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)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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. Ref.3
Sequence similarities	Belongs to the LSB1 family. Contains 1 SH3 domain.

Ontologies

Keywords
Domain	SH3 domain
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
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
Amino acid modifications
	Modified residue	48	1	Phosphoserine Ref.8
	Modified residue	114	1	Phosphoserine Ref.7
	Modified residue	116	1	Phosphoserine Ref.7
	Cross-link	41		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5 Ref.6
	Cross-link	79		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5 Ref.6

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: 9169869] [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: 10512884] [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: 10407277] [Abstract] Cited for: FUNCTION.
[5]	"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: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, MASS SPECTROMETRY. Strain: SUB592.
[6]	"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: 14557538] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, MASS SPECTROMETRY.
[7]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-116, MASS SPECTROMETRY.
[8]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, MASS SPECTROMETRY.
+	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. 12 interactions.
MINT	MINT-375073.
STRING	P53281.
Proteomic databases
PeptideAtlas	P53281.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR136W; YGR136W; YGR136W.
GeneID	853037.
KEGG	sce:YGR136W.
NMPDR	fig|4932.3.peg.2771.
Organism-specific databases
CYGD	YGR136w.
SGD	S000003368. LSB1.
Phylogenomic databases
eggNOG	fuNOG11568.
GeneTree	EFGT00050000000904.
HOGENOM	HBG396736.
OMA	EHLSEDW.
OrthoDB	EOG4N606F.
Gene expression databases
ArrayExpress	P53281.
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:	December 14, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program