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TRXR1 (human)

Overview TRXR1 a cytoplasmic pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine residue which is required for the catalytic activity. Note: This description may include information from UniProtKB. Protein type: EC 1.8.1.9; Nucleotide Metabolism - pyrimidine; Nuclear receptor co-regulator; Oxidoreductase Cellular Component: mitochondrion; cytoplasm; nucleolus; nucleus; cytosol Molecular Function: thioredoxin-disulfide reductase activity; FAD binding; electron carrier activity; protein disulfide oxidoreductase activity; NADP binding Biological Process: cell proliferation; mesoderm formation; nucleobase, nucleoside and nucleotide metabolic process; nucleobase, nucleoside and nucleotide interconversion; cell redox homeostasis; hydrogen peroxide catabolic process; cellular lipid metabolic process; signal transduction Reference #:  Q16881 (UniProtKB) Alt. Names/Synonyms: Gene associated with retinoic and IFN-induced mortality 12 protein; Gene associated with retinoic and interferon-induced mortality 12 protein; GRIM-12; GRIM12; KDRF; KM-102-derived reductase-like factor; MGC9145; oxidoreductase; thioredoxin reductase 1; Thioredoxin reductase 1, cytoplasmic; thioredoxin reductase GRIM-12; Thioredoxin reductase TR1; TR; TR1; TRXR1; TXNR; TXNRD1 Gene Symbols: TXNRD1 Molecular weight: 70,906 Da Basal Isoelectric point: 7.16  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below TRXR1 1W1C - A/B=161-649 (human) 2CFY - A/B/C/D/E/F=151-649 (human) 2J3N - A/B/C/D/E/F=151-649 (human) 2ZZ0 - A/D/C/B=150-649 (human) 2ZZB - A/D/C/B=150-649 (human) 2ZZC - A/D/C/B=150-649 (human) 3QFA - A/B=1-499 (human) 3QFB - A/B=1-499 (human) 1H6V (rat) 3EAN (rat) 3EAO (rat)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1W1C 2CFY 2J3N 2ZZ0 2ZZB 2ZZC 3QFA 3QFB  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  NURSA  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human ► Hide Isoforms
0	1		-	gap
0	1		-	gap
0	36		Y161-p	PEDLPKSyDyDLIII
0	48		Y163-p	DLPKSyDyDLIIIGG
0	1		Y184-p	AAKEAAQyGKKVMVL
0	1		K217-u	VNVGCIPkkLMHQAA
0	2		K218-u	NVGCIPkkLMHQAAL
0	1		Q231	ALLGQALQDSRNYGW
0	1		K239-a	DSRNYGWkVEETVkH
0	2		K239-u	DSRNYGWkVEETVkH
0	2		K245-u	WkVEETVkHDWDRMI
0	1		K274	RVALREKKVVyENAy
0	20		Y277-p	LREKKVVyENAyGQF
0	540		Y281-p	KVVyENAyGQFIGPH
0	1		K296-a	RIKATNNkGkEkIYS
0	2		K296	RIKATNNKGkEkIYS
0	1		K298-a	KATNNkGkEkIYSAE
0	1		K300-a	TNNkGkEkIYSAERF
0	4		Y302	NkGkEkIYSAERFLI
0	2		K385-u	FDQDMANkIGEHMEE
0	1		K396-u	HMEEHGIkFIRQFVP
0	1		K405-a	IRQFVPIkVEQIEAG
0	4		K405-u	IRQFVPIkVEQIEAG
0	1		T413-p	VEQIEAGtPGRLRVV
0	1		Y434-p	EEIIEGEyNTVMLAI
0	1		K449-u	GRDACTRkIGLETVG
0	2		K458-u	GLETVGVkINEKTGk
0	1		K465-u	kINEKTGkIPVTDEE
0	1		Y555-p	NIEVYHSyFWPLEWT
0	1		Y572-p	SRDNNKCyAKIICNT
0	12		K580-u	AKIICNTkDNERVVG
0	2		K607-u	QGFAAALkCGLTKKQ

	TRXR1 iso3
S30-p	RKPRPRRssRLLAGE
S31-p	KPRPRRssRLLAGEK
Y110	PEDLPKSYDYDLIII
Y112	DLPKSYDYDLIIIGG
Y133	AAKEAAQYGKKVMVL
K166	VNVGCIPKKLMHQAA
K167	NVGCIPKKLMHQAAL
Q180	ALLGQALQDSRNYGW
K188	DSRNYGWKVEETVKH
K188	DSRNYGWKVEETVKH
K194	WKVEETVKHDWDRMI
K223	RVALREKKVVYENAY
Y226	LREKKVVYENAYGQF
Y230	KVVYENAYGQFIGPH
K245	RIKATNNKGKEKIyS
K245	RIKATNNKGKEKIyS
K247	KATNNKGKEKIySAE
K249	TNNKGKEKIySAERF
Y251-p	NKGKEKIySAERFLI
K334	FDQDMANKIGEHMEE
K345	HMEEHGIKFIRQFVP
K354	IRQFVPIKVEQIEAG
K354	IRQFVPIKVEQIEAG
T362	VEQIEAGTPGRLRVV
Y383	EEIIEGEYNTVMLAI
K398	GRDACTRKIGLETVG
K407	GLETVGVKINEKTGK
K414	KINEKTGKIPVTDEE
Y504	NIEVYHSYFWPLEWT
Y521	SRDNNKCYAKIICNT
K529	AKIICNTKDNERVVG
K556	QGFAAALKCGLTKKQ

	mouse
-	gap
-	gap
Y125	SKDPPGSYDFDLIII
F127	DPPGSYDFDLIIIGG
F148	AAKEAAKFDKKVLVL
K181	VNVGCIPKKLMHQAA
K182	NVGCIPKKLMHQAAL
K195-u	ALLGQALkDSRNYGW
K203	DSRNYGWKVEDTVkH
K203-u	DSRNYGWkVEDTVkH
K209-u	WkVEDTVkHDWEKMT
K238-u	RVALREKkVVYENAy
Y241	LREKkVVYENAyGRF
Y245-p	kVVYENAyGRFIGPH
K260-a	RIVATNNkGKEkIYS
K260-u	RIVATNNkGKEkIYS
K262	VATNNkGKEkIYSAE
K264-a	TNNkGKEkIYSAERF
Y266	NkGKEkIYSAERFLI
K349-u	FDQDMANkIGEHMEE
K360	HMEEHGIKFIRQFVP
K369	IRQFVPTKIEQIEAG
K369-u	IRQFVPTkIEQIEAG
T377	IEQIEAGTPGRLRVT
F398	EETIEGEFNTVLLAV
T413	GRDSCTRTIGLETVG
K422-u	GLETVGVkINEKTGK
K429	kINEKTGKIPVTDEE
F519	NIEVYHSFFWPLEWT
Y536	SRDNNKCYAKIICNL
K544-u	AKIICNLkDDERVVG
K571	QGFAAALKCGLTKQQ

	rat
-	gap
-	gap
Y11	SKDAPKSYDFDLIII
F13	DAPKSYDFDLIIIGG
F34	AAKEAAKFDKKVMVL
K67	VNVGCIPKKLMHQAA
K68	NVGCIPKKLMHQAAL
K81	ALLGQALKDSRNYGW
K89	DSRNYGWKLEDTVKH
K89	DSRNYGWKLEDTVKH
K95	WKLEDTVKHDWEKMT
K124	RVALREKKVVYENAY
Y127	LREKKVVYENAYGKF
Y131	KVVYENAYGKFIGPH
K146	KIMATNNKGKEKVYS
K146	KIMATNNKGKEKVYS
K148	MATNNKGKEKVYSAE
K150	TNNKGKEKVYSAERF
Y152	NKGKEKVYSAERFLI
K235	FDQDMANKIGEHMEE
K246	HMEEHGIKFIRQFVP
K255	IRQFVPTKIEQIEAG
K255	IRQFVPTKIEQIEAG
T263	IEQIEAGTPGRLKVT
F284	EETIEDEFNTVLLAV
T299	GRDSCTRTIGLETVG
K308	GLETVGVKINEKTGK
K315	KINEKTGKIPVTDEE
F405	NIEVYHSFFWPLEWT
Y422	SRDNNKCYAKVICNL
K430	AKVICNLKDNERVVG
K457	QGFAAALKCGLTKQQ

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