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Vacuolar protein sorting-associated protein 72 homolog (Protein YL-1)

 VPS72_DROME             Reviewed;         351 AA.
Q9VKM6;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 125.
RecName: Full=Vacuolar protein sorting-associated protein 72 homolog;
AltName: Full=Protein YL-1;
Name=YL-1; ORFNames=CG4621;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
IDENTIFICATION IN THE TIP60 COMPLEX, AND FUNCTION.
PubMed=15528408; DOI=10.1126/science.1103455;
Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,
Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
"Acetylation by Tip60 is required for selective histone variant
exchange at DNA lesions.";
Science 306:2084-2087(2004).
[5]
FUNCTION, AND PROBABLE INTERACTION WITH HIS2AV.
PubMed=16299513; DOI=10.1038/nsmb1023;
Wu W.-H., Alami S., Luk E., Wu C.-H., Sen S., Mizuguchi G., Wei D.,
Wu C.;
"Swc2 is a widely conserved H2AZ-binding module essential for ATP-
dependent histone exchange.";
Nat. Struct. Mol. Biol. 12:1064-1071(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-59 AND SER-68,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Part of the Tip60 chromatin-remodeling complex which is
involved in DNA repair. Upon induction of DNA double-strand
breaks, this complex acetylates phosphorylated H2AV in nucleosomes
and exchanges it with unmodified H2AV.
{ECO:0000269|PubMed:15528408, ECO:0000269|PubMed:16299513}.
-!- SUBUNIT: Interacts with H2AV (Probable). Component of the Tip60
chromatin-remodeling complex which contains the catalytic subunit
Tip60 and the subunits Domino, Tra1, Brd8, E(Pc), DMAP1, Pontin,
Reptin, Ing3, Act87E, BAP55, Mrg15, MrgBP, Gas41 and YL-1.
{ECO:0000269|PubMed:15528408, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the VPS72/YL1 family. {ECO:0000305}.
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EMBL; AE014134; AAF53038.1; -; Genomic_DNA.
EMBL; AY122237; AAM52749.1; -; mRNA.
RefSeq; NP_001285823.1; NM_001298894.1.
RefSeq; NP_609475.1; NM_135631.4.
UniGene; Dm.12184; -.
PDB; 5CHL; X-ray; 1.89 A; A=2-75.
PDBsum; 5CHL; -.
SMR; Q9VKM6; -.
BioGrid; 60585; 10.
IntAct; Q9VKM6; 5.
STRING; 7227.FBpp0079735; -.
iPTMnet; Q9VKM6; -.
PaxDb; Q9VKM6; -.
PRIDE; Q9VKM6; -.
EnsemblMetazoa; FBtr0080146; FBpp0079735; FBgn0032321.
EnsemblMetazoa; FBtr0340549; FBpp0309447; FBgn0032321.
GeneID; 34516; -.
KEGG; dme:Dmel_CG4621; -.
UCSC; CG4621-RA; d. melanogaster.
CTD; 34516; -.
FlyBase; FBgn0032321; YL-1.
eggNOG; KOG2897; Eukaryota.
eggNOG; ENOG41119RU; LUCA.
InParanoid; Q9VKM6; -.
KO; K11664; -.
OMA; CERTFVT; -.
OrthoDB; EOG091G0BQW; -.
PhylomeDB; Q9VKM6; -.
GenomeRNAi; 34516; -.
PRO; PR:Q9VKM6; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0032321; -.
ExpressionAtlas; Q9VKM6; baseline and differential.
Genevisible; Q9VKM6; DM.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IPI:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR008895; Vps72/YL1.
InterPro; IPR013272; Vps72/YL1_C.
PANTHER; PTHR13275; PTHR13275; 1.
Pfam; PF05764; YL1; 1.
Pfam; PF08265; YL1_C; 1.
SMART; SM00993; YL1_C; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Coiled coil; Complete proteome;
DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 351 Vacuolar protein sorting-associated
protein 72 homolog.
/FTId=PRO_0000239006.
DNA_BIND 156 208 {ECO:0000255}.
COILED 142 202 {ECO:0000255}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
TURN 9 14 {ECO:0000244|PDB:5CHL}.
HELIX 15 30 {ECO:0000244|PDB:5CHL}.
HELIX 31 33 {ECO:0000244|PDB:5CHL}.
TURN 56 59 {ECO:0000244|PDB:5CHL}.
TURN 62 64 {ECO:0000244|PDB:5CHL}.
SEQUENCE 351 AA; 40442 MW; CB2D4B48CD09BDDE CRC64;
MAASRSRRNN AGNKIAHLLN EEEEDDFYKT SYGGFQEDEE DKEYEQKDEE EDVVDSDFSI
DENDEPVSDQ EEAPEKKRKR GVVNTKAYKE TKPAVKKETK ATPALHKKRP GGGVTKRRPR
PRFTVLDSGR KSIRTSTAIK TQATKIRLKE LDDARKRKKK KVRVEDYMPT QEELLEEAKI
TEEENTKSLE KFQKMELEKK KSRPTKRTFS GPTIRYHSLT MPAMRKPTRG ANPAVDSKDL
AGKCERTFVT IENDFNDKVF QSLFRHKAPP KASNGICPIT RLPARYFDPI TQQPYYSIQA
FKILREAYYM QLEQQGGGSE QPELAKWLEW RKLVKENRLK ASAAASKNGD N


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