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P97493

- THIOM_MOUSE

UniProt

P97493 - THIOM_MOUSE

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Protein

Thioredoxin, mitochondrial

Gene
Txn2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential By similarity. Possesses a dithiol-reducing activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei84 – 841Deprotonates C-terminal active site Cys By similarity
Active sitei90 – 901Nucleophile By similarity
Sitei91 – 911Contributes to redox potential value By similarity
Sitei92 – 921Contributes to redox potential value By similarity
Active sitei93 – 931Nucleophile By similarity

GO - Molecular functioni

  1. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to nutrient levels Source: Ensembl
  3. glycerol ether metabolic process Source: InterPro
  4. response to axon injury Source: Ensembl
  5. response to drug Source: Ensembl
  6. response to glucose Source: Ensembl
  7. response to hormone Source: Ensembl
  8. response to hypoxia Source: Ensembl
  9. response to nutrient Source: Ensembl
  10. response to organic cyclic compound Source: Ensembl
  11. response to oxidative stress Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin, mitochondrial
Short name:
MTRX
Short name:
Mt-Trx
Alternative name(s):
Thioredoxin-2
Gene namesi
Name:Txn2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1929468. Txn2.

Subcellular locationi

GO - Cellular componenti

  1. dendrite Source: Ensembl
  2. mitochondrion Source: MGI
  3. neuronal cell body Source: Ensembl
  4. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5959Mitochondrion By similarityAdd
BLAST
Chaini60 – 166107Thioredoxin, mitochondrialPRO_0000034151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi90 ↔ 93Redox-active By similarity
Modified residuei152 – 1521N6-acetyllysine; alternate By similarity
Modified residuei152 – 1521N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP97493.
PaxDbiP97493.
PRIDEiP97493.

PTM databases

PhosphoSiteiP97493.

Expressioni

Gene expression databases

BgeeiP97493.
CleanExiMM_TXN2.
GenevestigatoriP97493.

Interactioni

Protein-protein interaction databases

IntActiP97493. 1 interaction.
MINTiMINT-4137662.
STRINGi10090.ENSMUSP00000105370.

Structurei

3D structure databases

ProteinModelPortaliP97493.
SMRiP97493. Positions 60-166.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 166106ThioredoxinAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.
Contains 1 thioredoxin domain.

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00530000064086.
HOGENOMiHOG000292977.
HOVERGENiHBG009243.
InParanoidiA2A440.
KOiK03671.
OMAiSFNVQDH.
PhylomeDBiP97493.
TreeFamiTF314517.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97493-1 [UniParc]FASTAAdd to Basket

« Hide

MAQRLLLGRF LTSVISRKPP QGVWASLTSK TLQTPQYNAG GLTVMPSPAR    50
TVHTTRVCLT TFNVQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL 100
EKMVAKQHGK VVMAKVDIDD HTDLAIEYEV SAVPTVLAIK NGDVVDKFVG 150
IKDEDQLEAF LKKLIG 166
Length:166
Mass (Da):18,255
Last modified:May 1, 1997 - v1
Checksum:iC9A803DF571F3A7D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U85089 mRNA. Translation: AAB41900.1.
AK002358 mRNA. Translation: BAB22037.1.
AK010917 mRNA. Translation: BAB27267.1.
AK147164 mRNA. Translation: BAE27729.1.
AK149855 mRNA. Translation: BAE29126.1.
AK167754 mRNA. Translation: BAE39789.1.
AK167925 mRNA. Translation: BAE39930.1.
AK168322 mRNA. Translation: BAE40261.1.
AL583886 Genomic DNA. Translation: CAM23427.1.
BC068182 mRNA. Translation: AAH68182.1.
CCDSiCCDS27606.1.
RefSeqiNP_064297.1. NM_019913.5.
UniGeneiMm.291917.
Mm.462887.

Genome annotation databases

EnsembliENSMUST00000005487; ENSMUSP00000005487; ENSMUSG00000005354.
ENSMUST00000109748; ENSMUSP00000105370; ENSMUSG00000005354.
GeneIDi56551.
KEGGimmu:56551.
UCSCiuc007wof.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U85089 mRNA. Translation: AAB41900.1 .
AK002358 mRNA. Translation: BAB22037.1 .
AK010917 mRNA. Translation: BAB27267.1 .
AK147164 mRNA. Translation: BAE27729.1 .
AK149855 mRNA. Translation: BAE29126.1 .
AK167754 mRNA. Translation: BAE39789.1 .
AK167925 mRNA. Translation: BAE39930.1 .
AK168322 mRNA. Translation: BAE40261.1 .
AL583886 Genomic DNA. Translation: CAM23427.1 .
BC068182 mRNA. Translation: AAH68182.1 .
CCDSi CCDS27606.1.
RefSeqi NP_064297.1. NM_019913.5.
UniGenei Mm.291917.
Mm.462887.

3D structure databases

ProteinModelPortali P97493.
SMRi P97493. Positions 60-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97493. 1 interaction.
MINTi MINT-4137662.
STRINGi 10090.ENSMUSP00000105370.

PTM databases

PhosphoSitei P97493.

Proteomic databases

MaxQBi P97493.
PaxDbi P97493.
PRIDEi P97493.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005487 ; ENSMUSP00000005487 ; ENSMUSG00000005354 .
ENSMUST00000109748 ; ENSMUSP00000105370 ; ENSMUSG00000005354 .
GeneIDi 56551.
KEGGi mmu:56551.
UCSCi uc007wof.1. mouse.

Organism-specific databases

CTDi 25828.
MGIi MGI:1929468. Txn2.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00530000064086.
HOGENOMi HOG000292977.
HOVERGENi HBG009243.
InParanoidi A2A440.
KOi K03671.
OMAi SFNVQDH.
PhylomeDBi P97493.
TreeFami TF314517.

Enzyme and pathway databases

Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSi TXN2. mouse.
NextBioi 312931.
PROi P97493.
SOURCEi Search...

Gene expression databases

Bgeei P97493.
CleanExi MM_TXN2.
Genevestigatori P97493.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
PANTHERi PTHR10438. PTHR10438. 1 hit.
Pfami PF00085. Thioredoxin. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 1 hit.
TIGRFAMsi TIGR01068. thioredoxin. 1 hit.
PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Miranda-Vizuete A., Gustafsson J.-A., Spyrou G.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Bone marrow, Kidney and Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  5. "The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice."
    Nonn L., Williams R.R., Erickson R.P., Powis G.
    Mol. Cell. Biol. 23:916-922(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTHIOM_MOUSE
AccessioniPrimary (citable) accession number: P97493
Secondary accession number(s): A2A440, Q545D5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi