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P38753 (HSE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Class E vacuolar protein-sorting machinery protein HSE1
Gene names
Name:HSE1
Ordered Locus Names:YHL002W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.3 Ref.4 Ref.7 Ref.9

Subunit structure

Component of the ESCRT-0 complex composed of HSE1 and VPS27. Interacts with the ESCRT-I subunit VPS23, the UBP7 deubiquitinase and the E3 ligase RSP5. Ref.3 Ref.7 Ref.9

Subcellular location

Endosome membrane; Peripheral membrane protein; Cytoplasmic side Ref.3 Ref.5.

Miscellaneous

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

Sequence similarities

Belongs to the STAM family.

Contains 1 SH3 domain.

Contains 1 UIM (ubiquitin-interacting motif) repeat.

Contains 1 VHS domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 452451Class E vacuolar protein-sorting machinery protein HSE1
PRO_0000202885

Regions

Domain15 – 145131VHS
Repeat162 – 18120UIM
Domain217 – 27660SH3

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue1621Phosphoserine Ref.8 Ref.10 Ref.11

Secondary structure

............ 452
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38753 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 026267836BBADF69

FASTA45251,161
        10         20         30         40         50         60 
MSSSAIKIRN ALLKATDPKL RSDNWQYILD VCDLVKEDPE DNGQEVMSLI EKRLEQQDAN 

        70         80         90        100        110        120 
VILRTLSLTV SLAENCGSRL RQEISSKNFT SLLYALIESH SVHITLKKAV TDVVKQLSDS 

       130        140        150        160        170        180 
FKDDPSLRAM GDLYDKIKRK APYLVQPNVP EKHNMSTQAD NSDDEELQKA LKMSLFEYEK 

       190        200        210        220        230        240 
QKKLQEQEKE SAEVLPQQQQ QHQQQNQAPA HKIPAQTVVR RVRALYDLTT NEPDELSFRK 

       250        260        270        280        290        300 
GDVITVLEQV YRDWWKGALR GNMGIFPLNY VTPIVEPSKE EIEKEKNKEA IVFSQKTTID 

       310        320        330        340        350        360 
QLHNSLNAAS KTGNSNEVLQ DPHIGDMYGS VTPLRPQVTR MLGKYAKEKE DMLSLRQVLA 

       370        380        390        400        410        420 
NAERSYNQLM DRAANAHISP PVPGPALYAG MTHANNTPVM PPQRQSYQSN EYSPYPSNLP 

       430        440        450 
IQHPTNSANN TPQYGYDLGY SVVSQPPPGY EQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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, SUBCELLULAR LOCATION.
[4]"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.
[5]"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].
[6]"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].
[7]"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 RSP5; VPS23 AND VPS27, FUNCTION OF THE ESCRT-0 COMPLEX.
[8]"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-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies."
Ren J., Kee Y., Huibregtse J.M., Piper R.C.
Mol. Biol. Cell 18:324-335(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RSP5 AND UBP7.
[10]"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-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10555 Genomic DNA. Translation: AAB68427.1.
BK006934 Genomic DNA. Translation: DAA06685.1.
PIRS46798.
RefSeqNP_011861.1. NM_001179082.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PJWX-ray3.01H288-375[»]
DisProtDP00635.
ProteinModelPortalP38753.
SMRP38753. Positions 1-149, 224-271, 288-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36423. 97 interactions.
DIPDIP-1742N.
IntActP38753. 44 interactions.
MINTMINT-386551.
STRING4932.YHL002W.

Proteomic databases

PaxDbP38753.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHL002W; YHL002W; YHL002W.
GeneID856387.
KEGGsce:YHL002W.

Organism-specific databases

CYGDYHL002w.
SGDS000000994. HSE1.

Phylogenomic databases

eggNOGNOG309509.
GeneTreeENSGT00700000104139.
HOGENOMHOG000094361.
KOK04705.
OMATNAMVGS.
OrthoDBEOG75MW70.

Enzyme and pathway databases

BioCycYEAST:G3O-31026-MONOMER.

Gene expression databases

GenevestigatorP38753.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
InterProIPR008942. ENTH_VHS.
IPR001452. SH3_domain.
IPR027423. Sorting_HSE1.
IPR003903. Ubiquitin-int_motif.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view]
PANTHERPTHR13856:SF44. PTHR13856:SF44. 1 hit.
PfamPF00018. SH3_1. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
SM00726. UIM. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
PS50330. UIM. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38753.
NextBio981893.

Entry information

Entry nameHSE1_YEAST
AccessionPrimary (citable) accession number: P38753
Secondary accession number(s): D3DKR2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references