Class E vacuolar protein-sorting machinery protein HSE1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38753 (HSE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Class E vacuolar protein-sorting machinery protein HSE1

Gene names

Name:	HSE1
Ordered Locus Names:	YHL002W

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	452 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. 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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endosome Membrane
Domain	SH3 domain
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.3. Source: SGD protein targeting to vacuole Inferred from mutant phenotype Ref.3. Source: SGD
Cellular_component	ESCRT-0 complex Inferred from physical interaction Ref.3. Source: SGD endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ubiquitin binding Inferred from direct assay Ref.3 PubMed 20150893. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VPS27	P40343	10	EBI-1382,EBI-20380

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 452

452

Class E vacuolar protein-sorting machinery protein HSE1

PRO_0000202885

Regions

Domain

15 – 145

131

VHS

Repeat

162 – 181

UIM

Domain

217 – 276

SH3

Amino acid modifications

Modified residue

162

Phosphoserine Ref.8 Ref.10 Ref.11

Modified residue

365

Phosphoserine Ref.11

Secondary structure

452

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P38753 [UniParc].

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

452

51,161

        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' referencesShow '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. Vaudin M. Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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, MASS SPECTROMETRY. 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]	"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-162, MASS SPECTROMETRY.
[11]	"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 AND SER-365, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U10555 Genomic DNA. Translation: AAB68427.1.
BK006934 Genomic DNA. Translation: DAA06685.1.

PIR

S46798.

RefSeq

NP_011861.1. NM_001179082.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PJW	X-ray	3.01	H	288-375	[»]

ProteinModelPortal

P38753.

SMR

P38753. Positions 14-127, 224-271, 288-375.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1742N.

IntAct

P38753. 15 interactions.

MINT

MINT-386551.

STRING

4932.YHL002W.

Proteomic databases

PaxDb

P38753.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YHL002W; YHL002W; YHL002W.

GeneID

856387.

KEGG

sce:YHL002W.

Organism-specific databases

CYGD

YHL002w.

SGD

S000000994. HSE1.

Phylogenomic databases

eggNOG

NOG309509.

GeneTree

ENSGT00700000104139.

HOGENOM

HOG000094361.

K04705.

OMA

ENCGSRL.

OrthoDB

EOG4KM2BT.

Enzyme and pathway databases

BioCyc

YEAST:G3O-31026-MONOMER.

Gene expression databases

Genevestigator

P38753.

GermOnline

YHL002W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.25.40.90. 1 hit.

InterPro

IPR008942. ENTH_VHS.
IPR000108. p67phox.
IPR001452. SH3_domain.
IPR027423. Sorting_HSE1.
IPR003903. Ubiquitin-int_motif.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view]

PANTHER

PTHR13856:SF44. PTHR13856:SF44. 1 hit.

Pfam

PF00018. SH3_1. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 1 hit.
SM00726. UIM. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]

SUPFAM

SSF48464. ENTH_VHS. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50002. SH3. 1 hit.
PS50330. UIM. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P38753.

NextBio

981893.

Entry information

Entry name

HSE1_YEAST

Accession

Primary (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:	May 29, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VIII

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents