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P25604 (STP22_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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:
Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
Alternative name(s):
ESCRT-I complex subunit VPS23
Vacuolar protein sorting-associated protein 23
Gene names
Name:STP22
Synonyms:VPS23
Ordered Locus Names:YCL008C
ORF Names:YCL8C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association to the ESCRT-0 complex. Required for vacuolar targeting of temperature-sensitive plasma membrane proteins STE2 and CAN1. Ref.1 Ref.7 Ref.8

Subunit structure

Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of STP22, VPS28, SRN2 and MVB12 in a 1:1:1:1 stoechiometry. Interacts with HSE1 and VPS27. Interactis with MVB12 and SRN2. Ref.8 Ref.10 Ref.11 Ref.15

Subcellular location

Cytoplasm. Endosome. Late endosome membrane; Peripheral membrane protein Probable Ref.1 Ref.7 Ref.8 Ref.10.

Domain

The UEV domain is required for the interaction of the complex with ubiquitin.

Miscellaneous

Present with 1360 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.

Contains 1 SB (steadiness box) domain.

Contains 1 UEV (ubiquitin E2 variant) domain.

Sequence caution

The sequence CAC42964.1 differs from that shown. Reason: Frameshift at position 294.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Endosome
Membrane
   DomainCoiled coil
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein modification process

Inferred from electronic annotation. Source: InterPro

late endosome to vacuole transport

Inferred from mutant phenotype PubMed 17145965. Source: SGD

negative regulation of protein polyubiquitination

Inferred from mutant phenotype PubMed 23645667. Source: SGD

protein targeting to membrane

Inferred from mutant phenotype Ref.8. Source: UniProtKB

protein targeting to vacuole

Inferred from mutant phenotype Ref.8. Source: UniProtKB

ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

Inferred by curator Ref.11. Source: SGD

   Cellular_componentESCRT I complex

Inferred from direct assay Ref.12. Source: SGD

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 20028738. Source: SGD

endosome

Inferred from direct assay Ref.8. Source: UniProtKB

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacid-amino acid ligase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 11743162PubMed 14737190PubMed 16429126Ref.14Ref.15PubMed 19841731PubMed 21505419. Source: IntAct

ubiquitin binding

Inferred from direct assay PubMed 19380877. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 385385Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
PRO_0000082605

Regions

Domain12 – 161150UEV
Domain322 – 38564SB
Coiled coil272 – 30029 Potential
Compositional bias155 – 20147Pro-rich

Experimental info

Mutagenesis851M → T: No interaction of the ESCRT-I complex with ubiquitin. Ref.8
Mutagenesis2541M → D: Defective in ESCRT-I cargo sorting; reduces MVB12 localization to MVBs; abolishes interaction with MVB12; reduces interaction with SRN2. Ref.15
Mutagenesis2861L → D: Defective in ESCRT-I cargo sorting. Ref.15
Mutagenesis3451L → D: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVBs). Ref.14
Mutagenesis3711F → D: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVBs). Ref.14

Secondary structure

............................................... 385
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25604 [UniParc].

Last modified October 24, 2003. Version 3.
Checksum: FEDE3BE79F063BCE

FASTA38543,330
        10         20         30         40         50         60 
MSANGKISVP EAVVNWLFKV IQPIYNDGRT TFHDSLALLD NFHSLRPRTR VFTHSDGTPQ 

        70         80         90        100        110        120 
LLLSIYGTIS TGEDGSSPHS IPVIMWVPSM YPVKPPFISI NLENFDMNTI SSSLPIQEYI 

       130        140        150        160        170        180 
DSNGWIALPI LHCWDPAAMN LIMVVQELMS LLHEPPQDQA PSLPPKPNTQ LQQEQNTPPL 

       190        200        210        220        230        240 
PPKPKSPHLK PPLPPPPPPQ PASNALDLMD MDNTDISPTN HHEMLQNLQT VVNELYREDV 

       250        260        270        280        290        300 
DYVADKILTR QTVMQESIAR FHEIIAIDKN HLRAVEQAIE QTMHSLNAQI DVLTANRAKV 

       310        320        330        340        350        360 
QQFSSTSHVD DEDVNSIAVA KTDGLNQLYN LVAQDYALTD TIECLSRMLH RGTIPLDTFV 

       370        380 
KQGRELARQQ FLVRWHIQRI TSPLS 

« Hide

References

« Hide 'large scale' references
[1]"Yeast mutants affecting possible quality control of plasma membrane proteins."
Li Y., Kane T., Tipper C., Spatrick P., Jenness D.D.
Mol. Cell. Biol. 19:3588-3599(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Gromadka R.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[5]"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.
[6]"Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-329.
Strain: ATCC 204508 / S288c.
[7]"Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking."
Babst M., Odorizzi G., Estepa E.J., Emr S.D.
Traffic 1:248-258(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I."
Katzmann D.J., Babst M., Emr S.D.
Cell 106:145-155(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-85.
[9]"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].
[10]"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: SUBCELLULAR LOCATION, INTERACTION WITH VPS27.
[11]"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: IDENTIFICATION IN THE ESCRT-1 COMPLEX, INTERACTION WITH HSE1 AND VPS27.
[12]"Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins."
Teo H., Veprintsev D.B., Williams R.L.
J. Biol. Chem. 279:28689-28696(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-161.
[13]"ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes."
Teo H., Gill D.J., Sun J., Perisic O., Veprintsev D.B., Vallis Y., Emr S.D., Williams R.L.
Cell 125:99-111(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 305-385 IN COMPLEX WITH VPS28 AND SRN2.
[14]"Structural and functional organization of the ESCRT-I trafficking complex."
Kostelansky M.S., Sun J., Lee S., Kim J., Ghirlando R., Hierro A., Emr S.D., Hurley J.H.
Cell 125:113-126(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 322-385 IN COMPLEX WITH VPS28 AND SRN2, MUTAGENESIS OF LEU-345 AND PHE-371.
[15]"Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer."
Kostelansky M.S., Schluter C., Tam Y.Y., Lee S., Ghirlando R., Beach B., Conibear E., Hurley J.H.
Cell 129:485-498(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 215-385, COMPOSITION OF THE ESCRT-I COMPLEX, INTERACTION WITH MVB12 AND SRN2, MUTAGENESIS OF MET-254 AND LEU-286.
[16]"Structural insight into the ESCRT-I/-II link and its role in MVB trafficking."
Gill D.J., Teo H., Sun J., Perisic O., Veprintsev D.B., Emr S.D., Williams R.L.
EMBO J. 26:600-612(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPOSITION OF THE ESCRT-I COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004731 Genomic DNA. Translation: AAB62820.1.
X59720 Genomic DNA. Translation: CAC42964.1. Frameshift.
AY260880 Genomic DNA. Translation: AAP21748.1.
BK006937 Genomic DNA. Translation: DAA07473.1.
PIRS74288.
RefSeqNP_009919.3. NM_001178657.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UZXX-ray1.85A1-161[»]
2CAZX-ray3.60A/D305-385[»]
2F66X-ray2.80A/D322-385[»]
2F6MX-ray2.10A/C322-385[»]
2P22X-ray2.70A215-385[»]
3R3QX-ray1.45A1-160[»]
3R42X-ray1.87A1-160[»]
ProteinModelPortalP25604.
SMRP25604. Positions 8-160, 218-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30973. 150 interactions.
DIPDIP-5827N.
IntActP25604. 10 interactions.
MINTMINT-468287.

Proteomic databases

MaxQBP25604.
PaxDbP25604.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL008C; YCL008C; YCL008C.
GeneID850349.
KEGGsce:YCL008C.

Organism-specific databases

CYGDYCL008c.
SGDS000000514. STP22.

Phylogenomic databases

eggNOGNOG317261.
GeneTreeENSGT00530000064004.
HOGENOMHOG000057121.
KOK12183.
OMANDGTVKQ.
OrthoDBEOG7XSTR7.

Enzyme and pathway databases

BioCycYEAST:G3O-29278-MONOMER.

Gene expression databases

GenevestigatorP25604.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR017916. Steadiness_box.
IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR008883. UEV_N.
[Graphical view]
PfamPF05743. UEV. 1 hit.
PF09454. Vps23_core. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS51312. SB. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
PS51322. UEV. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25604.
NextBio965809.
PROP25604.

Entry information

Entry nameSTP22_YEAST
AccessionPrimary (citable) accession number: P25604
Secondary accession number(s): D6VR04 expand/collapse secondary AC list , P87010, P87279, Q86ZT3, Q8NIM6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 24, 2003
Last modified: July 9, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: 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