TXD17_HUMAN - dbPTM
TXD17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TXD17_HUMAN
UniProt AC Q9BRA2
Protein Name Thioredoxin domain-containing protein 17
Gene Name TXNDC17
Organism Homo sapiens (Human).
Sequence Length 123
Subcellular Localization Cytoplasm .
Protein 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..
Protein Sequence MARYEEVSVSGFEEFHRAVEQHNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNNDFRKNLKVTAVPTLLKYGTPQKLVESECLQANLVEMLFSED
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MARYEEVSV
------CCCCEEEEC
23.8219413330
8PhosphorylationMARYEEVSVSGFEEF
CCCCEEEECCCHHHH
17.5325849741
25SuccinylationAVEQHNGKTIFAYFT
HHHHHCCCEEEEEEE
43.7123954790
25AcetylationAVEQHNGKTIFAYFT
HHHHHCCCEEEEEEE
43.7126051181
25UbiquitinationAVEQHNGKTIFAYFT
HHHHHCCCEEEEEEE
43.7121890473
26PhosphorylationVEQHNGKTIFAYFTG
HHHHCCCEEEEEEEC
23.7920068231
30PhosphorylationNGKTIFAYFTGSKDA
CCCEEEEEEECCCCC
7.3028152594
32PhosphorylationKTIFAYFTGSKDAGG
CEEEEEEECCCCCCC
28.0628152594
34PhosphorylationIFAYFTGSKDAGGKS
EEEEEECCCCCCCCC
25.0628152594
35UbiquitinationFAYFTGSKDAGGKSW
EEEEECCCCCCCCCC
53.6021890473
35AcetylationFAYFTGSKDAGGKSW
EEEEECCCCCCCCCC
53.6026051181
40AcetylationGSKDAGGKSWCPDCV
CCCCCCCCCCCCCCC
39.6123749302
40UbiquitinationGSKDAGGKSWCPDCV
CCCCCCCCCCCCCCC
39.61-
46GlutathionylationGKSWCPDCVQAEPVV
CCCCCCCCCCCHHHH
1.1522555962
74AcetylationIYCQVGEKPYWKDPN
EEEEECCCCCCCCCC
37.1627452117
78AcetylationVGEKPYWKDPNNDFR
ECCCCCCCCCCCHHH
58.4223954790
78UbiquitinationVGEKPYWKDPNNDFR
ECCCCCCCCCCCHHH
58.4221906983
89AcetylationNDFRKNLKVTAVPTL
CHHHHHCCCCCCCCH
47.1125953088
89UbiquitinationNDFRKNLKVTAVPTL
CHHHHHCCCCCCCCH
47.1121890473
91PhosphorylationFRKNLKVTAVPTLLK
HHHHCCCCCCCCHHH
21.9823911959
95PhosphorylationLKVTAVPTLLKYGTP
CCCCCCCCHHHHCCC
37.8227067055
98UbiquitinationTAVPTLLKYGTPQKL
CCCCCHHHHCCCHHH
44.7521890473
98AcetylationTAVPTLLKYGTPQKL
CCCCCHHHHCCCHHH
44.7525038526
104UbiquitinationLKYGTPQKLVESECL
HHHCCCHHHHHHHHH
56.56-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TXD17_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TXD17_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TXD17_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INS_HUMANINSphysical
14607844
NEU1_HUMANOXTphysical
14607844
NEU2_HUMANAVPphysical
14607844
DYL1_HUMANDYNLL1physical
14607843
COF1_HUMANCFL1physical
14607843
WDR1_HUMANWDR1physical
22939629
TYSY_HUMANTYMSphysical
22939629
TXNL1_HUMANTXNL1physical
22939629
VINEX_HUMANSORBS3physical
22939629
UBP3_HUMANUSP3physical
22939629
UBE2H_HUMANUBE2Hphysical
22939629
UBP5_HUMANUSP5physical
22939629
UBA3_HUMANUBA3physical
22939629
UBE2N_HUMANUBE2Nphysical
22939629
UBE2K_HUMANUBE2Kphysical
22939629
VATA_HUMANATP6V1Aphysical
22939629
VATC1_HUMANATP6V1C1physical
22939629
WIPI3_HUMANWDR45Bphysical
22939629
UPAR_HUMANPLAURphysical
22939629
NALP5_HUMANNLRP5physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TXD17_HUMAN

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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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