UniProtKB - Q01105 (SET_HUMAN)
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- BLAST>sp|Q01105|SET_HUMAN Protein SET OS=Homo sapiens OX=9606 GN=SET PE=1 SV=3 MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNE QASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYL TRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLT KRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDD EEGEGEEDDDDDEEEEGLEDIDEEGDEDEGEEDEDDDEGEEGEEDEGEDD
- Align
Protein SET
SET
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 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"Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks."
Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J.
J. Biol. Chem. 276:43285-43293(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH AN32A, PROTEOLYTIC CLEAVAGE AT LYS-179 BY GZMA (ISOFORM 2), SUBCELLULAR LOCATION. - Ref.18"Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN NME1 INHIBITION, INTERACTION WITH NME1, SUBCELLULAR LOCATION, DESCRIPTION OF THE SET COMPLEX, PROTEOLYTIC CLEAVAGE BY GZMA.
<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
- DNA binding Source: UniProtKB-KW
- histone binding Source: UniProtKB <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
- protein phosphatase inhibitor activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- protein phosphatase regulator activity Source: UniProtKB <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
<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
- DNA replication Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- negative regulation of histone acetylation Source: UniProtKB <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
- negative regulation of neuron apoptotic process Source: MGI <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- 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
- nucleosome assembly Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- nucleosome disassembly Source: UniProtKB <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 mRNA stability Source: Reactome
- 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, DNA-binding |
| Biological process | Host-virus interaction |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2299718 Condensation of Prophase Chromosomes R-HSA-450520 HuR (ELAVL1) binds and stabilizes mRNA |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q01105 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Protein SETAlternative name(s): HLA-DR-associated protein II Inhibitor of granzyme A-activated DNase Short name: IGAAD PHAPII Phosphatase 2A inhibitor I2PP2A Short name: I-2PP2A Template-activating factor I Short name: TAF-I |
| <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:SET |
| <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:ENSG00000119335.16 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10760 SET |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600960 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q01105 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endoplasmic reticulum
Cytosol
Nucleus
Note: In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavage by GZMA, moves rapidly to the nucleus, where it is found in the nucleoplasm, avoiding the nucleolus. Similar translocation to the nucleus is also observed for lymphocyte-activated killer cells after the addition of calcium.
Cytosol
- cytosol Source: UniProtKB-SubCell
Endoplasmic reticulum
- endoplasmic reticulum 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
Nucleus
- nucleoplasm Source: HPA
- 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
Other locations
- cytoplasm 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
- lipid droplet Source: HPA
- perinuclear region of cytoplasm 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-containing 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
<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
Cytoplasm, Endoplasmic reticulum, Nucleus<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
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 283 – 284 | Breakpoint for translocation to form SET-CAN oncogene | 2 |
<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 - Diseasei
Disease mutation, Proto-oncogeneOrganism-specific databases
DisGeNET More...DisGeNETi | 6418 |
Open Targets More...OpenTargetsi | ENSG00000119335 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35678 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SET |
Domain mapping of disease mutations (DMDM) More...DMDMi | 46397790 |
<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 | RemovedBy 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 | |||
| <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_0000185662 | 2 – 290 | Protein SETAdd BLAST | 289 |
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,N,N-trimethylalanineBy 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 | 7 | 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 | 28 | 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 | 63 | 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 | 68 | 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 | 146 | PhosphotyrosineBy 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 | 150 | 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 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 | 154 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | |||
| <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 | 172 | 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 | ||
| Isoform 2 (identifier: Q01105-2) | |||||
| <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 | 11 | 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 | 15 | 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 | 24 | 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 <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.16"Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks."
Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J.
J. Biol. Chem. 276:43285-43293(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH AN32A, PROTEOLYTIC CLEAVAGE AT LYS-179 BY GZMA (ISOFORM 2), SUBCELLULAR LOCATION. - Ref.18"Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN NME1 INHIBITION, INTERACTION WITH NME1, SUBCELLULAR LOCATION, DESCRIPTION OF THE SET COMPLEX, PROTEOLYTIC CLEAVAGE BY GZMA. - Ref.22"The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TREX1, IDENTIFICATION IN THE SET COMPLEX, PROTEOLYTIC CLEAVAGE BY GZMA, SUBCELLULAR LOCATION.
<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 | Q01105 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q01105 |
PeptideAtlas More...PeptideAtlasi | Q01105 |
PRoteomics IDEntifications database More...PRIDEi | Q01105 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57917 57918 [Q01105-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q01105-1 [Q01105-1] Q01105-2 [Q01105-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q01105 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q01105 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q01105 |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000119335 |
CleanEx database of gene expression profiles More...CleanExi | HS_SET |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q01105 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q01105 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB005232 HPA063683 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Identification and characterization of SEB, a novel protein that binds to the acute undifferentiated leukemia-associated protein SET."
Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D., Ueda K., Adachi Y.
Eur. J. Biochem. 268:1340-1351(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SETBP1. - Ref.16"Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks."
Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J.
J. Biol. Chem. 276:43285-43293(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH AN32A, PROTEOLYTIC CLEAVAGE AT LYS-179 BY GZMA (ISOFORM 2), SUBCELLULAR LOCATION. - Ref.17"HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A."
Fan Z., Beresford P.J., Zhang D., Lieberman J.
Mol. Cell. Biol. 22:2810-2820(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HMGB2, IDENTIFICATION IN THE SET COMPLEX. - Ref.18"Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN NME1 INHIBITION, INTERACTION WITH NME1, SUBCELLULAR LOCATION, DESCRIPTION OF THE SET COMPLEX, PROTEOLYTIC CLEAVAGE BY GZMA. - Ref.22"The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TREX1, IDENTIFICATION IN THE SET COMPLEX, PROTEOLYTIC CLEAVAGE BY GZMA, SUBCELLULAR LOCATION. - Ref.23"Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SGO1. - Ref.26"FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4."
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.
PLoS ONE 4:E5071-E5071(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH APBB1. - Ref.34"Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity."
Muto S., Senda M., Akai Y., Sato L., Suzuki T., Nagai R., Senda T., Horikoshi M.
Proc. Natl. Acad. Sci. U.S.A. 104:4285-4290(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-238, DNA-BINDING, DOMAINS, SUBUNIT.
<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.19"Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-I proteins and inhibits nucleosome assembly but not regulation of histone acetylation by INHAT."
van Leeuwen H., Okuwaki M., Hong R., Chakravarti D., Nagata K., O'Hare P.
J. Gen. Virol. 84:2501-2510(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HERPES SIMPLEX VIRUS 1 VP22 (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
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| FAM111B | Q6SJ93 | 3 | EBI-1053182,EBI-6309082 | |
| FOXO1 | Q12778 | 5 | EBI-1053182,EBI-1108782 | |
| MDM2 | Q00987 | 2 | EBI-1053182,EBI-389668 | |
| MEOX2 | P50222 | 3 | EBI-1053182,EBI-748397 | |
| PRKAR1A | P10644 | 2 | EBI-1053182,EBI-476431 | |
| PTMA | P06454 | 3 | EBI-1053182,EBI-2682091 | |
| RAC1 | P63000 | 8 | EBI-1053182,EBI-413628 | |
| SDCBP | O00560 | 3 | EBI-1053182,EBI-727004 | |
| TAF1A | Q15573 | 2 | EBI-1053182,EBI-2510647 | |
| TAF1B | Q53T94 | 3 | EBI-1053182,EBI-1560239 | |
| TAF1C | Q15572 | 4 | EBI-1053182,EBI-2510659 | |
| TBP | P20226 | 4 | EBI-1053182,EBI-355371 | |
| THAP7 | Q9BT49 | 6 | EBI-1053182,EBI-741350 | |
| UBTF | P17480 | 4 | EBI-1053182,EBI-396235 |
<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
- histone binding Source: UniProtKB <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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112316, 130 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q01105 |
Database of interacting proteins More...DIPi | DIP-33561N |
Protein interaction database and analysis system More...IntActi | Q01105, 119 interactors |
Molecular INTeraction database More...MINTi | Q01105 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000361777 |
<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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 37 – 88 | 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 | 52 | |
| <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 | 94 – 100 | 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 | 103 – 106 | 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 | 111 – 116 | 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 | 117 – 119 | 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 | 120 – 127 | 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 | 135 – 141 | 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 | 145 – 148 | 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 | 150 – 156 | 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 | 166 – 168 | 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 | 203 – 206 | 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 | 215 – 223 | 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 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 | 224 – 227 | 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 | 230 – 233 | 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 | Q01105 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q01105 |
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 | Q01105 |
<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 | 31 – 78 | DimerizationAdd BLAST | 48 | |
| <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 | 79 – 225 | Earmuff domainAdd BLAST | 147 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 239 – 290 | Asp/Glu-rich (highly acidic)Add BLAST | 52 |
<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.34"Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity."
Muto S., Senda M., Akai Y., Sato L., Suzuki T., Nagai R., Senda T., Horikoshi M.
Proc. Natl. Acad. Sci. U.S.A. 104:4285-4290(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-238, DNA-BINDING, DOMAINS, SUBUNIT.
<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 | KOG1508 Eukaryota ENOG410XQRX LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000062882 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000232096 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG014779 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q01105 |
KEGG Orthology (KO) More...KOi | K11290 |
Identification of Orthologs from Complete Genome Data More...OMAi | PVALMNH |
Database of Orthologous Groups More...OrthoDBi | EOG091G00YT |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q01105 |
TreeFam database of animal gene trees More...TreeFami | TF313386 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037231 NAP-like_sf IPR002164 NAP_family |
The PANTHER Classification System More...PANTHERi | PTHR11875 PTHR11875, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00956 NAP, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF143113 SSF143113, 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 (4)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 4 <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
MAPKRQSPLP PQKKKPRPPP ALGPEETSAS AGLPKKGEKE QQEAIEHIDE
60 70 80 90 100
VQNEIDRLNE QASEEILKVE QKYNKLRQPF FQKRSELIAK IPNFWVTTFV
110 120 130 140 150
NHPQVSALLG EEDEEALHYL TRVEVTEFED IKSGYRIDFY FDENPYFENK
160 170 180 190 200
VLSKEFHLNE SGDPSSKSTE IKWKSGKDLT KRSSQTQNKA SRKRQHEEPE
210 220 230 240 250
SFFTWFTDHS DAGADELGEV IKDDIWPNPL QYYLVPDMDD EEGEGEEDDD
260 270 280 290
DDEEEEGLED IDEEGDEDEG EEDEDDDEGE EGEEDEGEDD
The sequence of this isoform differs from the canonical sequence as follows:
1-37: MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MSAPAAKVSKKELNSNHDGADETS
10 20 30 40 50
MSAPAAKVSK KELNSNHDGA DETSEKEQQE AIEHIDEVQN EIDRLNEQAS
60 70 80 90 100
EEILKVEQKY NKLRQPFFQK RSELIAKIPN FWVTTFVNHP QVSALLGEED
110 120 130 140 150
EEALHYLTRV EVTEFEDIKS GYRIDFYFDE NPYFENKVLS KEFHLNESGD
160 170 180 190 200
PSSKSTEIKW KSGKDLTKRS SQTQNKASRK RQHEEPESFF TWFTDHSDAG
210 220 230 240 250
ADELGEVIKD DIWPNPLQYY LVPDMDDEEG EGEEDDDDDE EEEGLEDIDE
260 270
EGDEDEGEED EDDDEGEEGE EDEGEDD
The sequence of this isoform differs from the canonical sequence as follows:
1-37: MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MPRSHQPPPPPH
10 20 30 40 50
MPRSHQPPPP PHEKEQQEAI EHIDEVQNEI DRLNEQASEE ILKVEQKYNK
60 70 80 90 100
LRQPFFQKRS ELIAKIPNFW VTTFVNHPQV SALLGEEDEE ALHYLTRVEV
110 120 130 140 150
TEFEDIKSGY RIDFYFDENP YFENKVLSKE FHLNESGDPS SKSTEIKWKS
160 170 180 190 200
GKDLTKRSSQ TQNKASRKRQ HEEPESFFTW FTDHSDAGAD ELGEVIKDDI
210 220 230 240 250
WPNPLQYYLV PDMDDEEGEG EEDDDDDEEE EGLEDIDEEG DEDEGEEDED
260
DDEGEEGEED EGEDD
The sequence of this isoform differs from the canonical sequence as follows:
1-37: MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MGCRDLLPSLKPTLL
10 20 30 40 50
MGCRDLLPSL KPTLLEKEQQ EAIEHIDEVQ NEIDRLNEQA SEEILKVEQK
60 70 80 90 100
YNKLRQPFFQ KRSELIAKIP NFWVTTFVNH PQVSALLGEE DEEALHYLTR
110 120 130 140 150
VEVTEFEDIK SGYRIDFYFD ENPYFENKVL SKEFHLNESG DPSSKSTEIK
160 170 180 190 200
WKSGKDLTKR SSQTQNKASR KRQHEEPESF FTWFTDHSDA GADELGEVIK
210 220 230 240 250
DDIWPNPLQY YLVPDMDDEE GEGEEDDDDD EEEEGLEDID EEGDEDEGEE
260
DEDDDEGEEG EEDEGEDD
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_078653 | 233 – 290 | Missing Probable disease-associated mutation found in a patient with congenital microcephaly and moderate intellecutal disability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 58 | ||
| Isoform 2 (identifier: Q01105-2) | |||||
| <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 varianti | 4 | P → QCombined 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 | ||
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_009868 | 1 – 37 | MAPKR…LPKKG → MSAPAAKVSKKELNSNHDGA DETS in isoform 2. 9 Publications <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
| 37 | |
| <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_045175 | 1 – 37 | MAPKR…LPKKG → MPRSHQPPPPPH in isoform 3. 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
| 37 | |
| <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_046741 | 1 – 37 | MAPKR…LPKKG → MGCRDLLPSLKPTLL in isoform 4. CuratedAdd BLAST | 37 |
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 | M93651 mRNA Translation: AAA60318.1 X75091 mRNA Translation: CAA52982.1 D45198 mRNA Translation: BAA08139.1 U51924 mRNA Translation: AAC50460.1 AY349172 mRNA Translation: AAQ79833.1 CR536543 mRNA Translation: CAG38780.1 CR542050 mRNA Translation: CAG46847.1 AK223556 mRNA Translation: BAD97276.1 AK300609 mRNA Translation: BAG62304.1 AL356481 Genomic DNA No translation available. AL359678 Genomic DNA No translation available. BC032749 mRNA Translation: AAH32749.1 EF534308 mRNA Translation: ABP96841.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS48037.1 [Q01105-1] CCDS59149.1 [Q01105-4] CCDS6907.1 [Q01105-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A57984 A45018 I59377 |
NCBI Reference Sequences More...RefSeqi | NP_001116293.1, NM_001122821.1 [Q01105-1] NP_001234929.1, NM_001248000.1 [Q01105-4] NP_001234930.1, NM_001248001.1 NP_003002.2, NM_003011.3 [Q01105-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.436687 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000322030; ENSP00000318012; ENSG00000119335 [Q01105-2] ENST00000372686; ENSP00000361771; ENSG00000119335 [Q01105-3] ENST00000372692; ENSP00000361777; ENSG00000119335 [Q01105-1] ENST00000409104; ENSP00000387321; ENSG00000119335 [Q01105-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6418 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6418 |
UCSC genome browser More...UCSCi | uc004bvu.5 human [Q01105-1] |
<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, Chromosomal rearrangement, 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 | |
|---|---|---|---|---|---|
| Q01105 | SET translocation (Myeloid leukemia-associated), isoform CRA_a | 290 | |||
| SET isoform 1 | 290 | ||||
| Uncharacterized protein | 290 | ||||
| SET nuclear proto-oncogene | 290 | ||||
| Q01105-2 | SET translocation (Myeloid leukemia-associated), isoform CRA_b | 277 | |||
| Protein SET isoform 2 | 277 | ||||
| SET isoform 2 | 277 | ||||
| Protein SET isoform 2 | 277 | ||||
| SET isoform 2 | 277 | ||||
| +29 | |||||
| Q01105-3 | Protein SET | 266 | |||
| SET isoform 5 | 266 | ||||
| Uncharacterized protein | 266 | ||||
| Uncharacterized protein | 266 | ||||
| protein SET isoform X4 | 266 | ||||
| +6 | |||||
| Q01105-4 | SET isoform 4 | 268 | |||
| Uncharacterized protein | 268 | ||||
| Uncharacterized protein | 268 | ||||
| SET nuclear proto-oncogene | 268 | ||||
| SET nuclear proto-oncogene | 268 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q01105 | SET translocation (Myeloid leukemia-associated), isoform CRA_a | 290 | |||
| SET isoform 1 | 290 | ||||
| Uncharacterized protein | 290 | ||||
| SET nuclear proto-oncogene | 290 | ||||
| Uncharacterized protein | 314 | ||||
| +135 | |||||
| Q01105-2 | SET translocation (Myeloid leukemia-associated), isoform CRA_b | 277 | |||
| Protein SET isoform 2 | 277 | ||||
| SET isoform 2 | 277 | ||||
| Protein SET isoform 2 | 277 | ||||
| SET isoform 2 | 277 | ||||
| +30 | |||||
| Q01105-3 | Protein SET | 266 | |||
| SET isoform 5 | 266 | ||||
| Uncharacterized protein | 266 | ||||
| Uncharacterized protein | 266 | ||||
| protein SET isoform X4 | 266 | ||||
| +12 | |||||
| Q01105-4 | SET-like protein | 270 | |||
| Putative dna replication factor/protein phosphatase inhibitor set/spr-2 (Fragment) | 334 | ||||
| protein SET-like | 329 | ||||
| UPI00071D09AA | 294 | ||||
| UPI00092E5FD5 | 289 | ||||
| +117 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q01105 | SET translocation (Myeloid leukemia-associated), isoform CRA_a | 290 | |||
| SET isoform 1 | 290 | ||||
| Uncharacterized protein | 290 | ||||
| SET nuclear proto-oncogene | 290 | ||||
| Uncharacterized protein | 314 | ||||
| +189 | |||||
| Q01105-3 | UPI00076268B1 | 341 | |||
| UPI000549D46C | 294 | ||||
| UPI000C2FC0E0 | 291 | ||||
| Uncharacterized protein | 290 | ||||
| UPI0004549C2D | 289 | ||||
| +278 | |||||
| Q01105-4 | UPI00076268B1 | 341 | |||
| UPI000549D46C | 294 | ||||
| UPI000C2FC0E0 | 291 | ||||
| Uncharacterized protein | 290 | ||||
| UPI0004549C2D | 289 | ||||
| +278 | |||||
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
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 | M93651 mRNA Translation: AAA60318.1 X75091 mRNA Translation: CAA52982.1 D45198 mRNA Translation: BAA08139.1 U51924 mRNA Translation: AAC50460.1 AY349172 mRNA Translation: AAQ79833.1 CR536543 mRNA Translation: CAG38780.1 CR542050 mRNA Translation: CAG46847.1 AK223556 mRNA Translation: BAD97276.1 AK300609 mRNA Translation: BAG62304.1 AL356481 Genomic DNA No translation available. AL359678 Genomic DNA No translation available. BC032749 mRNA Translation: AAH32749.1 EF534308 mRNA Translation: ABP96841.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS48037.1 [Q01105-1] CCDS59149.1 [Q01105-4] CCDS6907.1 [Q01105-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A57984 A45018 I59377 |
NCBI Reference Sequences More...RefSeqi | NP_001116293.1, NM_001122821.1 [Q01105-1] NP_001234929.1, NM_001248000.1 [Q01105-4] NP_001234930.1, NM_001248001.1 NP_003002.2, NM_003011.3 [Q01105-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.436687 |
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 |
| 2E50 | X-ray | 2.30 | A/B/P/Q | 38-238 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q01105 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q01105 | |||||
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 | 112316, 130 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q01105 |
Database of interacting proteins More...DIPi | DIP-33561N |
Protein interaction database and analysis system More...IntActi | Q01105, 119 interactors |
Molecular INTeraction database More...MINTi | Q01105 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000361777 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q01105 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q01105 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q01105 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SET |
Domain mapping of disease mutations (DMDM) More...DMDMi | 46397790 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q01105 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q01105 |
PeptideAtlas More...PeptideAtlasi | Q01105 |
PRoteomics IDEntifications database More...PRIDEi | Q01105 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57917 57918 [Q01105-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q01105-1 [Q01105-1] Q01105-2 [Q01105-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 6418 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000322030; ENSP00000318012; ENSG00000119335 [Q01105-2] ENST00000372686; ENSP00000361771; ENSG00000119335 [Q01105-3] ENST00000372692; ENSP00000361777; ENSG00000119335 [Q01105-1] ENST00000409104; ENSP00000387321; ENSG00000119335 [Q01105-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6418 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6418 |
UCSC genome browser More...UCSCi | uc004bvu.5 human [Q01105-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6418 |
DisGeNET More...DisGeNETi | 6418 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000119335.16 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SET |
Human Gene Nomenclature Database More...HGNCi | HGNC:10760 SET |
Human Protein Atlas More...HPAi | CAB005232 HPA063683 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600960 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q01105 |
Open Targets More...OpenTargetsi | ENSG00000119335 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35678 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1508 Eukaryota ENOG410XQRX LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000062882 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000232096 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG014779 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q01105 |
KEGG Orthology (KO) More...KOi | K11290 |
Identification of Orthologs from Complete Genome Data More...OMAi | PVALMNH |
Database of Orthologous Groups More...OrthoDBi | EOG091G00YT |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q01105 |
TreeFam database of animal gene trees More...TreeFami | TF313386 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2299718 Condensation of Prophase Chromosomes R-HSA-450520 HuR (ELAVL1) binds and stabilizes mRNA |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q01105 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SET human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q01105 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Protein_SET |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 6418 |
Protein Ontology More...PROi | PR:Q01105 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000119335 |
CleanEx database of gene expression profiles More...CleanExi | HS_SET |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q01105 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q01105 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037231 NAP-like_sf IPR002164 NAP_family |
The PANTHER Classification System More...PANTHERi | PTHR11875 PTHR11875, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00956 NAP, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF143113 SSF143113, 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 | SET_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 | Q01105Primary (citable) accession number: Q01105 Secondary accession number(s): A5A5H4 , A6NGV1, B4DUE2, Q15541, Q5VXV1, Q5VXV2, Q6FHZ5 | |
| <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: | April 1, 1993 |
| Last sequence update: | April 13, 2004 | |
| Last modified: | July 18, 2018 | |
| This is version 193 of the entry and version 3 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 9
Human chromosome 9: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or 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
