Skip Header

Contribute Send feedback
Read comments (?) or add your own

P37370 (VRP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. 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
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:
Verprolin
Gene names
Name:VRP1
Synonyms:END5, MDP2
Ordered Locus Names:YLR337C
ORF Names:L8300.13
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length817 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in cytoskeletal organization and cellular growth. May exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins (e.g. profilin) or proteins possessing SH3 domains.

Subcellular location

Cytoplasm › cytoskeleton Probable Ref.4.

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the verprolin family.

Contains 2 WH2 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 817817Verprolin
PRO_0000065929

Regions

Domain30 – 4718WH2 1
Domain87 – 10620WH2 2
Compositional bias5 – 1410Poly-Pro
Compositional bias239 – 2457Poly-Pro
Compositional bias349 – 3579Poly-Pro
Compositional bias396 – 40611Poly-Pro
Compositional bias424 – 4318Poly-Pro
Compositional bias462 – 4687Poly-Ser
Compositional bias704 – 7085Poly-Pro

Amino acid modifications

Modified residue2571Phosphothreonine Ref.5
Modified residue4661Phosphoserine Ref.5
Modified residue4671Phosphoserine Ref.5
Modified residue5191Phosphoserine Ref.6
Modified residue5221Phosphoserine Ref.6
Modified residue5241Phosphoserine Ref.6
Modified residue6951Phosphoserine Ref.6
Modified residue7031Phosphoserine Ref.6
Modified residue7121Phosphothreonine Ref.6
Modified residue7201Phosphoserine Ref.6
Modified residue7361Phosphothreonine Ref.5 Ref.6
Modified residue7601Phosphoserine Ref.6
Modified residue7621Phosphoserine Ref.6
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3831N-linked (GlcNAc...) Potential
Glycosylation7841N-linked (GlcNAc...) Potential
Glycosylation7961N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3081P → R in CAA81388. Ref.1
Sequence conflict3501A → R in CAA81388. Ref.1
Sequence conflict6891V → E in CAA81388. Ref.1
Sequence conflict710 – 817108PSTMD…LTLFT → HLRWIPVPLIAPVKTLNNGY FLQVDRRCNTSIIRIQINQM LM Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37370 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 24C7522D5B1CA1C8

FASTA81782,594
        10         20         30         40         50         60 
MAGAPAPPPP PPPPALGGSA PKPAKSVMQG RDALLGDIRK GMKLKKAETN DRSAPIVGGG 

        70         80         90        100        110        120 
VVSSASGSSG TVSSKGPSMS APPIPGMGAP QLGDILAGGI PKLKHINNNA STKPSPSASA 

       130        140        150        160        170        180 
PPIPGAVPSV AAPPIPNAPL SPAPAVPSIP SSSAPPIPDI PSSAAPPIPI VPSSPAPPLP 

       190        200        210        220        230        240 
LSGASAPKVP QNRPHMPSVR PAHRSHQRKS SNISLPSVSA PPLPSASLPT HVSNPPQAPP 

       250        260        270        280        290        300 
PPPTPTIGLD SKNIKPTDNA VSPPSSEVPA GGLPFLAEIN ARRSERGAVE GVSSTKIQTE 

       310        320        330        340        350        360 
NHKSPSQPPL PSSAPPIPTS HAPPLPPTAP PPPSLPNVTS APKKATSAPA PPPPPLPAAM 

       370        380        390        400        410        420 
SSASTNSVKA TPVPPTLAPP LPNTTSVPPN KASSMPAPPP PPPPPPGAFS TSSALSASSI 

       430        440        450        460        470        480 
PLAPLPPPPP PSVATSVPSA PPPPPTLTTN KPSASSKQSK ISSSSSSSAV TPGGPLPFLA 

       490        500        510        520        530        540 
EIQKKRDDRF VVGGDTGYTT QDKQEDVIGS SKDDNVRPSP ISPSINPPKQ SSQNGMSFLD 

       550        560        570        580        590        600 
EIESKLHKQT SSNAFNAPPP HTDAMAPPLP PSAPPPPITS LPTPTASGDD HTNDKSETVL 

       610        620        630        640        650        660 
GMKKAKAPAL PGHVPPPPVP PVLSDDSKNN VPAASLLHDV LPSSNLEKPP SPPVAAAPPL 

       670        680        690        700        710        720 
PTFSAPSLPQ QSVSTSIPSP PPVAPTLSVR TETESISKNP TKSPPPPPSP STMDTGTSNS 

       730        740        750        760        770        780 
PSKNLKQRLF STGGSTLQHK HNTHTNQPDV DVGRYTIGGS NSIVGAKSGN ERIVIDDSRF 

       790        800        810 
KWTNVSQMPK PRPFQNKTKL YPSGKGSSVP LDLTLFT

« Hide

References

« Hide 'large scale' references
[1]"A proline-rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiae."
Donnelly S.F.H., Pocklington M.J., Pallota D., Orr E.
Mol. Microbiol. 10:585-596(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A364.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-466; SER-467 AND THR-736, MASS SPECTROMETRY.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; SER-522; SER-524; SER-695; SER-703; THR-712; SER-720; THR-736; SER-760 AND SER-762, MASS SPECTROMETRY.
[7]"Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z26645 Genomic DNA. Translation: CAA81388.1.
U19028 Genomic DNA. Translation: AAB67263.1.
BK006945 Genomic DNA. Translation: DAA09643.1.
PIRS51342.
RefSeqNP_013441.1. NM_001182226.1.

3D structure databases

ProteinModelPortalP37370.
SMRP37370. Positions 28-58.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-860N.
IntActP37370. 25 interactions.
MINTMINT-374755.

Proteomic databases

PaxDbP37370.
PeptideAtlasP37370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR337C; YLR337C; YLR337C.
GeneID851051.
KEGGsce:YLR337C.

Organism-specific databases

CYGDYLR337c.
SGDS000004329. VRP1.

Phylogenomic databases

eggNOGNOG149184.
GeneTreeENSGT00690000102034.
OMAHIAGERQ.
OrthoDBEOG405W9W.

Gene expression databases

ArrayExpressP37370.
GenevestigatorP37370.
GermOnlineYLR337C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR003124. WH2_dom.
[Graphical view]
PfamPF02205. WH2. 2 hits.
[Graphical view]
SMARTSM00246. WH2. 2 hits.
[Graphical view]
PROSITEPS51082. WH2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio967664.

Entry information

Entry nameVRP1_YEAST
AccessionPrimary (citable) accession number: P37370
Secondary accession number(s): D6VYX7, Q06133
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: April 3, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents