P40343 (VPS27_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar protein sorting-associated protein 27

Alternative name(s):
Golgi retention defective protein 11

Gene names

Name:	VPS27
Synonyms:	DID7, GRD11, SSV17, VPL23, VPT27
Ordered Locus Names:	YNR006W
ORF Names:	N2038

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	622 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ref.23 Ref.25 Ref.28 Ref.30
Subunit structure	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. Ref.14 Ref.15 Ref.17 Ref.18 Ref.23 Ref.25 Ref.28 Ref.35
Subcellular location	Endosome membrane; Peripheral membrane protein; Cytoplasmic side Ref.13 Ref.17 Ref.20 Ref.24 Ref.28 Ref.29.
Domain	The FYVE domain is involved in the binding to phosphatidylinositol 3-phosphate (PtdIns3P) which is required for the association to endosomal membranes. Ref.10 Ref.13 Ref.14 Ref.19 Both IUM domains are necessary for efficient binding to ubiquitin. Ref.10 Ref.13 Ref.14 Ref.19
Miscellaneous	Present with 172 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the VPS27 family. Contains 1 FYVE-type zinc finger. Contains 2 UIM (ubiquitin-interacting motif) repeats. Contains 1 VHS domain.

Ontologies

Keywords
Cellular component	Endosome Membrane
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	late endosome to vacuole transport Inferred from mutant phenotype Ref.15. Source: SGD protein retention in Golgi apparatus Inferred from mutant phenotype Ref.7. Source: SGD protein targeting to vacuole Inferred from mutant phenotype Ref.15. Source: SGD
Cellular_component	ESCRT-0 complex Inferred from physical interaction Ref.15. Source: SGD endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-3-phosphate binding Inferred from direct assay Ref.10. Source: SGD ubiquitin binding Inferred from direct assay Ref.15PubMed 20150893. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSE1	P38753	10	EBI-20380,EBI-1382
SEC28	P40509	2	EBI-20380,EBI-4884

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 622

622

Vacuolar protein sorting-associated protein 27

PRO_0000065893

Regions

Domain

18 – 149

132

VHS

Repeat

258 – 277

20

UIM 1

Repeat

301 – 320

20

UIM 2

Zinc finger

170 – 230

61

FYVE-type

Amino acid modifications

Modified residue

155

1

Phosphoserine Ref.32

Modified residue

157

1

Phosphoserine Ref.26 Ref.27 Ref.32

Modified residue

274

1

Phosphoserine Ref.32

Modified residue

279

1

Phosphoserine Ref.32

Modified residue

280

1

Phosphoserine Ref.32

Modified residue

495

1

Phosphoserine Ref.26 Ref.27 Ref.31 Ref.32

Modified residue

497

1

Phosphothreonine Ref.32

Modified residue

613

1

Phosphoserine Ref.32

Experimental info

Mutagenesis

185 – 186

2

LL → AA: Decreases the association to PtdIns(3)P containing membranes.

Mutagenesis

193

1

R → A: Decreases the association to PtdIns(3)P containing membranes. Ref.13

Mutagenesis

270

1

S → D: Reduces strongly the ubiquitin-binding activity. Ref.14

Mutagenesis

313

1

S → D: Reduces strongly the ubiquitin-binding activity. Ref.14

Sequence conflict

321 – 322

2

KL → NV in AAA96002. Ref.1

Secondary structure

1

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622

Helix Strand Turn

Details...

Turn

177 – 179

3

Turn

193 – 195

3

Helix

201 – 203

3

Beta strand

206 – 210

5

Helix

211 – 213

3

Beta strand

215 – 221

7

Helix

223 – 229

7

Beta strand

251 – 253

3

Helix

259 – 272

14

Helix

274 – 276

3

Helix

304 – 318

15

Helix

352 – 369

18

Turn

375 – 379

5

Helix

381 – 436

56

Sequences

	Sequence		Length	Mass (Da)
	P40343 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: 76C4501B0EBC9C84	FASTA	622	70,974
	10 20 30 40 50 60 MSVSTPSELD ALIEQATSES IPNGDLDLPI ALEISDVLRS RRVNPKDSMR CIKKRILNTA 70 80 90 100 110 120 DNPNTQLSSW KLTNICVKNG GTPFIKEICS REFMDTMEHV ILREDSNEEL SELVKTILYE 130 140 150 160 170 180 LYVAFKNDSQ LNYVAKVYDK LISRGIKFPE KLTLSNSPTA MFDSKTPADW IDSDACMICS 190 200 210 220 230 240 KKFSLLNRKH HCRSCGGVFC QEHSSNSIPL PDLGIYEPVR VCDSCFEDYD LKRHDDSKKS 250 260 270 280 290 300 KKHRHKRKKD RDYSTPEDEE ELIRKAIELS LKESRNSASS EPIVPVVESK NEVKRQEIEE 310 320 330 340 350 360 EEDPDLKAAI QESLREAEEA KLRSERQKAS RQMQPQQPSP QPQPIHSVDL SDEEKDSIYM 370 380 390 400 410 420 FASLVEKMKS RPLNEILEDS KLQNLAQRVF ASKARLNYAL NDKAQKYNTL IEMNGKISEI 430 440 450 460 470 480 MNIYDRLLEQ QLQSINLSQQ YTLPQVPSDP YNYLTENVQN PAESYQTPPL QQLSSHQYKP 490 500 510 520 530 540 QQDVSRQQSV KANSSPTTNI DHLKTIDVTP HAQQKPQSHV ELAPSDPPYP KEEAEDEGTQ 550 560 570 580 590 600 AVQDEESSTQ ESRERPYPVE TENGETSINK RPQGITRYDF PTVPARKFVQ PESTVPLPAS 610 620 SSEIPIKEER PPSPQEELLI EL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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].
[21]	"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].
[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 AND SER-495, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, MASS SPECTROMETRY.
[32]	"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-155; SER-157; SER-274; SER-279; SER-280; SER-495; THR-497 AND SER-613, MASS SPECTROMETRY.
[33]	"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.
[34]	"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.
[35]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U24218 Genomic DNA. Translation: AAA96002.1.
X77395 Genomic DNA. Translation: CAA54574.1.
Z71620 Genomic DNA. Translation: CAA96282.1.
BK006947 Genomic DNA. Translation: DAA10547.1.

PIR

S45129.

RefSeq

NP_014403.3. NM_001183183.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O06	X-ray	1.45	A	301-320	[»]
1Q0V	NMR	-	A	250-329	[»]
1Q0W	NMR	-	A	256-278	[»]
1VFY	X-ray	1.15	A	163-229	[»]
2KDI	NMR	-	A	258-277	[»]
2PJW	X-ray	3.01	V	348-438	[»]
3R42	X-ray	1.87	B	445-453	[»]

ProteinModelPortal

P40343.

SMR

P40343. Positions 1-231, 250-329, 348-438.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1741N.

IntAct

P40343. 5 interactions.

MINT

MINT-386565.

STRING

4932.YNR006W.

Proteomic databases

PaxDb

P40343.

PeptideAtlas

P40343.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNR006W; YNR006W; YNR006W.

GeneID

855739.

KEGG

sce:YNR006W.
sce:YNR013C.

Organism-specific databases

SGD

S000005289. VPS27.

Phylogenomic databases

eggNOG

NOG257212.

GeneTree

ENSGT00670000098022.

HOGENOM

HOG000000859.

KO

K12182.
K14430.

OMA

DACMICS.

OrthoDB

EOG40VZXZ.

Gene expression databases

Genevestigator

P40343.

GermOnline

YNR006W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.25.40.90. 1 hit.
3.30.40.10. 1 hit.

InterPro

IPR008942. ENTH_VHS.
IPR017073. Ubi-bd_Hrs_VPS27.
IPR003903. Ubiquitin-int_motif.
IPR002014. VHS.
IPR018205. VHS_subgr.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF01363. FYVE. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]

PIRSF

PIRSF036956. Hrs_Vps27. 1 hit.

SMART

SM00064. FYVE. 1 hit.
SM00726. UIM. 2 hits.
SM00288. VHS. 1 hit.
[Graphical view]

SUPFAM

SSF48464. ENTH_VHS. 1 hit.
SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS50330. UIM. 2 hits.
PS50179. VHS. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P40343.

NextBio

980133.

Entry information

Entry name

VPS27_YEAST

Accession

Primary (citable) accession number: P40343
Secondary accession number(s): D6W1I1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program