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Q06449 (PIN3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
[PSI+] inducibility protein 3
Alternative name(s):
LAS seventeen-binding protein 2
Short name=LAS17-binding protein 2
Gene names
Name:PIN3
Synonyms:LSB2
Ordered Locus Names:YPR154W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Overproduction promotes the de novo induction of the [PSI+] prion form of SUP35. The prion-inducing effect depends on the association with the actin cytoskeleton. Also implicated in prion maintenance during heat stress. Ref.11

Subunit structure

Interacts with LAS17, RSP5 and SUP35. Ref.4 Ref.10 Ref.11

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeletonactin patch. Note: When overexpressed, localizes to punctate structures which are reminiscent of cortical actin patches. Transiently colocalizes with SUP35 aggregates during prionogenesis. Ref.6 Ref.11

Induction

By heat shock. Can thereby reach physiological protein levels high enough to promote prion-formation. Ref.11

Domain

The PY motif is recognized directly by the WW domains of RSP5.

Post-translational modification

Ubiquitinated by RSP5. Ubiquitination reduces the protein abundance and its prion-inducing ability. Ref.10 Ref.11

Miscellaneous

Present with 2190 molecules/cell in log phase SD medium.

Although this protein promotes prion formation and it has a Asn/Gln-rich prion-like domain, it does not seem to have a prion form by itself.

Sequence similarities

Belongs to the LSB1 family.

Contains 1 SH3 domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 215214[PSI+] inducibility protein 3
PRO_0000268696

Regions

Domain54 – 11360SH3
Motif124 – 1274PY motif
Compositional bias122 – 1254Poly-Pro
Compositional bias126 – 18156Asn/Gln-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue521Phosphoserine Ref.9
Modified residue551Phosphoserine Ref.9
Cross-link80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Experimental info

Mutagenesis801K → R: Abolishes formation of ubiquitinated protein forms. Ref.11
Mutagenesis911W → S: Abolishes interaction with LAS17, but not with SUP35. Blocks colocalization with actin, aggregation, and prion-inducing ability. Ref.11
Mutagenesis124 – 1252PP → AA: Abolishes RSP5 binding site and consequently ubiquitination.
Mutagenesis174 – 1752QQ → AA: Reduces, but does not abolish the ability to promote [PSI+] induction.

Secondary structure

........... 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06449 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 37C95425B02FB284

FASTA21523,539
        10         20         30         40         50         60 
MSASLINRSL TNIRTELDFL KGSNVISNDV YDQINKSLPA KWDPANAPRN ASPASLEYVE 

        70         80         90        100        110        120 
ALYQFDPQQD GDLGLKPGDK VQLLEKLSPE WYKGSCNGRT GIFPANYVKP AFSGSNGPSN 

       130        140        150        160        170        180 
LPPPPQYKAQ ELQQIPTQNS AASSYQQQPF PPPSTNYYQQ PQQQPQQAPP PQQQQQQQQH 

       190        200        210 
QSSHSHLKSF GSKLGNAAIF GAGASIGSDI VNNIF 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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]"Prions affect the appearance of other prions: the story of [PIN(+)]."
Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W.
Cell 106:171-182(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PRION FORMATION.
[6]"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].
[7]"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].
[8]"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-80.
Strain: SUB592.
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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.
[11]"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: FUNCTION, UBIQUITINATION BY RSP5, MUTAGENESIS OF LYS-80; TRP-91; 124-PRO-PRO-125 AND 174-GLN-GLN-175, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH LAS17 AND SUP35.
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"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].
[14]"Structural genomics of yeast SH3 domains."
Kursula P., Kursula I., Lehmann F., Zou P., Song Y.H., Wilmanns M.
Submitted (JUN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 57-112.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28371 Genomic DNA. Translation: AAB68051.1.
AY692989 Genomic DNA. Translation: AAT93008.1.
BK006949 Genomic DNA. Translation: DAA11566.1.
PIRS61138.
RefSeqNP_015480.1. NM_001184251.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YNZX-ray2.20A57-112[»]
1ZX6X-ray1.60A57-112[»]
ProteinModelPortalQ06449.
SMRQ06449. Positions 57-112.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36321. 51 interactions.
DIPDIP-6257N.
IntActQ06449. 45 interactions.
MINTMINT-374980.
STRING4932.YPR154W.

Proteomic databases

PaxDbQ06449.
PeptideAtlasQ06449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR154W; YPR154W; YPR154W.
GeneID856277.
KEGGsce:YPR154W.

Organism-specific databases

CYGDYPR154w.
SGDS000006358. PIN3.

Phylogenomic databases

eggNOGNOG298780.
GeneTreeENSGT00510000054224.
HOGENOMHOG000195703.
OMAYVKPAFS.
OrthoDBEOG75MW70.

Enzyme and pathway databases

BioCycYEAST:G3O-34285-MONOMER.

Gene expression databases

GenevestigatorQ06449.

Family and domain databases

InterProIPR001452. SH3_domain.
[Graphical view]
PfamPF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ06449.
NextBio981592.

Entry information

Entry namePIN3_YEAST
AccessionPrimary (citable) accession number: Q06449
Secondary accession number(s): D6W4F0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references