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Protein

AP-1-like transcription factor YAP1

Gene

YAP1

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

Functioni

Transcription activator involved in oxidative stress response and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including the thioredoxin system (TRX2, TRR1), the glutaredoxin system (GSH1, GLR1), superoxide dismutase (SOD1, SOD2), glutathione peroxidase (GPX2), and thiol-specific peroxidases (TSA1, AHP1). The induction of some of these genes requires the cooperative action of both, YAP1 and SKN7. YAP1 preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of YAP1 is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress (as well as carbon stress, but not increased temperature, acidic pH, or ionic stress) induces nuclear accumulation and as a result YAP1 transcriptional activity. Nuclear export is restored when disulfide bonds are reduced by thioredoxin (TRX2), whose expression is controlled by YAP1, providing a mechanism for negative autoregulation. When overexpressed, YAP1 confers pleiotropic drug-resistance and increases cellular tolerance to cadmium, iron chelators and zinc.13 Publications

GO - Molecular functioni

GO - Biological processi

  • regulation of endoplasmic reticulum unfolded protein response Source: SGD
  • regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: SGD
  • response to cadmium ion Source: UniProtKB-KW
  • response to drug Source: SGD
  • response to heat Source: SGD
  • response to metal ion Source: SGD
  • response to singlet oxygen Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cadmium resistance, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32612-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1-like transcription factor YAP1
Alternative name(s):
Phenanthroline resistance protein PAR1
Pleiotropic drug resistance protein PDR4
Gene namesi
Name:YAP1
Synonyms:PAR1, PDR4, SNQ3
Ordered Locus Names:YML007W
ORF Names:YM9571.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML007W.
SGDiS000004466. YAP1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Oxidized YAP1 is found predominantly in the nucleus, while reduced YAP1 is continuously exported to the cytoplasm by CRM1. Nuclear import requires the karyopherin PSE1/KAP121 and is independent on YAP1 oxidation state.

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi78Q → A: Dominant negative transcription activator. 1 Publication1
Mutagenesisi620C → T: Constitutive nuclear location and transcription activation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000765211 – 650AP-1-like transcription factor YAP1Add BLAST650

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9PhosphoserineCombined sources1
Modified residuei14PhosphoserineCombined sources1
Modified residuei17PhosphoserineCombined sources1
Modified residuei165PhosphothreonineCombined sources1
Modified residuei204PhosphoserineCombined sources1
Disulfide bondi303 ↔ 598In nuclear retained form1 Publication
Disulfide bondi310 ↔ 629In nuclear retained form1 Publication
Modified residuei372PhosphoserineCombined sources1
Modified residuei528PhosphoserineCombined sources1
Disulfide bondi598 ↔ 629In nuclear retained form1 Publication
Disulfide bondi598 ↔ 620In nuclear retained form1 Publication
Disulfide bondi598Interchain (with C-36 in HYR1); transient; in linked form1 Publication
Disulfide bondi620 ↔ 629In nuclear retained form1 Publication

Post-translational modificationi

Depending on the oxidative stress inducing agent, YAP1 can undergo two distinct conformational changes, both involving disulfide bond formation, and both masking the nuclear export signal, thus abolishing nuclear export by CRM1. The disulfide stress-inducing agent diamide leads to the formation of one of three possible disulfide bonds in the c-CRD. Whereas, peroxide stress induces the formation of a disulfide bond between Cys-303 and Cys-598 (and the possibly stabilizing bond between Cys-310 and Cys-629) which is dependent on the hydroperoxide sensing peroxiredoxin HYR1/GPX3/ORP1 and YBP1.2 Publications

Keywords - PTMi

Disulfide bond, Oxidation, Phosphoprotein

Proteomic databases

MaxQBiP19880.
PRIDEiP19880.

PTM databases

iPTMnetiP19880.

Expressioni

Inductioni

YAP1 expression is at least partially regulated at the level of translation. A small upstream open reading frame (uORF) retains the 40S ribosomal subunit. By leaky scanning it then proceeds and reinitiates at the functional YAP1 ORF.

Interactioni

Subunit structurei

Homodimer (By similarity). YAP1 interacts independent of oxidation state in the cytoplasm with the karyopherin PSE1/KAP121 (and less strongly with KAP123). The reduced form of YAP1 interacts in the nucleus with the nuclear export protein CRM1, and in the cytoplasm with YBP1 and the peroxiredoxin HYR1/GPX3/ORP1. Interacts with RBG1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CNB1P252962EBI-31265,EBI-3968
YBP1P383154EBI-31265,EBI-20985

Protein-protein interaction databases

BioGridi35163. 171 interactors.
DIPiDIP-1752N.
IntActiP19880. 41 interactors.
MINTiMINT-505627.

Structurei

Secondary structure

1650
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi289 – 291Combined sources3
Beta strandi292 – 294Combined sources3
Beta strandi298 – 300Combined sources3
Helixi301 – 308Combined sources8
Helixi598 – 606Combined sources9
Helixi616 – 623Combined sources8
Turni624 – 626Combined sources3
Helixi638 – 646Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SSENMR-A279-313[»]
B565-650[»]
ProteinModelPortaliP19880.
SMRiP19880.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19880.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 127bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni67 – 90Basic motifPROSITE-ProRule annotationAdd BLAST24
Regioni92 – 120Leucine-zipperPROSITE-ProRule annotationAdd BLAST29
Regioni220 – 378Transcription activation 1 (PubMed:8182076)1 PublicationAdd BLAST159
Regioni430 – 537Transcription activation 2 (PubMed:8182076)1 PublicationAdd BLAST108

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi5 – 16Nuclear localization signalAdd BLAST12
Motifi50 – 59Nuclear localization signal10
Motifi614 – 621Nuclear export signal8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi411 – 414Poly-Asn4
Compositional biasi517 – 521Poly-Asp5

Domaini

YAP1 contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-303, Cys-310 and Cys-315) and c-CRD (Cys-598, Cys-620 and Cys-629), respectively. Cys-315 is not conserved in orthologs in other yeast species. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein CRM1 interacts only in the absence of disulfide bonds within the c-CRD or between the c-CRD and the n-CRD.

Sequence similaritiesi

Belongs to the bZIP family. YAP subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00530000069148.
HOGENOMiHOG000142347.
InParanoidiP19880.
KOiK09043.
OMAiCSERGVV.
OrthoDBiEOG092C4KCZ.

Family and domain databases

Gene3Di1.10.238.100. 1 hit.
InterProiIPR004827. bZIP.
IPR013910. TF_PAP1.
IPR023167. Yap1_redox_dom.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
PF08601. PAP1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19880-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVSTAKRSL DVVSPGSLAE FEGSKSRHDE IENEHRRTGT RDGEDSEQPK
60 70 80 90 100
KKGSKTSKKQ DLDPETKQKR TAQNRAAQRA FRERKERKMK ELEKKVQSLE
110 120 130 140 150
SIQQQNEVEA TFLRDQLITL VNELKKYRPE TRNDSKVLEY LARRDPNLHF
160 170 180 190 200
SKNNVNHSNS EPIDTPNDDI QENVKQKMNF TFQYPLDNDN DNDNSKNVGK
210 220 230 240 250
QLPSPNDPSH SAPMPINQTQ KKLSDATDSS SATLDSLSNS NDVLNNTPNS
260 270 280 290 300
STSMDWLDNV IYTNRFVSGD DGSNSKTKNL DSNMFSNDFN FENQFDEQVS
310 320 330 340 350
EFCSKMNQVC GTRQCPIPKK PISALDKEVF ASSSILSSNS PALTNTWESH
360 370 380 390 400
SNITDNTPAN VIATDATKYE NSFSGFGRLG FDMSANHYVV NDNSTGSTDS
410 420 430 440 450
TGSTGNKNKK NNNNSDDVLP FISESPFDMN QVTNFFSPGS TGIGNNAASN
460 470 480 490 500
TNPSLLQSSK EDIPFINANL AFPDDNSTNI QLQPFSESQS QNKFDYDMFF
510 520 530 540 550
RDSSKEGNNL FGEFLEDDDD DKKAANMSDD ESSLIKNQLI NEEPELPKQY
560 570 580 590 600
LQSVPGNESE ISQKNGSSLQ NADKINNGND NDNDNDVVPS KEGSLLRCSE
610 620 630 640 650
IWDRITTHPK YSDIDVDGLC SELMAKAKCS ERGVVINAED VQLALNKHMN
Length:650
Mass (Da):72,533
Last modified:October 1, 1993 - v2
Checksum:i192F20FA71027688
GO

Sequence cautioni

The sequence CAA37827 differs from that shown. Reason: Frameshift at positions 291 and 306.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti316P → S in CAA43195 (PubMed:1889413).Curated1
Sequence conflicti586D → E in CAA41536 (PubMed:2542125).Curated1
Sequence conflicti648H → D in CAA37827 (PubMed:2060792).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58693 Genomic DNA. Translation: CAA41536.1.
X53830 Genomic DNA. Translation: CAA37827.1. Frameshift.
X60780 Genomic DNA. Translation: CAA43195.1.
X63268 Genomic DNA. Translation: CAA44917.1.
Z49810 Genomic DNA. Translation: CAA89945.1.
BK006946 Genomic DNA. Translation: DAA09892.1.
PIRiS16706.
RefSeqiNP_013707.1. NM_001182362.1.

Genome annotation databases

EnsemblFungiiYML007W; YML007W; YML007W.
GeneIDi855005.
KEGGisce:YML007W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58693 Genomic DNA. Translation: CAA41536.1.
X53830 Genomic DNA. Translation: CAA37827.1. Frameshift.
X60780 Genomic DNA. Translation: CAA43195.1.
X63268 Genomic DNA. Translation: CAA44917.1.
Z49810 Genomic DNA. Translation: CAA89945.1.
BK006946 Genomic DNA. Translation: DAA09892.1.
PIRiS16706.
RefSeqiNP_013707.1. NM_001182362.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SSENMR-A279-313[»]
B565-650[»]
ProteinModelPortaliP19880.
SMRiP19880.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35163. 171 interactors.
DIPiDIP-1752N.
IntActiP19880. 41 interactors.
MINTiMINT-505627.

PTM databases

iPTMnetiP19880.

Proteomic databases

MaxQBiP19880.
PRIDEiP19880.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML007W; YML007W; YML007W.
GeneIDi855005.
KEGGisce:YML007W.

Organism-specific databases

EuPathDBiFungiDB:YML007W.
SGDiS000004466. YAP1.

Phylogenomic databases

GeneTreeiENSGT00530000069148.
HOGENOMiHOG000142347.
InParanoidiP19880.
KOiK09043.
OMAiCSERGVV.
OrthoDBiEOG092C4KCZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-32612-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP19880.
PROiP19880.

Family and domain databases

Gene3Di1.10.238.100. 1 hit.
InterProiIPR004827. bZIP.
IPR013910. TF_PAP1.
IPR023167. Yap1_redox_dom.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
PF08601. PAP1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiYAP1_YEAST
AccessioniPrimary (citable) accession number: P19880
Secondary accession number(s): D6VZG8, P22631, Q06840
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: November 30, 2016
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

One of 8 closely related fungi-specific YAP proteins (YAP1 to YAP8), which all seem to be transcription activators of the environmental stress response and metabolism control pathways and to have similar but not identical DNA binding specificities.
Present with 1600 molecules/cell in log phase SD medium.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.