P19880 (YAP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AP-1-like transcription factor YAP1

Alternative name(s):
Phenanthroline resistance protein PAR1
Pleiotropic drug resistance protein PDR4

Gene names

Name:	YAP1
Synonyms:	PAR1, PDR4, SNQ3
Ordered Locus Names:	YML007W
ORF Names:	YM9571.12

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	650 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Subunit structure	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. Ref.9 Ref.15 Ref.21
Subcellular location	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. Ref.16 Ref.22
Induction	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.
Domain	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. Ref.8
Post-translational modification	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.
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.
Sequence similarities	Belongs to the bZIP family. YAP subfamily. Contains 1 bZIP (basic-leucine zipper) domain.
Sequence caution	The sequence CAA37827.1 differs from that shown. Reason: Frameshift at positions 291 and 306.

Ontologies

Keywords
Biological process	Cadmium resistance Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Disulfide bond Oxidation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance Inferred from mutant phenotype PubMed 15575969. Source: SGD regulation of transcription from RNA polymerase II promoter in response to oxidative stress Inferred from direct assay PubMed 11056165. Source: SGD response to cadmium ion Inferred from electronic annotation. Source: UniProtKB-KW response to drug Inferred from mutant phenotype PubMed 15713640. Source: SGD response to heat Inferred from mutant phenotype PubMed 10809786. Source: SGD response to metal ion Inferred from mutant phenotype PubMed 8360174. Source: SGD response to singlet oxygen Inferred from mutant phenotype PubMed 16862604. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 11914276Ref.18PubMed 22842922Ref.22. Source: SGD nucleus Inferred from direct assay PubMed 11914276Ref.18PubMed 22842922Ref.22. Source: SGD
Molecular_function	sequence-specific DNA binding Inferred from direct assay PubMed 19158363. Source: SGD sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 11056165. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YBP1	P38315	4	EBI-31265,EBI-20985

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 650

650

AP-1-like transcription factor YAP1

PRO_0000076521

Regions

Domain

64 – 127

64

bZIP

Region

67 – 90

24

Basic motif By similarity

Region

92 – 120

29

Leucine-zipper By similarity

Region

220 – 378

159

Transcription activation 1

Region

430 – 537

108

Transcription activation 2

Motif

5 – 16

12

Nuclear localization signal

Motif

50 – 59

10

Nuclear localization signal

Motif

614 – 621

8

Nuclear export signal

Compositional bias

411 – 414

4

Poly-Asn

Compositional bias

517 – 521

5

Poly-Asp

Amino acid modifications

Modified residue

14

1

Phosphoserine Ref.28 Ref.29 Ref.32

Modified residue

17

1

Phosphoserine Ref.32

Modified residue

204

1

Phosphoserine Ref.31 Ref.32

Modified residue

372

1

Phosphoserine Ref.32

Modified residue

403

1

Phosphoserine Ref.32

Modified residue

503

1

Phosphoserine Ref.31 Ref.32

Modified residue

504

1

Phosphoserine Ref.30 Ref.32

Modified residue

528

1

Phosphoserine Ref.29 Ref.31 Ref.32

Modified residue

532

1

Phosphoserine Ref.32

Modified residue

533

1

Phosphoserine Ref.32

Modified residue

594

1

Phosphoserine Ref.31

Disulfide bond

303 ↔ 598

In nuclear retained form; alternate Ref.19 Ref.20

Disulfide bond

310 ↔ 629

In nuclear retained form; alternate Ref.19 Ref.20

Disulfide bond

598 ↔ 629

In nuclear retained form; alternate Ref.19 Ref.20

Disulfide bond

598 ↔ 620

In nuclear retained form; alternate Ref.19 Ref.20

Disulfide bond

598

Interchain (with C-36 in HYR1); transient Ref.19 Ref.20

Disulfide bond

620 ↔ 629

In nuclear retained form; alternate Ref.19 Ref.20

Experimental info

Mutagenesis

78

1

Q → A: Dominant negative transcription activator. Ref.8

Mutagenesis

620

1

C → T: Constitutive nuclear location and transcription activation. Ref.22

Sequence conflict

316

1

P → S in CAA43195. Ref.4

Sequence conflict

586

1

D → E in CAA41536. Ref.1

Sequence conflict

648

1

H → D in CAA37827. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

650

Helix Strand Turn

Details...

Helix

289 – 291

3

Beta strand

292 – 294

3

Beta strand

298 – 300

3

Helix

301 – 308

8

Helix

598 – 606

9

Helix

616 – 623

8

Turn

624 – 626

3

Helix

638 – 646

9

Sequences

	Sequence		Length	Mass (Da)
	P19880 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 192F20FA71027688	FASTA	650	72,533
	10 20 30 40 50 60 MSVSTAKRSL DVVSPGSLAE FEGSKSRHDE IENEHRRTGT RDGEDSEQPK KKGSKTSKKQ 70 80 90 100 110 120 DLDPETKQKR TAQNRAAQRA FRERKERKMK ELEKKVQSLE SIQQQNEVEA TFLRDQLITL 130 140 150 160 170 180 VNELKKYRPE TRNDSKVLEY LARRDPNLHF SKNNVNHSNS EPIDTPNDDI QENVKQKMNF 190 200 210 220 230 240 TFQYPLDNDN DNDNSKNVGK QLPSPNDPSH SAPMPINQTQ KKLSDATDSS SATLDSLSNS 250 260 270 280 290 300 NDVLNNTPNS STSMDWLDNV IYTNRFVSGD DGSNSKTKNL DSNMFSNDFN FENQFDEQVS 310 320 330 340 350 360 EFCSKMNQVC GTRQCPIPKK PISALDKEVF ASSSILSSNS PALTNTWESH SNITDNTPAN 370 380 390 400 410 420 VIATDATKYE NSFSGFGRLG FDMSANHYVV NDNSTGSTDS TGSTGNKNKK NNNNSDDVLP 430 440 450 460 470 480 FISESPFDMN QVTNFFSPGS TGIGNNAASN TNPSLLQSSK EDIPFINANL AFPDDNSTNI 490 500 510 520 530 540 QLQPFSESQS QNKFDYDMFF RDSSKEGNNL FGEFLEDDDD DKKAANMSDD ESSLIKNQLI 550 560 570 580 590 600 NEEPELPKQY LQSVPGNESE ISQKNGSSLQ NADKINNGND NDNDNDVVPS KEGSLLRCSE 610 620 630 640 650 IWDRITTHPK YSDIDVDGLC SELMAKAKCS ERGVVINAED VQLALNKHMN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast YAP1 encodes a novel form of the jun family of transcriptional activator proteins." Moye-Rowley W.S., Harshman K.D., Parker C.S. Genes Dev. 3:283-292(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization of PDR4, a Saccharomyces cerevisiae gene that confers pleiotropic drug resistance in high-copy number: identity with YAP1, encoding a transcriptional activator." Hussain M., Lenard J. Gene 101:149-152(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The SNQ3 gene of Saccharomyces cerevisiae confers hyper-resistance to several functionally unrelated chemicals." Hertle K., Haase E., Brendel M. Curr. Genet. 19:429-433(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Identification and characterization of a Saccharomyces cerevisiae gene (PAR1) conferring resistance to iron chelators." Schnell N., Entian K.-D. Eur. J. Biochem. 200:487-493(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"The PAR1 (YAP1/SNQ3) gene of Saccharomyces cerevisiae, a c-jun homologue, is involved in oxygen metabolism." Schnell N., Krems B., Entian K.-D. Curr. Genet. 21:269-273(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Transcriptional activation mediated by the yeast AP-1 protein is required for normal cadmium tolerance." Wemmie J.A., Wu A.L., Harshman K.D., Parker C.S., Moye-Rowley W.S. J. Biol. Chem. 269:14690-14697(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TRANSCRIPTION ACTIVATION DOMAIN, MUTAGENESIS OF GLN-78.
[9]	"Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on polyribosomes with Gcn1." Wout P.K., Sattlegger E., Sullivan S.M., Maddock J.R. Eukaryot. Cell 8:1061-1071(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBG1.
[10]	"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.
[11]	"Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor." Yan C., Lee L.H., Davis L.I. EMBO J. 17:7416-7429(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, NUCLEAR EXPORT BY CRM1, NUCLEAR EXPORT SIGNAL.
[12]	"The yeast transcription factor genes YAP1 and YAP2 are subject to differential control at the levels of both translation and mRNA stability." Vilela C., Linz B., Rodrigues-Pousada C., McCarthy J.E. Nucleic Acids Res. 26:1150-1159(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, POST-TRANSCRIPTIONAL EXPRESSION CONTROL.
[13]	"Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast." Lee J., Godon C., Lagniel G., Spector D., Garin J., Labarre J., Toledano M.B. J. Biol. Chem. 274:16040-16046(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COOPERATIVITY WITH SKN7, YAP1 DEPENDENT GENES.
[14]	"H2O2 sensing through oxidation of the Yap1 transcription factor." Delaunay A., Isnard A.D., Toledano M.B. EMBO J. 19:5157-5166(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, REDUCTION BY THIOREDOXINS.
[15]	"Nuclear import of the yeast AP-1-like transcription factor Yap1p is mediated by transport receptor Pse1p, and this import step is not affected by oxidative stress." Isoyama T., Murayama A., Nomoto A., Kuge S. J. Biol. Chem. 276:21863-21869(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, NUCLEAR IMPORT, INTERACTION WITH PSE1.
[16]	"Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation." Kuge S., Arita M., Murayama A., Maeta K., Izawa S., Inoue Y., Nomoto A. Mol. Cell. Biol. 21:6139-6150(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]	"A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation." Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B. Cell 111:471-481(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, OXIDATION BY HYR1/GPX3.
[18]	"Yap1 accumulates in the nucleus in response to carbon stress in Saccharomyces cerevisiae." Wiatrowski H.A., Carlson M. Eukaryot. Cell 2:19-26(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"The redox domain of the Yap1p transcription factor contains two disulfide bonds." Wood M.J., Andrade E.C., Storz G. Biochemistry 42:11982-11991(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, OXIDATION, DISULFIDE BONDS.
[20]	"Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling." Azevedo D., Tacnet F., Delaunay A., Rodrigues-Pousada C., Toledano M.B. Free Radic. Biol. Med. 35:889-900(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ELICITOR SPECIFIC DISULFIDE BONDS.
[21]	"Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor." Veal E.A., Ross S.J., Malakasi P., Peacock E., Morgan B.A. J. Biol. Chem. 278:30896-30904(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH YBP1.
[22]	"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: MUTAGENESIS OF CYS-620, SUBCELLULAR LOCATION.
[23]	"A large-scale study of Yap1p-dependent genes in normal aerobic and H2O2-stress conditions: the role of Yap1p in cell proliferation control in yeast." Dumond H., Danielou N., Pinto M., Bolotin-Fukuhara M. Mol. Microbiol. 36:830-845(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TRANSCRIPTION PROFILING.
[24]	"Genomic expression programs in the response of yeast cells to environmental changes." Gasch A.P., Spellman P.T., Kao C.M., Carmel-Harel O., Eisen M.B., Storz G., Botstein D., Brown P.O. Mol. Biol. Cell 11:4241-4257(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TRANSCRIPTION PROFILING.
[25]	"Transcription factors regulating the response to oxidative stress in yeast." Moye-Rowley W.S. Antioxid. Redox Signal. 4:123-140(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[26]	"Thiol-based regulatory switches." Paget M.S., Buttner M.J. Annu. Rev. Genet. 37:91-121(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[27]	"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].
[28]	"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-14, MASS SPECTROMETRY. Strain: YAL6B.
[29]	"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-14 AND SER-528, MASS SPECTROMETRY. Strain: ADR376.
[30]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, MASS SPECTROMETRY.
[31]	"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-204; SER-503; SER-528 AND SER-594, MASS SPECTROMETRY.
[32]	"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-14; SER-17; SER-204; SER-372; SER-403; SER-503; SER-504; SER-528; SER-532 AND SER-533, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

S16706.

RefSeq

NP_013707.1. NM_001182362.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SSE	NMR	-	A	279-313	[»]
			B	565-650	[»]

ProteinModelPortal

P19880.

SMR

P19880. Positions 63-125, 279-313, 565-650.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1752N.

IntAct

P19880. 40 interactions.

MINT

MINT-505627.

Proteomic databases

PaxDb

P19880.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YML007W; YML007W; YML007W.

GeneID

855005.

KEGG

sce:YML007W.

Organism-specific databases

CYGD

YML007w.

SGD

S000004466. YAP1.

Phylogenomic databases

eggNOG

NOG72873.

GeneTree

ENSGT00530000069148.

HOGENOM

HOG000142347.

KO

K09043.

OMA

WDRITAH.

OrthoDB

EOG43R6XD.

Gene expression databases

Genevestigator

P19880.

GermOnline

YML007W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.238.100. 1 hit.

InterPro

IPR004827. bZIP.
IPR013910. TF_PAP1.
IPR023167. Yap1_redox_dom.
[Graphical view]

Pfam

PF00170. bZIP_1. 1 hit.
PF08601. PAP1. 1 hit.
[Graphical view]

SMART

SM00338. BRLZ. 1 hit.
[Graphical view]

PROSITE

PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P19880.

NextBio

978163.

Entry information

Entry name

YAP1_YEAST

Accession

Primary (citable) accession number: P19880
Secondary accession number(s): D6VZG8, P22631, Q06840

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program