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Q03388 (VPS72_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar protein sorting-associated protein 72
Alternative name(s):
SWR complex protein 2
Gene names
Name:VPS72
Synonyms:SWC2
Ordered Locus Names:YDR485C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the catalytic exchange of histone H2A for the H2A variant HTZ1, an euchromatin-specific factor, leading to chromatin remodeling and changes in transcription of targeted genes. Indirectly involved in vacuolar protein sorting. Ref.5 Ref.6 Ref.9 Ref.10

Subunit structure

Belongs to the SWR1 complex at least composed of ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWR1 and HTZ1. Interacts with HTZ1. Ref.6 Ref.9 Ref.10 Ref.11

Subcellular location

Nucleus Ref.7.

Miscellaneous

Present with 358 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the VPS72/YL1 family.

Sequence caution

The sequence AAB64928.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAT93172.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Vacuolar protein sorting-associated protein 72
PRO_0000065909

Regions

Region1 – 281281Interaction with HTZ1
Coiled coil28 – 6336 Potential
Coiled coil121 – 15030 Potential
Coiled coil204 – 28178 Potential
Compositional bias57 – 8529Asp-rich
Compositional bias315 – 34329Lys-rich

Amino acid modifications

Modified residue4251Phosphoserine Ref.12

Sequences

Sequence LengthMass (Da)Tools
Q03388 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 6D3053EBB610DB95

FASTA79590,580
        10         20         30         40         50         60 
MSDEGADKSL DTNTEFIIQT RSRRSNAGNK LQKLLEQELR DIESTKRQIS SYKNGNDDEE 

        70         80         90        100        110        120 
DEIGLLFQED EDDEDFEMMA KDDDDEGEEK EDETQSIRKE PSQASSEQAA DDLMFSSSES 

       130        140        150        160        170        180 
EDSSNENDED AEEKEIRRQE LLSRKKRNKR LQKGPVVIKK QKPKPKSGEA IPRSHHTHEQ 

       190        200        210        220        230        240 
LNAETLLLNT RRTSKRSSVM ENTMKVYEKL SKAEKKRKII QERIRKHKEQ ESQHMLTQEE 

       250        260        270        280        290        300 
RLRIAKETEK LNILSLDKFK EQEVWKKENR LALQKRQKQK FQPNETILQF LSTAWLMTPA 

       310        320        330        340        350        360 
MELEDRKYWQ EQLNKRDKKK KKYPRKPKKN LNLGKQDASD DKKRESEESI KNDGDVNSLG 

       370        380        390        400        410        420 
ENSSSVHNQK RIEETSTNDT VEGESSPDAA VSRVNSDELK PTALPDVTLD AIANKQSTVD 

       430        440        450        460        470        480 
EAPNSQPQKN IITNEQKITN VGEPIQNLHN EEIKDEMVSA LESRENTFEN SSPAAQVVSQ 

       490        500        510        520        530        540 
RDNSATPTPS NSTGTEDTIL ISPDTDIKGE PEPCLKTEGI ENLSHNVPQE TKSNTDVSFL 

       550        560        570        580        590        600 
KQVTFTDHPQ VAIIDTEESP SKKDTANVDE SSAENSLSTQ TYEGPEQLTS RNFVTLYDFP 

       610        620        630        640        650        660 
NAPPNLKDFN TNLFGDRWSY TNGLSATQRP QDMKTVFHSI LPSPPQSSVP SPTVDISLDL 

       670        680        690        700        710        720 
SALANFPSFG EYDKKIVHQI NTEINKDLEI KIKTQPPTGV FLANGIRKKC LITNKECQYF 

       730        740        750        760        770        780 
DPRTGVPYSD VEAYKIIQRI QDPISKEEGR SDIKRDETTN EDSDDQVRFK WFGFKNGGIY 

       790 
LDLSQRPAKG VPEGF 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[5]"Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae."
Bonangelino C.J., Chavez E.M., Bonifacino J.S.
Mol. Biol. Cell 13:2486-2501(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1."
Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A., Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A., Hughes T.R., Buratowski S., Greenblatt J.F.
Mol. Cell 12:1565-1576(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS71; SWC3; SWC4; SWC5; SWR1 AND HTZ1.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex."
Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.
Science 303:343-348(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS71; SWC3; SWC4; SWC5; SWR1 AND HTZ1.
[10]"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin."
Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J.
PLoS Biol. 2:587-599(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACT1; ARP4; RVB1; RVB2; ARP6; YAF9; VPS71; SWC3; SWC4; SWC5; SWR1 AND HTZ1.
[11]"Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange."
Wu W.-H., Alami S., Luk E., Wu C.-H., Sen S., Mizuguchi G., Wei D., Wu C.
Nat. Struct. Mol. Biol. 12:1064-1071(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTZ1.
[12]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33050 Genomic DNA. Translation: AAB64928.1. Different initiation.
AY693153 Genomic DNA. Translation: AAT93172.1. Different initiation.
BK006938 Genomic DNA. Translation: DAA12318.1.
PIRS69652.
RefSeqNP_010773.4. NM_001180793.3.

3D structure databases

ProteinModelPortalQ03388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32537. 350 interactions.
DIPDIP-1008N.
IntActQ03388. 14 interactions.
MINTMINT-2782183.
STRING4932.YDR485C.

Proteomic databases

MaxQBQ03388.
PaxDbQ03388.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR485C; YDR485C; YDR485C.
GeneID852096.
KEGGsce:YDR485C.

Organism-specific databases

CYGDYDR485c.
SGDS000002893. VPS72.

Phylogenomic databases

eggNOGNOG253988.
HOGENOMHOG000141998.
KOK11664.
OMALLFQEDE.
OrthoDBEOG78PVK3.

Enzyme and pathway databases

BioCycYEAST:G3O-30010-MONOMER.

Gene expression databases

GenevestigatorQ03388.

Family and domain databases

InterProIPR008895. YL1.
IPR013272. YL1_C.
[Graphical view]
PfamPF05764. YL1. 1 hit.
PF08265. YL1_C. 1 hit.
[Graphical view]
SMARTSM00993. YL1_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970433.
PROQ03388.

Entry information

Entry nameVPS72_YEAST
AccessionPrimary (citable) accession number: Q03388
Secondary accession number(s): D6VTA8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: June 11, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families