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P39743 (RV167_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reduced viability upon starvation protein 167
Gene names
Name:RVS167
Ordered Locus Names:YDR388W
ORF Names:D9509.8
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Subunit structure

Binds to actin. Interacts with ABP1, GYL1, GYP5, PCL2 and YBR108W. Ref.4 Ref.5 Ref.6 Ref.10 Ref.11

Subcellular location

Cytoplasmcytoskeleton.

Post-translational modification

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. Ref.6 Ref.7

Miscellaneous

Present with 14600 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 BAR domain.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 482481Reduced viability upon starvation protein 167
PRO_0000192961

Regions

Domain17 – 254238BAR
Domain421 – 48262SH3
Coiled coil31 – 6434 Potential
Coiled coil174 – 20431 Potential
Compositional bias292 – 427136Ala/Gly/Pro-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue2991Phosphoserine; by FUS3 and PHO85 Ref.7
Modified residue3211Phosphoserine; by FUS3 and PHO85 Ref.7
Modified residue3791Phosphoserine; by FUS3 and PHO85 Ref.7
Cross-link481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Sequences

Sequence LengthMass (Da)Tools
P39743 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 3F0AB53EBCC95A5B

FASTA48252,774
        10         20         30         40         50         60 
MSFKGFTKAV SRAPQSFRQK FKMGEQTEDP VYEDAERRFQ ELEQETKKLS EESKRYSTAV 

        70         80         90        100        110        120 
NGMLTHQIGF AKSMEEIFKP ISGKMSDPNA TIPEDNPQGI EASEQYRAIV AELQETLKPD 

       130        140        150        160        170        180 
LALVEEKIVT PCQELLKIIT YIRKMATKRN HKKLDLDRHL NTYNKHEKKK EPTAKDEERL 

       190        200        210        220        230        240 
YKAQAQVEVA QQEYDYYNDL LKTQLPILFS LEAEFVKPLF VSFYFMQLNI FYTLYNRLQD 

       250        260        270        280        290        300 
MKIPYFDLNS DIVESYIAKK GNVEEQTDAL TITHFKLGYS KAKLEMTRRK YGVATAEGSP 

       310        320        330        340        350        360 
VSGASSGVGY GAGYDPATAT SPTPTGYGYG AAAPSYAAQP AAQYGTAAAV GTAAAVGTAA 

       370        380        390        400        410        420 
GAAAGAVPGT YPQYAAAQSP PLTGLGFQQS PQQQQGPPPA YSNPLTSPVA GTPAAAVAAA 

       430        440        450        460        470        480 
PGVETVTALY DYQAQAAGDL SFPAGAVIEI VQRTPDVNEW WTGRYNGQQG VFPGNYVQLN 


KN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M92092 Genomic DNA. Translation: AAA35051.1.
U32274 Genomic DNA. Translation: AAB64830.1.
BK006938 Genomic DNA. Translation: DAA12232.1.
PIRS40887.
RefSeqNP_010676.1. NM_001180696.1.

3D structure databases

ProteinModelPortalP39743.
SMRP39743. Positions 4-210, 394-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32449. 544 interactions.
DIPDIP-770N.
IntActP39743. 94 interactions.
MINTMINT-369996.
STRING4932.YDR388W.

Proteomic databases

PaxDbP39743.
PeptideAtlasP39743.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR388W; YDR388W; YDR388W.
GeneID851996.
KEGGsce:YDR388W.

Organism-specific databases

CYGDYDR388w.
SGDS000002796. RVS167.

Phylogenomic databases

eggNOGNOG280437.
HOGENOMHOG000199510.
OMAQEYDYYN.
OrthoDBEOG7CRV0F.

Enzyme and pathway databases

BioCycYEAST:G3O-29936-MONOMER.

Gene expression databases

GenevestigatorP39743.

Family and domain databases

Gene3D1.20.1270.60. 1 hit.
InterProIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF03114. BAR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970172.

Entry information

Entry nameRV167_YEAST
AccessionPrimary (citable) accession number: P39743
Secondary accession number(s): D6VT22
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families