TRXR2_HUMAN - dbPTM
TRXR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRXR2_HUMAN
UniProt AC Q9NNW7
Protein Name Thioredoxin reductase 2, mitochondrial
Gene Name TXNRD2
Organism Homo sapiens (Human).
Sequence Length 524
Subcellular Localization Mitochondrion .
Protein Description Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling..
Protein Sequence MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG
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
19PhosphorylationGGRFRWRTQAVAGGV
CCCCHHHHHHHHCCH
17.5824114839
40PhosphorylationAAAGQRDYDLLVVGG
HHCCCCCCEEEEECC
15.6420068231
49PhosphorylationLLVVGGGSGGLACAK
EEEECCCCCHHHHHH
32.7220068231
56AcetylationSGGLACAKEAAQLGR
CCHHHHHHHHHHCCC
48.0125038526
70PhosphorylationRKVAVVDYVEPSPQG
CCEEEEEEEECCCCC
8.63-
94UbiquitinationVNVGCIPKKLMHQAA
EECCCCCHHHHHHHH
38.33-
137AcetylationEAVQNHVKSLNWGHR
HHHHHHHHHCCCCCC
41.4923236377
138PhosphorylationAVQNHVKSLNWGHRV
HHHHHHHHCCCCCCC
26.3324702127
153AcetylationQLQDRKVKYFNIKAS
EECCCEEEEEEEEEE
47.3525825284
153MalonylationQLQDRKVKYFNIKAS
EECCCEEEEEEEEEE
47.3526320211
172MalonylationHTVCGVAKGGKEILL
CCEEEEEECCCEEEE
66.8326320211
172AcetylationHTVCGVAKGGKEILL
CCEEEEEECCCEEEE
66.8326051181
172SuccinylationHTVCGVAKGGKEILL
CCEEEEEECCCEEEE
66.8327452117
175SuccinylationCGVAKGGKEILLSAD
EEEEECCCEEEECCC
50.69-
175SuccinylationCGVAKGGKEILLSAD
EEEEECCCEEEECCC
50.69-
175AcetylationCGVAKGGKEILLSAD
EEEEECCCEEEECCC
50.6920167786
180PhosphorylationGGKEILLSADHIIIA
CCCEEEECCCEEEEE
28.3624719451
215AcetylationSDDIFWLKESPGKTL
CCCEEEEECCCCCEE
46.9025038526
238PhosphorylationLECAGFLTGIGLDTT
HHHHHHHHCCCCCCC
25.21-
244PhosphorylationLTGIGLDTTIMMRSI
HHCCCCCCCHHHCCC
24.22-
245PhosphorylationTGIGLDTTIMMRSIP
HCCCCCCCHHHCCCC
13.42-
250PhosphorylationDTTIMMRSIPLRGFD
CCCHHHCCCCCCCCC
15.6324719451
303 (in isoform 2)Ubiquitination-50.77-
314 (in isoform 2)Ubiquitination-4.98-
324PhosphorylationGRVPDTRSLNLEKAG
CCCCCCCCCCHHHCC
24.5724719451
329SuccinylationTRSLNLEKAGVDTSP
CCCCCHHHCCCCCCC
54.31-
329SuccinylationTRSLNLEKAGVDTSP
CCCCCHHHCCCCCCC
54.31-
334PhosphorylationLEKAGVDTSPDTQKI
HHHCCCCCCCCCCEE
39.4925262027
335PhosphorylationEKAGVDTSPDTQKIL
HHCCCCCCCCCCEEE
19.1321815630
338PhosphorylationGVDTSPDTQKILVDS
CCCCCCCCCEEEECC
34.8425262027
432AcetylationEVYHAHYKPLEFTVA
EEEECCCCCEEEEEC
33.0126051181
506AcetylationTCSEEVVKLRISKRS
CCCHHHHHHHHHCCC
36.9023954790

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 TRXR2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRXR2_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 TRXR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRS6A_HUMANPSMC3physical
11463857
NCOR1_HUMANNCOR1physical
11463857
NCOA2_HUMANNCOA2physical
12612084
TF2H1_HUMANGTF2H1physical
15625236
ALDR_HUMANAKR1B1physical
26344197
TRXR1_HUMANTXNRD1physical
28514442

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 TRXR2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-153, AND MASS SPECTROMETRY.

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