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Protein

Thioredoxin reductase 2, mitochondrial

Gene

TXNRD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADUniRule annotationCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei497 – 4971Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 7030FADBy similarityAdd
BLAST

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. mercury (II) reductase activity Source: InterPro
  3. mercury ion binding Source: InterPro
  4. NADP binding Source: InterPro
  5. thioredoxin-disulfide reductase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. detoxification of mercury ion Source: InterPro
  3. response to oxygen radical Source: UniProtKB
  4. response to reactive oxygen species Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.8.1.9. 2681.
ReactomeiREACT_264249. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 2, mitochondrial (EC:1.8.1.9)
Alternative name(s):
Selenoprotein Z
Short name:
SelZ
TR-beta
Thioredoxin reductase TR3
Gene namesi
Name:TXNRD2
Synonyms:KIAA1652, TRXR2
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:18155. TXNRD2.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

Orphaneti361. Familial glucocorticoid deficiency.
154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA38302.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636MitochondrionSequence AnalysisAdd
BLAST
Chaini37 – 524488Thioredoxin reductase 2, mitochondrialPRO_0000030288Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi86 ↔ 91Redox-activeBy similarity
Modified residuei175 – 1751N6-succinyllysineBy similarity
Modified residuei329 – 3291N6-succinyllysineBy similarity
Cross-linki522 ↔ 523Cysteinyl-selenocysteine (Cys-Sec)By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9NNW7.
PaxDbiQ9NNW7.
PRIDEiQ9NNW7.

PTM databases

PhosphoSiteiQ9NNW7.

Expressioni

Tissue specificityi

Highly expressed in the prostate, ovary, liver, testis, uterus, colon and small intestine. Intermediate levels in brain, skeletal muscle, heart and spleen. Low levels in placenta, pancreas, thymus and peripheral blood leukocytes. According to PubMed:10608886, high levels in kidney, whereas according to PubMed:9923614, levels are low.3 Publications

Gene expression databases

BgeeiQ9NNW7.
GenevestigatoriQ9NNW7.

Organism-specific databases

HPAiCAB002007.
HPA003323.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi115836. 10 interactions.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1Emodel-A/B36-524[»]
ProteinModelPortaliQ9NNW7.
SMRiQ9NNW7. Positions 37-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00390000007578.
HOVERGENiHBG004959.
InParanoidiQ9NNW7.
KOiK00384.
OMAiVMRTVGI.
PhylomeDBiQ9NNW7.
TreeFamiTF314782.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NNW7-1) [UniParc]FASTAAdd to basket

Also known as: AlphaCurated

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.

« Hide

        10         20         30         40         50
MAAMAVALRG LGGRFRWRTQ AVAGGVRGAA RGAAAGQRDY DLLVVGGGSG
60 70 80 90 100
GLACAKEAAQ LGRKVAVVDY VEPSPQGTRW GLGGTCVNVG CIPKKLMHQA
110 120 130 140 150
ALLGGLIQDA PNYGWEVAQP VPHDWRKMAE AVQNHVKSLN WGHRVQLQDR
160 170 180 190 200
KVKYFNIKAS FVDEHTVCGV AKGGKEILLS ADHIIIATGG RPRYPTHIEG
210 220 230 240 250
ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI GLDTTIMMRS
260 270 280 290 300
IPLRGFDQQM SSMVIEHMAS HGTRFLRGCA PSRVRRLPDG QLQVTWEDST
310 320 330 340 350
TGKEDTGTFD TVLWAIGRVP DTRSLNLEKA GVDTSPDTQK ILVDSREATS
360 370 380 390 400
VPHIYAIGDV VEGRPELTPI AIMAGRLLVQ RLFGGSSDLM DYDNVPTTVF
410 420 430 440 450
TPLEYGCVGL SEEEAVARHG QEHVEVYHAH YKPLEFTVAG RDASQCYVKM
460 470 480 490 500
VCLREPPQLV LGLHFLGPNA GEVTQGFALG IKCGASYAQV MRTVGIHPTC
510 520
SEEVVKLRIS KRSGLDPTVT GCUG
Length:524
Mass (Da):56,507
Last modified:February 25, 2008 - v3
Checksum:iB575A185A2183DAC
GO
Isoform 2 (identifier: Q9NNW7-2) [UniParc]FASTAAdd to basket

Also known as: BetaCurated

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MAAMAVALRGLGGRFRWRTQAVAGGVRGAA → MEDQ

Show »
Length:498
Mass (Da):53,970
Checksum:i7B255499E2F1881E
GO
Isoform 3 (identifier: Q9NNW7-3) [UniParc]FASTAAdd to basket

Also known as: SelZf2

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Show »
Length:428
Mass (Da):46,841
Checksum:iCA7963D57A19ADAB
GO
Isoform 4 (identifier: Q9NNW7-4) [UniParc]FASTAAdd to basket

Also known as: SelZf1

The sequence of this isoform differs from the canonical sequence as follows:
     1-247: Missing.

Show »
Length:277
Mass (Da):30,291
Checksum:i80F3E412BF2738F3
GO

Sequence cautioni

The sequence AAD25167.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAG47635.1 differs from that shown. Reason: Erroneous termination at position 523. Translated as Sec.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331Missing in AAG47635 (Ref. 6) Curated
Sequence conflicti285 – 2851R → K in AAG47635 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141R → L.
Corresponds to variant rs45593642 [ dbSNP | Ensembl ].
VAR_051777
Natural varianti66 – 661A → S.3 Publications
Corresponds to variant rs5748469 [ dbSNP | Ensembl ].
VAR_051778
Natural varianti299 – 2991S → R.
Corresponds to variant rs5992495 [ dbSNP | Ensembl ].
VAR_051779
Natural varianti370 – 3701I → T.3 Publications
Corresponds to variant rs1139793 [ dbSNP | Ensembl ].
VAR_051780

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 247247Missing in isoform 4. 1 PublicationVSP_008306Add
BLAST
Alternative sequencei1 – 9696Missing in isoform 3. 1 PublicationVSP_008305Add
BLAST
Alternative sequencei1 – 3030MAAMA…VRGAA → MEDQ in isoform 2. CuratedVSP_008304Add
BLAST

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei523 – 5231Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171054 mRNA. Translation: AAD51324.1.
AF106697 mRNA. Translation: AAD19597.1.
AF044212 mRNA. Translation: AAD25167.1. Different initiation.
AB019694 mRNA. Translation: BAA77601.2.
AB019695 mRNA. Translation: BAA77602.2.
AF166126 mRNA. Translation: AAF21431.1.
AF166127 mRNA. Translation: AAF21432.1.
AF201385 mRNA. Translation: AAG47635.1. Sequence problems.
AC000078 Genomic DNA. No translation available.
AC000080 Genomic DNA. No translation available.
AC000090 Genomic DNA. No translation available.
BC007489 mRNA. Translation: AAH07489.3.
CCDSiCCDS42981.1. [Q9NNW7-1]
RefSeqiNP_001269441.1. NM_001282512.1.
NP_006431.2. NM_006440.4. [Q9NNW7-1]
UniGeneiHs.443430.

Genome annotation databases

GeneIDi10587.
KEGGihsa:10587.
UCSCiuc002zqq.1. human. [Q9NNW7-4]
uc021wlj.1. human. [Q9NNW7-1]

Polymorphism databases

DMDMi182705230.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171054 mRNA. Translation: AAD51324.1.
AF106697 mRNA. Translation: AAD19597.1.
AF044212 mRNA. Translation: AAD25167.1. Different initiation.
AB019694 mRNA. Translation: BAA77601.2.
AB019695 mRNA. Translation: BAA77602.2.
AF166126 mRNA. Translation: AAF21431.1.
AF166127 mRNA. Translation: AAF21432.1.
AF201385 mRNA. Translation: AAG47635.1. Sequence problems.
AC000078 Genomic DNA. No translation available.
AC000080 Genomic DNA. No translation available.
AC000090 Genomic DNA. No translation available.
BC007489 mRNA. Translation: AAH07489.3.
CCDSiCCDS42981.1. [Q9NNW7-1]
RefSeqiNP_001269441.1. NM_001282512.1.
NP_006431.2. NM_006440.4. [Q9NNW7-1]
UniGeneiHs.443430.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1Emodel-A/B36-524[»]
ProteinModelPortaliQ9NNW7.
SMRiQ9NNW7. Positions 37-518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115836. 10 interactions.

Chemistry

ChEMBLiCHEMBL2096978.

PTM databases

PhosphoSiteiQ9NNW7.

Polymorphism databases

DMDMi182705230.

Proteomic databases

MaxQBiQ9NNW7.
PaxDbiQ9NNW7.
PRIDEiQ9NNW7.

Protocols and materials databases

DNASUi10587.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi10587.
KEGGihsa:10587.
UCSCiuc002zqq.1. human. [Q9NNW7-4]
uc021wlj.1. human. [Q9NNW7-1]

Organism-specific databases

CTDi10587.
GeneCardsiGC22M019863.
H-InvDBHIX0016244.
HGNCiHGNC:18155. TXNRD2.
HPAiCAB002007.
HPA003323.
MIMi606448. gene.
neXtProtiNX_Q9NNW7.
Orphaneti361. Familial glucocorticoid deficiency.
154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA38302.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00390000007578.
HOVERGENiHBG004959.
InParanoidiQ9NNW7.
KOiK00384.
OMAiVMRTVGI.
PhylomeDBiQ9NNW7.
TreeFamiTF314782.

Enzyme and pathway databases

BRENDAi1.8.1.9. 2681.
ReactomeiREACT_264249. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiTXNRD2. human.
GenomeRNAii10587.
NextBioi40203.
PROiQ9NNW7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NNW7.
GenevestigatoriQ9NNW7.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases."
    Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., Gladyshev V.N.
    J. Biol. Chem. 274:24522-24530(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning, sequencing and functional expression of a novel human thioredoxin reductase."
    Gasdaska P.Y., Berggren M.M., Berry M.J., Powis G.
    FEBS Lett. 442:105-111(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-66.
    Tissue: Fetal heart and Placenta.
  3. "Human mitochondrial thioredoxin reductase: cDNA cloning, expression and genomic organization."
    Miranda-Vizuete A., Damdimopoulos A.E., Pedrajas J.R., Gustafsson J.-A., Spyrou G.
    Eur. J. Biochem. 261:405-412(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Adrenal gland and Testis.
  4. Toji S., Yano M., Tamai K.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), VARIANT THR-370.
  5. "Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif."
    Lescure A., Gautheret D., Carbon P., Krol A.
    J. Biol. Chem. 274:38147-38154(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, VARIANT THR-370.
    Tissue: Cervix carcinoma.
  6. Kim J.-R., Lee Y.H., Lee S.-R., Kim B.H., Rhee S.G., Kim J.H.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), VARIANTS SER-66 AND THR-370.
  7. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 40-524, VARIANT SER-66.
    Tissue: Skin.
  9. "Heterogeneity within animal thioredoxin reductases: evidence for alternative first exon splicing."
    Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N.
    J. Biol. Chem. 276:3106-3114(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTRXR2_HUMAN
AccessioniPrimary (citable) accession number: Q9NNW7
Secondary accession number(s): O95840
, Q96IJ2, Q9H2Z5, Q9NZV3, Q9NZV4, Q9P2Y0, Q9P2Y1, Q9UQU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 18, 2003
Last sequence update: February 25, 2008
Last modified: March 31, 2015
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond. The selenocysteine residue is essential for enzymatic activity (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.