Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Thioredoxin domain-containing protein 17  

UniProtKB / Swiss-Prot ID :  TXD17_HUMAN

Gene Name (Synonyms) : 
TXNDC17, TXNL5  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  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. 

Protein Sequence MARYEEVSVSGFEEFHRAVEQHNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQ...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MARYEE
---
23.82UniProtKB
Link-
25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QHNGKTIFA
43.71Phosphositeplus
Link
26PhosphothreonineHNGKTIFAY
23.79HPRD
Link
26PhosphothreonineHNGKTIFAY
23.79Phosphositeplus
Link
30PhosphotyrosineTIFAYFTGS
7.30HPRD
Link
30PhosphotyrosineTIFAYFTGS
7.30Phosphositeplus
Link
32PhosphothreonineFAYFTGSKD
28.06HPRD
Link
32PhosphothreonineFAYFTGSKD
28.06Phosphositeplus
Link
34PhosphoserineYFTGSKDAG
25.06HPRD
Link
34PhosphoserineYFTGSKDAG
25.06Phosphositeplus
Link
78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KPYWKDPNN
58.42Phosphositeplus
Link
78N6-acetyllysineKPYWKDPNN
58.42HPRD
Link
78N6-acetyllysineKPYWKDPNN
58.42Phosphositeplus
Link
78N6-acetyllysine.KPYWKDPNN
58.42UniProtKB
Link
89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RKNLKVTAV
47.11Phosphositeplus
Link
98Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PTLLKYGTP
44.75Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
INS_HUMANin vitroHPRD:11656HPRD14607844
NEU2_HUMANin vitroHPRD:11656HPRD14607844
DYL1_HUMANin vitroHPRD:11656HPRD14607843
TRXR1_HUMANin vitroHPRD:11656HPRD14607844
NEU1_HUMANin vitroHPRD:11656HPRD14607844
INS_HUMANENSP00000250101STRING
INS_HUMANENSP00000250101STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures