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P25604

- STP22_YEAST

UniProt

P25604 - STP22_YEAST

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
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (24 Oct 2003)
      Previous versions | rss
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    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. protein binding Source: IntAct
    3. 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

    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
    4. late endosome membrane Source: UniProtKB-SubCell

    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. 150 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.
    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

    MSANGKISVP EAVVNWLFKV IQPIYNDGRT TFHDSLALLD NFHSLRPRTR    50
    VFTHSDGTPQ LLLSIYGTIS TGEDGSSPHS IPVIMWVPSM YPVKPPFISI 100
    NLENFDMNTI SSSLPIQEYI DSNGWIALPI LHCWDPAAMN LIMVVQELMS 150
    LLHEPPQDQA PSLPPKPNTQ LQQEQNTPPL PPKPKSPHLK PPLPPPPPPQ 200
    PASNALDLMD MDNTDISPTN HHEMLQNLQT VVNELYREDV DYVADKILTR 250
    QTVMQESIAR FHEIIAIDKN HLRAVEQAIE QTMHSLNAQI DVLTANRAKV 300
    QQFSSTSHVD DEDVNSIAVA KTDGLNQLYN LVAQDYALTD TIECLSRMLH 350
    RGTIPLDTFV KQGRELARQQ FLVRWHIQRI TSPLS 385
    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. 150 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.
    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

    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 1, 2014
    This is version 131 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