62481; -.
DR PeptideAtlas; Q62481; -.
DR PRIDE; Q62481; -.
DR ProteomicsDB; 275189; -.
DR Antibodypedia; 20319; 188 antibodies from 31 providers.
DR DNASU; 21427; -.
DR Ensembl; ENSMUST00000009102; ENSMUSP00000009102; ENSMUSG00000008958.
DR GeneID; 21427; -.
DR KEGG; mmu:21427; -.
DR UCSC; uc008qia.1; mouse.
DR CTD; 6944; -.
DR MGI; MGI:1202305; Vps72.
DR VEuPathDB; HostDB:ENSMUSG00000008958; -.
DR eggNOG; KOG2897; Eukaryota.
DR GeneTree; ENSGT00390000017503; -.
DR HOGENOM; CLU_040862_0_0_1; -.
DR InParanoid; Q62481; -.
DR OMA; VNTKAYK; -.
DR OrthoDB; 1468037at2759; -.
DR PhylomeDB; Q62481; -.
DR TreeFam; TF314532; -.
DR BioGRID-ORCS; 21427; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Vps72; mouse.
DR PRO; PR:Q62481; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q62481; protein.
DR Bgee; ENSMUSG00000008958; Expressed in ventricular zone and 225 other tissues.
DR Genevisible; Q62481; MM.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IPI: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:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IDA:MGI.
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..368
FT /note="Vacuolar protein sorting-associated protein 72
FT homolog"
FT /id="PRO_0000066284"
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 339..361
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 341..356
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"
FT CONFLICT 75
FT /note="A -> S (in Ref. 3; AAH04834)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="A -> V (in Ref. 1; BAA07758 and 2; BAE33106)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="T -> A (in Ref. 3; AAH04834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 40784 MW; 1A7F0FB6456D81C3 CRC64;
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD
FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK VSTPASSSQK AREEKTLLPL
ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE ELLREAKITE
ELNLRSLETY ERLEADKKKQ VHKKRKCPGP IITYHSVTVP LVGEPGPKEE NVDVEGLDPA
PTASALAPHA GTGTGAAAAT PPAHCSRTFI TFSDDATFEE WFPQGRPPKV PVREVCPVTH
RPALYRDPVT DIPYATARAF KIIREAYKKY ITAHGLPPTA SALGPGPPPP EPLPGSGPRA
LRQKIVIK
