Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Thioredoxin reductase 1, cytoplasmic  

UniProtKB / Swiss-Prot ID :  TRXR1_HUMAN

Gene Name (Synonyms) : 
TXNRD1, GRIM12, KDRF  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (By similarity). Isoform 4: Cytoplasm. Nucleus. Isoform 5: Cytoplasm. 

Protein Function :  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 MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTATADSRALLQAYIDGHSVVI...
Predicted Secondary Structure CCCCCCCCCCCCCCEEEECCCHHHHHHHHHHHHCCCCEEEEECCCCCCCCCCCCCCCCCCCCCCCHHHHH...
Protein Variant
LocationDescription
365D -> G (in dbSNP:rs1127954). VAR_051776
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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
Predicted PTM Sites
Protein Variant
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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
160PhosphoserineDLPKSYDYD
EEEECCCCE
22.69HPRD
Link
161PhosphotyrosineLPKSYDYDL
EEECCCCEE
25.34HPRD
Link
161PhosphotyrosineLPKSYDYDL
EEECCCCEE
25.34PhosphoELM
Link
161PhosphotyrosineLPKSYDYDL
EEECCCCEE
25.34Phosphositeplus
Link
161Phosphotyrosine.LPKSYDYDL
EEECCCCEE
25.34UniProtKB
Link
163PhosphotyrosineKSYDYDLII
ECCCCEEEE
12.38HPRD
Link
163PhosphotyrosineKSYDYDLII
ECCCCEEEE
12.38PhosphoELM
Link
163PhosphotyrosineKSYDYDLII
ECCCCEEEE
12.38Phosphositeplus
Link
163Phosphotyrosine.KSYDYDLII
ECCCCEEEE
12.38UniProtKB
Link
201PhosphothreonineTPLGTRWGL
CCCHHHHHH
30.82HPRD
Link
218Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CIPKKLMHQ
CEEEEEECC
45.76Phosphositeplus
Link
239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NYGWKVEET
HHHHHHHHC
35.09Phosphositeplus
Link
239N6-acetyllysineNYGWKVEET
HHHHHHHHC
35.09HPRD
Link
239N6-acetyllysineNYGWKVEET
HHHHHHHHC
35.09Phosphositeplus
Link
239N6-acetyllysine.NYGWKVEET
HHHHHHHHC
35.09UniProtKB
Link
245Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EETVKHDWD
HHCCCEEEE
43.18Phosphositeplus
Link
277PhosphotyrosineKKVVYENAY
ECCCCEEEE
13.37Phosphositeplus
Link
281PhosphotyrosineYENAYGQFI
CEEEEEEEC
24.04HPRD
Link
281PhosphotyrosineYENAYGQFI
CEEEEEEEC
24.04HPRD
Link
281PhosphotyrosineYENAYGQFI
CEEEEEEEC
24.04PhosphoELM
Link
281PhosphotyrosineYENAYGQFI
CEEEEEEEC
24.04Phosphositeplus
Link
281Phosphotyrosine.YENAYGQFI
CEEEEEEEC
24.04UniProtKB
Link
385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DMANKIGEH
EEEECCHHH
42.42Phosphositeplus
Link
396Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EHGIKFIRQ
HHCCCCCEE
39.05Phosphositeplus
Link
405Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FVPIKVEQI
EEEECCCCE
33.38Phosphositeplus
Link
405N6-acetyllysineFVPIKVEQI
EEEECCCCE
33.38HPRD
Link
405N6-acetyllysineFVPIKVEQI
EEEECCCCE
33.38Phosphositeplus
Link
405N6-acetyllysine.FVPIKVEQI
EEEECCCCE
33.38UniProtKB
Link
413PhosphothreonineIEAGTPGRL
EEEEEECCC
29.62Phosphositeplus
Link
449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ACTRKIGLE
HHHHHHHHH
23.99Phosphositeplus
Link
458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TVGVKINEK
HHHHHCCCH
33.61Phosphositeplus
Link
465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EKTGKIPVT
CHHHHHHHH
49.41Phosphositeplus
Link
572PhosphotyrosineNNKCYAKII
16.73HPRD
Link-
572PhosphotyrosineNNKCYAKII
16.73Phosphositeplus
Link-
572Phosphotyrosine.NNKCYAKII
16.73UniProtKB
Link-
580Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ICNTKDNER
44.56Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PP16A_HUMANyeast 2-hybridHPRD:03068HPRD16169070
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
PRDX5_HUMANENSP00000347020STRING
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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
"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
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures