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Protein

AP-1-like transcription activator YAP2

Gene

CAD1

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 closely related to YAP1. Like YAP1, its activity can be induced by cadmium and peroxide stress, probably involving similar mechanisms inducing nuclear accumulation and thus transcription activation. YAP2, like YAP1, preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3', but does not activate transcription of genes known to be activated by YAP1 in response to oxidative stress (such as TRX2, SSA1, GSH1). It is still not clear whether it is involved in oxidative stress response. When overexpressed, it confers pleiotropic drug-resistance and increases cellular tolerance to cadmium, iron chelators and zinc.4 Publications

GO - Molecular functioni

GO - Biological processi

  • cellular response to cadmium ion Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
  • transcription from RNA polymerase II promoter Source: GOC
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-29964-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1-like transcription activator YAP2
Alternative name(s):
Cadmium resistance protein 1
Transcription factor CAD1
Gene namesi
Name:CAD1
Synonyms:YAP2
Ordered Locus Names:YDR423C
ORF Names:D9461.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR423C.
SGDiS000002831. CAD1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409AP-1-like transcription activator YAP2PRO_0000076522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi356 ↔ 387In nuclear retained form; alternate
Disulfide bondi356 ↔ 378In nuclear retained form; alternate
Disulfide bondi378 ↔ 387In nuclear retained form; alternate

Post-translational modificationi

Oxidative stress inducing agents may induce a conformational change involving disulfide bond formation between the conserved cysteine residues of the n-CRD (Cys-356, Cys-378 and Cys-387), masking as a result the nuclear export signal and thus causing nuclear accumulation.By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP24813.
PeptideAtlasiP24813.

Expressioni

Inductioni

YAP2 expression is at least partially regulated at the level of mRNA stability. Two small upstream open reading frames (uORF) in its mRNA cause increased RNA decay. The translation initiation factor eIF2 counteracts this effect by causing reinitiation at the functional initiation site, thus suppressing RNA decay.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi32482. 34 interactions.
DIPiDIP-4491N.
IntActiP24813. 4 interactions.
MINTiMINT-539300.

Structurei

3D structure databases

ProteinModelPortaliP24813.
SMRiP24813. Positions 49-100, 356-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 10664bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 6924Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni71 – 9929Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Domaini

YAP2/CAD1 contains a C-terminal cysteine rich domain (c-CRD), but lacks the N-terminal CRD (n-CRD). It probably also contains embedded in the c-CRD a nuclear export signal, with which the nuclear export protein CRM1 may interact in the absence of disulfide bond formation within the c-CRD.

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00530000069148.
InParanoidiP24813.
KOiK09043.
OrthoDBiEOG7GFBHK.

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.

P24813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNILRKGQQ IYLAGDMKKQ MLLNKDGTPK RKVGRPGRKR IDSEAKSRRT
60 70 80 90 100
AQNRAAQRAF RDRKEAKMKS LQERVELLEQ KDAQNKTTTD FLLCSLKSLL
110 120 130 140 150
SEITKYRAKN SDDERILAFL DDLQEQQKRE NEKGTSTAVS KAAKELPSPN
160 170 180 190 200
SDENMTVNTS IEVQPHTQEN EKVMWNIGSW NAPSLTNSWD SPPGNRTGAV
210 220 230 240 250
TIGDESINGS EMPDFSLDLV SNDRQTGLEA LDYDIHNYFP QHSERLTAEK
260 270 280 290 300
IDTSACQCEI DQKYLPYETE DDTLFPSVLP LAVGSQCNNI CNRKCIGTKP
310 320 330 340 350
CSNKEIKCDL ITSHLLNQKS LASVLPVAAS HTKTIRTQSE AIEHISSAIS
360 370 380 390 400
NGKASCYHIL EEISSLPKYS SLDIDDLCSE LIIKAKCTDD CKIVVKARDL

QSALVRQLL
Length:409
Mass (Da):45,752
Last modified:October 1, 1993 - v2
Checksum:i21133AAAF40B0ED7
GO

Sequence cautioni

The sequence AAA34463.1 differs from that shown. Reason: Frameshift at positions 286 and 339. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361P → L in AAA34463 (PubMed:1514324).Curated
Sequence conflicti90 – 901D → N in AAA34463 (PubMed:1514324).Curated
Sequence conflicti102 – 1021E → K in AAA34463 (PubMed:1514324).Curated
Sequence conflicti125 – 1251E → Q in AAA34463 (PubMed:1514324).Curated
Sequence conflicti131 – 1311N → D in AAA34463 (PubMed:1514324).Curated
Sequence conflicti142 – 1421A → V in AAA34463 (PubMed:1514324).Curated
Sequence conflicti145 – 1451E → G in AAA34463 (PubMed:1514324).Curated
Sequence conflicti327 – 3271V → L in AAB29937 (PubMed:8107671).Curated
Sequence conflicti337 – 3371T → I in AAB29937 (PubMed:8107671).Curated
Sequence conflicti347 – 3471S → I in AAB29937 (PubMed:8107671).Curated
Sequence conflicti354 – 3541A → P in AAB29937 (PubMed:8107671).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14289 Unassigned DNA. Translation: AAA02920.1.
X69106 mRNA. Translation: CAA48858.1.
S68847 Genomic DNA. Translation: AAB29937.1.
U33007 Genomic DNA. Translation: AAB64878.1.
M58331 Genomic DNA. Translation: AAA34463.1. Frameshift.
BK006938 Genomic DNA. Translation: DAA12263.1.
PIRiA48890.
RefSeqiNP_010711.3. NM_001180731.3.

Genome annotation databases

EnsemblFungiiYDR423C; YDR423C; YDR423C.
GeneIDi852033.
KEGGisce:YDR423C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14289 Unassigned DNA. Translation: AAA02920.1.
X69106 mRNA. Translation: CAA48858.1.
S68847 Genomic DNA. Translation: AAB29937.1.
U33007 Genomic DNA. Translation: AAB64878.1.
M58331 Genomic DNA. Translation: AAA34463.1. Frameshift.
BK006938 Genomic DNA. Translation: DAA12263.1.
PIRiA48890.
RefSeqiNP_010711.3. NM_001180731.3.

3D structure databases

ProteinModelPortaliP24813.
SMRiP24813. Positions 49-100, 356-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32482. 34 interactions.
DIPiDIP-4491N.
IntActiP24813. 4 interactions.
MINTiMINT-539300.

Proteomic databases

MaxQBiP24813.
PeptideAtlasiP24813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR423C; YDR423C; YDR423C.
GeneIDi852033.
KEGGisce:YDR423C.

Organism-specific databases

EuPathDBiFungiDB:YDR423C.
SGDiS000002831. CAD1.

Phylogenomic databases

GeneTreeiENSGT00530000069148.
InParanoidiP24813.
KOiK09043.
OrthoDBiEOG7GFBHK.

Enzyme and pathway databases

BioCyciYEAST:G3O-29964-MONOMER.

Miscellaneous databases

PROiP24813.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast bZip proteins mediate pleiotropic drug and metal resistance."
    Wu A., Wemmie J.A., Edgington N.P., Goebl M., Guevara J.L., Moye-Rowley S.W.
    J. Biol. Chem. 268:18850-18858(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Overexpression of YAP2, coding for a new yAP protein, and YAP1 in Saccharomyces cerevisiae alleviates growth inhibition caused by 1,10-phenanthroline."
    Bossier P., Fernandes L., Rocha D., Rodrigues-Pousada C.
    J. Biol. Chem. 268:23640-23645(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: W303A.
  3. "Stress-induced transcriptional activation mediated by YAP1 and YAP2 genes that encode the Jun family of transcriptional activators in Saccharomyces cerevisiae."
    Hirata D., Yano K., Miyakawa T.
    Mol. Gen. Genet. 242:250-256(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OXIDATIVE STRESS RESPONSE OF YAP2.
    Strain: ATCC 200060 / W303.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Molecular cloning and analysis of autonomous replicating sequence of Candida maltosa."
    Sasnauskas K., Jomantiene R., Lebediene E., Lebedys J., Januska A., Janulaitis A.
    Yeast 8:253-259(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-363.
    Strain: ATCC 64665 / S288c / DC5.
  7. "The role of the YAP1 and YAP2 genes in the regulation of the adaptive oxidative stress responses of Saccharomyces cerevisiae."
    Stephen D.W., Rivers S.L., Jamieson D.J.
    Mol. Microbiol. 16:415-423(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, OXIDATIVE STRESS RESPONSE OF YAP2.
  8. "Yap, a novel family of eight bZIP proteins in Saccharomyces cerevisiae with distinct biological functions."
    Fernandes L., Rodrigues-Pousada C., Struhl K.
    Mol. Cell. Biol. 17:6982-6993(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  9. "Regulation of yAP-1 nuclear localization in response to oxidative stress."
    Kuge S., Jones N., Nomoto A.
    EMBO J. 16:1710-1720(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Post-termination ribosome interactions with the 5'UTR modulate yeast mRNA stability."
    Vilela C., Ramirez C.V., Linz B., Rodrigues-Pousada C., McCarthy J.E.
    EMBO J. 18:3139-3152(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, POST-TRANSCRIPTIONAL EXPRESSION CONTROL.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYAP2_YEAST
AccessioniPrimary (citable) accession number: P24813
Secondary accession number(s): D6VT53, Q02259
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 155 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 623 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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