TRXR1_HUMAN - dbPTM
TRXR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRXR1_HUMAN
UniProt AC Q16881
Protein Name Thioredoxin reductase 1, cytoplasmic
Gene Name TXNRD1
Organism Homo sapiens (Human).
Sequence Length 649
Subcellular Localization Cytoplasm.
Isoform 4: Cytoplasm. Nucleus.
Isoform 5: Cytoplasm.
Protein Description Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid..
Protein Sequence MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTATADSRALLQAYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQTEDGRALEGTLSELAAETDLPVVFVKQRKIGGHGPTLKAYQEGRLQKLLKMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCUG
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
1 (in isoform 5)Acetylation-10.0519413330
2 (in isoform 4)Phosphorylation-21.2423090842
11PhosphorylationAEGKAVAAAAPTELQ
HHCHHHEEECCCCHH		9.5015592455
12 (in isoform 4)Phosphorylation-12.3023090842
13PhosphorylationGKAVAAAAPTELQTK
CHHHEEECCCCHHCC		13.5615592455
19PhosphorylationAAPTELQTKGKNGDG
ECCCCHHCCCCCCCC		55.1523828894
30 (in isoform 3)Phosphorylation-37.55-
30UbiquitinationNGDGRRRSAKDHHPG
CCCCCCCCCCCCCCC		37.55-
31 (in isoform 3)Phosphorylation-21.34-
39PhosphorylationKDHHPGKTLPENPAG
CCCCCCCCCCCCCCC		54.16-
50PhosphorylationNPAGFTSTATADSRA
CCCCCCCCCCCCHHH		25.60-
51AcetylationPAGFTSTATADSRAL
CCCCCCCCCCCHHHH		10.6819608861
51UbiquitinationPAGFTSTATADSRAL
CCCCCCCCCCCHHHH		10.6819608861
68UbiquitinationAYIDGHSVVIFSRST
HHHCCCEEEEEECCC		2.9621890473
68UbiquitinationAYIDGHSVVIFSRST
HHHCCCEEEEEECCC		2.9621890473
68 (in isoform 5)Ubiquitination-2.9621890473
73 (in isoform 2)Ubiquitination-25.82-
89AcetylationVKKLFKSLCVPYFVL
HHHHHHHHCCEEEEE		3.3519608861
89UbiquitinationVKKLFKSLCVPYFVL
HHHHHHHHCCEEEEE		3.3519608861
89 (in isoform 5)Ubiquitination-3.3521890473
95 (in isoform 5)Ubiquitination-3.1521890473
112 (in isoform 2)Ubiquitination-30.3321890473
127PhosphorylationLPVVFVKQRKIGGHG
CCEEEEECCCCCCCC		46.7419605366
131PhosphorylationFVKQRKIGGHGPTLK
EEECCCCCCCCCCHH		25.6919605366
133 (in isoform 2)Ubiquitination-33.5721890473
138MethylationGGHGPTLKAYQEGRL
CCCCCCHHHHHHHHH		47.7583364241
139 (in isoform 2)Ubiquitination-17.8521890473
141AcetylationGPTLKAYQEGRLQKL
CCCHHHHHHHHHHHH		52.0719608861
141UbiquitinationGPTLKAYQEGRLQKL
CCCHHHHHHHHHHHH		52.0719608861
150MethylationGRLQKLLKMNGPEDL
HHHHHHHHHHCCCCC		40.5383364245
160PhosphorylationGPEDLPKSYDYDLII
CCCCCCCCCCCCEEE		22.6928152594
161PhosphorylationPEDLPKSYDYDLIII
CCCCCCCCCCCEEEE		25.3421082442
163PhosphorylationDLPKSYDYDLIIIGG
CCCCCCCCCEEEECC		12.3821082442
167 (in isoform 3)Ubiquitination-2.8821890473
168 (in isoform 2)Ubiquitination-3.13-
172PhosphorylationLIIIGGGSGGLAAAK
EEEECCCCHHHHHHH		32.7220068231
179UbiquitinationSGGLAAAKEAAQYGK
CHHHHHHHHHHHHCC		43.06-
179AcetylationSGGLAAAKEAAQYGK
CHHHHHHHHHHHHCC		43.0626051181
183 (in isoform 6)Ubiquitination-55.3421890473
184PhosphorylationAAKEAAQYGKKVMVL
HHHHHHHHCCEEEEE		26.6220068231
1862-HydroxyisobutyrylationKEAAQYGKKVMVLDF
HHHHHHCCEEEEEEE		36.94-
187UbiquitinationEAAQYGKKVMVLDFV
HHHHHCCEEEEEEEC		31.06-
1872-HydroxyisobutyrylationEAAQYGKKVMVLDFV
HHHHHCCEEEEEEEC		31.06-
188 (in isoform 3)Ubiquitination-3.5021890473
188 (in isoform 4)Ubiquitination-3.5021890473
194 (in isoform 3)Ubiquitination-6.6421890473
194 (in isoform 4)Ubiquitination-6.6421890473
195PhosphorylationVMVLDFVTPTPLGTR
EEEEEECCCCCCCCC		22.8027050516
197PhosphorylationVLDFVTPTPLGTRWG
EEEECCCCCCCCCCC		23.0621955146
201PhosphorylationVTPTPLGTRWGLGGT
CCCCCCCCCCCCCCC		30.8220068231
204 (in isoform 6)Ubiquitination-15.9121890473
208PhosphorylationTRWGLGGTCVNVGCI
CCCCCCCCEEECCCC		16.1021955146
210 (in isoform 6)Ubiquitination-6.9821890473
217UbiquitinationVNVGCIPKKLMHQAA
EECCCCCHHHHHHHH		38.3319608861
217UbiquitinationVNVGCIPKKLMHQAA
EECCCCCHHHHHHHH		38.33-
217AcetylationVNVGCIPKKLMHQAA
EECCCCCHHHHHHHH		38.3326051181
218SuccinylationNVGCIPKKLMHQAAL
ECCCCCHHHHHHHHH		45.76-
218UbiquitinationNVGCIPKKLMHQAAL
ECCCCCHHHHHHHHH		45.7621890473
2182-HydroxyisobutyrylationNVGCIPKKLMHQAAL
ECCCCCHHHHHHHHH		45.76-
218SuccinylationNVGCIPKKLMHQAAL
ECCCCCHHHHHHHHH		45.7621890473
222UbiquitinationIPKKLMHQAALLGQA
CCHHHHHHHHHHHHH		17.8621890473
235 (in isoform 5)Ubiquitination-43.5521890473
239AcetylationDSRNYGWKVEETVKH
HHHHHCCCHHHHHHC		35.0919608861
239UbiquitinationDSRNYGWKVEETVKH
HHHHHCCCHHHHHHC		35.0921906983
2392-HydroxyisobutyrylationDSRNYGWKVEETVKH
HHHHHCCCHHHHHHC		35.09-
239 (in isoform 1)Ubiquitination-35.0921890473
245AcetylationWKVEETVKHDWDRMI
CCHHHHHHCCHHHHH		43.1825825284
245UbiquitinationWKVEETVKHDWDRMI
CCHHHHHHCCHHHHH		43.1821906983
245 (in isoform 1)Ubiquitination-43.1821890473
246 (in isoform 5)Ubiquitination-36.7421890473
255UbiquitinationWDRMIEAVQNHIGSL
HHHHHHHHHHHHHCC		3.6721890473
255UbiquitinationWDRMIEAVQNHIGSL
HHHHHHHHHHHHHCC		3.6721890473
255AcetylationWDRMIEAVQNHIGSL
HHHHHHHHHHHHHCC		3.6719608861
255UbiquitinationWDRMIEAVQNHIGSL
HHHHHHHHHHHHHCC		3.6719608861
255 (in isoform 5)Ubiquitination-3.6721890473
274UbiquitinationRVALREKKVVYENAY
HHEEEECEEEEECCC		31.98-
274MalonylationRVALREKKVVYENAY
HHEEEECEEEEECCC		31.9826320211
274AcetylationRVALREKKVVYENAY
HHEEEECEEEEECCC		31.9826051181
277PhosphorylationLREKKVVYENAYGQF
EEECEEEEECCCCCC		13.3727273156
279 (in isoform 2)Ubiquitination-22.3021890473
281PhosphorylationKVVYENAYGQFIGPH
EEEEECCCCCCCCCC		24.0425159151
290 (in isoform 2)Ubiquitination-3.0221890473
298AcetylationKATNNKGKEKIYSAE
EECCCCCCCEEEEEE		58.4011921349
299 (in isoform 2)Ubiquitination-54.0421890473
299 (in isoform 5)Ubiquitination-54.0421890473
300UbiquitinationTNNKGKEKIYSAERF
CCCCCCCEEEEEEEE		50.89-
3002-HydroxyisobutyrylationTNNKGKEKIYSAERF
CCCCCCCEEEEEEEE		50.89-
300MalonylationTNNKGKEKIYSAERF
CCCCCCCEEEEEEEE		50.8926320211
300AcetylationTNNKGKEKIYSAERF
CCCCCCCEEEEEEEE		50.8925953088
302PhosphorylationNKGKEKIYSAERFLI
CCCCCEEEEEEEEEE		16.9428152594
303PhosphorylationKGKEKIYSAERFLIA
CCCCEEEEEEEEEEE		27.4228152594
307AcetylationKIYSAERFLIATGER
EEEEEEEEEEECCCC		4.3319608861
307UbiquitinationKIYSAERFLIATGER
EEEEEEEEEEECCCC		4.3319608861
308 (in isoform 5)Ubiquitination-3.0521890473
315 (in isoform 5)Ubiquitination-25.6021890473
317PhosphorylationATGERPRYLGIPGDK
ECCCCCCEECCCCCC		16.3828102081
324UbiquitinationYLGIPGDKEYCISSD
EECCCCCCCEECCCC		57.40-
324AcetylationYLGIPGDKEYCISSD
EECCCCCCCEECCCC		57.4025953088
334 (in isoform 3)Ubiquitination-10.1721890473
334 (in isoform 4)Ubiquitination-10.1721890473
343 (in isoform 2)Ubiquitination-30.6021890473
345 (in isoform 3)Ubiquitination-4.5221890473
345 (in isoform 4)Ubiquitination-4.5221890473
350 (in isoform 6)Ubiquitination-6.8221890473
352 (in isoform 2)Ubiquitination-6.8721890473
354 (in isoform 3)Ubiquitination-16.7521890473
354 (in isoform 4)Ubiquitination-16.7521890473
359 (in isoform 2)Ubiquitination-4.1121890473
361 (in isoform 6)Ubiquitination-19.3521890473
370 (in isoform 6)Ubiquitination-3.6421890473
382SulfoxidationLRGFDQDMANKIGEH
HCCCCHHHHHHHHHH		3.5330846556
383 (in isoform 2)Ubiquitination-23.58-
385UbiquitinationFDQDMANKIGEHMEE
CCHHHHHHHHHHHHH		42.4221906983
3852-HydroxyisobutyrylationFDQDMANKIGEHMEE
CCHHHHHHHHHHHHH		42.42-
385AcetylationFDQDMANKIGEHMEE
CCHHHHHHHHHHHHH		42.4225953088
385 (in isoform 1)Ubiquitination-42.4221890473
390SulfoxidationANKIGEHMEEHGIKF
HHHHHHHHHHHCCCC		5.8630846556
396UbiquitinationHMEEHGIKFIRQFVP
HHHHHCCCCHHHHCC		39.0521906983
396 (in isoform 1)Ubiquitination-39.0521890473
398 (in isoform 3)Ubiquitination-2.6221890473
398 (in isoform 4)Ubiquitination-2.6221890473
405AcetylationIRQFVPIKVEQIEAG
HHHHCCEEEEEECCC		33.3819608861
405SumoylationIRQFVPIKVEQIEAG
HHHHCCEEEEEECCC		33.38-
405UbiquitinationIRQFVPIKVEQIEAG
HHHHCCEEEEEECCC		33.3821890473
405SuccinylationIRQFVPIKVEQIEAG
HHHHCCEEEEEECCC		33.3823954790
405 (in isoform 1)Ubiquitination-33.3821890473
405UbiquitinationIRQFVPIKVEQIEAG
HHHHCCEEEEEECCC		33.3822053931
407 (in isoform 3)Ubiquitination-40.6221890473
407 (in isoform 4)Ubiquitination-40.6221890473
409UbiquitinationVPIKVEQIEAGTPGR
CCEEEEEECCCCCCC		2.1921890473
413PhosphorylationVEQIEAGTPGRLRVV
EEEECCCCCCCEEEE		29.6229255136
414 (in isoform 3)Ubiquitination-25.6221890473
414 (in isoform 4)Ubiquitination-25.6221890473
414 (in isoform 6)Ubiquitination-25.6221890473
423 (in isoform 6)Ubiquitination-21.5921890473
430 (in isoform 5)Ubiquitination-6.6921890473
430 (in isoform 6)Ubiquitination-6.6921890473
434PhosphorylationEEIIEGEYNTVMLAI
HHHHEECCCEEEEEE		27.30-
449UbiquitinationGRDACTRKIGLETVG
CHHHHCCCCCCEEEE		23.99-
449MalonylationGRDACTRKIGLETVG
CHHHHCCCCCCEEEE		23.9926320211
449 (in isoform 1)Ubiquitination-23.9921890473
458UbiquitinationGLETVGVKINEKTGK
CCEEEEEEEECCCCC		33.6121906983
458AcetylationGLETVGVKINEKTGK
CCEEEEEEEECCCCC		33.6125953088
458 (in isoform 1)Ubiquitination-33.6121890473
463PhosphorylationGVKINEKTGKIPVTD
EEEEECCCCCCCCCC		37.2121601212
465UbiquitinationKINEKTGKIPVTDEE
EEECCCCCCCCCCHH		49.4121906983
465 (in isoform 1)Ubiquitination-49.4121890473
469PhosphorylationKTGKIPVTDEEQTNV
CCCCCCCCCHHHCCC		32.13-
474PhosphorylationPVTDEEQTNVPYIYA
CCCCHHHCCCCEEEE		41.27-
474 (in isoform 2)Ubiquitination-41.2721890473
478PhosphorylationEEQTNVPYIYAIGDI
HHHCCCCEEEEECHH		11.41-
493PhosphorylationLEDKVELTPVAIQAG
HHCCCCCCHHHHHHH		11.3823312004
508PhosphorylationRLLAQRLYAGSTVKC
HHHHHHHHCCCCEEC		15.8828152594
514UbiquitinationLYAGSTVKCDYENVP
HHCCCCEECCCCCCC		22.83-
529 (in isoform 3)Ubiquitination-43.0321890473
529 (in isoform 4)Ubiquitination-43.0321890473
539UbiquitinationACGLSEEKAVEKFGE
CCCCCHHHHHHHHCC		54.39-
539AcetylationACGLSEEKAVEKFGE
CCCCCHHHHHHHHCC		54.3925953088
545 (in isoform 6)Ubiquitination-52.9921890473
555PhosphorylationNIEVYHSYFWPLEWT
CEEEEEEEECCEEEE		9.06-
5702-HydroxyisobutyrylationIPSRDNNKCYAKIIC
ECCCCCCEEEEEEEE		34.57-
572PhosphorylationSRDNNKCYAKIICNT
CCCCCEEEEEEEEEC		16.7315592455
574UbiquitinationDNNKCYAKIICNTKD
CCCEEEEEEEEECCC		13.21-
574AcetylationDNNKCYAKIICNTKD
CCCEEEEEEEEECCC		13.2125953088
580UbiquitinationAKIICNTKDNERVVG
EEEEEECCCCCEEEE		44.562190698
5802-HydroxyisobutyrylationAKIICNTKDNERVVG
EEEEEECCCCCEEEE		44.56-
580AcetylationAKIICNTKDNERVVG
EEEEEECCCCCEEEE		44.5626051181
580 (in isoform 1)Ubiquitination-44.5621890473
607UbiquitinationQGFAAALKCGLTKKQ
HHHHHHHHCCCCHHH		22.87-
613UbiquitinationLKCGLTKKQLDSTIG
HHCCCCHHHHHCCCC		51.35-
617PhosphorylationLTKKQLDSTIGIHPV
CCHHHHHCCCCCCHH		30.4321601212
631PhosphorylationVCAEVFTTLSVTKRS
HHHCCEEEEEECCCC		12.9321601212
633PhosphorylationAEVFTTLSVTKRSGA
HCCEEEEEECCCCCC		26.1621601212
638PhosphorylationTLSVTKRSGASILQA
EEEECCCCCCCHHCC		40.0222617229
641PhosphorylationVTKRSGASILQAGCU
ECCCCCCCHHCCCCC		27.6222617229
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 TRXR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRXR1_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 TRXR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLRX2_HUMANGLRX2physical
14676218
ISG15_HUMANISG15physical
16009940
P53_HUMANTP53physical
15824742
APEX1_HUMANAPEX1physical
15824742
TXD17_HUMANTXNDC17physical
22939629
IPO5_HUMANIPO5physical
22863883
TBA1C_HUMANTUBA1Cphysical
22863883
PNCB_HUMANNAPRTphysical
26344197
TRI25_HUMANTRIM25physical
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 TRXR1_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-239 AND LYS-405, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-161; TYR-163; TYR-281AND TYR-572, AND MASS SPECTROMETRY.

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