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Protein

LAS seventeen-binding protein 1

Gene

LSB1

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

Involved in resistance to EDTA.1 Publication

GO - Biological processi

  1. negative regulation of Arp2/3 complex-mediated actin nucleation Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-30842-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
LAS seventeen-binding protein 1
Short name:
LAS17-binding protein 1
Gene namesi
Name:LSB1
Ordered Locus Names:YGR136W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR136w.
SGDiS000003368. LSB1.

Subcellular locationi

GO - Cellular componenti

  1. actin cortical patch Source: SGD
  2. cytoplasm Source: SGD
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901W → S: Abolishes interaction with LAS17, but not with SUP35. Blocks colocalization with actin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 241240LAS seventeen-binding protein 1PRO_0000202825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Cross-linki41 – 41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei48 – 481Phosphoserine1 Publication
Cross-linki79 – 79Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei114 – 1141Phosphoserine1 Publication
Modified residuei116 – 1161Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated by RSP5.4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP53281.
PaxDbiP53281.
PeptideAtlasiP53281.

Expressioni

Gene expression databases

GenevestigatoriP53281.

Interactioni

Subunit structurei

Interacts with LAS17, RSP5 and SUP35.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACF2Q121684EBI-23329,EBI-32973
AIM21P405635EBI-23329,EBI-25376
AIM3P382663EBI-23329,EBI-21584
APP1P539334EBI-23329,EBI-28798
GYL1Q043222EBI-23329,EBI-27427

Protein-protein interaction databases

BioGridi33384. 32 interactions.
DIPiDIP-1863N.
IntActiP53281. 29 interactions.
MINTiMINT-375073.
STRINGi4932.YGR136W.

Structurei

3D structure databases

ProteinModelPortaliP53281.
SMRiP53281. Positions 56-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 11260SH3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi135 – 1384PY motif

Domaini

The PY motif is recognized directly by the WW domains of RSP5.By similarity

Sequence similaritiesi

Belongs to the LSB1 family.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG136033.
GeneTreeiENSGT00510000054224.
HOGENOMiHOG000195703.
InParanoidiP53281.
OMAiSQTKQNV.
OrthoDBiEOG75MW70.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53281-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSASLVNRSL KNIRNELEFL KESNVISGDI FELINSKLPE KWDGNQRSPQ
60 70 80 90 100
NADTEEYVEA LYDFEAQQDG DLSLKTGDKI QVLEKISPDW YRGKSNNKIG
110 120 130 140 150
IFPANYVKPA FTRSASPKSA EAASSSTVSR PSVPPPSYEP AASQYPSQQV
160 170 180 190 200
SAPYAPPAGY MQAPPPQQQQ APLPYPPPFT NYYQQPQQQY APPSQQAPVE
210 220 230 240
AQPQQSSGAS SAFKSFGSKL GNAAIFGAGS AIGSDIVNSI F
Length:241
Mass (Da):26,139
Last modified:October 1, 1996 - v1
Checksum:i5F0B1361AF84AA79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72921 Genomic DNA. Translation: CAA97149.1.
BK006941 Genomic DNA. Translation: DAA08229.1.
PIRiS64445.
RefSeqiNP_011652.1. NM_001181265.1.

Genome annotation databases

EnsemblFungiiYGR136W; YGR136W; YGR136W.
GeneIDi853037.
KEGGisce:YGR136W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72921 Genomic DNA. Translation: CAA97149.1.
BK006941 Genomic DNA. Translation: DAA08229.1.
PIRiS64445.
RefSeqiNP_011652.1. NM_001181265.1.

3D structure databases

ProteinModelPortaliP53281.
SMRiP53281. Positions 56-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33384. 32 interactions.
DIPiDIP-1863N.
IntActiP53281. 29 interactions.
MINTiMINT-375073.
STRINGi4932.YGR136W.

Proteomic databases

MaxQBiP53281.
PaxDbiP53281.
PeptideAtlasiP53281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR136W; YGR136W; YGR136W.
GeneIDi853037.
KEGGisce:YGR136W.

Organism-specific databases

CYGDiYGR136w.
SGDiS000003368. LSB1.

Phylogenomic databases

eggNOGiNOG136033.
GeneTreeiENSGT00510000054224.
HOGENOMiHOG000195703.
InParanoidiP53281.
OMAiSQTKQNV.
OrthoDBiEOG75MW70.

Enzyme and pathway databases

BioCyciYEAST:G3O-30842-MONOMER.

Miscellaneous databases

NextBioi972938.

Gene expression databases

GenevestigatoriP53281.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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 LAS17.
  4. Cited for: FUNCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79.
    Strain: SUB592.
  7. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
    Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79.
  8. "Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast."
    Gupta R., Kus B., Fladd C., Wasmuth J., Tonikian R., Sidhu S., Krogan N.J., Parkinson J., Rotin D.
    Mol. Syst. Biol. 3:116-116(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY RSP5.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: UBIQUITINATION BY RSP5, INTERACTION WITH RSP5.
  12. "Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton."
    Chernova T.A., Romanyuk A.V., Karpova T.S., Shanks J.R., Ali M., Moffatt N., Howie R.L., O'Dell A., McNally J.G., Liebman S.W., Chernoff Y.O., Wilkinson K.D.
    Mol. Cell 43:242-252(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-90, INTERACTION WITH LAS17 AND SUP35.
  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 nameiLSB1_YEAST
AccessioniPrimary (citable) accession number: P53281
Secondary accession number(s): D6VUR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.