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Protein

Vacuolar protein sorting-associated protein 27

Gene

VPS27

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. Controls exit from the prevacuolar compartment (PVC) in both the forward direction to the vacuole and the return to the Golgi. Allows VPS10 to return to the (trans-Golgi network) TGN from the PVC. Might also function as an alternate adapter in the COPIb clathrin-like coat.16 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri170 – 23061FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol-3-phosphate binding Source: SGD
  • ubiquitin binding Source: SGD

GO - Biological processi

  • late endosome to vacuole transport Source: SGD
  • protein retention in Golgi apparatus Source: SGD
  • protein targeting to vacuole Source: SGD
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33324-MONOMER.
ReactomeiR-SCE-432720. Lysosome Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 27
Alternative name(s):
Golgi retention defective protein 11
Gene namesi
Name:VPS27
Synonyms:DID7, GRD11, SSV17, VPL23, VPT27
Ordered Locus Names:YNR006W
ORF Names:N2038
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNR006W.
SGDiS000005289. VPS27.

Subcellular locationi

GO - Cellular componenti

  • endosome Source: SGD
  • endosome membrane Source: UniProtKB-SubCell
  • ESCRT-0 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi185 – 1862LL → AA: Decreases the association to PtdIns(3)P containing membranes. 1 Publication
Mutagenesisi193 – 1931R → A: Decreases the association to PtdIns(3)P containing membranes. 1 Publication
Mutagenesisi270 – 2701S → D: Reduces strongly the ubiquitin-binding activity. 1 Publication
Mutagenesisi313 – 3131S → D: Reduces strongly the ubiquitin-binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Vacuolar protein sorting-associated protein 27PRO_0000065893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei495 – 4951PhosphoserineCombined sources
Modified residuei613 – 6131PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40343.
PeptideAtlasiP40343.

PTM databases

iPTMnetiP40343.

Interactioni

Subunit structurei

Component of the ESCRT-0 complex composed of HSE1 and VPS27. Interacts with ENT3 and ENT5, the ESCRT-I subunits VPS23 and VPS28 and with the COPIb subunits SEC27, SEC28 and SEC33.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSE1P3875310EBI-20380,EBI-1382
SEC28P405092EBI-20380,EBI-4884
STP22P256047EBI-20380,EBI-411625
UBBP0CG536EBI-20380,EBI-5333021From a different organism.

GO - Molecular functioni

  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi35831. 393 interactions.
DIPiDIP-1741N.
IntActiP40343. 7 interactions.
MINTiMINT-386565.

Structurei

Secondary structure

1
622
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni177 – 1793Combined sources
Turni193 – 1953Combined sources
Helixi201 – 2033Combined sources
Beta strandi206 – 2105Combined sources
Helixi211 – 2133Combined sources
Beta strandi215 – 2217Combined sources
Helixi223 – 2308Combined sources
Beta strandi251 – 2533Combined sources
Helixi259 – 27214Combined sources
Helixi274 – 2763Combined sources
Helixi304 – 31815Combined sources
Helixi352 – 36918Combined sources
Turni375 – 3795Combined sources
Helixi381 – 43656Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O06X-ray1.45A301-320[»]
1Q0VNMR-A249-329[»]
1Q0WNMR-A255-278[»]
1VFYX-ray1.15A163-230[»]
2KDINMR-A258-277[»]
2PJWX-ray3.01V348-438[»]
3R42X-ray1.87B445-453[»]
ProteinModelPortaliP40343.
SMRiP40343. Positions 1-231, 250-329, 348-438.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40343.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 149132VHSPROSITE-ProRule annotationAdd
BLAST
Domaini258 – 27720UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini301 – 32020UIM 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The FYVE domain is involved in the binding to phosphatidylinositol 3-phosphate (PtdIns3P) which is required for the association to endosomal membranes.
Both IUM domains are necessary for efficient binding to ubiquitin.

Sequence similaritiesi

Belongs to the VPS27 family.Curated
Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 2 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation
Contains 1 VHS domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri170 – 23061FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00670000098022.
HOGENOMiHOG000000859.
InParanoidiP40343.
KOiK12182.
OMAiACMICSK.
OrthoDBiEOG7RBZJM.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR008942. ENTH_VHS.
IPR017073. Ubi-bd_Hrs_VPS27.
IPR003903. UIM_dom.
IPR002014. VHS_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF02809. UIM. 2 hits.
PF00790. VHS. 1 hit.
[Graphical view]
PIRSFiPIRSF036956. Hrs_Vps27. 1 hit.
SMARTiSM00064. FYVE. 1 hit.
SM00726. UIM. 2 hits.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50330. UIM. 2 hits.
PS50179. VHS. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40343-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVSTPSELD ALIEQATSES IPNGDLDLPI ALEISDVLRS RRVNPKDSMR
60 70 80 90 100
CIKKRILNTA DNPNTQLSSW KLTNICVKNG GTPFIKEICS REFMDTMEHV
110 120 130 140 150
ILREDSNEEL SELVKTILYE LYVAFKNDSQ LNYVAKVYDK LISRGIKFPE
160 170 180 190 200
KLTLSNSPTA MFDSKTPADW IDSDACMICS KKFSLLNRKH HCRSCGGVFC
210 220 230 240 250
QEHSSNSIPL PDLGIYEPVR VCDSCFEDYD LKRHDDSKKS KKHRHKRKKD
260 270 280 290 300
RDYSTPEDEE ELIRKAIELS LKESRNSASS EPIVPVVESK NEVKRQEIEE
310 320 330 340 350
EEDPDLKAAI QESLREAEEA KLRSERQKAS RQMQPQQPSP QPQPIHSVDL
360 370 380 390 400
SDEEKDSIYM FASLVEKMKS RPLNEILEDS KLQNLAQRVF ASKARLNYAL
410 420 430 440 450
NDKAQKYNTL IEMNGKISEI MNIYDRLLEQ QLQSINLSQQ YTLPQVPSDP
460 470 480 490 500
YNYLTENVQN PAESYQTPPL QQLSSHQYKP QQDVSRQQSV KANSSPTTNI
510 520 530 540 550
DHLKTIDVTP HAQQKPQSHV ELAPSDPPYP KEEAEDEGTQ AVQDEESSTQ
560 570 580 590 600
ESRERPYPVE TENGETSINK RPQGITRYDF PTVPARKFVQ PESTVPLPAS
610 620
SSEIPIKEER PPSPQEELLI EL
Length:622
Mass (Da):70,974
Last modified:October 5, 2010 - v3
Checksum:i76C4501B0EBC9C84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti321 – 3222KL → NV in AAA96002 (PubMed:7593183).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24218 Genomic DNA. Translation: AAA96002.1.
X77395 Genomic DNA. Translation: CAA54574.1.
Z71620 Genomic DNA. Translation: CAA96282.1.
BK006947 Genomic DNA. Translation: DAA10547.1.
PIRiS45129.
RefSeqiNP_014403.3. NM_001183183.3.

Genome annotation databases

EnsemblFungiiYNR006W; YNR006W; YNR006W.
GeneIDi855739.
KEGGisce:YNR006W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24218 Genomic DNA. Translation: AAA96002.1.
X77395 Genomic DNA. Translation: CAA54574.1.
Z71620 Genomic DNA. Translation: CAA96282.1.
BK006947 Genomic DNA. Translation: DAA10547.1.
PIRiS45129.
RefSeqiNP_014403.3. NM_001183183.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O06X-ray1.45A301-320[»]
1Q0VNMR-A249-329[»]
1Q0WNMR-A255-278[»]
1VFYX-ray1.15A163-230[»]
2KDINMR-A258-277[»]
2PJWX-ray3.01V348-438[»]
3R42X-ray1.87B445-453[»]
ProteinModelPortaliP40343.
SMRiP40343. Positions 1-231, 250-329, 348-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35831. 393 interactions.
DIPiDIP-1741N.
IntActiP40343. 7 interactions.
MINTiMINT-386565.

PTM databases

iPTMnetiP40343.

Proteomic databases

MaxQBiP40343.
PeptideAtlasiP40343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR006W; YNR006W; YNR006W.
GeneIDi855739.
KEGGisce:YNR006W.

Organism-specific databases

EuPathDBiFungiDB:YNR006W.
SGDiS000005289. VPS27.

Phylogenomic databases

GeneTreeiENSGT00670000098022.
HOGENOMiHOG000000859.
InParanoidiP40343.
KOiK12182.
OMAiACMICSK.
OrthoDBiEOG7RBZJM.

Enzyme and pathway databases

BioCyciYEAST:G3O-33324-MONOMER.
ReactomeiR-SCE-432720. Lysosome Vesicle Biogenesis.

Miscellaneous databases

EvolutionaryTraceiP40343.
PROiP40343.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR008942. ENTH_VHS.
IPR017073. Ubi-bd_Hrs_VPS27.
IPR003903. UIM_dom.
IPR002014. VHS_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF02809. UIM. 2 hits.
PF00790. VHS. 1 hit.
[Graphical view]
PIRSFiPIRSF036956. Hrs_Vps27. 1 hit.
SMARTiSM00064. FYVE. 1 hit.
SM00726. UIM. 2 hits.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50330. UIM. 2 hits.
PS50179. VHS. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae."
    Piper R.C., Cooper A.A., Yang H., Stevens T.H.
    J. Cell Biol. 131:603-617(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Twelve open reading frames revealed in the 23.6 kb segment flanking the centromere on the Saccharomyces cerevisiae chromosome XIV right arm."
    Verhasselt P., Aert R., Voet M., Volckaert G.
    Yeast 10:1355-1361(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases."
    Robinson J.S., Klionsky D.J., Banta L.M., Emr S.D.
    Mol. Cell. Biol. 8:4936-4948(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants."
    Raymond C.K., Howald-Stevenson I., Vater C.A., Stevens T.H.
    Mol. Biol. Cell 3:1389-1402(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The newly identified yeast GRD genes are required for retention of late-Golgi membrane proteins."
    Nothwehr S.F., Bryant N.J., Stevens T.H.
    Mol. Cell. Biol. 16:2700-2707(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Two separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention."
    Bryant N.J., Stevens T.H.
    J. Cell Biol. 136:287-297(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant."
    Luo W.-J., Chang A.
    J. Cell Biol. 138:731-746(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains."
    Burd C.G., Emr S.D.
    Mol. Cell 2:157-162(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, PHOSPHATIDYLINOSITOL 3-PHOSPHATE BINDING.
  11. "Pep12p is a multifunctional yeast syntaxin that controls entry of biosynthetic, endocytic and retrograde traffic into the prevacuolar compartment."
    Gerrard S.R., Levi B.P., Stevens T.H.
    Traffic 1:259-269(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase."
    Dupre S., Haguenauer-Tsapis R.
    Mol. Cell. Biol. 21:4482-4494(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs."
    Stahelin R.V., Long F., Diraviyam K., Bruzik K.S., Murray D., Cho W.
    J. Biol. Chem. 277:26379-26388(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF 185-LEU-LEU-186 AND ARG-193.
  14. "Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis."
    Shih S.C., Katzmann D.J., Schnell J.D., Sutanto M., Emr S.D., Hicke L.
    Nat. Cell Biol. 4:389-393(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS, INTERACTION WITH UBIQUITIN, MUTAGENESIS OF SER-270 AND SER-313.
  15. "The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting."
    Bilodeau P.S., Urbanowski J.L., Winistorfer S.C., Piper R.C.
    Nat. Cell Biol. 4:534-539(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ESCRT-0 COMPLEX, FUNCTION OF THE ESCRT-0 COMPLEX.
  16. "Ordering of compartments in the yeast endocytic pathway."
    Prescianotto-Baschong C., Riezman H.
    Traffic 3:37-49(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Vps27 recruits ESCRT machinery to endosomes during MVB sorting."
    Katzmann D.J., Stefan C.J., Babst M., Emr S.D.
    J. Cell Biol. 162:413-423(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS23 AND VPS28.
  18. "Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome."
    Bilodeau P.S., Winistorfer S.C., Kearney W.R., Robertson A.D., Piper R.C.
    J. Cell Biol. 163:237-243(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ESCRT-0 COMPLEX, INTERACTION WITH UBIQUITIN.
  19. "Computer modeling of the membrane interaction of FYVE domains."
    Diraviyam K., Stahelin R.V., Cho W., Murray D.
    J. Mol. Biol. 328:721-736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  20. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  21. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  22. "Yeast Mn2+ transporter, Smf1p, is regulated by ubiquitin-dependent vacuolar protein sorting."
    Eguez L., Chung Y.-S., Kuchibhatla A., Paidhungat M., Garrett S.
    Genetics 167:107-117(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body."
    Eugster A., Pecheur E.-I., Michel F., Winsor B., Letourneur F., Friant S.
    Mol. Biol. Cell 15:3031-3041(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ENT3 AND ENT5.
  24. "Essential role for the myotubularin-related phosphatase Ymr1p and the synaptojanin-like phosphatases Sjl2p and Sjl3p in regulation of phosphatidylinositol 3-phosphate in yeast."
    Parrish W.R., Stefan C.J., Emr S.D.
    Mol. Biol. Cell 15:3567-3579(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  25. "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae."
    Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H.
    Traffic 5:194-210(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSE1 AND VPS23, FUNCTION OF THE ESCRT-0 COMPLEX.
  26. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  27. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  28. "Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast."
    Gabriely G., Kama R., Gerst J.E.
    Mol. Cell. Biol. 27:526-540(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SEC27; SEC28 AND SEC33.
  29. "Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast."
    Kama R., Robinson M., Gerst J.E.
    Mol. Cell. Biol. 27:605-621(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  30. "Efficient cargo sorting by ESCRT-I and the subsequent release of ESCRT-I from multivesicular bodies requires the subunit Mvb12."
    Curtiss M., Jones C., Babst M.
    Mol. Biol. Cell 18:636-645(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  31. "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-157 AND SER-613, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "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].
  33. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p."
    Misra S., Hurley J.H.
    Cell 97:657-666(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 163-230.
  35. "Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation."
    Swanson K.A., Kang R.S., Stamenova S.D., Hicke L., Radhakrishnan I.
    EMBO J. 22:4597-4606(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 250-329.
  36. "Structure and ubiquitin binding of the ubiquitin-interacting motif."
    Fisher R.D., Wang B., Alam S.L., Higginson D.S., Robinson H., Sundquist W.I., Hill C.P.
    J. Biol. Chem. 278:28976-28984(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 301-320, INTERACTION WITH UBIQUITIN.

Entry informationi

Entry nameiVPS27_YEAST
AccessioniPrimary (citable) accession number: P40343
Secondary accession number(s): D6W1I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 5, 2010
Last modified: June 8, 2016
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 172 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.