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P53281

- LSB1_YEAST

UniProt

P53281 - LSB1_YEAST

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Protein

LAS seventeen-binding protein 1

Gene
LSB1, YGR136W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in resistance to EDTA.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct

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

Cytoplasm. Nucleus. Cytoplasmcytoskeletonactin patch 2 Publications

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 RSP5.2 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 11260SH3Add
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.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG136033.
GeneTreeiENSGT00510000054224.
HOGENOMiHOG000195703.
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

MSASLVNRSL KNIRNELEFL KESNVISGDI FELINSKLPE KWDGNQRSPQ    50
NADTEEYVEA LYDFEAQQDG DLSLKTGDKI QVLEKISPDW YRGKSNNKIG 100
IFPANYVKPA FTRSASPKSA EAASSSTVSR PSVPPPSYEP AASQYPSQQV 150
SAPYAPPAGY MQAPPPQQQQ APLPYPPPFT NYYQQPQQQY APPSQQAPVE 200
AQPQQSSGAS SAFKSFGSKL GNAAIFGAGS AIGSDIVNSI F 241
Length:241
Mass (Da):26,139
Last modified:October 1, 1996 - v1
Checksum:i5F0B1361AF84AA79
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Z72921 Genomic DNA. Translation: CAA97149.1 .
BK006941 Genomic DNA. Translation: DAA08229.1 .
PIRi S64445.
RefSeqi NP_011652.1. NM_001181265.1.

3D structure databases

ProteinModelPortali P53281.
SMRi P53281. Positions 56-111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33384. 32 interactions.
DIPi DIP-1863N.
IntActi P53281. 29 interactions.
MINTi MINT-375073.
STRINGi 4932.YGR136W.

Proteomic databases

MaxQBi P53281.
PaxDbi P53281.
PeptideAtlasi P53281.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR136W ; YGR136W ; YGR136W .
GeneIDi 853037.
KEGGi sce:YGR136W.

Organism-specific databases

CYGDi YGR136w.
SGDi S000003368. LSB1.

Phylogenomic databases

eggNOGi NOG136033.
GeneTreei ENSGT00510000054224.
HOGENOMi HOG000195703.
OMAi SQTKQNV.
OrthoDBi EOG75MW70.

Enzyme and pathway databases

BioCyci YEAST:G3O-30842-MONOMER.

Miscellaneous databases

NextBioi 972938.

Gene expression databases

Genevestigatori P53281.

Family and domain databases

InterProi IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 102 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

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