YEAST:TRX2

From GONUTS

Jump to: navigation, search

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (taxon:559292)
Gene Name(s)	TRX2 ( synonyms: TRX1 )
Protein Name(s)	Thioredoxin-2 Thioredoxin II TR-II Thioredoxin-1
External Links
UniProt Identifier	TRX2_YEAST
UniProt Accessions	P22803, D6VUZ2,
EMBL	M59168, M62648, U40843, Z49133, Z72994, AY557817, BK006941,
PIR	S15049,
RefSeq	NP_011725.1,
PDB	2FA4, 2HSY, 3PIN,
IntAct	P22803,
Pfam	PF00085,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C
	GO:0045454	cell redox homeostasis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017936	P
	GO:0009263	deoxyribonucleotide biosynthetic process	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0215	P
	GO:0000103	sulfate assimilation	PMID:2026619^[1]	IGI: Inferred from Genetic Interaction	SGD:S000004033	P
	GO:0006890	retrograde vesicle-mediated transport, Golgi to ER	PMID:9813082^[2]	IDA: Inferred from Direct Assay		P
	GO:0006888	ER to Golgi vesicle-mediated transport	PMID:9813082^[2]	IDA: Inferred from Direct Assay		P
	GO:0000139	Golgi membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0134	C
	GO:0005829	cytosol	PMID:8603912^[3]	IDA: Inferred from Direct Assay		C
	GO:0080058	protein deglutathionylation	PMID:20074363^[4]	IGI: Inferred from Genetic Interaction	SGD:S000004033	P
	GO:0045454	cell redox homeostasis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013766	P
	GO:0015031	protein transport	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0653	P
	GO:0005515	protein binding	PMID:11805837^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P38885	F
	GO:0045454	cell redox homeostasis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017937	P
	GO:0045454	cell redox homeostasis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005746	P
	GO:0042144	vacuole fusion, non-autophagic	PMID:9657146^[6]	IDA: Inferred from Direct Assay		P
	GO:0000011	vacuole inheritance	PMID:8603912^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0080058	protein deglutathionylation	PMID:20074363^[4]	IDA: Inferred from Direct Assay		P
	GO:0005515	protein binding	PMID:16272220^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P34760	F
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C
	GO:0005794	Golgi apparatus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0333	C
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005515	protein binding	PMID:11283351^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P05318	F
	GO:0006662	glycerol ether metabolic process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005746	P
	GO:0045454	cell redox homeostasis	PMID:11169096^[9]	TAS: Traceable Author Statement		P
	GO:0005515	protein binding	PMID:16272220^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P38013	F
	GO:0000324	fungal-type vacuole	PMID:9657146^[6]	IPI: Inferred from Physical Interaction		C
	GO:0009055	electron carrier activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005746	F
	GO:0000011	vacuole inheritance	PMID:9015301^[10]	IMP: Inferred from Mutant Phenotype		P
	GO:0022900	electron transport chain	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0249	P
	GO:0006810	transport	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0813	P
	GO:0006275	regulation of DNA replication	PMID:7929110^[11]	IGI: Inferred from Genetic Interaction	SGD:S000004033	P
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0015035	protein disulfide oxidoreductase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005746	F
	GO:0000011	vacuole inheritance	PMID:8603912^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0000011	vacuole inheritance	PMID:9015301^[10]	IMP: Inferred from Mutant Phenotype		P
	GO:0000103	sulfate assimilation	PMID:2026619^[1]	IGI: Inferred from Genetic Interaction	SGD:S000004033	P
	GO:0000139	Golgi membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0134	C
	GO:0000324	fungal-type vacuole	PMID:9657146^[6]	IPI: Inferred from Physical Interaction		C
	GO:0005515	protein binding	PMID:11283351^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P05318	F
	GO:0005515	protein binding	PMID:11805837^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P38885	F
	GO:0005515	protein binding	PMID:16272220^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P34760	F
	GO:0005515	protein binding	PMID:16272220^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P38013	F
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C
	GO:0005794	Golgi apparatus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0333	C
	GO:0005829	cytosol	PMID:8603912^[3]	IDA: Inferred from Direct Assay		C
	GO:0006275	regulation of DNA replication	PMID:7929110^[11]	IGI: Inferred from Genetic Interaction	SGD:S000004033	P
	GO:0006662	glycerol ether metabolic process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005746	P
	GO:0006810	transport	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0813	P
	GO:0006888	ER to Golgi vesicle-mediated transport	PMID:9813082^[2]	IDA: Inferred from Direct Assay		P
	GO:0006890	retrograde vesicle-mediated transport, Golgi to ER	PMID:9813082^[2]	IDA: Inferred from Direct Assay		P
	GO:0009055	electron carrier activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005746	F
	GO:0009263	deoxyribonucleotide biosynthetic process	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0215	P
	GO:0015031	protein transport	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0653	P
	GO:0015035	protein disulfide oxidoreductase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005746	F
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0022900	electron transport chain	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0249	P
	GO:0042144	vacuole fusion, non-autophagic	PMID:9657146^[6]	IDA: Inferred from Direct Assay		P
	GO:0045454	cell redox homeostasis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005746	P
	GO:0045454	cell redox homeostasis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013766	P
	GO:0045454	cell redox homeostasis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017937	P
	GO:0045454	cell redox homeostasis	PMID:11169096^[9]	TAS: Traceable Author Statement		P
	GO:0080058	protein deglutathionylation	PMID:20074363^[4]	IDA: Inferred from Direct Assay		P
	GO:0080058	protein deglutathionylation	PMID:20074363^[4]	IGI: Inferred from Genetic Interaction	SGD:S000004033	P
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Muller EG (1991) Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. J Biol Chem 266: 9194-202 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Spang A & Schekman R (1998) Reconstitution of retrograde transport from the Golgi to the ER in vitro. J Cell Biol 143: 589-99 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Xu Z & Wickner W (1996) Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae. J Cell Biol 132: 787-94 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Greetham D et al. (2010) Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae. BMC Biochem 11: 3 PubMed GONUTS page
↑ ^5.0 ^5.1 Ho Y et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415: 180-3 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Xu Z et al. (1998) LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell 93: 1125-34 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Vignols F et al. (2005) A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo. Proc Natl Acad Sci U S A 102: 16729-34 PubMed GONUTS page
↑ ^8.0 ^8.1 Ito T et al. (2001) A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci U S A 98: 4569-74 PubMed GONUTS page
↑ ^9.0 ^9.1 Grant CM (2001) Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol Microbiol 39: 533-41 PubMed GONUTS page
↑ ^10.0 ^10.1 Xu Z et al. (1997) A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to promote yeast vacuole inheritance. J Cell Biol 136: 299-306 PubMed GONUTS page
↑ ^11.0 ^11.1 Muller EG (1994) Deoxyribonucleotides are maintained at normal levels in a yeast thioredoxin mutant defective in DNA synthesis. J Biol Chem 269: 24466-71 PubMed GONUTS page

[PMID:2026619-0] 1.0 ^1.1 Muller EG (1991) Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. J Biol Chem 266: 9194-202 PubMed GONUTS page

[PMID:9813082-1] 2.0 ^2.1 ^2.2 ^2.3 Spang A & Schekman R (1998) Reconstitution of retrograde transport from the Golgi to the ER in vitro. J Cell Biol 143: 589-99 PubMed GONUTS page

[PMID:8603912-2] 3.0 ^3.1 ^3.2 ^3.3 Xu Z & Wickner W (1996) Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae. J Cell Biol 132: 787-94 PubMed GONUTS page

[PMID:20074363-3] 4.0 ^4.1 ^4.2 ^4.3 Greetham D et al. (2010) Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae. BMC Biochem 11: 3 PubMed GONUTS page

[PMID:11805837-4] 5.0 ^5.1 Ho Y et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415: 180-3 PubMed GONUTS page

[PMID:9657146-5] 6.0 ^6.1 ^6.2 ^6.3 Xu Z et al. (1998) LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell 93: 1125-34 PubMed GONUTS page

[PMID:16272220-6] 7.0 ^7.1 ^7.2 ^7.3 Vignols F et al. (2005) A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo. Proc Natl Acad Sci U S A 102: 16729-34 PubMed GONUTS page

[PMID:11283351-7] 8.0 ^8.1 Ito T et al. (2001) A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci U S A 98: 4569-74 PubMed GONUTS page

[PMID:11169096-8] 9.0 ^9.1 Grant CM (2001) Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol Microbiol 39: 533-41 PubMed GONUTS page

[PMID:9015301-9] 10.0 ^10.1 Xu Z et al. (1997) A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to promote yeast vacuole inheritance. J Cell Biol 136: 299-306 PubMed GONUTS page

[PMID:7929110-10] 11.0 ^11.1 Muller EG (1994) Deoxyribonucleotides are maintained at normal levels in a yeast thioredoxin mutant defective in DNA synthesis. J Biol Chem 269: 24466-71 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

YEAST:TRX2

Contents

Annotations

Notes

References

c

d

e

f

g

m

n

p

p cont.

r

s

t

v

Personal tools

Namespaces

Variants

Views

Actions

Search

Navigation

Cacao

Journal Clubs

page contributors

Toolbox