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P39743

- RV167_YEAST

UniProt

P39743 - RV167_YEAST

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Protein

Reduced viability upon starvation protein 167

Gene
RVS167, YDR388W, D9509.8
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 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
Complete GO annotation...

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
Complete GO annotation...

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 PHO851 Publication
Modified residuei321 – 3211Phosphoserine; by FUS3 and PHO851 Publication
Modified residuei379 – 3791Phosphoserine; by FUS3 and PHO851 Publication
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. 544 interactions.
DIPiDIP-770N.
IntActiP39743. 94 interactions.
MINTiMINT-369996.
STRINGi4932.YDR388W.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 254238BARAdd
BLAST
Domaini421 – 48262SH3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili31 – 6434 Reviewed predictionAdd
BLAST
Coiled coili174 – 20431 Reviewed predictionAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 BAR domain.
Contains 1 SH3 domain.

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

« Hide

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. 544 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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 133 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.

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

Similar proteinsi