CPLM-003821

Genbank Nucleotide ID

Protein Synonyms/Alias

Trx; ATL-derived factor; ADF

Mus musculus (Mouse)

Position	Peptide	Type	References
3	*****MVKLIESKEA	acetylation	[1, 2]
8	MVKLIESKEAFQEAL	acetylation	[1, 3, 4, 5]
8	MVKLIESKEAFQEAL	succinylation	[5]
8	MVKLIESKEAFQEAL	ubiquitination	[6]
39	CGPCKMIKPFFHSLC	acetylation	[1, 2, 4, 5, 7, 8]
39	CGPCKMIKPFFHSLC	succinylation	[5]
39	CGPCKMIKPFFHSLC	ubiquitination	[6]
81	MPTFQFYKKGQKVGE	acetylation	[1, 2]
85	QFYKKGQKVGEFSGA	acetylation	[5]
85	QFYKKGQKVGEFSGA	succinylation	[5]
94	GEFSGANKEKLEASI	acetylation	[1, 5, 7]
94	GEFSGANKEKLEASI	succinylation	[5]
96	FSGANKEKLEASITE	acetylation	[7]

[1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[3] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
[4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[8] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]

Functional Description

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (By similarity).

DOMAIN 2 105 Thioredoxin.
ACT_SITE 32 32 Nucleophile (By similarity).
ACT_SITE 35 35 Nucleophile (By similarity).
MOD_RES 3 3 N6-acetyllysine (By similarity).
MOD_RES 39 39 N6-acetyllysine (By similarity).
MOD_RES 62 62 S-nitrosocysteine (By similarity).
MOD_RES 69 69 S-nitrosocysteine (By similarity).
MOD_RES 73 73 S-nitrosocysteine; alternate (By
DISULFID 32 35 Redox-active (By similarity).
DISULFID 73 73 Interchain; alternate (By similarity).

Acetylation; Activator; Complete proteome; Cytoplasm; Disulfide bond; Electron transport; Nucleus; Redox-active center; Reference proteome; S-nitrosylation; Secreted; Transcription; Transcription regulation; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030424; C:axon; IEA:Compara.
GO:0005829; C:cytosol; IDA:MGI.
GO:0030425; C:dendrite; IEA:Compara.
GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:MGI.
GO:0043025; C:neuronal cell body; IEA:Compara.
GO:0005634; C:nucleus; IDA:MGI.
GO:0009055; F:electron carrier activity; IEA:InterPro.
GO:0015037; F:peptide disulfide oxidoreductase activity; IDA:MGI.
GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO:0016999; P:antibiotic metabolic process; IEA:Compara.
GO:0045454; P:cell redox homeostasis; IDA:MGI.
GO:0035690; P:cellular response to drug; IEA:Compara.
GO:0071333; P:cellular response to glucose stimulus; IEA:Compara.
GO:0071455; P:cellular response to hyperoxia; IEA:Compara.
GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
GO:0046826; P:negative regulation of protein export from nucleus; IDA:MGI.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
GO:0033158; P:regulation of protein import into nucleus, translocation; ISS:UniProtKB.
GO:0014823; P:response to activity; IEA:Compara.
GO:0048678; P:response to axon injury; IEA:Compara.
GO:0071548; P:response to dexamethasone stimulus; IEA:Compara.
GO:0009314; P:response to radiation; ISS:UniProtKB.
GO:0010269; P:response to selenium ion; IEA:Compara.
GO:0097068; P:response to thyroxine stimulus; IEA:Compara.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR005746; Thioredoxin.
IPR012336; Thioredoxin-like_fold.
IPR017937; Thioredoxin_CS.
IPR013766; Thioredoxin_domain.

PF00085; Thioredoxin

PS00194; THIOREDOXIN_1
PS51352; THIOREDOXIN_2

PR00421; THIOREDOXIN.