CPLM-020068

Genbank Nucleotide ID

Thioredoxin domain-containing protein 17

Protein Synonyms/Alias

14 kDa thioredoxin-related protein; TRP14; Protein 42-9-9; Thioredoxin-like protein 5

Homo sapiens (Human)

Position	Peptide	Type	References
25	AVEQHNGKTIFAYFT	ubiquitination	[1, 2]
35	FAYFTGSKDAGGKSW	ubiquitination	[1, 2]
40	GSKDAGGKSWCPDCV	ubiquitination	[3, 4]
78	VGEKPYWKDPNNDFR	acetylation	[5]
78	VGEKPYWKDPNNDFR	ubiquitination	[1, 2, 6]
89	NDFRKNLKVTAVPTL	ubiquitination	[1, 2, 3, 4, 6, 7]
98	TAVPTLLKYGTPQKL	ubiquitination	[1, 2, 3, 4, 6, 7, 8]

[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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[5] 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]
[6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]

Functional Description

Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.

DOMAIN 41 123 Thioredoxin.
ACT_SITE 43 43 Nucleophile.
ACT_SITE 46 46 Nucleophile.
MOD_RES 2 2 N-acetylalanine.
DISULFID 43 46 Redox-active.

3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Redox-active center; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; IDA:UniProtKB.
GO:0009055; F:electron carrier activity; IDA:UniProtKB.
GO:0004601; F:peroxidase activity; IDA:UniProtKB.
GO:0047134; F:protein-disulfide reductase activity; IDA:UniProtKB.
GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.

IPR010357; DUF953_thioredox.
IPR012336; Thioredoxin-like_fold.

PS00194; THIOREDOXIN_1
PS51352; THIOREDOXIN_2