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P25604

- STP22_YEAST

UniProt

P25604 - STP22_YEAST

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Protein

Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease

Gene

STP22

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

Functioni

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 CAN1.3 Publications

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ubiquitin binding Source: SGD

GO - Biological processi

  1. cellular protein modification process Source: InterPro
  2. late endosome to vacuole transport Source: SGD
  3. negative regulation of protein polyubiquitination Source: SGD
  4. protein targeting to membrane Source: UniProtKB
  5. protein targeting to vacuole Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29278-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:STP22
Synonyms:VPS23
Ordered Locus Names:YCL008C
ORF Names:YCL8C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCL008c.
SGDiS000000514. STP22.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic side of plasma membrane Source: SGD
  2. endosome Source: UniProtKB
  3. ESCRT I complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851M → T: No interaction of the ESCRT-I complex with ubiquitin. 1 Publication
Mutagenesisi254 – 2541M → D: Defective in ESCRT-I cargo sorting; reduces MVB12 localization to MVBs; abolishes interaction with MVB12; reduces interaction with SRN2. 1 Publication
Mutagenesisi286 – 2861L → D: Defective in ESCRT-I cargo sorting. 1 Publication
Mutagenesisi345 – 3451L → D: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVBs). 1 Publication
Mutagenesisi371 – 3711F → D: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVBs). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permeasePRO_0000082605Add
BLAST

Proteomic databases

MaxQBiP25604.
PaxDbiP25604.

Expressioni

Gene expression databases

GenevestigatoriP25604.

Interactioni

Subunit structurei

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 SRN2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HOF1Q050802EBI-411625,EBI-5412
HSE1P387533EBI-411625,EBI-1382
LSB3P436033EBI-411625,EBI-22980
MVB12P429396EBI-411625,EBI-23478
PEX13P806672EBI-411625,EBI-13206
SRN2Q991765EBI-411625,EBI-18076
VPS27P403437EBI-411625,EBI-20380
VPS28Q027672EBI-411625,EBI-20387
YSC84P327932EBI-411625,EBI-24460

Protein-protein interaction databases

BioGridi30973. 154 interactions.
DIPiDIP-5827N.
IntActiP25604. 10 interactions.
MINTiMINT-468287.

Structurei

Secondary structure

1
385
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2111
Turni22 – 243
Helixi28 – 4114
Beta strandi45 – 539
Beta strandi59 – 7012
Beta strandi73 – 764
Beta strandi80 – 867
Turni89 – 935
Beta strandi97 – 1004
Helixi102 – 1043
Turni107 – 1093
Helixi116 – 1194
Beta strandi124 – 1263
Helixi129 – 1324
Helixi136 – 1383
Helixi141 – 15010
Helixi219 – 24628
Helixi248 – 2514
Helixi254 – 28936
Helixi291 – 30313
Helixi314 – 3163
Helixi323 – 35129
Helixi356 – 38126
Turni382 – 3843

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP25604.
SMRiP25604. Positions 8-160, 218-385.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25604.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 161150UEVPROSITE-ProRule annotationAdd
BLAST
Domaini322 – 38564SBPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili272 – 30029Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi155 – 20147Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.PROSITE-ProRule annotation
Contains 1 SB (steadiness box) domain.PROSITE-ProRule annotation
Contains 1 UEV (ubiquitin E2 variant) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG317261.
GeneTreeiENSGT00530000064004.
HOGENOMiHOG000057121.
InParanoidiP25604.
KOiK12183.
OMAiNDGTVKQ.
OrthoDBiEOG7XSTR7.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR017916. Steadiness_box.
IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR008883. UEV_N.
[Graphical view]
PfamiPF05743. UEV. 1 hit.
PF09454. Vps23_core. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS51312. SB. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
PS51322. UEV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25604-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSANGKISVP EAVVNWLFKV IQPIYNDGRT TFHDSLALLD NFHSLRPRTR
60 70 80 90 100
VFTHSDGTPQ LLLSIYGTIS TGEDGSSPHS IPVIMWVPSM YPVKPPFISI
110 120 130 140 150
NLENFDMNTI SSSLPIQEYI DSNGWIALPI LHCWDPAAMN LIMVVQELMS
160 170 180 190 200
LLHEPPQDQA PSLPPKPNTQ LQQEQNTPPL PPKPKSPHLK PPLPPPPPPQ
210 220 230 240 250
PASNALDLMD MDNTDISPTN HHEMLQNLQT VVNELYREDV DYVADKILTR
260 270 280 290 300
QTVMQESIAR FHEIIAIDKN HLRAVEQAIE QTMHSLNAQI DVLTANRAKV
310 320 330 340 350
QQFSSTSHVD DEDVNSIAVA KTDGLNQLYN LVAQDYALTD TIECLSRMLH
360 370 380
RGTIPLDTFV KQGRELARQQ FLVRWHIQRI TSPLS
Length:385
Mass (Da):43,330
Last modified:October 24, 2003 - v3
Checksum:iFEDE3BE79F063BCE
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS74288.
RefSeqiNP_009919.3. NM_001178657.1.

Genome annotation databases

EnsemblFungiiYCL008C; YCL008C; YCL008C.
GeneIDi850349.
KEGGisce:YCL008C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S74288.
RefSeqi NP_009919.3. NM_001178657.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UZX X-ray 1.85 A 1-161 [» ]
2CAZ X-ray 3.60 A/D 305-385 [» ]
2F66 X-ray 2.80 A/D 322-385 [» ]
2F6M X-ray 2.10 A/C 322-385 [» ]
2P22 X-ray 2.70 A 215-385 [» ]
3R3Q X-ray 1.45 A 1-160 [» ]
3R42 X-ray 1.87 A 1-160 [» ]
ProteinModelPortali P25604.
SMRi P25604. Positions 8-160, 218-385.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 30973. 154 interactions.
DIPi DIP-5827N.
IntActi P25604. 10 interactions.
MINTi MINT-468287.

Proteomic databases

MaxQBi P25604.
PaxDbi P25604.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCL008C ; YCL008C ; YCL008C .
GeneIDi 850349.
KEGGi sce:YCL008C.

Organism-specific databases

CYGDi YCL008c.
SGDi S000000514. STP22.

Phylogenomic databases

eggNOGi NOG317261.
GeneTreei ENSGT00530000064004.
HOGENOMi HOG000057121.
InParanoidi P25604.
KOi K12183.
OMAi NDGTVKQ.
OrthoDBi EOG7XSTR7.

Enzyme and pathway databases

BioCyci YEAST:G3O-29278-MONOMER.

Miscellaneous databases

EvolutionaryTracei P25604.
NextBioi 965809.
PROi P25604.

Gene expression databases

Genevestigatori P25604.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR017916. Steadiness_box.
IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR008883. UEV_N.
[Graphical view ]
Pfami PF05743. UEV. 1 hit.
PF09454. Vps23_core. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS51312. SB. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
PS51322. UEV. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiSTP22_YEAST
AccessioniPrimary (citable) accession number: P25604
Secondary accession number(s): D6VR04
, P87010, P87279, Q86ZT3, Q8NIM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 24, 2003
Last modified: October 29, 2014
This is version 132 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 1360 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3