P53281 (LSB1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
LAS seventeen-binding protein 1
Short name=LAS17-binding protein 1

Gene names

Name:	LSB1
Ordered Locus Names:	YGR136W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in resistance to EDTA. Ref.4
Subunit structure	Interacts with LAS17, RSP5 and SUP35. Ref.3 Ref.11 Ref.12
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › actin patch Ref.5 Ref.12.
Domain	The PY motif is recognized directly by the WW domains of RSP5 By similarity.
Post-translational modification	Ubiquitinated by RSP5. Ref.8 Ref.11
Sequence similarities	Belongs to the LSB1 family. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	SH3 domain
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	actin cortical patch Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay PubMed 11914276Ref.5PubMed 22842922. Source: SGD nucleus Inferred from direct assay Ref.5PubMed 22842922. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LAS17	Q12446	9	EBI-23329,EBI-10022
RSP5	P39940	2	EBI-23329,EBI-16219

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 241	241	LAS seventeen-binding protein 1		PRO_0000202825
Regions
	Domain	53 – 112	60	SH3
	Motif	135 – 138	4	PY motif
Amino acid modifications
	Modified residue	48	1	Phosphoserine Ref.10
	Modified residue	114	1	Phosphoserine Ref.9
	Modified residue	116	1	Phosphoserine Ref.9
	Cross-link	41		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6 Ref.7
	Cross-link	79		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6 Ref.7
Experimental info
	Mutagenesis	90	1	W → S: Abolishes interaction with LAS17, but not with SUP35. Blocks colocalization with actin. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	P53281 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 5F0B1361AF84AA79	FASTA	241	26,139
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Chemotyping of yeast mutants using robotics." Rieger K.-J., El-Alama M., Stein G., Bradshaw C., Slonimski P.P., Maundrell K. Yeast 15:973-986(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"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].
[6]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
[11]	"Yeast Rsp5 ubiquitin ligase affects the actin cytoskeleton in vivo and in vitro." Kaminska J., Spiess M., Stawiecka-Mirota M., Monkaityte R., Haguenauer-Tsapis R., Urban-Grimal D., Winsor B., Zoladek T. Eur. J. Cell Biol. 90:1016-1028(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z72921 Genomic DNA. Translation: CAA97149.1. BK006941 Genomic DNA. Translation: DAA08229.1.
PIR	S64445.
RefSeq	NP_011652.1. NM_001181265.1.
3D structure databases
ProteinModelPortal	P53281.
SMR	P53281. Positions 56-111.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1863N.
IntAct	P53281. 11 interactions.
MINT	MINT-375073.
STRING	4932.YGR136W.
Proteomic databases
PaxDb	P53281.
PeptideAtlas	P53281.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR136W; YGR136W; YGR136W.
GeneID	853037.
KEGG	sce:YGR136W.
Organism-specific databases
CYGD	YGR136w.
SGD	S000003368. LSB1.
Phylogenomic databases
eggNOG	NOG136033.
GeneTree	ENSGT00510000054224.
HOGENOM	HOG000195703.
OMA	EHLSEDW.
OrthoDB	EOG4N606F.
Gene expression databases
Genevestigator	P53281.
GermOnline	YGR136W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000108. p67phox. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00499. P67PHOX. PR00452. SH3DOMAIN.
SMART	SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972938.

Entry information

Entry name

LSB1_YEAST

Accession

Primary (citable) accession number: P53281
Secondary accession number(s): D6VUR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program