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Protein

Reduced viability upon starvation protein 167

Gene

RVS167

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

  • cytoskeletal protein binding Source: SGD
  • identical protein binding Source: IntAct

GO - Biological processi

  • actin cortical patch localization Source: SGD
  • endocytosis Source: SGD
  • lipid tube assembly Source: SGD
  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR388W.
SGDiS000002796. RVS167.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • mating projection tip Source: SGD
  • Rvs161p-Rvs167p complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 482481Reduced viability upon starvation protein 167PRO_0000192961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
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.
PeptideAtlasiP39743.

PTM databases

iPTMnetiP39743.

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
ACF2Q1216810EBI-14500,EBI-32973
ACF4P471295EBI-14500,EBI-25556
AIM3P382668EBI-14500,EBI-21584
ALY2P470293EBI-14500,EBI-25974
APP1P539339EBI-14500,EBI-28798
ASR1Q068346EBI-14500,EBI-33224
BRE2P431324EBI-14500,EBI-27115
BSP1Q066045EBI-14500,EBI-37047
CRN1Q064402EBI-14500,EBI-4950
CTF3Q127483EBI-14500,EBI-30457
ERT1P381404EBI-14500,EBI-21048
ESF1Q063442EBI-14500,EBI-34121
GTS1P409564EBI-14500,EBI-7968
GYL1Q0432218EBI-14500,EBI-27427
GYP5Q1234411EBI-14500,EBI-38508
HCA4P204486EBI-14500,EBI-5612
HIF1Q123733EBI-14500,EBI-31911
KIN2P131862EBI-14500,EBI-9723
KTI11Q3E8402EBI-14500,EBI-2055307
LAS17Q1244620EBI-14500,EBI-10022
LSB3P436033EBI-14500,EBI-22980
MLC1P531412EBI-14500,EBI-10988
MYO5Q044393EBI-14500,EBI-11687
PMT1P337753EBI-14500,EBI-13567
POL32P471102EBI-14500,EBI-6084
PRP28P233942EBI-14500,EBI-13858
RAD1P067773EBI-14500,EBI-14752
RAD23P326286EBI-14500,EBI-14668
RAD33Q042312EBI-14500,EBI-27726
RAD34Q066653EBI-14500,EBI-35404
RSP5P399404EBI-14500,EBI-16219
RTG2P326082EBI-14500,EBI-16322
RUP1Q122422EBI-14500,EBI-38794
RVS161P2534335EBI-14500,EBI-14490
SAW1P397356EBI-14500,EBI-20627
SEC8P328552EBI-14500,EBI-16896
SGT1Q084462EBI-14500,EBI-17070
SGV1P232932EBI-14500,EBI-17078
SHP1P342238EBI-14500,EBI-17093
SLA1P327903EBI-14500,EBI-17313
SWD2P361042EBI-14500,EBI-26608
SYF1Q040482EBI-14500,EBI-540
TPA1P400323EBI-14500,EBI-22536
UBP14P382372EBI-14500,EBI-19893
UBP6P435932EBI-14500,EBI-19852
VRP1P373703EBI-14500,EBI-20502
YBP2P531693EBI-14500,EBI-23796
YCR043CP253612EBI-14500,EBI-21909
YDR239CQ037802EBI-14500,EBI-30094
YOL098CQ124962EBI-14500,EBI-29300
YPR091CQ068333EBI-14500,EBI-37290

GO - Molecular functioni

  • cytoskeletal protein binding Source: SGD
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32449. 553 interactions.
DIPiDIP-770N.
IntActiP39743. 194 interactions.
MINTiMINT-369996.

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

HOGENOMiHOG000199510.
InParanoidiP39743.
KOiK12562.
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

        10         20         30         40         50
MSFKGFTKAV SRAPQSFRQK FKMGEQTEDP VYEDAERRFQ ELEQETKKLS
60 70 80 90 100
EESKRYSTAV NGMLTHQIGF AKSMEEIFKP ISGKMSDPNA TIPEDNPQGI
110 120 130 140 150
EASEQYRAIV AELQETLKPD LALVEEKIVT PCQELLKIIT YIRKMATKRN
160 170 180 190 200
HKKLDLDRHL NTYNKHEKKK EPTAKDEERL YKAQAQVEVA QQEYDYYNDL
210 220 230 240 250
LKTQLPILFS LEAEFVKPLF VSFYFMQLNI FYTLYNRLQD MKIPYFDLNS
260 270 280 290 300
DIVESYIAKK GNVEEQTDAL TITHFKLGYS KAKLEMTRRK YGVATAEGSP
310 320 330 340 350
VSGASSGVGY GAGYDPATAT SPTPTGYGYG AAAPSYAAQP AAQYGTAAAV
360 370 380 390 400
GTAAAVGTAA GAAAGAVPGT YPQYAAAQSP PLTGLGFQQS PQQQQGPPPA
410 420 430 440 450
YSNPLTSPVA GTPAAAVAAA PGVETVTALY DYQAQAAGDL SFPAGAVIEI
460 470 480
VQRTPDVNEW WTGRYNGQQG VFPGNYVQLN KN
Length:482
Mass (Da):52,774
Last modified:February 1, 1995 - v1
Checksum:i3F0AB53EBCC95A5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi32449. 553 interactions.
DIPiDIP-770N.
IntActiP39743. 194 interactions.
MINTiMINT-369996.

PTM databases

iPTMnetiP39743.

Proteomic databases

MaxQBiP39743.
PeptideAtlasiP39743.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YDR388W.
SGDiS000002796. RVS167.

Phylogenomic databases

HOGENOMiHOG000199510.
InParanoidiP39743.
KOiK12562.
OMAiQEYDYYN.
OrthoDBiEOG7CRV0F.

Enzyme and pathway databases

BioCyciYEAST:G3O-29936-MONOMER.

Miscellaneous databases

NextBioi970172.
PROiP39743.

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]
ProtoNetiSearch...

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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [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: April 13, 2016
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.