UniProtKB - Q15084 (PDIA6_HUMAN)
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- BLAST>sp|Q15084|PDIA6_HUMAN Protein disulfide-isomerase A6 OS=Homo sapiens OX=9606 GN=PDIA6 PE=1 SV=1 MALLVLGLVSCTFFLAVNGLYSSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQR LTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNRPEDYQGGRTG EAIVDAALSALRQLVKDRLGGRSGGYSSGKQGRSDSSSKKDVIELTDDSFDKNVLDSEDV WMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTI KIFQKGESPVDYDGGRTRSDIVSRALDLFSDNAPPPELLEIINEDIAKRTCEEHQLCVVA VLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGFGYPAMA AINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFPTIVEREPWDGRDGELP VEDDIDLSDVELDDLGKDEL
- Align
Protein disulfide-isomerase A6
PDIA6
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"A role for the thiol isomerase protein ERP5 in platelet function."
Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T., Authi K.S., Gibbins J.M.
Blood 105:1500-1507(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 20-34, FUNCTION, ENZYME ACTIVITY, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.10"Functional analysis of human P5, a protein disulfide isomerase homologue."
Kikuchi M., Doi E., Tsujimoto I., Horibe T., Tsujimoto Y.
J. Biochem. 132:451-455(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF CYS-55; CYS-58; CYS-190 AND CYS-193. - Ref.26"Protein disulfide isomerase A6 controls the decay of IRE1alpha signaling via disulfide-dependent association."
Eletto D., Eletto D., Dersh D., Gidalevitz T., Argon Y.
Mol. Cell 53:562-576(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ERN1 AND EIF2AK3, MUTAGENESIS OF CYS-58 AND CYS-193.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"A role for the thiol isomerase protein ERP5 in platelet function."
Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T., Authi K.S., Gibbins J.M.
Blood 105:1500-1507(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 20-34, FUNCTION, ENZYME ACTIVITY, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.10"Functional analysis of human P5, a protein disulfide isomerase homologue."
Kikuchi M., Doi E., Tsujimoto I., Horibe T., Tsujimoto Y.
J. Biochem. 132:451-455(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF CYS-55; CYS-58; CYS-190 AND CYS-193.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 55 | NucleophileBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 56 | Contributes to redox potential valueBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 57 | Contributes to redox potential valueBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 58 | NucleophileBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 118 | Lowers pKa of C-terminal Cys of first active siteBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 190 | NucleophileBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 191 | Contributes to redox potential valueBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 192 | Contributes to redox potential valueBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 193 | NucleophileBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 256 | Lowers pKa of C-terminal Cys of second active siteBy similarity | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- peptide disulfide oxidoreductase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein disulfide isomerase activity Source: GO_Central
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- apoptotic cell clearance Source: GO_Central
- cell redox homeostasis Source: InterPro
- cellular protein metabolic process Source: Reactome
- IRE1-mediated unfolded protein response Source: Reactome
- post-translational protein modification Source: Reactome
- protein folding Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- response to endoplasmic reticulum stress Source: GO_Central
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Chaperone, Isomerase |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-381038. XBP1(S) activates chaperone genes. R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). R-HSA-8957275. Post-translational protein phosphorylation. |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Protein disulfide-isomerase A6 (EC:5.3.4.12 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Alternative name(s): Endoplasmic reticulum protein 5 Short name: ER protein 5 Short name: ERp5 Protein disulfide isomerase P5 Thioredoxin domain-containing protein 7 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:PDIA6 Synonyms:ERP5, P5, TXNDC7 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000143870.12. |
Human Gene Nomenclature Database More...HGNCi | HGNC:30168. PDIA6. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 611099. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q15084. |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum lumen 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"A role for the thiol isomerase protein ERP5 in platelet function."
Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T., Authi K.S., Gibbins J.M.
Blood 105:1500-1507(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 20-34, FUNCTION, ENZYME ACTIVITY, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Endoplasmic reticulum lumen 1 Publication
Plasma membrane
- Cell membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"A role for the thiol isomerase protein ERP5 in platelet function."
Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T., Authi K.S., Gibbins J.M.
Blood 105:1500-1507(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 20-34, FUNCTION, ENZYME ACTIVITY, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Cell membrane 1 Publication
Other locations
- Melanosome 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.12"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. - Ref.14"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545).1 Publication- Melanosome 2 Publications
- Ref.12"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cytosol
- cytosol Source: HPA
Endoplasmic reticulum
- endoplasmic reticulum Source: HPA
- endoplasmic reticulum chaperone complex Source: ParkinsonsUK-UCL
- endoplasmic reticulum lumen Source: Reactome
- endoplasmic reticulum membrane Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular space Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- melanosome Source: UniProtKB-SubCell
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Endoplasmic reticulum, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 55 | C → S: 50% decrease in enzyme activity; when associated with S-58. Abolishes enzyme activity; when associated with S-58; S-190 and S-193. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 58 | C → A: Accelerates dephosphorylation of ERN1; when associated with A-193. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 58 | C → S: 50% decrease in enzyme activity; when associated with S-55. 90% decrease in enzyme activity; when associated with S-193. Abolishes enzyme activity; when associated with S-55; S-190 and S-193. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 190 | C → S: 25% decrease in enzyme activity; when associated with S-193. Abolishes enzyme activity; when associated with S-55; S-58 and S-193. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 193 | C → A: Accelerates dephosphorylation of ERN1; when associated with A-58. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 193 | C → S: 90% decrease in enzyme activity; when associated with S-58. 25% decrease in enzyme activity; when associated with S-190. Abolishes enzyme activity; when associated with S-55; S-58 and S-190. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 10130. |
Open Targets More...OpenTargetsi | ENSG00000143870. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134977905. |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2146308. |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 2501205. |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 19 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 19 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000034236 | 20 – 440 | Protein disulfide-isomerase A6Add BLAST | 421 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 55 ↔ 58 | Redox-activePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 129 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 156 | Phosphoserine; by FAM20C1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 158 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 190 ↔ 193 | Redox-activePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 428 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q15084. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q15084. |
PeptideAtlas More...PeptideAtlasi | Q15084. |
PRoteomics IDEntifications database More...PRIDEi | Q15084. |
2D gel databases
USC-OGP 2-DE database More...OGPi | Q15084. |
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00644989. Q15084. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q15084. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q15084. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q15084. |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression"><span class="caps">P92958</span></a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="http://www.uniprot.org/uniprot/O14734#expression"><span class="caps">O14734</span></a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"A role for the thiol isomerase protein ERP5 in platelet function."
Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T., Authi K.S., Gibbins J.M.
Blood 105:1500-1507(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 20-34, FUNCTION, ENZYME ACTIVITY, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000143870. |
CleanEx database of gene expression profiles More...CleanExi | HS_PDIA6. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q15084. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q15084. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB034347. HPA034652. HPA034653. |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"A role for the thiol isomerase protein ERP5 in platelet function."
Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T., Authi K.S., Gibbins J.M.
Blood 105:1500-1507(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 20-34, FUNCTION, ENZYME ACTIVITY, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.11"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]Cited for: COMPONENT OF A CHAPERONE COMPLEX. - Ref.16"Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands."
Kaiser B.K., Yim D., Chow I.-T., Gonzalez S., Dai Z., Mann H.H., Strong R.K., Groh V., Spies T.
Nature 447:482-486(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MICA. - Ref.26"Protein disulfide isomerase A6 controls the decay of IRE1alpha signaling via disulfide-dependent association."
Eletto D., Eletto D., Dersh D., Gidalevitz T., Argon Y.
Mol. Cell 53:562-576(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ERN1 AND EIF2AK3, MUTAGENESIS OF CYS-58 AND CYS-193.
<p>This subsection of the ‘<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>’ section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| PRDX4 | Q13162 | 2 | EBI-1043087,EBI-2211957 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115434. 107 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q15084. |
Protein interaction database and analysis system More...IntActi | Q15084. 45 interactors. |
Molecular INTeraction database More...MINTi | Q15084. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000272227. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 28 – 30 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 32 – 34 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 35 – 38 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 39 – 41 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 46 – 51 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 56 – 71 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 72 – 75 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 76 – 82 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 83 – 85 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 87 – 92 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 100 – 104 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 120 – 139 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 162 – 164 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 167 – 169 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 170 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 174 – 176 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 178 – 186 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 191 – 211 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 214 – 221 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 222 – 224 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 226 – 231 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 236 – 243 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 247 – 252 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 258 – 271 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1X5D | NMR | - | A | 161-280 | [»] | |
| 3VWW | X-ray | 1.93 | A/B | 25-140 | [»] | |
| 3W8J | X-ray | 2.10 | A/B | 20-140 | [»] | |
| 4EF0 | X-ray | 1.50 | A/B | 27-140 | [»] | |
| 4GWR | X-ray | 1.81 | A/B | 160-274 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q15084. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q15084. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q15084. |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 20 – 133 | Thioredoxin 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 114 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 154 – 287 | Thioredoxin 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 134 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 437 – 440 | Prevents secretion from ERPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi | 4 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 422 – 434 | Asp/Glu-rich (acidic)Add BLAST | 13 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Redox-active center, Repeat, SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0191. Eukaryota. COG0526. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00860000133723. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000012631. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG053548. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q15084. |
KEGG Orthology (KO) More...KOi | K09584. |
Identification of Orthologs from Complete Genome Data More...OMAi | PHILDCD. |
Database of Orthologous Groups More...OrthoDBi | EOG091G07Z0. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q15084. |
TreeFam database of animal gene trees More...TreeFami | TF315231. |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005788. Disulphide_isomerase. IPR036249. Thioredoxin-like_sf. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00085. Thioredoxin. 2 hits. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52833. SSF52833. 3 hits. |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01126. pdi_dom. 2 hits. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
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.
10 20 30 40 50
MALLVLGLVS CTFFLAVNGL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF
60 70 80 90 100
YAPWCGHCQR LTPEWKKAAT ALKDVVKVGA VDADKHHSLG GQYGVQGFPT
110 120 130 140 150
IKIFGSNKNR PEDYQGGRTG EAIVDAALSA LRQLVKDRLG GRSGGYSSGK
160 170 180 190 200
QGRSDSSSKK DVIELTDDSF DKNVLDSEDV WMVEFYAPWC GHCKNLEPEW
210 220 230 240 250
AAAASEVKEQ TKGKVKLAAV DATVNQVLAS RYGIRGFPTI KIFQKGESPV
260 270 280 290 300
DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKRT CEEHQLCVVA
310 320 330 340 350
VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQSELETALG
360 370 380 390 400
IGGFGYPAMA AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG
410 420 430 440
GAFPTIVERE PWDGRDGELP VEDDIDLSDV ELDDLGKDEL
The sequence of this isoform differs from the canonical sequence as follows:
1-6: MALLVL → MRRDLREKLVWVCRPLAPVEVPANISSDFQPCSPTSPAHSLSRKSPIMYPSTTMANAP
10 20 30 40 50
MRRDLREKLV WVCRPLAPVE VPANISSDFQ PCSPTSPAHS LSRKSPIMYP
60 70 80 90 100
STTMANAPGL VSCTFFLAVN GLYSSSDDVI ELTPSNFNRE VIQSDSLWLV
110 120 130 140 150
EFYAPWCGHC QRLTPEWKKA ATALKDVVKV GAVDADKHHS LGGQYGVQGF
160 170 180 190 200
PTIKIFGSNK NRPEDYQGGR TGEAIVDAAL SALRQLVKDR LGGRSGGYSS
210 220 230 240 250
GKQGRSDSSS KKDVIELTDD SFDKNVLDSE DVWMVEFYAP WCGHCKNLEP
260 270 280 290 300
EWAAAASEVK EQTKGKVKLA AVDATVNQVL ASRYGIRGFP TIKIFQKGES
310 320 330 340 350
PVDYDGGRTR SDIVSRALDL FSDNAPPPEL LEIINEDIAK RTCEEHQLCV
360 370 380 390 400
VAVLPHILDT GAAGRNSYLE VLLKLADKYK KKMWGWLWTE AGAQSELETA
410 420 430 440 450
LGIGGFGYPA MAAINARKMK FALLKGSFSE QGINEFLREL SFGRGSTAPV
460 470 480 490
GGGAFPTIVE REPWDGRDGE LPVEDDIDLS DVELDDLGKD EL
The sequence of this isoform differs from the canonical sequence as follows:
1-5: MALLV → MI
10 20 30 40 50
MILGLVSCTF FLAVNGLYSS SDDVIELTPS NFNREVIQSD SLWLVEFYAP
60 70 80 90 100
WCGHCQRLTP EWKKAATALK DVVKVGAVDA DKHHSLGGQY GVQGFPTIKI
110 120 130 140 150
FGSNKNRPED YQGGRTGEAI VDAALSALRQ LVKDRLGGRS GGYSSGKQGR
160 170 180 190 200
SDSSSKKDVI ELTDDSFDKN VLDSEDVWMV EFYAPWCGHC KNLEPEWAAA
210 220 230 240 250
ASEVKEQTKG KVKLAAVDAT VNQVLASRYG IRGFPTIKIF QKGESPVDYD
260 270 280 290 300
GGRTRSDIVS RALDLFSDNA PPPELLEIIN EDIAKRTCEE HQLCVVAVLP
310 320 330 340 350
HILDTGAAGR NSYLEVLLKL ADKYKKKMWG WLWTEAGAQS ELETALGIGG
360 370 380 390 400
FGYPAMAAIN ARKMKFALLK GSFSEQGINE FLRELSFGRG STAPVGGGAF
410 420 430
PTIVEREPWD GRDGELPVED DIDLSDVELD DLGKDEL
The sequence of this isoform differs from the canonical sequence as follows:
1-6: MALLVL → MYPSTTMANAP
10 20 30 40 50
MYPSTTMANA PGLVSCTFFL AVNGLYSSSD DVIELTPSNF NREVIQSDSL
60 70 80 90 100
WLVEFYAPWC GHCQRLTPEW KKAATALKDV VKVGAVDADK HHSLGGQYGV
110 120 130 140 150
QGFPTIKIFG SNKNRPEDYQ GGRTGEAIVD AALSALRQLV KDRLGGRSGG
160 170 180 190 200
YSSGKQGRSD SSSKKDVIEL TDDSFDKNVL DSEDVWMVEF YAPWCGHCKN
210 220 230 240 250
LEPEWAAAAS EVKEQTKGKV KLAAVDATVN QVLASRYGIR GFPTIKIFQK
260 270 280 290 300
GESPVDYDGG RTRSDIVSRA LDLFSDNAPP PELLEIINED IAKRTCEEHQ
310 320 330 340 350
LCVVAVLPHI LDTGAAGRNS YLEVLLKLAD KYKKKMWGWL WTEAGAQSEL
360 370 380 390 400
ETALGIGGFG YPAMAAINAR KMKFALLKGS FSEQGINEFL RELSFGRGST
410 420 430 440
APVGGGAFPT IVEREPWDGR DGELPVEDDI DLSDVELDDL GKDEL
The sequence of this isoform differs from the canonical sequence as follows:
1-6: MALLVL → MRIITAPASKVSRGSNELMILARRSDRGSPTSPAHSLSRKSPIMYPSTTMANAP
10 20 30 40 50
MRIITAPASK VSRGSNELMI LARRSDRGSP TSPAHSLSRK SPIMYPSTTM
60 70 80 90 100
ANAPGLVSCT FFLAVNGLYS SSDDVIELTP SNFNREVIQS DSLWLVEFYA
110 120 130 140 150
PWCGHCQRLT PEWKKAATAL KDVVKVGAVD ADKHHSLGGQ YGVQGFPTIK
160 170 180 190 200
IFGSNKNRPE DYQGGRTGEA IVDAALSALR QLVKDRLGGR SGGYSSGKQG
210 220 230 240 250
RSDSSSKKDV IELTDDSFDK NVLDSEDVWM VEFYAPWCGH CKNLEPEWAA
260 270 280 290 300
AASEVKEQTK GKVKLAAVDA TVNQVLASRY GIRGFPTIKI FQKGESPVDY
310 320 330 340 350
DGGRTRSDIV SRALDLFSDN APPPELLEII NEDIAKRTCE EHQLCVVAVL
360 370 380 390 400
PHILDTGAAG RNSYLEVLLK LADKYKKKMW GWLWTEAGAQ SELETALGIG
410 420 430 440 450
GFGYPAMAAI NARKMKFALL KGSFSEQGIN EFLRELSFGR GSTAPVGGGA
460 470 480
FPTIVEREPW DGRDGELPVE DDIDLSDVEL DDLGKDEL
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 64 | E → K in BAH12614 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 187 | A → V in BAH12614 (PubMed:14702039).Curated | 1 |
Natural variant
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D49489 mRNA. Translation: BAA08450.1. AK127433 mRNA. Translation: BAC86977.1. AK131234 mRNA. Translation: BAG54757.1. AK289428 mRNA. Translation: BAF82117.1. AK294347 mRNA. Translation: BAH11740.1. AK297547 mRNA. Translation: BAH12614.1. AC092687 Genomic DNA. Translation: AAY24070.1. CH471053 Genomic DNA. Translation: EAX00950.1. BC001312 mRNA. Translation: AAH01312.1. U79278 mRNA. Translation: AAB50217.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1675.1. [Q15084-1] CCDS62852.1. [Q15084-3] CCDS62853.1. [Q15084-4] CCDS62854.1. [Q15084-2] CCDS62855.1. [Q15084-5] |
Protein sequence database of the Protein Information Resource More...PIRi | JC4369. |
NCBI Reference Sequences More...RefSeqi | NP_001269633.1. NM_001282704.1. [Q15084-2] NP_001269634.1. NM_001282705.1. [Q15084-5] NP_001269635.1. NM_001282706.1. [Q15084-4] NP_001269636.1. NM_001282707.1. [Q15084-3] NP_005733.1. NM_005742.3. [Q15084-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.212102. Hs.580464. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000272227; ENSP00000272227; ENSG00000143870. [Q15084-1] ENST00000381611; ENSP00000371024; ENSG00000143870. [Q15084-4] ENST00000404371; ENSP00000385385; ENSG00000143870. [Q15084-2] ENST00000404824; ENSP00000384459; ENSG00000143870. [Q15084-5] ENST00000540494; ENSP00000438778; ENSG00000143870. [Q15084-3] ENST00000617249; ENSP00000481892; ENSG00000143870. [Q15084-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10130. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10130. |
UCSC genome browser More...UCSCi | uc002rau.5. human. [Q15084-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D49489 mRNA. Translation: BAA08450.1. AK127433 mRNA. Translation: BAC86977.1. AK131234 mRNA. Translation: BAG54757.1. AK289428 mRNA. Translation: BAF82117.1. AK294347 mRNA. Translation: BAH11740.1. AK297547 mRNA. Translation: BAH12614.1. AC092687 Genomic DNA. Translation: AAY24070.1. CH471053 Genomic DNA. Translation: EAX00950.1. BC001312 mRNA. Translation: AAH01312.1. U79278 mRNA. Translation: AAB50217.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1675.1. [Q15084-1] CCDS62852.1. [Q15084-3] CCDS62853.1. [Q15084-4] CCDS62854.1. [Q15084-2] CCDS62855.1. [Q15084-5] |
Protein sequence database of the Protein Information Resource More...PIRi | JC4369. |
NCBI Reference Sequences More...RefSeqi | NP_001269633.1. NM_001282704.1. [Q15084-2] NP_001269634.1. NM_001282705.1. [Q15084-5] NP_001269635.1. NM_001282706.1. [Q15084-4] NP_001269636.1. NM_001282707.1. [Q15084-3] NP_005733.1. NM_005742.3. [Q15084-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.212102. Hs.580464. |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1X5D | NMR | - | A | 161-280 | [»] | |
| 3VWW | X-ray | 1.93 | A/B | 25-140 | [»] | |
| 3W8J | X-ray | 2.10 | A/B | 20-140 | [»] | |
| 4EF0 | X-ray | 1.50 | A/B | 27-140 | [»] | |
| 4GWR | X-ray | 1.81 | A/B | 160-274 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q15084. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q15084. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115434. 107 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q15084. |
Protein interaction database and analysis system More...IntActi | Q15084. 45 interactors. |
Molecular INTeraction database More...MINTi | Q15084. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000272227. |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2146308. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q15084. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q15084. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q15084. |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 2501205. |
2D gel databases
USC-OGP 2-DE database More...OGPi | Q15084. |
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00644989. Q15084. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q15084. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q15084. |
PeptideAtlas More...PeptideAtlasi | Q15084. |
PRoteomics IDEntifications database More...PRIDEi | Q15084. |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 10130. |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000272227; ENSP00000272227; ENSG00000143870. [Q15084-1] ENST00000381611; ENSP00000371024; ENSG00000143870. [Q15084-4] ENST00000404371; ENSP00000385385; ENSG00000143870. [Q15084-2] ENST00000404824; ENSP00000384459; ENSG00000143870. [Q15084-5] ENST00000540494; ENSP00000438778; ENSG00000143870. [Q15084-3] ENST00000617249; ENSP00000481892; ENSG00000143870. [Q15084-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10130. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10130. |
UCSC genome browser More...UCSCi | uc002rau.5. human. [Q15084-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 10130. |
DisGeNET More...DisGeNETi | 10130. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000143870.12. |
GeneCards: human genes, protein and diseases More...GeneCardsi | PDIA6. |
Human Gene Nomenclature Database More...HGNCi | HGNC:30168. PDIA6. |
Human Protein Atlas More...HPAi | CAB034347. HPA034652. HPA034653. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 611099. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q15084. |
Open Targets More...OpenTargetsi | ENSG00000143870. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134977905. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0191. Eukaryota. COG0526. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00860000133723. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000012631. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG053548. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q15084. |
KEGG Orthology (KO) More...KOi | K09584. |
Identification of Orthologs from Complete Genome Data More...OMAi | PHILDCD. |
Database of Orthologous Groups More...OrthoDBi | EOG091G07Z0. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q15084. |
TreeFam database of animal gene trees More...TreeFami | TF315231. |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-381038. XBP1(S) activates chaperone genes. R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). R-HSA-8957275. Post-translational protein phosphorylation. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | PDIA6. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q15084. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 10130. |
Protein Ontology More...PROi | PR:Q15084. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000143870. |
CleanEx database of gene expression profiles More...CleanExi | HS_PDIA6. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q15084. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q15084. HS. |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005788. Disulphide_isomerase. IPR036249. Thioredoxin-like_sf. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00085. Thioredoxin. 2 hits. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52833. SSF52833. 3 hits. |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01126. pdi_dom. 2 hits. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | PDIA6_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q15084Primary (citable) accession number: Q15084 Secondary accession number(s): B3KY95 , B5MCQ5, B7Z254, B7Z4M8, F8WA83, Q53RC7, Q6ZSH5, Q99778 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
| Last sequence update: | November 1, 1997 | |
| Last modified: | March 28, 2018 | |
| This is version 198 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |