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Q16881 (TRXR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin reductase 1, cytoplasmic

Short name=TR
EC=1.8.1.9
Alternative name(s):
Gene associated with retinoic and interferon-induced mortality 12 protein
Short name=GRIM-12
Short name=Gene associated with retinoic and IFN-induced mortality 12 protein
KM-102-derived reductase-like factor
Thioredoxin reductase TR1
Gene names
Name:TXNRD1
Synonyms:GRIM12, KDRF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length649 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3 Ref.15 Ref.17 Ref.20

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homodimer. Isoform 4 interacts with ESR1 and ESR2. Interacts with HERC5. Ref.15 Ref.17 Ref.19

Subcellular location

Cytoplasm By similarity Ref.17.

Isoform 4: Cytoplasm Ref.17. Nucleus Ref.17.

Isoform 5: Cytoplasm Ref.17.

Tissue specificity

Isoform 1 is expressed predominantly in Leydig cells (at protein level). Also expressed in ovary, spleen, heart, liver, kidney and pancreas and in a number of cancer cell lines. Isoform 4 is widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver. Ref.2 Ref.17 Ref.20

Induction

Isoform 5 is induced by a combination of interferon-beta and retinoic acid (at protein level). Isoform 1 is induced by estradiol or testosterone in HeLa cells. Ref.3 Ref.20

Domain

The N-terminal glutaredoxin domain found in isoform 1 does not contain the C-P-Y-C redox-active motif normally found in glutaredoxins and has been found to be inactive in classical glutaredoxin assays. Ref.16

Post-translational modification

The N-terminus of isoform 5 is blocked.

ISGylated Probable. Ref.19

Miscellaneous

The thioredoxin reductase active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Contains 1 glutaredoxin domain.

Sequence caution

The sequence AAB35418.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence AAC69621.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence AAF15900.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence AAV38446.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence AAZ67916.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence BAA13674.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence BAH11490.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence BAH12374.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence BAH14140.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence CAA04503.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence CAA62629.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence CAG38744.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

The sequence EAW97745.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
Selenocysteine
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Ensembl

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular lipid metabolic process

Traceable author statement. Source: Reactome

mesoderm formation

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

signal transduction

Non-traceable author statement PubMed 8921404. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

thioredoxin-disulfide reductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAV1Q031354EBI-716617,EBI-603614

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16881-1)

Also known as: V; TXNRD1_v3;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Minor isoform.
Isoform 2 (identifier: Q16881-2)

Also known as: II; TXNRD1_v4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.
     107-138: LEGTLSELAAETDLPVVFVKQRKIGGHGPTLK → MLSRLVLNSWAQAIIRPRPPKVLGLQVTTFSE
Isoform 3 (identifier: Q16881-3)

Also known as: III; TXNRD1_v5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.
     52-100: TADSRALLQA...VPYFVLELDQ → MQQVMLTCKG...LTRSALLLCH
Isoform 4 (identifier: Q16881-4)

Also known as: IV; TXNRD1_v2; TrxR1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.
     99-101: DQT → MSC
Isoform 5 (identifier: Q16881-5)

Also known as: I; TXNRD1_v1; TrxR1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-150: Missing.
Note: Major isoform. The N-terminus of the sequence is processed into a mature form that lacks residues Met-151 and Asn-152 at the N-terminus.
Isoform 6 (identifier: Q16881-6)

Also known as: VI;

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: MGCAEGKAVA...IGGHGPTLKA → MPVDDYWLCL...QERNVQFGLA
Isoform 7 (identifier: Q16881-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-188: Missing.
Note: No experimental confirmation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 649649Thioredoxin reductase 1, cytoplasmic
PRO_0000030286

Regions

Domain56 – 156101Glutaredoxin
Nucleotide binding192 – 20918FAD By similarity

Sites

Active site6221Proton acceptor By similarity

Amino acid modifications

Non-standard residue6481Selenocysteine Ref.14
Modified residue2181N6-succinyllysine By similarity
Modified residue2811Phosphotyrosine Ref.18
Disulfide bond209 ↔ 214Redox-active By similarity
Cross-link647 ↔ 648Cysteinyl-selenocysteine (Cys-Sec) By similarity

Natural variations

Alternative sequence1 – 188188Missing in isoform 7.
VSP_053819
Alternative sequence1 – 150150Missing in isoform 5.
VSP_031558
Alternative sequence1 – 139139MGCAE…PTLKA → MPVDDYWLCLPASCARPFVQ TVRVVQSCPHCCWFPGVLPS VPEPLRMPAMLPTGSHSAVL PPSHCSTAPPSTSQEPSSSA DPKLCLSPPTSDSRQERNVQ FGLA in isoform 6.
VSP_031559
Alternative sequence1 – 106106Missing in isoform 2.
VSP_031560
Alternative sequence1 – 9898Missing in isoform 4.
VSP_031561
Alternative sequence1 – 5151Missing in isoform 3.
VSP_031562
Alternative sequence52 – 10049TADSR…LELDQ → MQQVMLTCKGVNRGHAVPAG PGRKPRPRRSSRLLAGEKHL TRSALLLCH in isoform 3.
VSP_031563
Alternative sequence99 – 1013DQT → MSC in isoform 4.
VSP_031564
Alternative sequence107 – 13832LEGTL…GPTLK → MLSRLVLNSWAQAIIRPRPP KVLGLQVTTFSE in isoform 2.
VSP_031565
Natural variant3651D → G. Ref.1 Ref.4
Corresponds to variant rs1127954 [ dbSNP | Ensembl ].
VAR_051776

Experimental info

Sequence conflict1531G → S in AAQ62473. Ref.4
Sequence conflict1811A → P in AAF15900. Ref.6
Sequence conflict1941V → G in AAF15900. Ref.6
Sequence conflict2001G → E in AAQ62469. Ref.4
Sequence conflict2021R → K in AAQ62463. Ref.4
Sequence conflict2151I → N in AAQ62463. Ref.4
Sequence conflict2971G → D in BAH11490. Ref.7
Sequence conflict3061R → S in AAB35418. Ref.1
Sequence conflict3061R → S in CAA62629. Ref.1
Sequence conflict3061R → S in AAL15432. Ref.4
Sequence conflict3651D → N in AAC69621. Ref.3
Sequence conflict4371V → A in BAH12374. Ref.7
Sequence conflict4411I → M in BAH12374. Ref.7
Sequence conflict4491K → R in CAG38744. Ref.8
Sequence conflict6411S → R in AAC69621. Ref.3

Secondary structure

........................................................................................... 649
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (V) (TXNRD1_v3) [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: 5A51C3F77EB03EFE

FASTA64970,906
        10         20         30         40         50         60 
MGCAEGKAVA AAAPTELQTK GKNGDGRRRS AKDHHPGKTL PENPAGFTST ATADSRALLQ 

        70         80         90        100        110        120 
AYIDGHSVVI FSRSTCTRCT EVKKLFKSLC VPYFVLELDQ TEDGRALEGT LSELAAETDL 

       130        140        150        160        170        180 
PVVFVKQRKI GGHGPTLKAY QEGRLQKLLK MNGPEDLPKS YDYDLIIIGG GSGGLAAAKE 

       190        200        210        220        230        240 
AAQYGKKVMV LDFVTPTPLG TRWGLGGTCV NVGCIPKKLM HQAALLGQAL QDSRNYGWKV 

       250        260        270        280        290        300 
EETVKHDWDR MIEAVQNHIG SLNWGYRVAL REKKVVYENA YGQFIGPHRI KATNNKGKEK 

       310        320        330        340        350        360 
IYSAERFLIA TGERPRYLGI PGDKEYCISS DDLFSLPYCP GKTLVVGASY VALECAGFLA 

       370        380        390        400        410        420 
GIGLDVTVMV RSILLRGFDQ DMANKIGEHM EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV 

       430        440        450        460        470        480 
AQSTNSEEII EGEYNTVMLA IGRDACTRKI GLETVGVKIN EKTGKIPVTD EEQTNVPYIY 

       490        500        510        520        530        540 
AIGDILEDKV ELTPVAIQAG RLLAQRLYAG STVKCDYENV PTTVFTPLEY GACGLSEEKA 

       550        560        570        580        590        600 
VEKFGEENIE VYHSYFWPLE WTIPSRDNNK CYAKIICNTK DNERVVGFHV LGPNAGEVTQ 

       610        620        630        640 
GFAAALKCGL TKKQLDSTIG IHPVCAEVFT TLSVTKRSGA SILQAGCUG 

« Hide

Isoform 2 (II) (TXNRD1_v4) [UniParc].

Checksum: 990DB8D334659B4D
Show »

FASTA54359,787
Isoform 3 (III) (TXNRD1_v5) [UniParc].

Checksum: 81F496F5BB85A49E
Show »

FASTA59865,567
Isoform 4 (IV) (TXNRD1_v2) (TrxR1b) [UniParc].

Checksum: F54B034AADF51E5B
Show »

FASTA55160,419
Isoform 5 (I) (TXNRD1_v1) (TrxR1a) [UniParc].

Checksum: C24BAEB4A573EABE
Show »

FASTA49954,754
Isoform 6 (VI) [UniParc].

Checksum: 9C635E1C6EA94934
Show »

FASTA61467,266
Isoform 7 [UniParc].

Checksum: 07D3A620A6BD82EA
Show »

FASTA46150,873

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a human thioredoxin reductase."
Gasdaska P.Y., Gasdaska J.R., Cochran S., Powis G.
FEBS Lett. 373:5-9(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PROTEIN SEQUENCE OF 153-161; 307-315 AND 585-607, VARIANT GLY-365.
Tissue: Placenta.
[2]"Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102."
Koishi R., Kawashima I., Yoshimura C., Sugawara M., Serizawa N.
J. Biol. Chem. 272:2570-2577(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 122-127 AND 147-151, TISSUE SPECIFICITY.
Tissue: Bone marrow stroma.
[3]"Thioredoxin reductase mediates cell death effects of the combination of beta interferon and retinoic acid."
Hofman E.R., Boyanapalli M., Lindner D.J., Weihua X., Hassel B.A., Jagus R., Gutierrez P.L., Kalvakolanu D.V.
Mol. Cell. Biol. 18:6493-6504(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INDUCTION.
Tissue: Mammary carcinoma.
[4]"Evidence for intriguingly complex transcription of human thioredoxin reductase 1."
Rundloef A.-K., Janard M., Miranda-Vizuete A., Arner E.S.
Free Radic. Biol. Med. 36:641-656(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), VARIANT GLY-365.
Tissue: Mammary gland, Ovary, Testis and Thymus.
[5]"Identification by ddPCR of thioredoxin reductase as a vitamin D regulated gene in human osteoblasts."
Schuetze N., Bachthaler M., Lechner A., Koehrle J., Jakob F.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[6]"Cloning and sequencing of thioredoxin reductase gene from human brain."
Xu L., Dai R., Xu J.Y.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Tissue: Brain.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Astrocyte, Thalamus and Trachea.
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[9]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[10]NIEHS SNPs program
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION.
Tissue: Trachea.
[13]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Lung.
[14]"Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene."
Gladyshev V.N., Jeang K.-T., Stadtman T.C.
Proc. Natl. Acad. Sci. U.S.A. 93:6146-6151(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 307-316; 449-456; 466-476 AND 638-649, BLOCKAGE OF N-TERMINUS, SELENOCYSTEINE AT SEC-648, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity."
Tamura T., Stadtman T.C.
Proc. Natl. Acad. Sci. U.S.A. 93:1006-1011(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HOMODIMERIZATION, CHARACTERIZATION, PRESENCE OF SELENOCYSTEINE.
[16]"Alternative splicing involving the thioredoxin reductase module in mammals: a glutaredoxin-containing thioredoxin reductase 1."
Su D., Gladyshev V.N.
Biochemistry 43:12177-12188(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6), DOMAIN.
[17]"An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling."
Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A., Spyrou G.
J. Biol. Chem. 279:38721-38729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ESR1 AND ESR2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY (ISOFORM 4).
[18]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HERC5, ISGYLATION.
[20]"Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1."
Dammeyer P., Damdimopoulos A.E., Nordman T., Jimenez A., Miranda-Vizuete A., Arner E.S.J.
J. Biol. Chem. 283:2814-2821(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION (ISOFORM 1).
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis."
Fritz-Wolf K., Urig S., Becker K.
J. Mol. Biol. 370:116-127(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) (ISOFORM 5).
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91247 mRNA. Translation: CAA62629.1. Sequence problems.
S79851 mRNA. Translation: AAB35418.1. Sequence problems.
D88687 mRNA. Translation: BAA13674.1. Sequence problems.
AF077367 mRNA. Translation: AAC69621.1. Sequence problems.
AY057105 mRNA. Translation: AAL15432.1.
AY344081 mRNA. Translation: AAQ62461.1.
AY344083 mRNA. Translation: AAQ62462.1.
AY344084 mRNA. Translation: AAQ62463.1.
AY344086 mRNA. Translation: AAQ62464.1.
AY344087 mRNA. Translation: AAQ62465.1.
AY344089 mRNA. Translation: AAQ62466.1.
AY344092 mRNA. Translation: AAQ62467.1.
AY344093 mRNA. Translation: AAQ62468.1.
AY344095 mRNA. Translation: AAQ62469.1.
AY344096 mRNA. Translation: AAQ62470.1.
AY344670 mRNA. Translation: AAQ62471.1.
AY344673 mRNA. Translation: AAQ62472.1.
AY344679 mRNA. Translation: AAQ62473.1.
AJ001050 mRNA. Translation: CAA04503.1. Sequence problems.
AF208018 mRNA. Translation: AAF15900.1. Sequence problems.
AK293322 mRNA. Translation: BAH11490.1. Sequence problems.
AK296495 mRNA. Translation: BAH12374.1. Sequence problems.
AK304241 mRNA. Translation: BAH14140.1. Sequence problems.
CR536506 mRNA. Translation: CAG38744.1. Sequence problems.
BT019640 mRNA. Translation: AAV38446.1. Sequence problems.
DQ157758 Genomic DNA. Translation: AAZ67916.1. Sequence problems.
AC089983 Genomic DNA. No translation available.
AC090107 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97745.1. Sequence problems.
BC018122 mRNA. Translation: AAH18122.2.
PIRS66677.
RefSeqNP_001087240.1. NM_001093771.2.
NP_001248374.1. NM_001261445.1.
NP_001248375.1. NM_001261446.1.
NP_003321.3. NM_003330.3.
NP_877393.1. NM_182729.2.
NP_877419.1. NM_182742.2.
NP_877420.1. NM_182743.2.
UniGeneHs.654922.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1Cmodel-A/B161-649[»]
2CFYX-ray2.70A/B/C/D/E/F151-649[»]
2J3NX-ray2.80A/B/C/D/E/F151-649[»]
2ZZ0X-ray2.80A/B/C/D150-649[»]
2ZZBX-ray3.20A/B/C/D150-649[»]
2ZZCX-ray2.60A/B/C/D150-649[»]
3QFAX-ray2.20A/B151-646[»]
3QFBX-ray2.60A/B151-646[»]
ProteinModelPortalQ16881.
SMRQ16881. Positions 59-644.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113147. 30 interactions.
IntActQ16881. 5 interactions.
MINTMINT-1525880.

Chemistry

BindingDBQ16881.
ChEMBLCHEMBL2096978.

PTM databases

PhosphoSiteQ16881.

Polymorphism databases

DMDM172046253.

2D gel databases

REPRODUCTION-2DPAGEIPI00554786.

Proteomic databases

PaxDbQ16881.
PRIDEQ16881.

Protocols and materials databases

DNASU7296.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000388854; ENSP00000373506; ENSG00000198431.
ENST00000429002; ENSP00000412045; ENSG00000198431.
ENST00000503506; ENSP00000421934; ENSG00000198431. [Q16881-5]
ENST00000524698; ENSP00000433425; ENSG00000198431. [Q16881-5]
ENST00000525566; ENSP00000434516; ENSG00000198431. [Q16881-1]
ENST00000526390; ENSP00000435123; ENSG00000198431. [Q16881-2]
ENST00000526580; ENSP00000433887; ENSG00000198431.
ENST00000526691; ENSP00000435929; ENSG00000198431. [Q16881-4]
ENST00000529546; ENSP00000434919; ENSG00000198431.
ENST00000540716; ENSP00000442709; ENSG00000198431.
GeneID7296.
KEGGhsa:7296.
UCSCuc010swp.3. human. [Q16881-1]
uc021rcy.2. human. [Q16881-4]

Organism-specific databases

CTD7296.
GeneCardsGC12P104609.
H-InvDBHIX0010939.
HGNCHGNC:12437. TXNRD1.
HPACAB004607.
CAB015834.
HPA001395.
HPA043871.
MIM601112. gene.
neXtProtNX_Q16881.
PharmGKBPA37093.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1249.
HOVERGENHBG004959.
InParanoidQ16881.
KOK00384.
OrthoDBEOG779NXG.
PhylomeDBQ16881.
TreeFamTF314782.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ16881.
BgeeQ16881.
GenevestigatorQ16881.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
3.40.30.10. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR002109. Glutaredoxin.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR012336. Thioredoxin-like_fold.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PANTHERPTHR22912:SF23. PTHR22912:SF23. 1 hit.
PfamPF00462. Glutaredoxin. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF52833. SSF52833. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01438. TGR. 1 hit.
PROSITEPS51354. GLUTAREDOXIN_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTXNRD1. human.
EvolutionaryTraceQ16881.
GeneWikiTXNRD1.
GenomeRNAi7296.
NextBio28527.
PROQ16881.
SOURCESearch...

Entry information

Entry nameTRXR1_HUMAN
AccessionPrimary (citable) accession number: Q16881
Secondary accession number(s): B7Z1F4 expand/collapse secondary AC list , B7Z3Y8, B7Z904, E9PMY9, F5H780, Q6FI31, Q6VB40, Q6VB41, Q6VB42, Q6VBP2, Q6VBP3, Q6VBP4, Q6VBP5, Q6VBP9, Q6VBQ0, Q6YNQ1, Q76P53, Q7LA96, Q8WVC8, Q99475, Q9UES8, Q9UH79
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 26, 2008
Last modified: April 16, 2014
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM