UniProt Accession

 THIOM_HUMAN; Q99757; Q5JZA0; Q6FH60; Q9UH29 

Genbank Protein ID

 AF480262; U78678; AF276920; CR456601; CR541896; CR541917; AL022313; CH471095; BC013726; BC050610 

Genbank Nucleotide ID

 AAN05576.1; AAB41631.1; AAF86467.1; CAG30487.1; CAG46694.1; CAG46715.1; CAQ06700.1; EAW60103.1; AAH13726.1; AAH50610.1 

Protein Name

 Thioredoxin, mitochondrial 

Protein Synonyms/Alias

 MTRX; Mt-Trx; Thioredoxin-2 

Gene Name

 TXN2 

Gene Synonyms/Alias

 TRX2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
102	ILGPRLEKMVAKQHG	ubiquitination	[1]
152	VDKFVGIKDEDQLEA	acetylation	[2]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Could be involved in the resistance to anti-tumor agents. Possesses a dithiol-reducing activity. 

Sequence Annotation

 DOMAIN 61 166 Thioredoxin.
 ACT_SITE 90 90 Nucleophile (By similarity).
 ACT_SITE 93 93 Nucleophile (By similarity).
 MOD_RES 152 152 N6-acetyllysine.
 DISULFID 90 93 Redox-active.  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Disulfide bond; Electron transport; Mitochondrion; Redox-active center; Reference proteome; Transit peptide; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 166 AA 

Protein Sequence

Gene Ontology

 GO:0030425; C:dendrite; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0031669; P:cellular response to nutrient levels; IEA:Compara.
 GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
 GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
 GO:0048678; P:response to axon injury; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0009749; P:response to glucose stimulus; IEA:Compara.
 GO:0009725; P:response to hormone stimulus; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0007584; P:response to nutrient; IEA:Compara.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0006979; P:response to oxidative stress; IEA:Compara. 

Interpro

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

Pfam

 PF00085; Thioredoxin 

SMART

  

PROSITE

 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 

PRINTS

 PR00421; THIOREDOXIN.