UniProtKB - P11142 (HSP7C_HUMAN)
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- BLAST>sp|P11142|HSP7C_HUMAN Heat shock cognate 71 kDa protein OS=Homo sapiens OX=9606 GN=HSPA8 PE=1 SV=1 MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA MNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVS SMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAA IAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN KSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTI PTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDI DANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKN SLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELE KVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
- Align
Heat shock cognate 71 kDa protein
HSPA8
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<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 that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
- Ref.40"HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting."
Stricher F., Macri C., Ruff M., Muller S.
Autophagy 9:1937-1954(2013) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW. - Ref.59"The human HSP70 family of chaperones: where do we stand?"
Radons J.
Cell Stress Chaperones 21:379-404(2016) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW.
<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.16"The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CITED1. - Ref.17"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSP90AA1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.32"A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR."
Yamamoto Y.H., Kimura T., Momohara S., Takeuchi M., Tani T., Kimata Y., Kadokura H., Kohno K.
Cell Struct. Funct. 35:107-116(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB12. - Ref.37"The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508."
Grove D.E., Fan C.Y., Ren H.Y., Cyr D.M.
Mol. Biol. Cell 22:301-314(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB12. - Ref.38"A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins."
Sopha P., Kadokura H., Yamamoto Y.H., Takeuchi M., Saito M., Tsuru A., Kohno K.
Cell Struct. Funct. 37:177-187(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB14. - Ref.44"Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase."
Matsumura Y., Sakai J., Skach W.R.
J. Biol. Chem. 288:31069-31079(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN ERAD, INTERACTION WITH STUB1. - Ref.49"Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro."
Rauch J.N., Gestwicki J.E.
J. Biol. Chem. 289:1402-1414(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BAG1; BAG2; BAG3 AND HSPH1. - Ref.54"Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure."
Goodwin E.C., Motamedi N., Lipovsky A., Fernandez-Busnadiego R., DiMaio D.
PLoS ONE 9:E94322-E94322(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB12 AND DNAJB14. - Ref.60"Non-canonical interactions between heat shock cognate protein 70 (Hsc70) and Bcl2-associated anthanogene (BAG) co-chaperones are important for client release."
Rauch J.N., Zuiderweg E.R., Gestwicki J.E.
J. Biol. Chem. 291:19848-19857(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BAG1 AND BAG3, REGION NBD, REGION SBD. - Ref.62"Tetrameric assembly of K(+) channels requires ER-located chaperone proteins."
Li K., Jiang Q., Bai X., Yang Y.F., Ruan M.Y., Cai S.Q.
Mol. Cell 65:52-65(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB12 AND DNAJB14.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 71 | ATP | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 12 – 15 | ATP | 4 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 202 – 204 | ATP | 3 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 268 – 275 | ATP | 8 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 339 – 342 | ATP | 4 |
<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
- ATPase activity Source: BHF-UCL <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
- ATPase activity, coupled Source: Reactome
- ATP binding Source: BHF-UCL <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
- C3HC4-type RING finger domain binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- cadherin binding Source: BHF-UCLInferred from high throughput direct assayi
- chaperone binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- enzyme binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- G-protein coupled receptor binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- heat shock protein binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- MHC class II protein complex binding Source: UniProtKBInferred from high throughput direct assayi
- phosphatidylserine binding Source: Ensembl
- protein binding, bridging Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- ubiquitin protein ligase binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- unfolded protein binding 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
<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
- ATP metabolic process Source: BHF-UCL <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
- cellular response to starvation Source: ParkinsonsUK-UCL <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
- chaperone cofactor-dependent protein refolding Source: Ensembl
- chaperone-mediated autophagy Source: ParkinsonsUK-UCL
- chaperone-mediated autophagy translocation complex disassembly Source: ParkinsonsUK-UCL
- chaperone-mediated protein transport involved in chaperone-mediated autophagy Source: ParkinsonsUK-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- clathrin coat disassembly Source: Ensembl
- cytokine-mediated signaling pathway Source: Reactome
- late endosomal microautophagy Source: Ensembl
- membrane organization Source: Reactome
- mRNA splicing, via spliceosome Source: Reactome
- negative regulation of supramolecular fiber organization Source: BHF-UCL <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
- negative regulation of transcription, DNA-templated 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
- neutrophil degranulation Source: Reactome
- positive regulation by host of viral genome replication Source: Ensembl
- positive regulation of mRNA splicing, via spliceosome Source: Ensembl
- protein folding Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- protein refolding 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 targeting to lysosome involved in chaperone-mediated autophagy Source: ParkinsonsUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of cell cycle Source: Ensembl
- regulation of cellular response to heat Source: Reactome
- regulation of mRNA stability Source: Reactome
- regulation of protein complex assembly Source: ParkinsonsUK-UCL <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
- regulation of protein complex stability Source: ParkinsonsUK-UCL
- regulation of protein import Source: ParkinsonsUK-UCL <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
- regulation of protein stability Source: ParkinsonsUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- response to unfolded protein Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- transcription, DNA-templated Source: UniProtKB-KW
- viral process Source: UniProtKB-KW
<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, Repressor |
| Biological process | Host-virus interaction, mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.6.3.51 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3371453 Regulation of HSF1-mediated heat shock response R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR) R-HSA-3371568 Attenuation phase R-HSA-3371571 HSF1-dependent transactivation R-HSA-432720 Lysosome Vesicle Biogenesis R-HSA-432722 Golgi Associated Vesicle Biogenesis R-HSA-447041 CHL1 interactions R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-6785807 Interleukin-4 and 13 signaling R-HSA-6798695 Neutrophil degranulation R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-8856828 Clathrin-mediated endocytosis R-HSA-8876725 Protein methylation R-HSA-888590 GABA synthesis, release, reuptake and degradation |
SIGNOR Signaling Network Open Resource More...SIGNORi | P11142 |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | P11142 Predicted |
<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: Heat shock cognate 71 kDa proteinAlternative name(s): Heat shock 70 kDa protein 8 Lipopolysaccharide-associated protein 1 Short name: LAP-1 Short name: LPS-associated protein 1 |
| <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:HSPA8 Synonyms:HSC70, HSP73, HSPA10 |
| <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 NCBI 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:ENSG00000109971.13 |
Human Gene Nomenclature Database More...HGNCi | HGNC:5241 HSPA8 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600816 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P11142 |
<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
Plasma membrane
Nucleus
Other locations
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.
Cytosol
- cytosol 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
Endosome
- late endosome Source: Ensembl
Extracellular region or secreted
- blood microparticle Source: UniProtKBInferred from high throughput direct assayi
- extracellular exosome 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
- extracellular region Source: Reactome
- extracellular space Source: UniProtKBInferred from high throughput direct assayi
Lysosome
- lumenal side of lysosomal membrane Source: ParkinsonsUK-UCL <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
- lysosomal lumen Source: ParkinsonsUK-UCL <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
- lysosomal membrane Source: ParkinsonsUK-UCL
Nucleus
- nucleolus Source: UniProtKB-SubCell
- nucleoplasm Source: Reactome
- nucleus 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
- spliceosomal complex Source: UniProtKB-KW
Plasma Membrane
- plasma membrane Source: Reactome
Other locations
- chaperone complex Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
- ficolin-1-rich granule lumen Source: Reactome
- focal adhesion Source: UniProtKBInferred from high throughput direct assayi
- intracellular Source: ParkinsonsUK-UCL <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
- melanosome Source: UniProtKB-SubCell
- membrane Source: UniProtKBInferred from high throughput direct assayi
- myelin sheath Source: Ensembl
- Prp19 complex 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
- ribonucleoprotein complex 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
- secretory granule lumen Source: Reactome
<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, Cytoplasm, Membrane, Nucleus, Spliceosome<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 | 561 | K → R: Complete loss of in vitro methylation by METTL21A. 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
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 3312 |
Open Targets More...OpenTargetsi | ENSG00000109971 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29507 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1275223 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 123648 |
<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined 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
| |||
| <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_0000078270 | 2 – 646 | Heat shock cognate 71 kDa proteinAdd BLAST | 645 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 | 2 | N-acetylserineCombined 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
| 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 | 108 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 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 | 153 | 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 | 246 | N6-acetyllysineCombined 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 | 319 | N6-acetyllysine; alternateCombined 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 | 319 | N6-succinyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 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 | 328 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 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 | 329 | 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 | 362 | 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 | 469 | Omega-N-methylarginineCombined 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 | 512 | N6-acetyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 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 | 512 | N6-succinyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 512 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined 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>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 512 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined 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>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 | 524 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 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 | 541 | 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 | 561 | N6,N6,N6-trimethyllysine; by METTL21A; alternate2 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
| 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 | 561 | N6,N6-dimethyllysine; alternateCombined 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 | 589 | N6-acetyllysineCombined 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 | 597 | N6-acetyllysineCombined 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 | 601 | N6-acetyllysineCombined 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<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.5
- Ref.6Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W., Bilsland A.E., Keith W.N.
Submitted (JAN-2010) to UniProtKB
<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.20"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]Cited for: ISGYLATION. - Ref.24"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HERC5, ISGYLATION.
<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
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P11142 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P11142 |
PeptideAtlas More...PeptideAtlasi | P11142 |
PRoteomics IDEntifications database More...PRIDEi | P11142 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52698 52699 [P11142-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P11142-1 [P11142-1] P11142-2 [P11142-2] |
2D gel databases
DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEi | P11142 |
USC-OGP 2-DE database More...OGPi | P11142 |
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00003865 |
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P11142 |
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P11142 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P11142 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P11142 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P11142 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P11142 |
<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">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</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.17"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSP90AA1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000109971 |
CleanEx database of gene expression profiles More...CleanExi | HS_HSPA8 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P11142 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P11142 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB002056 HPA052504 |
<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 which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
33 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"BAG-1 modulates the chaperone activity of Hsp70/Hsc70."
Takayama S., Bimston D.N., Matsuzawa S.-I., Freeman B.C., Aime-Sempe C., Xie Z., Morimoto R.I., Reed J.C.
EMBO J. 16:4887-4896(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH BAG1, DOMAIN. - Ref.13"Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines."
Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M., Kochel K., Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T., Yamada M., Reed J.C.
Cancer Res. 58:3116-3131(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH BAG1. - Ref.14"Molecular chaperones as HSF1-specific transcriptional repressors."
Shi Y., Mosser D.D., Morimoto R.I.
Genes Dev. 12:654-666(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSF1. - Ref.16"The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CITED1. - Ref.17"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSP90AA1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.18"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PACRG. - Ref.19"Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions."
Liou S.T., Wang C.
Arch. Biochem. Biophys. 435:253-263(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TTC1. - Ref.21"Phosphorylation and binding partner analysis of the TSC1-TSC2 complex."
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M.
Biochem. Biophys. Res. Commun. 333:818-826(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TSC2, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.22"HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome."
Westhoff B., Chapple J.P., van der Spuy J., Hoehfeld J., Cheetham M.E.
Curr. Biol. 15:1058-1064(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB2. - Ref.24"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HERC5, ISGYLATION. - Ref.25"HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain."
Han C., Chen T., Li N., Yang M., Wan T., Cao X.
Biochem. Biophys. Res. Commun. 353:280-285(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJC9. - Ref.26"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION. - Ref.29"Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; EMSY; MATR3; ZNF335; TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5. - Ref.32"A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR."
Yamamoto Y.H., Kimura T., Momohara S., Takeuchi M., Tani T., Kimata Y., Kadokura H., Kohno K.
Cell Struct. Funct. 35:107-116(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB12. - Ref.33"Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha."
Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.
J. Biol. Chem. 285:7827-7837(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TRIM5. - Ref.37"The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508."
Grove D.E., Fan C.Y., Ren H.Y., Cyr D.M.
Mol. Biol. Cell 22:301-314(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB12. - Ref.38"A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins."
Sopha P., Kadokura H., Yamamoto Y.H., Takeuchi M., Saito M., Tsuru A., Kohno K.
Cell Struct. Funct. 37:177-187(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB14. - Ref.41"The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex."
Smith M.C., Scaglione K.M., Assimon V.A., Patury S., Thompson A.D., Dickey C.A., Southworth D.R., Paulson H.L., Gestwicki J.E., Zuiderweg E.R.
Biochemistry 52:5354-5364(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH STUB1. - Ref.42"The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3."
Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D., Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J., Gao Z., Tian H., Li Y. , Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J., Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G., Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.
Immunity 39:272-285(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FOXP3. - Ref.43"Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]Cited for: METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, INTERACTION WITH METTL21A. - Ref.44"Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase."
Matsumura Y., Sakai J., Skach W.R.
J. Biol. Chem. 288:31069-31079(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN ERAD, INTERACTION WITH STUB1. - Ref.46"High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PRKN. - Ref.47"The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic reticulum stress."
Choi J., Djebbar S., Fournier A., Labrie C.
Cell Stress Chaperones 19:439-446(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJC12. - Ref.48"Degradation of AF1Q by chaperone-mediated autophagy."
Li P., Ji M., Lu F., Zhang J., Li H., Cui T., Li Wang X., Tang D., Ji C.
Exp. Cell Res. 327:48-56(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MLLT11. - Ref.49"Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro."
Rauch J.N., Gestwicki J.E.
J. Biol. Chem. 289:1402-1414(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BAG1; BAG2; BAG3 AND HSPH1. - Ref.50"RING finger protein RNF207, a novel regulator of cardiac excitation."
Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E., Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.
J. Biol. Chem. 289:33730-33740(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RNF207. - Ref.54"Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure."
Goodwin E.C., Motamedi N., Lipovsky A., Fernandez-Busnadiego R., DiMaio D.
PLoS ONE 9:E94322-E94322(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB12 AND DNAJB14. - Ref.56"Structural and functional analysis of Hikeshi, a new nuclear transport receptor of Hsp70s."
Song J., Kose S., Watanabe A., Son S.Y., Choi S., Hong H., Yamashita E., Park I.Y., Imamoto N., Lee S.J.
Acta Crystallogr. D 71:473-483(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSPA8. - Ref.58"DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to corruption in 60S ribosome subunit maturation."
Tummala H., Walne A.J., Williams M., Bockett N., Collopy L., Cardoso S., Ellison A., Wynn R., Leblanc T., Fitzgibbon J., Kelsell D.P., van Heel D.A., Payne E., Plagnol V., Dokal I., Vulliamy T.
Am. J. Hum. Genet. 99:115-124(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJC21. - Ref.60"Non-canonical interactions between heat shock cognate protein 70 (Hsc70) and Bcl2-associated anthanogene (BAG) co-chaperones are important for client release."
Rauch J.N., Zuiderweg E.R., Gestwicki J.E.
J. Biol. Chem. 291:19848-19857(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BAG1 AND BAG3, REGION NBD, REGION SBD. - Ref.61"ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation."
Seo J.H., Park J.H., Lee E.J., Vo T.T., Choi H., Kim J.Y., Jang J.K., Wee H.J., Lee H.S., Jang S.H., Park Z.Y., Jeong J., Lee K.J., Seok S.H., Park J.Y., Lee B.J., Lee M.N., Oh G.T., Kim K.W.
Nat. Commun. 7:12882-12882(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HOPX; STUB1; HSP40 AND HSP90. - Ref.62"Tetrameric assembly of K(+) channels requires ER-located chaperone proteins."
Li K., Jiang Q., Bai X., Yang Y.F., Ruan M.Y., Cai S.Q.
Mol. Cell 65:52-65(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJB12 AND DNAJB14. - Ref.63"ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic pre-assembly of dynein arms."
Cho K.J., Noh S.H., Han S.M., Choi W.I., Kim H.Y., Yu S., Lee J.S., Rim J.H., Lee M.G., Hildebrandt F., Gee H.Y.
PLoS Genet. 14:E1007316-E1007316(2018) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZMYND10.
<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.15"HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells."
Sainis L., Angelidis C., Pagoulatos G.N., Lazaridis L.
Cell Stress Chaperones 5:132-138(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SV40 VP1 (MICROBIAL INFECTION).
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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
<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
- C3HC4-type RING finger domain binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- cadherin binding Source: BHF-UCLInferred from high throughput direct assayi
- chaperone binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- enzyme binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- G-protein coupled receptor binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- heat shock protein binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein binding, bridging Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ubiquitin protein ligase binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- unfolded protein binding 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-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109544, 575 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P11142 |
Database of interacting proteins More...DIPi | DIP-32874N |
Protein interaction database and analysis system More...IntActi | P11142, 251 interactors |
Molecular INTeraction database More...MINTi | P11142 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000227378 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P11142 |
<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 | 7 – 10 | 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 | 13 – 22 | 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 | 10 | |
| <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 | 25 – 28 | 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 | 36 – 39 | 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 | 42 – 44 | 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 | 49 – 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 | 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 | 53 – 57 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 58 – 61 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 63 – 65 | 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 | 70 – 72 | 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 DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 73 – 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 | 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 | 81 – 87 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 91 – 97 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 100 – 107 | 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 | 110 – 114 | 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 | 116 – 135 | 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 | 136 – 138 | 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 | 141 – 146 | 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 | 152 – 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 | 13 | |
| <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 | 168 – 174 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 175 – 182 | 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 | 185 – 187 | 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 | 188 – 191 | 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 | 193 – 201 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 204 – 213 | 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 | 10 | |
| <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 | 216 – 225 | 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 | 10 | |
| <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 | 230 – 249 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 253 – 255 | 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 | 257 – 276 | 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 | 278 – 288 | 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 | 11 | |
| <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 | 291 – 298 | 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 | 299 – 305 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 307 – 312 | 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 | 314 – 324 | 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 | 11 | |
| <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 | 328 – 330 | 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 | 333 – 338 | 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 | 339 – 342 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 344 – 353 | 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 | 10 | |
| <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 DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 354 – 356 | 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 | 357 – 360 | 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 DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 365 – 367 | 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 | 368 – 380 | 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 | 13 | |
| <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 | 541 – 556 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 564 – 582 | 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 | 19 | |
| <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 | 594 – 612 | 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 | 19 | |
| <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 | 613 – 616 | 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 | 641 – 644 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P11142 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P11142 |
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 | P11142 |
<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
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 2 – 386 | Nucleotide-binding domain (NBD)1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 385 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 186 – 377 | Interaction with BAG1Add BLAST | 192 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 394 – 509 | Substrate-binding domain (SBD)1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 116 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<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"BAG-1 modulates the chaperone activity of Hsp70/Hsc70."
Takayama S., Bimston D.N., Matsuzawa S.-I., Freeman B.C., Aime-Sempe C., Xie Z., Morimoto R.I., Reed J.C.
EMBO J. 16:4887-4896(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH BAG1, DOMAIN.
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0101 Eukaryota COG0443 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00910000144045 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000228135 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG051845 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P11142 |
KEGG Orthology (KO) More...KOi | K03283 |
Identification of Orthologs from Complete Genome Data More...OMAi | AYTKNQD |
Database of Orthologous Groups More...OrthoDBi | EOG091G03SF |
Database for complete collections of gene phylogenies More...PhylomeDBi | P11142 |
TreeFam database of animal gene trees More...TreeFami | TF105042 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.1270.10, 1 hit 2.60.34.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR018181 Heat_shock_70_CS IPR029048 HSP70_C_sf IPR029047 HSP70_peptide-bd_sf IPR013126 Hsp_70_fam |
The PANTHER Classification System More...PANTHERi | PTHR19375 PTHR19375, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00012 HSP70, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00301 HEATSHOCK70 |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF100920 SSF100920, 1 hit SSF100934 SSF100934, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00297 HSP70_1, 1 hit PS00329 HSP70_2, 1 hit PS01036 HSP70_3, 1 hit |
<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 (2)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 2 <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
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR
110 120 130 140 150
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF
160 170 180 190 200
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK
260 270 280 290 300
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
310 320 330 340 350
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL
360 370 380 390 400
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS
410 420 430 440 450
LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490 500
KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK
510 520 530 540 550
ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK
560 570 580 590 600
ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
610 620 630 640
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
The sequence of this isoform differs from the canonical sequence as follows:
464-616: Missing.
10 20 30 40 50
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR
110 120 130 140 150
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF
160 170 180 190 200
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK
260 270 280 290 300
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
310 320 330 340 350
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL
360 370 380 390 400
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS
410 420 430 440 450
LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490
KDNNLLGKFE LTGMPGGMPG GFPGGGAPPS GGASSGPTIE EVD
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_049619 | 32 | D → Y. Corresponds to variant dbSNP:rs11551602Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_049620 | 459 | F → L. Corresponds to variant dbSNP:rs11551598Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002427 | 464 – 616 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 153 |
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 | Y00371 Genomic DNA Translation: CAA68445.1 AB034951 mRNA Translation: BAB18615.1 AF352832 mRNA Translation: AAK17898.1 BC016179 mRNA Translation: AAH16179.1 BC016660 mRNA Translation: AAH16660.1 BC019816 mRNA Translation: AAH19816.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS44754.1 [P11142-2] CCDS8440.1 [P11142-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A27077 |
NCBI Reference Sequences More...RefSeqi | NP_006588.1, NM_006597.5 [P11142-1] NP_694881.1, NM_153201.3 [P11142-2] XP_011541100.1, XM_011542798.1 [P11142-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.180414 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1] ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2] ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1] ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3312 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3312 |
UCSC genome browser More...UCSCi | uc001pyp.5 human [P11142-1] |
<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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P11142 | Heat shock cognate 71 kDa protein | 646 | |||
| Heat shock cognate 71 kDa protein | 646 | ||||
| Epididymis luminal protein 33 | 646 | ||||
| HSPA8 isoform 16 | 646 | ||||
| Heat shock protein family A (Hsp70) member 8 (Fragment) | 646 | ||||
| +75 | |||||
| P11142-2 | HSPA8 isoform 5 | 493 | |||
| Heat shock protein family A (Hsp70) member 8 | 493 | ||||
| Heat shock cognate 71 kDa protein | 493 | ||||
| Heat shock protein family A (Hsp70) member 8 | 493 | ||||
| HSPA8 isoform 5 | 493 | ||||
| +7 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P11142 | Heat shock cognate 71 kDa protein | 646 | |||
| Heat shock cognate 71 kDa protein | 646 | ||||
| Epididymis luminal protein 33 | 646 | ||||
| HSPA8 isoform 16 | 646 | ||||
| Heat shock protein family A (Hsp70) member 8 (Fragment) | 646 | ||||
| +75 | |||||
| P11142-2 | Heat shock 70kDa protein 8 isoform 2 variant (Fragment) | 493 | |||
| UPI000CA00CA2 | 550 | ||||
| Heat shock 70 kDa protein cognate | 506 | ||||
| UPI0005215330 | 500 | ||||
| UPI0003F09020 | 499 | ||||
| +51 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P11142 | Heat shock cognate 71 kDa protein | 646 | |||
| Heat shock cognate 71 kDa protein | 646 | ||||
| Epididymis luminal protein 33 | 646 | ||||
| HSPA8 isoform 16 | 646 | ||||
| Heat shock protein family A (Hsp70) member 8 (Fragment) | 646 | ||||
| +121 | |||||
| P11142-2 | Chaperone protein DnaK | 647 | |||
| Chaperone protein DnaK | 647 | ||||
| UPI0003F989B2 | 649 | ||||
| Chaperone protein DnaK | 649 | ||||
| UPI0005B52A33 | 649 | ||||
| +123 | |||||
<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 | Y00371 Genomic DNA Translation: CAA68445.1 AB034951 mRNA Translation: BAB18615.1 AF352832 mRNA Translation: AAK17898.1 BC016179 mRNA Translation: AAH16179.1 BC016660 mRNA Translation: AAH16660.1 BC019816 mRNA Translation: AAH19816.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS44754.1 [P11142-2] CCDS8440.1 [P11142-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A27077 |
NCBI Reference Sequences More...RefSeqi | NP_006588.1, NM_006597.5 [P11142-1] NP_694881.1, NM_153201.3 [P11142-2] XP_011541100.1, XM_011542798.1 [P11142-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.180414 |
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 |
| 3AGY | X-ray | 1.85 | C/D/F | 639-646 | [»] | |
| 3AGZ | X-ray | 2.51 | C/D/E/F | 639-646 | [»] | |
| 3ESK | X-ray | 2.05 | B | 635-646 | [»] | |
| 3FZF | X-ray | 2.20 | A | 4-381 | [»] | |
| 3FZH | X-ray | 2.00 | A | 4-381 | [»] | |
| 3FZK | X-ray | 2.10 | A | 4-381 | [»] | |
| 3FZL | X-ray | 2.20 | A | 4-381 | [»] | |
| 3FZM | X-ray | 2.30 | A | 4-381 | [»] | |
| 3LDQ | X-ray | 1.90 | A | 4-381 | [»] | |
| 3M3Z | X-ray | 2.10 | A | 4-381 | [»] | |
| 4H5N | X-ray | 1.86 | A/B | 2-384 | [»] | |
| 4H5R | X-ray | 1.64 | A/B | 2-384 | [»] | |
| 4H5T | X-ray | 1.90 | A | 2-384 | [»] | |
| 4H5V | X-ray | 1.75 | A | 2-384 | [»] | |
| 4H5W | X-ray | 1.94 | A/B | 2-384 | [»] | |
| 4HWI | X-ray | 2.27 | A | 5-381 | [»] | |
| 4KBQ | X-ray | 2.91 | C/D | 541-646 | [»] | |
| 5AQF | X-ray | 1.88 | A/C | 1-381 | [»] | |
| 5AQG | X-ray | 2.24 | A/C/E | 1-381 | [»] | |
| 5AQH | X-ray | 2.00 | A | 1-381 | [»] | |
| 5AQI | X-ray | 1.98 | A/C | 1-381 | [»] | |
| 5AQJ | X-ray | 1.96 | A/C/E | 1-381 | [»] | |
| 5AQK | X-ray | 2.09 | A | 1-381 | [»] | |
| 5AQL | X-ray | 1.69 | A/C | 1-381 | [»] | |
| 5AQM | X-ray | 1.63 | A/C | 1-381 | [»] | |
| 5AQN | X-ray | 2.45 | A/C/E | 1-381 | [»] | |
| 5AQO | X-ray | 2.12 | A/C/E | 1-381 | [»] | |
| 5AQP | X-ray | 2.08 | A/C/E | 1-381 | [»] | |
| 5AQQ | X-ray | 2.72 | A/C/E | 1-381 | [»] | |
| 5AQR | X-ray | 1.91 | A/C/E | 1-381 | [»] | |
| 5AQS | X-ray | 2.00 | A/C | 1-381 | [»] | |
| 5AQT | X-ray | 1.90 | A | 1-381 | [»] | |
| 5AQU | X-ray | 1.92 | A | 1-381 | [»] | |
| 5AQV | X-ray | 1.75 | A | 1-381 | [»] | |
| 6B1I | X-ray | 2.30 | A/B | 5-381 | [»] | |
| 6B1M | X-ray | 1.90 | A/B | 5-381 | [»] | |
| 6B1N | X-ray | 1.80 | A/B | 5-381 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P11142 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P11142 | |||||
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 | 109544, 575 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P11142 |
Database of interacting proteins More...DIPi | DIP-32874N |
Protein interaction database and analysis system More...IntActi | P11142, 251 interactors |
Molecular INTeraction database More...MINTi | P11142 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000227378 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P11142 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1275223 |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | P11142 Predicted |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P11142 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P11142 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P11142 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 123648 |
2D gel databases
DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEi | P11142 |
USC-OGP 2-DE database More...OGPi | P11142 |
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00003865 |
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P11142 |
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P11142 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P11142 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P11142 |
PeptideAtlas More...PeptideAtlasi | P11142 |
PRoteomics IDEntifications database More...PRIDEi | P11142 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52698 52699 [P11142-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P11142-1 [P11142-1] P11142-2 [P11142-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 3312 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1] ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2] ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1] ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3312 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3312 |
UCSC genome browser More...UCSCi | uc001pyp.5 human [P11142-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 3312 |
DisGeNET More...DisGeNETi | 3312 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000109971.13 |
GeneCards: human genes, protein and diseases More...GeneCardsi | HSPA8 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0033867 |
Human Gene Nomenclature Database More...HGNCi | HGNC:5241 HSPA8 |
Human Protein Atlas More...HPAi | CAB002056 HPA052504 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600816 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P11142 |
Open Targets More...OpenTargetsi | ENSG00000109971 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29507 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0101 Eukaryota COG0443 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00910000144045 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000228135 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG051845 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P11142 |
KEGG Orthology (KO) More...KOi | K03283 |
Identification of Orthologs from Complete Genome Data More...OMAi | AYTKNQD |
Database of Orthologous Groups More...OrthoDBi | EOG091G03SF |
Database for complete collections of gene phylogenies More...PhylomeDBi | P11142 |
TreeFam database of animal gene trees More...TreeFami | TF105042 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.6.3.51 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3371453 Regulation of HSF1-mediated heat shock response R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR) R-HSA-3371568 Attenuation phase R-HSA-3371571 HSF1-dependent transactivation R-HSA-432720 Lysosome Vesicle Biogenesis R-HSA-432722 Golgi Associated Vesicle Biogenesis R-HSA-447041 CHL1 interactions R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-6785807 Interleukin-4 and 13 signaling R-HSA-6798695 Neutrophil degranulation R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-8856828 Clathrin-mediated endocytosis R-HSA-8876725 Protein methylation R-HSA-888590 GABA synthesis, release, reuptake and degradation |
SIGNOR Signaling Network Open Resource More...SIGNORi | P11142 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | HSPA8 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P11142 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | HSPA8 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 3312 |
CutDB - Proteolytic event database More...PMAP-CutDBi | P11142 |
Protein Ontology More...PROi | PR:P11142 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000109971 |
CleanEx database of gene expression profiles More...CleanExi | HS_HSPA8 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P11142 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P11142 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.1270.10, 1 hit 2.60.34.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR018181 Heat_shock_70_CS IPR029048 HSP70_C_sf IPR029047 HSP70_peptide-bd_sf IPR013126 Hsp_70_fam |
The PANTHER Classification System More...PANTHERi | PTHR19375 PTHR19375, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00012 HSP70, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00301 HEATSHOCK70 |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF100920 SSF100920, 1 hit SSF100934 SSF100934, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00297 HSP70_1, 1 hit PS00329 HSP70_2, 1 hit PS01036 HSP70_3, 1 hit |
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 | HSP7C_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 | P11142Primary (citable) accession number: P11142 Secondary accession number(s): Q9H3R6 | |
| <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: | July 1, 1989 |
| Last sequence update: | July 1, 1989 | |
| Last modified: | July 18, 2018 | |
| This is version 224 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<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 - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
