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Q06449

- PIN3_YEAST

UniProt

Q06449 - PIN3_YEAST

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Protein

[PSI+] inducibility protein 3

Gene

PIN3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Biological processi

  1. negative regulation of Arp2/3 complex-mediated actin nucleation Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-34285-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
[PSI+] inducibility protein 3
Alternative name(s):
LAS seventeen-binding protein 2
Short name:
LAS17-binding protein 2
Gene namesi
Name:PIN3
Synonyms:LSB2
Ordered Locus Names:YPR154W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPR154w.
SGDiS000006358. PIN3.

Subcellular locationi

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.

GO - Cellular componenti

  1. actin cortical patch Source: SGD
  2. cytoplasm Source: SGD
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801K → R: Abolishes formation of ubiquitinated protein forms. 1 Publication
Mutagenesisi91 – 911W → S: Abolishes interaction with LAS17, but not with SUP35. Blocks colocalization with actin, aggregation, and prion-inducing ability. 1 Publication
Mutagenesisi124 – 1252PP → AA: Abolishes RSP5 binding site and consequently ubiquitination. 1 Publication
Mutagenesisi174 – 1752QQ → AA: Reduces, but does not abolish the ability to promote [PSI+] induction. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 215214[PSI+] inducibility protein 3PRO_0000268696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei52 – 521Phosphoserine1 Publication
Modified residuei55 – 551Phosphoserine1 Publication
Cross-linki80 – 80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated by RSP5. Ubiquitination reduces the protein abundance and its prion-inducing ability.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ06449.
PaxDbiQ06449.
PeptideAtlasiQ06449.

Expressioni

Inductioni

By heat shock. Can thereby reach physiological protein levels high enough to promote prion-formation.1 Publication

Gene expression databases

GenevestigatoriQ06449.

Interactioni

Subunit structurei

Interacts with LAS17, RSP5 and SUP35.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APP1P539334EBI-35523,EBI-28798
LAS17Q124464EBI-35523,EBI-10022
VTC4P470752EBI-35523,EBI-25789
YIL108WP404833EBI-35523,EBI-25176

Protein-protein interaction databases

BioGridi36321. 51 interactions.
DIPiDIP-6257N.
IntActiQ06449. 45 interactions.
MINTiMINT-374980.
STRINGi4932.YPR154W.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 614
Beta strandi80 – 867
Beta strandi88 – 969
Beta strandi99 – 1046
Helixi105 – 1073
Beta strandi108 – 1103

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YNZX-ray2.20A57-112[»]
1ZX6X-ray1.60A57-112[»]
ProteinModelPortaliQ06449.
SMRiQ06449. Positions 57-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06449.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 11360SH3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi124 – 1274PY motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 1254Poly-Pro
Compositional biasi126 – 18156Asn/Gln-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the LSB1 family.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG298780.
GeneTreeiENSGT00510000054224.
HOGENOMiHOG000195703.
InParanoidiQ06449.
OMAiYVKPAFS.
OrthoDBiEOG75MW70.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06449-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSASLINRSL TNIRTELDFL KGSNVISNDV YDQINKSLPA KWDPANAPRN
60 70 80 90 100
ASPASLEYVE ALYQFDPQQD GDLGLKPGDK VQLLEKLSPE WYKGSCNGRT
110 120 130 140 150
GIFPANYVKP AFSGSNGPSN LPPPPQYKAQ ELQQIPTQNS AASSYQQQPF
160 170 180 190 200
PPPSTNYYQQ PQQQPQQAPP PQQQQQQQQH QSSHSHLKSF GSKLGNAAIF
210
GAGASIGSDI VNNIF
Length:215
Mass (Da):23,539
Last modified:November 1, 1996 - v1
Checksum:i37C95425B02FB284
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28371 Genomic DNA. Translation: AAB68051.1.
AY692989 Genomic DNA. Translation: AAT93008.1.
BK006949 Genomic DNA. Translation: DAA11566.1.
PIRiS61138.
RefSeqiNP_015480.1. NM_001184251.1.

Genome annotation databases

EnsemblFungiiYPR154W; YPR154W; YPR154W.
GeneIDi856277.
KEGGisce:YPR154W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28371 Genomic DNA. Translation: AAB68051.1 .
AY692989 Genomic DNA. Translation: AAT93008.1 .
BK006949 Genomic DNA. Translation: DAA11566.1 .
PIRi S61138.
RefSeqi NP_015480.1. NM_001184251.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YNZ X-ray 2.20 A 57-112 [» ]
1ZX6 X-ray 1.60 A 57-112 [» ]
ProteinModelPortali Q06449.
SMRi Q06449. Positions 57-112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36321. 51 interactions.
DIPi DIP-6257N.
IntActi Q06449. 45 interactions.
MINTi MINT-374980.
STRINGi 4932.YPR154W.

Proteomic databases

MaxQBi Q06449.
PaxDbi Q06449.
PeptideAtlasi Q06449.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPR154W ; YPR154W ; YPR154W .
GeneIDi 856277.
KEGGi sce:YPR154W.

Organism-specific databases

CYGDi YPR154w.
SGDi S000006358. PIN3.

Phylogenomic databases

eggNOGi NOG298780.
GeneTreei ENSGT00510000054224.
HOGENOMi HOG000195703.
InParanoidi Q06449.
OMAi YVKPAFS.
OrthoDBi EOG75MW70.

Enzyme and pathway databases

BioCyci YEAST:G3O-34285-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q06449.
NextBioi 981592.

Gene expression databases

Genevestigatori Q06449.

Family and domain databases

InterProi IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. 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. 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. 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.

Entry informationi

Entry nameiPIN3_YEAST
AccessioniPrimary (citable) accession number: Q06449
Secondary accession number(s): D6W4F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2190 molecules/cell in log phase SD medium.1 Publication
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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3