O95881 · TXD12_HUMAN
- ProteinThioredoxin domain-containing protein 12
- GeneTXNDC12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids172 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol-disulfide oxidase activity.
Catalytic activity
- [protein]-disulfide + 2 glutathione = [protein]-dithiol + glutathione disulfideThis reaction proceeds in the backward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
25 μM | Asn-Arg-Cys-Ser-Gln-Gly-Ser-Cys-Trp-Asn |
pH Dependence
Optimum pH is 6.5.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum lumen | |
Molecular Function | protein-disulfide reductase (glutathione) activity | |
Molecular Function | protein-disulfide reductase activity | |
Biological Process | negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThioredoxin domain-containing protein 12
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95881
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 66 | Loss of protein-disulfide reductase (glutathione) activity. Loss of the formation of disulfide bonds in substrate. | ||||
Sequence: C → S | ||||||
Mutagenesis | 69 | Loss of protein-disulfide reductase (glutathione) activity. Loss of the formation of disulfide bonds in substrate. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 162 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: METRPRLGATCLLGFSFLLLVISSDG | ||||||
Chain | PRO_0000034189 | 27-172 | Thioredoxin domain-containing protein 12 | |||
Sequence: HNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDPSGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEAQERLTGDAFRKKHLEDEL | ||||||
Disulfide bond | 66↔69 | Redox-active | ||||
Sequence: CGAC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95881 | CAMLG P49069 | 5 | EBI-2564581, EBI-1748958 | |
BINARY | O95881 | DPF2 Q92785 | 3 | EBI-2564581, EBI-359932 | |
BINARY | O95881 | FKBP7 Q9Y680 | 3 | EBI-2564581, EBI-3918971 | |
BINARY | O95881 | KLHL2 O95198 | 4 | EBI-2564581, EBI-746999 | |
BINARY | O95881 | SGTA O43765 | 3 | EBI-2564581, EBI-347996 | |
BINARY | O95881 | SGTB Q96EQ0 | 6 | EBI-2564581, EBI-744081 | |
BINARY | O95881 | UBQLN1 Q9UMX0 | 4 | EBI-2564581, EBI-741480 | |
BINARY | O95881 | UBQLN1 Q9UMX0-2 | 3 | EBI-2564581, EBI-10173939 | |
BINARY | O95881 | UBQLN2 Q9UHD9 | 3 | EBI-2564581, EBI-947187 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-156 | Thioredoxin | ||||
Sequence: HNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDPSGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEAQE | ||||||
Motif | 169-172 | Prevents secretion from ER | ||||
Sequence: EDEL |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length172
- Mass (Da)19,206
- Last updated1999-05-01 v1
- Checksum3092E9515A7C4094
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 102 | in Ref. 6; AAH08913 | ||||
Sequence: D → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF543416 EMBL· GenBank· DDBJ | AAN34781.1 EMBL· GenBank· DDBJ | mRNA | ||
AF131758 EMBL· GenBank· DDBJ | AAD20035.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358982 EMBL· GenBank· DDBJ | AAQ89341.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075409 EMBL· GenBank· DDBJ | BAG52132.1 EMBL· GenBank· DDBJ | mRNA | ||
AL445685 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC001493 EMBL· GenBank· DDBJ | AAH01493.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008953 EMBL· GenBank· DDBJ | AAH08953.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008913 EMBL· GenBank· DDBJ | AAH08913.1 EMBL· GenBank· DDBJ | mRNA |