LAS seventeen-binding protein 3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P43603 (LSB3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
LAS seventeen-binding protein 3
Short name=LAS17-binding protein 3

Gene names

Name:	LSB3
Ordered Locus Names:	YFR024C-A
ORF Names:	YFR024C

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Interacts with LAS17. Ref.4
Subcellular location	Cytoplasm Ref.7.
Post-translational modification	Phosphorylation of Ser-397 is induced 2-fold in response to mating pheromone.
Miscellaneous	Present with 18000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SH3YL1 family. Contains 1 SH3 domain.
Sequence caution	The sequence BAA09263.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cortical patch localization Inferred from mutant phenotype PubMed 19158382. Source: SGD
Cellular_component	cellular bud neck Inferred from direct assay Ref.7. Source: SGD mitochondrion Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ACF2	Q12168	4	EBI-22980,EBI-32973
ACF4	P47129	3	EBI-22980,EBI-25556
AIM3	P38266	3	EBI-22980,EBI-21584
APP1	P53933	5	EBI-22980,EBI-28798
BSP1	Q06604	4	EBI-22980,EBI-37047
CUE5	Q08412	5	EBI-22980,EBI-37580
ERT1	P38140	2	EBI-22980,EBI-21048
GTS1	P40956	2	EBI-22980,EBI-7968
GYL1	Q04322	3	EBI-22980,EBI-27427
HUA1	P40325	3	EBI-22980,EBI-23614
LAS17	Q12446	14	EBI-22980,EBI-10022
SLA1	P32790	6	EBI-22980,EBI-17313

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 459

459

LAS seventeen-binding protein 3

PRO_0000202691

Regions

Domain

400 – 459

SH3

Compositional bias

229 – 284

Asp-rich

Amino acid modifications

Modified residue

270

Phosphoserine Ref.11

Modified residue

272

Phosphoserine Ref.11

Modified residue

275

Phosphothreonine Ref.11

Modified residue

300

Phosphoserine Ref.6 Ref.10 Ref.11 Ref.12

Modified residue

303

Phosphoserine Ref.6 Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

393

Phosphothreonine Ref.10 Ref.12

Modified residue

396

Phosphothreonine Ref.12

Modified residue

397

Phosphoserine Ref.9 Ref.12

Modified residue

399

Phosphoserine Ref.12

Modified residue

401

Phosphoserine Ref.12

Modified residue

402

Phosphoserine Ref.10 Ref.12

Modified residue

410

Phosphoserine Ref.12

Modified residue

416

Phosphoserine Ref.12

Secondary structure

459

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P43603 [UniParc].

Last modified July 22, 2008. Version 3.
Checksum: F486C787B5771AAC
Show »

FASTA

459

49,344

        10         20         30         40         50         60 
MGINNPIPRS LKSETKKAAK ILASFVKPNQ VFGADQVIPP DVLKRAKGLA IITILKAGFL 

        70         80         90        100        110        120 
FSGRAGSGVI VARLKDGTWS APSAIAMAGA GAGGMVGIEL TDFVFILNTQ DAVKSFSEFG 

       130        140        150        160        170        180 
TITLGGNVSV SAGPLGRSAE AAASASAGGV AAVFAYSKSK GLFAGVSVEG SAIIERREAN 

       190        200        210        220        230        240 
RKFYGDNCTA KMILSGRIRP PPAVDPLFRV LESRAFNYRP SNGGRGSFDD DEDDYYDDDD 

       250        260        270        280        290        300 
YYNDIPSSFS STDASSTRPN TRSTRRRAQS GSRYTFDDDD DDDDYGTGYS RNSRLAPTNS 

       310        320        330        340        350        360 
GGSGGKLDDP SGASSYYASH RRSGTAQSRA RSSRNRWADD EYDDYDDDYE SGYRRGNGRD 

       370        380        390        400        410        420 
RTKDREVDDL SNRFSKSRIS SASTPQTSQG RFTAPTSPST SSPKAVALYS FAGEESGDLP 

       430        440        450 
FRKGDVITIL KKSDSQNDWW TGRVNGREGI FPANYVELV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database (SGD) Unpublished observations (JUN-2008) Cited for: REVISION OF GENE MODEL.
[4]	"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.
[5]	"Test of intron predictions reveals novel splice sites, alternatively spliced mRNAs and new introns in meiotically regulated genes of yeast." Davis C.A., Grate L., Spingola M., Ares M. Jr. Nucleic Acids Res. 28:1700-1706(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF INTRON.
[6]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300 AND SER-303, MASS SPECTROMETRY. Strain: 2124.
[7]	"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].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-397, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-303; THR-393 AND SER-402, MASS SPECTROMETRY. Strain: ADR376.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-272; THR-275; SER-300 AND SER-303, MASS SPECTROMETRY.
[12]	"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-300; SER-303; THR-393; THR-396; SER-397; SER-399; SER-401; SER-402; SER-410 AND SER-416, MASS SPECTROMETRY.
[13]	"Crystal structure of the SH3 domain from a S.cerevisiae hypothetical 40.4 kDa protein at 1.39 A resolution." Kursula P., Lehmann F., Song Y.H., Wilmanns M. Submitted (APR-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 393-451.
[14]	"Yeast SH3 domain structural genomics." Kursula P., Kursula I., Lehmann F., Song Y.H., Wilmanns M. Submitted (APR-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 393-451.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D50617 Genomic DNA. Translation: BAA09263.1. Sequence problems.
BK006940 Genomic DNA. Translation: DAA12464.1.

RefSeq

NP_219497.4. NM_001180865.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OOT	X-ray	1.39	A	401-459	[»]
1SSH	X-ray	1.40	A	401-459	[»]

ProteinModelPortal

P43603.

SMR

P43603. Positions 368-459.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2753N.
DIP-6259N.

IntAct

P43603. 92 interactions.

MINT

MINT-374953.

STRING

4932.YFR024C-A.

Proteomic databases

PaxDb

P43603.

PeptideAtlas

P43603.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YFR024C-A; YFR024C-A; YFR024C-A.

GeneID

850580.

KEGG

sce:YFR024C-A.
sce:YFR026C.

Organism-specific databases

CYGD

YFR024c-a.

SGD

S000002968. LSB3.

Phylogenomic databases

eggNOG

COG2930.

GeneTree

ENSGT00510000048137.

HOGENOM

HOG000215564.

OMA

HDDVVWE.

OrthoDB

EOG4643NB.

Gene expression databases

Genevestigator

P43603.

GermOnline

YFR024C-A. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001452. SH3_domain.
IPR007461. Ysc84_actin-binding.
[Graphical view]

Pfam

PF04366. DUF500. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P43603.

NextBio

966409.

Entry information

Entry name

LSB3_YEAST

Accession

Primary (citable) accession number: P43603
Secondary accession number(s): D6VTQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	July 22, 2008
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VI

Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents