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Q03337

- TRS31_YEAST

UniProt

Q03337 - TRS31_YEAST

Protein

Trafficking protein particle complex subunit 31

Gene

TRS31

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 98 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation.4 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. ER to Golgi vesicle-mediated transport Source: SGD
    3. positive regulation of Rab GTPase activity Source: GOC

    Keywords - Biological processi

    Autophagy, ER-Golgi transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29999-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trafficking protein particle complex subunit 31
    Short name:
    TRAPP subunit 31
    Alternative name(s):
    Transport protein particle 31 kDa subunit
    Gene namesi
    Name:TRS31
    Ordered Locus Names:YDR472W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR472w.
    SGDiS000002880. TRS31.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. pre-autophagosomal structure Source: UniProtKB-SubCell
    3. TRAPPIII protein complex Source: SGD
    4. TRAPPII protein complex Source: SGD
    5. TRAPPI protein complex Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283Trafficking protein particle complex subunit 31PRO_0000211585Add
    BLAST

    Proteomic databases

    MaxQBiQ03337.
    PaxDbiQ03337.

    Expressioni

    Gene expression databases

    GenevestigatoriQ03337.

    Interactioni

    Subunit structurei

    Part of the multisubunit TRAPP (transport protein particle) I complex composed of BET3, BET5, TRS20, TRS23, TRS31 and TRS33. Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS85, TRS120 and TRS130. Part of the multisubunit TRAPP (transport protein particle) III complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33 and TRS85.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BET3P3614913EBI-38770,EBI-3567
    TRS20P383345EBI-38770,EBI-19468

    Protein-protein interaction databases

    BioGridi32525. 57 interactions.
    DIPiDIP-1709N.
    IntActiQ03337. 10 interactions.
    MINTiMINT-401389.
    STRINGi4932.YDR472W.

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 583
    Helixi59 – 7618
    Helixi83 – 897
    Helixi97 – 1015
    Beta strandi170 – 1723
    Helixi176 – 1838
    Helixi187 – 1904
    Beta strandi197 – 2015
    Beta strandi209 – 2157
    Beta strandi217 – 2193
    Helixi228 – 2314
    Turni241 – 2433
    Beta strandi251 – 2533
    Beta strandi264 – 2674
    Helixi272 – 2776

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CUEX-ray3.70B/H/N/T1-283[»]
    ProteinModelPortaliQ03337.
    SMRiQ03337. Positions 54-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03337.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5128.
    GeneTreeiENSGT00390000000976.
    HOGENOMiHOG000176758.
    OMAiSANERLQ.
    OrthoDBiEOG7XSTS0.

    Family and domain databases

    InterProiIPR024096. NO_sig/Golgi_transp_ligand-bd.
    IPR016696. TRAPP-I_su5.
    IPR007194. TRAPP_component.
    [Graphical view]
    PANTHERiPTHR20902. PTHR20902. 1 hit.
    PfamiPF04051. TRAPP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017479. TRAPP_I_complex_Trs31. 1 hit.
    SUPFAMiSSF111126. SSF111126. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q03337-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQRIIQPSA SDQQFPGKSD GYEYTVGPKQ AITSEASTTY IPSRIYSESL    50
    LFKRQEASLS AMAFLFQEMI SQLHRTCKTA GDFETKLSDY GHNIGIRLLE 100
    LLNFRASVSP SSLPRASAFL SQNESSSKLS NASNSPGMLA NSSTATSASA 150
    NERLQEKQTE SLSNYITKMR RRDLKILDIL QFIHGTLWSY LFNHVSDDLV 200
    KSSERDNEYM IVDNFPTLTQ FIPGENVSCE YFVCGIIKGF LFNAGFPCGV 250
    TAHRMPQGGH SQRTVYLIQF DRQVLDREGL RFG 283
    Length:283
    Mass (Da):31,722
    Last modified:November 1, 1996 - v1
    Checksum:i857BBA3E03423D42
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33050 Genomic DNA. Translation: AAB64914.1.
    BK006938 Genomic DNA. Translation: DAA12306.1.
    PIRiS69639.
    RefSeqiNP_010760.3. NM_001180780.3.

    Genome annotation databases

    EnsemblFungiiYDR472W; YDR472W; YDR472W.
    GeneIDi852083.
    KEGGisce:YDR472W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33050 Genomic DNA. Translation: AAB64914.1 .
    BK006938 Genomic DNA. Translation: DAA12306.1 .
    PIRi S69639.
    RefSeqi NP_010760.3. NM_001180780.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CUE X-ray 3.70 B/H/N/T 1-283 [» ]
    ProteinModelPortali Q03337.
    SMRi Q03337. Positions 54-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32525. 57 interactions.
    DIPi DIP-1709N.
    IntActi Q03337. 10 interactions.
    MINTi MINT-401389.
    STRINGi 4932.YDR472W.

    Proteomic databases

    MaxQBi Q03337.
    PaxDbi Q03337.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR472W ; YDR472W ; YDR472W .
    GeneIDi 852083.
    KEGGi sce:YDR472W.

    Organism-specific databases

    CYGDi YDR472w.
    SGDi S000002880. TRS31.

    Phylogenomic databases

    eggNOGi COG5128.
    GeneTreei ENSGT00390000000976.
    HOGENOMi HOG000176758.
    OMAi SANERLQ.
    OrthoDBi EOG7XSTS0.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29999-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q03337.
    NextBioi 970397.
    PROi Q03337.

    Gene expression databases

    Genevestigatori Q03337.

    Family and domain databases

    InterProi IPR024096. NO_sig/Golgi_transp_ligand-bd.
    IPR016696. TRAPP-I_su5.
    IPR007194. TRAPP_component.
    [Graphical view ]
    PANTHERi PTHR20902. PTHR20902. 1 hit.
    Pfami PF04051. TRAPP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017479. TRAPP_I_complex_Trs31. 1 hit.
    SUPFAMi SSF111126. SSF111126. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion."
      Sacher M., Jiang Y., Barrowman J., Scarpa A., Burston J., Zhang L., Schieltz D., Yates J.R. III, Abeliovich H., Ferro-Novick S.
      EMBO J. 17:2494-2503(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE TRAPP II COMPLEX.
    4. "TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport."
      Sacher M., Barrowman J., Wang W., Horecka J., Zhang Y., Pypaert M., Ferro-Novick S.
      Mol. Cell 7:433-442(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE TRAPP II COMPLEX, IDENTIFICATION IN THE TRAPP II COMPLEX, FUNCTION OF THE TRAPP I COMPLEX, IDENTIFICATION IN THE TRAPP I COMPLEX, SUBCELLULAR LOCATION.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Molecular architecture of the TRAPPII complex and implications for vesicle tethering."
      Yip C.K., Berscheminski J., Walz T.
      Nat. Struct. Mol. Biol. 17:1298-1304(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TRAP II COMPLEX, FUNCTION OF THE TRAP II COMPLEX.
    8. Cited for: IDENTIFICATION IN THE TRAPP III COMPLEX, SUBCELLULAR LOCATION, FUNCTION OF THE TRAPP III COMPLEX.

    Entry informationi

    Entry nameiTRS31_YEAST
    AccessioniPrimary (citable) accession number: Q03337
    Secondary accession number(s): D6VT96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8350 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3