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P39743

- RV167_YEAST

UniProt

P39743 - RV167_YEAST

Protein

Reduced viability upon starvation protein 167

Gene

RVS167

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 134 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level. Could be implicated in cytoskeletal reorganization in response to environmental stresses and could act in the budding site selection mechanism.1 Publication

    GO - Molecular functioni

    1. cytoskeletal protein binding Source: SGD
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct

    GO - Biological processi

    1. actin cortical patch localization Source: SGD
    2. endocytosis Source: SGD
    3. lipid tube assembly Source: SGD
    4. vesicle-mediated transport Source: SGD

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29936-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Reduced viability upon starvation protein 167
    Gene namesi
    Name:RVS167
    Ordered Locus Names:YDR388W
    ORF Names:D9509.8
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR388w.
    SGDiS000002796. RVS167.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. mating projection tip Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 482481Reduced viability upon starvation protein 167PRO_0000192961Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei299 – 2991Phosphoserine; by FUS3 and PHO852 Publications
    Modified residuei321 – 3211Phosphoserine; by FUS3 and PHO852 Publications
    Modified residuei379 – 3791Phosphoserine; by FUS3 and PHO852 Publications
    Cross-linki481 – 481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Phosphorylated redundantly by cyclin-dependent kinase PHO85 in association with PCL1,2-type cyclins or by MAP kinase FUS3. Phosphorylation inhibits interaction with complexes involved in actin cytoskeleton function.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP39743.
    PaxDbiP39743.
    PeptideAtlasiP39743.

    Expressioni

    Gene expression databases

    GenevestigatoriP39743.

    Interactioni

    Subunit structurei

    Binds to actin. Interacts with ABP1, GYL1, GYP5, PCL2 and YBR108W.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-14500,EBI-14500
    ABP1P158916EBI-14500,EBI-2036
    ACF2Q121689EBI-14500,EBI-32973
    ACF4P471295EBI-14500,EBI-25556
    AIM3P382666EBI-14500,EBI-21584
    APP1P539339EBI-14500,EBI-28798
    BSP1Q066045EBI-14500,EBI-37047
    ERT1P381404EBI-14500,EBI-21048
    GTS1P409564EBI-14500,EBI-7968
    GYL1Q043228EBI-14500,EBI-27427
    GYP5Q123444EBI-14500,EBI-38508
    LAS17Q1244612EBI-14500,EBI-10022
    MYO5Q044393EBI-14500,EBI-11687
    RVS161P2534314EBI-14500,EBI-14490
    SEC8P328552EBI-14500,EBI-16896
    VRP1P373703EBI-14500,EBI-20502
    YDR239CQ037802EBI-14500,EBI-30094
    YPR091CQ068333EBI-14500,EBI-37290

    Protein-protein interaction databases

    BioGridi32449. 545 interactions.
    DIPiDIP-770N.
    IntActiP39743. 94 interactions.
    MINTiMINT-369996.
    STRINGi4932.YDR388W.

    Structurei

    3D structure databases

    ProteinModelPortaliP39743.
    SMRiP39743. Positions 4-210, 394-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 254238BARPROSITE-ProRule annotationAdd
    BLAST
    Domaini421 – 48262SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili31 – 6434Sequence AnalysisAdd
    BLAST
    Coiled coili174 – 20431Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi292 – 427136Ala/Gly/Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BAR domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG280437.
    HOGENOMiHOG000199510.
    OMAiQEYDYYN.
    OrthoDBiEOG7CRV0F.

    Family and domain databases

    Gene3Di1.20.1270.60. 1 hit.
    InterProiIPR027267. AH/BAR-dom.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF03114. BAR. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P39743-1 [UniParc]FASTAAdd to Basket

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    MSFKGFTKAV SRAPQSFRQK FKMGEQTEDP VYEDAERRFQ ELEQETKKLS    50
    EESKRYSTAV NGMLTHQIGF AKSMEEIFKP ISGKMSDPNA TIPEDNPQGI 100
    EASEQYRAIV AELQETLKPD LALVEEKIVT PCQELLKIIT YIRKMATKRN 150
    HKKLDLDRHL NTYNKHEKKK EPTAKDEERL YKAQAQVEVA QQEYDYYNDL 200
    LKTQLPILFS LEAEFVKPLF VSFYFMQLNI FYTLYNRLQD MKIPYFDLNS 250
    DIVESYIAKK GNVEEQTDAL TITHFKLGYS KAKLEMTRRK YGVATAEGSP 300
    VSGASSGVGY GAGYDPATAT SPTPTGYGYG AAAPSYAAQP AAQYGTAAAV 350
    GTAAAVGTAA GAAAGAVPGT YPQYAAAQSP PLTGLGFQQS PQQQQGPPPA 400
    YSNPLTSPVA GTPAAAVAAA PGVETVTALY DYQAQAAGDL SFPAGAVIEI 450
    VQRTPDVNEW WTGRYNGQQG VFPGNYVQLN KN 482
    Length:482
    Mass (Da):52,774
    Last modified:February 1, 1995 - v1
    Checksum:i3F0AB53EBCC95A5B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M92092 Genomic DNA. Translation: AAA35051.1.
    U32274 Genomic DNA. Translation: AAB64830.1.
    BK006938 Genomic DNA. Translation: DAA12232.1.
    PIRiS40887.
    RefSeqiNP_010676.1. NM_001180696.1.

    Genome annotation databases

    EnsemblFungiiYDR388W; YDR388W; YDR388W.
    GeneIDi851996.
    KEGGisce:YDR388W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M92092 Genomic DNA. Translation: AAA35051.1 .
    U32274 Genomic DNA. Translation: AAB64830.1 .
    BK006938 Genomic DNA. Translation: DAA12232.1 .
    PIRi S40887.
    RefSeqi NP_010676.1. NM_001180696.1.

    3D structure databases

    ProteinModelPortali P39743.
    SMRi P39743. Positions 4-210, 394-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32449. 545 interactions.
    DIPi DIP-770N.
    IntActi P39743. 94 interactions.
    MINTi MINT-369996.
    STRINGi 4932.YDR388W.

    Proteomic databases

    MaxQBi P39743.
    PaxDbi P39743.
    PeptideAtlasi P39743.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR388W ; YDR388W ; YDR388W .
    GeneIDi 851996.
    KEGGi sce:YDR388W.

    Organism-specific databases

    CYGDi YDR388w.
    SGDi S000002796. RVS167.

    Phylogenomic databases

    eggNOGi NOG280437.
    HOGENOMi HOG000199510.
    OMAi QEYDYYN.
    OrthoDBi EOG7CRV0F.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29936-MONOMER.

    Miscellaneous databases

    NextBioi 970172.

    Gene expression databases

    Genevestigatori P39743.

    Family and domain databases

    Gene3Di 1.20.1270.60. 1 hit.
    InterProi IPR027267. AH/BAR-dom.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF03114. BAR. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns."
      Bauer F., Urdaci M., Aigle M., Crouzet M.
      Mol. Cell. Biol. 13:5070-5084(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 26109 / X2180.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Defining protein interactions with yeast actin in vivo."
      Amberg D.C., Basart E., Botstein D.
      Nat. Struct. Biol. 2:28-35(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACTIN.
    5. "In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions."
      Colwill K., Field D., Moore L., Friesen J., Andrews B.
      Genetics 152:881-893(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ABP1.
    6. "Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton."
      Lee J., Colwill K., Aneliunas V., Tennyson C.N., Moore L., Ho Y., Andrews B.J.
      Curr. Biol. 8:1310-1321(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH PCL2.
    7. "Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation."
      Friesen H., Murphy K., Breitkreutz A., Tyers M., Andrews B.J.
      Mol. Biol. Cell 14:3027-3040(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-299; SER-321 AND SER-379.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-481.
      Strain: SUB592.
    10. "Interaction of the Saccharomyces cerevisiae cortical actin patch protein Rvs167p with proteins involved in ER to Golgi vesicle trafficking."
      Friesen H., Colwill K., Robertson K., Schub O., Andrews B.
      Genetics 170:555-568(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GYL1 AND GYP5.
    11. "Characterizing the sphingolipid signaling pathway that remediates defects associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and Rvs167p."
      Germann M., Swain E., Bergman L., Nickels J.T. Jr.
      J. Biol. Chem. 280:4270-4278(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YBR108W.
    12. "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].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRV167_YEAST
    AccessioniPrimary (citable) accession number: P39743
    Secondary accession number(s): D6VT22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 134 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 14600 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3