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Protein

Proline-rich protein LAS17

Gene

LAS17

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

GO - Molecular functioni

  • actin binding Source: SGD

GO - Biological processi

  • actin cortical patch localization Source: SGD
  • actin filament organization Source: SGD
  • actin filament polymerization Source: SGD
  • actin nucleation Source: SGD
  • endocytosis Source: InterPro
  • positive regulation of actin filament bundle assembly Source: SGD
  • positive regulation of Arp2/3 complex-mediated actin nucleation Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-33692-MONOMER.
ReactomeiREACT_305965. Regulation of actin dynamics for phagocytic cup formation.
REACT_358186. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-rich protein LAS17
Gene namesi
Name:LAS17
Ordered Locus Names:YOR181W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR181w.
EuPathDBiFungiDB:YOR181W.
SGDiS000005707. LAS17.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Proline-rich protein LAS17PRO_0000084361Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei334 – 3341Phosphothreonine1 Publication
Modified residuei337 – 3371Phosphoserine1 Publication
Modified residuei588 – 5881Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12446.
PaxDbiQ12446.

Interactioni

Subunit structurei

Interacts with KRE6, LSB3, LSB5 and YSC84.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARC40P383282EBI-10022,EBI-2777
BZZ1P3882214EBI-10022,EBI-3889
END3P390133EBI-10022,EBI-6460
HOF1Q050803EBI-10022,EBI-5412
LSB3P436039EBI-10022,EBI-22980
LSB5P253693EBI-10022,EBI-10218
MYO3P360063EBI-10022,EBI-11670
MYO5Q044397EBI-10022,EBI-11687
PEX13P806672EBI-10022,EBI-13206
PIN3Q064494EBI-10022,EBI-35523
RVS167P3974312EBI-10022,EBI-14500
SHO1P400735EBI-10022,EBI-18140
SLA1P327906EBI-10022,EBI-17313
SLA2P333383EBI-10022,EBI-17323
VRP1P373706EBI-10022,EBI-20502
YSC84P327937EBI-10022,EBI-24460

Protein-protein interaction databases

BioGridi34576. 155 interactions.
DIPiDIP-963N.
IntActiQ12446. 38 interactions.
MINTiMINT-370148.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZUKX-ray1.90C350-360[»]
ProteinModelPortaliQ12446.
SMRiQ12446. Positions 28-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12446.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 127112WH1PROSITE-ProRule annotationAdd
BLAST
Domaini547 – 56721WH2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi185 – 529345Pro-richAdd
BLAST
Compositional biasi185 – 1906Poly-Pro
Compositional biasi323 – 3297Poly-Pro
Compositional biasi342 – 3487Poly-Pro
Compositional biasi352 – 3587Poly-Pro
Compositional biasi385 – 3917Poly-Pro
Compositional biasi427 – 4315Poly-Pro
Compositional biasi470 – 4745Poly-Pro
Compositional biasi503 – 5075Poly-Pro
Compositional biasi520 – 5267Poly-Pro

Sequence similaritiesi

Contains 1 WH1 domain.PROSITE-ProRule annotation
Contains 1 WH2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG270974.
GeneTreeiENSGT00730000110895.
HOGENOMiHOG000111174.
InParanoidiQ12446.
OMAiTNDATHF.
OrthoDBiEOG71K6CX.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH-like_dom.
IPR000697. WH1/EVH1_dom.
IPR003124. WH2_dom.
IPR028297. Wsp1/Las17_fungal.
[Graphical view]
PANTHERiPTHR23202:SF2. PTHR23202:SF2. 1 hit.
PfamiPF00568. WH1. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00461. WH1. 1 hit.
SM00246. WH2. 1 hit.
[Graphical view]
PROSITEiPS50229. WH1. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLNSSDKE IIKRALPKAS NKIIDVTVAR LYIAYPDKNE WQYTGLSGAL
60 70 80 90 100
ALVDDLVGNT FFLKLVDING HRGVIWDQEL YVNFEYYQDR TFFHTFEMEE
110 120 130 140 150
CFAGLLFVDI NEASHFLKRV QKRERYANRK TLLNKNAVAL TKKVREEQKS
160 170 180 190 200
QVVHGPRGES LIDNQRKRYN YEDVDTIPTT KHKAPPPPPP TAETFDSDQT
210 220 230 240 250
SSFSDINSTT ASAPTTPAPA LPPASPEVRK EETHPKHSLP PLPNQFAPLP
260 270 280 290 300
DPPQHNSPPQ NNAPSQPQSN PFPFPIPEIP STQSATNPFP FPVPQQQFNQ
310 320 330 340 350
APSMGIPQQN RPLPQLPNRN NRPVPPPPPM RTTTEGSGVR LPAPPPPPRR
360 370 380 390 400
GPAPPPPPHR HVTSNTLNSA GGNSLLPQAT GRRGPAPPPP PRASRPTPNV
410 420 430 440 450
TMQQNPQQYN NSNRPFGYQT NSNMSSPPPP PVTTFNTLTP QMTAATGQPA
460 470 480 490 500
VPLPQNTQAP SQATNVPVAP PPPPASLGQS QIPQSAPSAP IPPTLPSTTS
510 520 530 540 550
AAPPPPPAFL TQQPQSGGAP APPPPPQMPA TSTSGGGSFA ETTGDAGRDA
560 570 580 590 600
LLASIRGAGG IGALRKVDKS QLDKPSVLLQ EARGESASPP AAAGNGGTPG
610 620 630
GPPASLADAL AAALNKRKTK VGAHDDMDNG DDW
Length:633
Mass (Da):67,572
Last modified:November 1, 1997 - v1
Checksum:i4488355563AA2645
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78487 Genomic DNA. Translation: BAA11386.1.
Z75089 Genomic DNA. Translation: CAA99390.1.
BK006948 Genomic DNA. Translation: DAA10953.1.
PIRiS62057.
RefSeqiNP_014824.1. NM_001183600.1.

Genome annotation databases

EnsemblFungiiYOR181W; YOR181W; YOR181W.
GeneIDi854353.
KEGGisce:YOR181W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78487 Genomic DNA. Translation: BAA11386.1.
Z75089 Genomic DNA. Translation: CAA99390.1.
BK006948 Genomic DNA. Translation: DAA10953.1.
PIRiS62057.
RefSeqiNP_014824.1. NM_001183600.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZUKX-ray1.90C350-360[»]
ProteinModelPortaliQ12446.
SMRiQ12446. Positions 28-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34576. 155 interactions.
DIPiDIP-963N.
IntActiQ12446. 38 interactions.
MINTiMINT-370148.

Proteomic databases

MaxQBiQ12446.
PaxDbiQ12446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR181W; YOR181W; YOR181W.
GeneIDi854353.
KEGGisce:YOR181W.

Organism-specific databases

CYGDiYOR181w.
EuPathDBiFungiDB:YOR181W.
SGDiS000005707. LAS17.

Phylogenomic databases

eggNOGiNOG270974.
GeneTreeiENSGT00730000110895.
HOGENOMiHOG000111174.
InParanoidiQ12446.
OMAiTNDATHF.
OrthoDBiEOG71K6CX.

Enzyme and pathway databases

BioCyciYEAST:G3O-33692-MONOMER.
ReactomeiREACT_305965. Regulation of actin dynamics for phagocytic cup formation.
REACT_358186. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

EvolutionaryTraceiQ12446.
NextBioi976446.
PROiQ12446.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH-like_dom.
IPR000697. WH1/EVH1_dom.
IPR003124. WH2_dom.
IPR028297. Wsp1/Las17_fungal.
[Graphical view]
PANTHERiPTHR23202:SF2. PTHR23202:SF2. 1 hit.
PfamiPF00568. WH1. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00461. WH1. 1 hit.
SM00246. WH2. 1 hit.
[Graphical view]
PROSITEiPS50229. WH1. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast mutants sensitive to local anesthetics."
    Toh-e A.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(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. "The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex."
    Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C., Soulard A., Moreau V., Winsor B.
    Mol. Biol. Cell 10:3521-3538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LSB3; LSB5 AND YSC84.
  5. "Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis-Golgi protein Kre6p."
    Li H., Page N., Bussey H.
    Yeast 19:1097-1112(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KRE6.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334 AND SER-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLAS17_YEAST
AccessioniPrimary (citable) accession number: Q12446
Secondary accession number(s): D6W2N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 130 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 8580 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.