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Q9NNW7

- TRXR2_HUMAN

UniProt

Q9NNW7 - TRXR2_HUMAN

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Protein

Thioredoxin reductase 2, mitochondrial

Gene
TXNRD2, KIAA1652, TRXR2
Organism
Homo sapiens (Human)
Status
Reviewed - 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

FAD By similarity.

Sites

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

Regions

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

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. NADP binding Source: InterPro
  3. protein binding Source: UniProtKB
  4. thioredoxin-disulfide reductase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. heart development Source: Ensembl
  3. hemopoiesis Source: Ensembl
  4. response to oxygen radical Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiREACT_172715. 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)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:18155. TXNRD2.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

Orphaneti154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA38302.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi86 ↔ 91Redox-active By similarityBy similarity
Modified residuei175 – 1751N6-succinyllysine By similarity
Modified residuei329 – 3291N6-succinyllysine By 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 1 Publication, high levels in kidney, whereas according to 1 Publication, levels are low.3 Publications

Gene expression databases

ArrayExpressiQ9NNW7.
BgeeiQ9NNW7.
GenevestigatoriQ9NNW7.

Organism-specific databases

HPAiCAB002007.
HPA003323.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi115836. 8 interactions.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1Emodel-A/B36-524[»]
ProteinModelPortaliQ9NNW7.
SMRiQ9NNW7. Positions 37-518.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG1249.
HOVERGENiHBG004959.
InParanoidiQ9NNW7.
KOiK00384.
OMAiHFTGPNA.
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. Align

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

Also known as: Alpha

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

MAAMAVALRG LGGRFRWRTQ AVAGGVRGAA RGAAAGQRDY DLLVVGGGSG    50
GLACAKEAAQ LGRKVAVVDY VEPSPQGTRW GLGGTCVNVG CIPKKLMHQA 100
ALLGGLIQDA PNYGWEVAQP VPHDWRKMAE AVQNHVKSLN WGHRVQLQDR 150
KVKYFNIKAS FVDEHTVCGV AKGGKEILLS ADHIIIATGG RPRYPTHIEG 200
ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI GLDTTIMMRS 250
IPLRGFDQQM SSMVIEHMAS HGTRFLRGCA PSRVRRLPDG QLQVTWEDST 300
TGKEDTGTFD TVLWAIGRVP DTRSLNLEKA GVDTSPDTQK ILVDSREATS 350
VPHIYAIGDV VEGRPELTPI AIMAGRLLVQ RLFGGSSDLM DYDNVPTTVF 400
TPLEYGCVGL SEEEAVARHG QEHVEVYHAH YKPLEFTVAG RDASQCYVKM 450
VCLREPPQLV LGLHFLGPNA GEVTQGFALG IKCGASYAQV MRTVGIHPTC 500
SEEVVKLRIS KRSGLDPTVT GCUG 524
Length:524
Mass (Da):56,507
Last modified:February 26, 2008 - v3
Checksum:iB575A185A2183DAC
GO
Isoform 2 (identifier: Q9NNW7-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

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

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. VSP_008306Add
BLAST
Alternative sequencei1 – 9696Missing in isoform 3. VSP_008305Add
BLAST
Alternative sequencei1 – 3030MAAMA…VRGAA → MEDQ in isoform 2. VSP_008304Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331Missing in AAG47635. 1 Publication
Sequence conflicti285 – 2851R → K in AAG47635. 1 Publication

Non-standard residue

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000400521; ENSP00000383365; ENSG00000184470. [Q9NNW7-1]
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS42981.1. [Q9NNW7-1 ]
RefSeqi NP_001269441.1. NM_001282512.1.
NP_006431.2. NM_006440.4. [Q9NNW7-1 ]
UniGenei Hs.443430.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W1E model - A/B 36-524 [» ]
ProteinModelPortali Q9NNW7.
SMRi Q9NNW7. Positions 37-518.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115836. 8 interactions.

Chemistry

BindingDBi Q9NNW7.
ChEMBLi CHEMBL2403.

PTM databases

PhosphoSitei Q9NNW7.

Polymorphism databases

DMDMi 182705230.

Proteomic databases

MaxQBi Q9NNW7.
PaxDbi Q9NNW7.
PRIDEi Q9NNW7.

Protocols and materials databases

DNASUi 10587.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000400521 ; ENSP00000383365 ; ENSG00000184470 . [Q9NNW7-1 ]
GeneIDi 10587.
KEGGi hsa:10587.
UCSCi uc002zqq.1. human. [Q9NNW7-4 ]
uc021wlj.1. human. [Q9NNW7-1 ]

Organism-specific databases

CTDi 10587.
GeneCardsi GC22M019863.
H-InvDB HIX0016244.
HGNCi HGNC:18155. TXNRD2.
HPAi CAB002007.
HPA003323.
MIMi 606448. gene.
neXtProti NX_Q9NNW7.
Orphaneti 154. Familial isolated dilated cardiomyopathy.
PharmGKBi PA38302.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1249.
HOVERGENi HBG004959.
InParanoidi Q9NNW7.
KOi K00384.
OMAi HFTGPNA.
PhylomeDBi Q9NNW7.
TreeFami TF314782.

Enzyme and pathway databases

Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSi TXNRD2. human.
GenomeRNAii 10587.
NextBioi 40203.
PROi Q9NNW7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NNW7.
Bgeei Q9NNW7.
Genevestigatori Q9NNW7.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. 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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01438. TGR. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1999) [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(1999) [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(1999) [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 (NOV-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(1999) [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 (NOV-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(1999) [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(2004) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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 19, 2003
Last sequence update: February 26, 2008
Last modified: September 3, 2014
This is version 141 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

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