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UniProtKB/Swiss-Prot entry P53281


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LSB1_YEAST
Primary accession number P53281
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 56)
Name and origin of the protein
Protein name LAS seventeen-binding protein 1
Synonym LAS17-binding protein 1
Gene name
Name: LSB1
OrderedLocusNames: YGR136W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[2]
INTERACTION WITH LAS17.
PubMed=10512884 [NCBI, ExPASy, EBI, Israel, Japan]
Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C., Soulard A., Moreau V., Winsor B.;
"The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex.";
Mol. Biol. Cell 10:3521-3538(1999).
[3]
FUNCTION.
DOI=10.1002/(SICI)1097-0061(199907)15:10B<973::AID-YEA402>3.3.CO;2-C; PubMed=10407277 [NCBI, ExPASy, EBI, Israel, Japan]
Rieger K.-J., El-Alama M., Stein G., Bradshaw C., Slonimski P.P., Maundrell K.;
"Chemotyping of yeast mutants using robotics.";
Yeast 15:973-986(1999).
[4]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, AND MASS SPECTROMETRY.
DOI=10.1038/nbt849; PubMed=12872131 [NCBI, ExPASy, EBI, Israel, Japan]
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.;
"A proteomics approach to understanding protein ubiquitination.";
Nat. Biotechnol. 21:921-926(2003).
[5]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135500100; PubMed=14557538 [NCBI, ExPASy, EBI, Israel, Japan]
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-116, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z72921; CAA97149.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64445; S64445.
RefSeq NP_011652.1; -.
3D structure databases
HSSP P29355; 1SEM. [HSSP ENTRY / PDB]
SMR P53281; 56-111.
ModBase P53281.
Protein-protein interaction databases
DIP DIP:1863N; -.
IntAct P53281; 14.
Organism-specific databases
CYGD YGR136w; -.
SGD S000003368; LSB1.
Yeast-GFP YGR136W.
Gene expression databases
GermOnline YGR136W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR000108; Neu_cyt_fact_2.
IPR001452; SH3.
IPR013315; Spectrin_alpha.
Graphical view of domain structure.
Pfam PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00499; P67PHOX.
PR00452; SH3DOMAIN.
PR01887; SPECTRNALPHA.
ProDom PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00326; SH3; 1.
SMART graphical view of domain structure.
PROSITE PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P53281; -.
Genome annotation databases
Ensembl YGR136W; Saccharomyces cerevisiae. [Contig view]
GeneID 853037; -.
GenomeReviews Y13135_GR; YGR136W.
KEGG sce:YGR136W; -.
NMPDR fig|4932.3.peg.2771; -.
Phylogenomic databases
HOGENOM P53281; -.
Other
LinkHub P53281; -.
NextBio 972938; -.
ProtoNet P53281.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Phosphoprotein; SH3 domain; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   241  241     LAS seventeen-binding protein 1. PRO_0000202825
DOMAIN   53   112  60     SH3. 
MOD_RES   48    48        Phosphoserine. 
MOD_RES   114   114        Phosphoserine. 
MOD_RES   116   116        Phosphoserine. 
CROSSLNK   41    41        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   79    79        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
Sequence information
Length: 241 AA [This is the length of the unprocessed precursor] Molecular weight: 26139 Da [This is the MW of the unprocessed precursor] CRC64: 5F0B1361AF84AA79 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSASLVNRSL KNIRNELEFL KESNVISGDI FELINSKLPE KWDGNQRSPQ NADTEEYVEA 

        70         80         90        100        110        120 
LYDFEAQQDG DLSLKTGDKI QVLEKISPDW YRGKSNNKIG IFPANYVKPA FTRSASPKSA 

       130        140        150        160        170        180 
EAASSSTVSR PSVPPPSYEP AASQYPSQQV SAPYAPPAGY MQAPPPQQQQ APLPYPPPFT 

       190        200        210        220        230        240 
NYYQQPQQQY APPSQQAPVE AQPQQSSGAS SAFKSFGSKL GNAAIFGAGS AIGSDIVNSI 


F 

P53281 in FASTA format

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