UniProtKB - Q969M7 (UBE2F_HUMAN)
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- BLAST>sp|Q969M7|UBE2F_HUMAN NEDD8-conjugating enzyme UBE2F OS=Homo sapiens OX=9606 GN=UBE2F PE=1 SV=1 MLTLASKLKRDDGLKGSRTAATASDSTRRVSVRDKLLVKEVAELEANLPCTCKVHFPDPN KLHCFQLTVTPDEGYYQGGKFQFETEVPDAYNMVPPKVKCLTKIWHPNITETGEICLSLL REHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKEDFRNKVDDYI KRYAR
- Align
NEDD8-conjugating enzyme UBE2F
UBE2F
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.6"E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification."
Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.
Mol. Cell 33:483-495(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-185 IN COMPLEX WITH UBA3, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH UBA3; NAE1 AND RBX2.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein neddylation
This protein is involved in the pathway protein neddylation, which is part of Protein modification.View all proteins of this organism that are known to be involved in the pathway protein neddylation and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 116 | Glycyl thioester intermediatePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- NEDD8 transferase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin protein ligase activity Source: GO_Central
- ubiquitin protein ligase binding Source: GO_Central
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- post-translational protein modification Source: Reactome
- protein neddylation 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>Keywordsi
Molecular function | Transferase |
Biological process | Ubl conjugation pathway |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-8951664. Neddylation. R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q969M7. |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00885. |
<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: NEDD8-conjugating enzyme UBE2F (EC:2.3.2.-)Alternative name(s): NEDD8 carrier protein UBE2F NEDD8 protein ligase UBE2F NEDD8-conjugating enzyme 2 RING-type E3 NEDD8 transferase UBE2F Ubiquitin-conjugating enzyme E2 F |
<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:UBE2F Synonyms:NCE2 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000184182.18. |
Human Gene Nomenclature Database More...HGNCi | HGNC:12480. UBE2F. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 617700. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q969M7. |
<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
<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
Organism-specific databases
DisGeNET More...DisGeNETi | 140739. |
Open Targets More...OpenTargetsi | ENSG00000184182. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA37130. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | UBE2F. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74751725. |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000263077 | 1 – 185 | NEDD8-conjugating enzyme UBE2FAdd BLAST | 185 |
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 | 1 | N-acetylmethionine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/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.8"Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes."
Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W., Bennett E.J., Schulman B.A.
Structure 21:42-53(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-25 IN COMPLEX WITH DCUN1D3, ACETYLATION AT MET-1.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
AcetylationProteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | Q969M7. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q969M7. |
PeptideAtlas More...PeptideAtlasi | Q969M7. |
PRoteomics IDEntifications database More...PRIDEi | Q969M7. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q969M7. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q969M7. |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression"><span class="caps">P92958</span></a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="http://www.uniprot.org/uniprot/O14734#expression"><span class="caps">O14734</span></a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.6"E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification."
Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.
Mol. Cell 33:483-495(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-185 IN COMPLEX WITH UBA3, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH UBA3; NAE1 AND RBX2.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000184182. |
CleanEx database of gene expression profiles More...CleanExi | HS_UBE2F. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q969M7. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q969M7. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA037444. |
<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.6"E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification."
Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.
Mol. Cell 33:483-495(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-185 IN COMPLEX WITH UBA3, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH UBA3; NAE1 AND RBX2. - Ref.8"Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes."
Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W., Bennett E.J., Schulman B.A.
Structure 21:42-53(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-25 IN COMPLEX WITH DCUN1D3, ACETYLATION AT MET-1.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ubiquitin protein ligase binding Source: GO_Central
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 126682. 15 interactors. |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q969M7. |
Protein interaction database and analysis system More...IntActi | Q969M7. 9 interactors. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000272930. |
<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 | 4 – 8 | 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 | 32 – 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 | 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 | 45 – 47 | 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 | 52 – 55 | 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 | 57 – 60 | 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 | 64 – 69 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 72 – 74 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 75 – 78 | 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 | 81 – 86 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 97 – 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 | 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 | 107 – 109 | 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 | 111 – 113 | 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 | 118 – 120 | 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 | 124 – 126 | 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 | 136 – 145 | 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 <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 146 – 150 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 153 – 155 | 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 | 159 – 167 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 169 – 183 | 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 | 15 |
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 |
2EDI | NMR | - | A | 26-185 | [»] | |
3FN1 | X-ray | 2.50 | B | 21-185 | [»] | |
4GBA | X-ray | 2.40 | F/G | 1-25 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q969M7. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q969M7. | |||||
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 | Q969M7. |
<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 | 1 – 29 | Interaction with UBA31 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
| 29 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0420. Eukaryota. ENOG410XS81. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00630000089859. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233456. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG098591. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q969M7. |
KEGG Orthology (KO) More...KOi | K10687. |
Identification of Orthologs from Complete Genome Data More...OMAi | WHPNISE. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0N8A. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q969M7. |
TreeFam database of animal gene trees More...TreeFami | TF101125. |
Family and domain databases
Conserved Domains Database More...CDDi | cd00195. UBCc. 1 hit. |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.10.110.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00179. UQ_con. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54495. SSF54495. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 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 (7)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.
This entry describes 7 <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
MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKE VAELEANLPC
60 70 80 90 100
TCKVHFPDPN KLHCFQLTVT PDEGYYQGGK FQFETEVPDA YNMVPPKVKC
110 120 130 140 150
LTKIWHPNIT ETGEICLSLL REHSIDGTGW APTRTLKDVV WGLNSLFTDL
160 170 180
LNFDDPLNIE AAEHHLRDKE DFRNKVDDYI KRYAR
The sequence of this isoform differs from the canonical sequence as follows:
170-185: EDFRNKVDDYIKRYAR → SPMLLLHRRTSGIKWMTTSNVMPDNKRGRLQAHGLCYSLSLT
10 20 30 40 50
MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKE VAELEANLPC
60 70 80 90 100
TCKVHFPDPN KLHCFQLTVT PDEGYYQGGK FQFETEVPDA YNMVPPKVKC
110 120 130 140 150
LTKIWHPNIT ETGEICLSLL REHSIDGTGW APTRTLKDVV WGLNSLFTDL
160 170 180 190 200
LNFDDPLNIE AAEHHLRDKS PMLLLHRRTS GIKWMTTSNV MPDNKRGRLQ
210
AHGLCYSLSL T
The sequence of this isoform differs from the canonical sequence as follows:
40-71: Missing.
10 20 30 40 50
MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKD EGYYQGGKFQ
60 70 80 90 100
FETEVPDAYN MVPPKVKCLT KIWHPNITET GEICLSLLRE HSIDGTGWAP
110 120 130 140 150
TRTLKDVVWG LNSLFTDLLN FDDPLNIEAA EHHLRDKEDF RNKVDDYIKR
YAR
The sequence of this isoform differs from the canonical sequence as follows:
118-120: SLL → RIF
121-185: Missing.
10 20 30 40 50
MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKE VAELEANLPC
60 70 80 90 100
TCKVHFPDPN KLHCFQLTVT PDEGYYQGGK FQFETEVPDA YNMVPPKVKC
110 120
LTKIWHPNIT ETGEICLRIF
The sequence of this isoform differs from the canonical sequence as follows:
72-185: DEGYYQGGKF...VDDYIKRYAR → ASQSEMPDQDLAPQHHRDRGNMSEFIERTFN
10 20 30 40 50
MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKE VAELEANLPC
60 70 80 90 100
TCKVHFPDPN KLHCFQLTVT PASQSEMPDQ DLAPQHHRDR GNMSEFIERT
FN
The sequence of this isoform differs from the canonical sequence as follows:
149-169: Missing.
10 20 30 40 50
MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKE VAELEANLPC
60 70 80 90 100
TCKVHFPDPN KLHCFQLTVT PDEGYYQGGK FQFETEVPDA YNMVPPKVKC
110 120 130 140 150
LTKIWHPNIT ETGEICLSLL REHSIDGTGW APTRTLKDVV WGLNSLFTED
160
FRNKVDDYIK RYAR
The sequence of this isoform differs from the canonical sequence as follows:
1-39: MLTLASKLKRDDGLKGSRTAATASDSTRRVSVRDKLLVK → MVLGAGPASPVSGSP
10 20 30 40 50
MVLGAGPASP VSGSPEVAEL EANLPCTCKV HFPDPNKLHC FQLTVTPDEG
60 70 80 90 100
YYQGGKFQFE TEVPDAYNMV PPKVKCLTKI WHPNITETGE ICLSLLREHS
110 120 130 140 150
IDGTGWAPTR TLKDVVWGLN SLFTDLLNFD DPLNIEAAEH HLRDKEDFRN
160
KVDDYIKRYA R
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 181 | K → E in BAF82752 (PubMed:14702039).Curated | 1 |
Alternative sequence
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF310723 mRNA. Translation: AAL26792.1. AK290063 mRNA. Translation: BAF82752.1. AK293334 mRNA. Translation: BAG56850.1. AK294107 mRNA. Translation: BAG57442.1. AK297502 mRNA. Translation: BAG59915.1. AK303094 mRNA. Translation: BAG64204.1. AC016776 Genomic DNA. Translation: AAY24220.1. CH471063 Genomic DNA. Translation: EAW71129.1. CH471063 Genomic DNA. Translation: EAW71132.1. BC010549 mRNA. Translation: AAH10549.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2523.1. [Q969M7-1] CCDS63175.1. [Q969M7-7] CCDS63176.1. [Q969M7-6] CCDS63177.1. [Q969M7-3] |
NCBI Reference Sequences More...RefSeqi | NP_001265234.1. NM_001278305.1. [Q969M7-1] NP_001265235.1. NM_001278306.1. [Q969M7-7] NP_001265236.1. NM_001278307.1. [Q969M7-3] NP_001265237.1. NM_001278308.1. [Q969M7-6] NP_542409.1. NM_080678.2. [Q969M7-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.471785. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000272930; ENSP00000272930; ENSG00000184182. [Q969M7-1] ENST00000409633; ENSP00000387299; ENSG00000184182. [Q969M7-6] ENST00000409953; ENSP00000386680; ENSG00000184182. [Q969M7-7] ENST00000414443; ENSP00000399183; ENSG00000184182. [Q969M7-3] ENST00000433241; ENSP00000393515; ENSG00000184182. [Q969M7-4] ENST00000441728; ENSP00000409749; ENSG00000184182. [Q969M7-5] ENST00000612130; ENSP00000478474; ENSG00000184182. [Q969M7-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 140739. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:140739. |
UCSC genome browser More...UCSCi | uc002vxk.4. human. [Q969M7-1] |
<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<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF310723 mRNA. Translation: AAL26792.1. AK290063 mRNA. Translation: BAF82752.1. AK293334 mRNA. Translation: BAG56850.1. AK294107 mRNA. Translation: BAG57442.1. AK297502 mRNA. Translation: BAG59915.1. AK303094 mRNA. Translation: BAG64204.1. AC016776 Genomic DNA. Translation: AAY24220.1. CH471063 Genomic DNA. Translation: EAW71129.1. CH471063 Genomic DNA. Translation: EAW71132.1. BC010549 mRNA. Translation: AAH10549.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2523.1. [Q969M7-1] CCDS63175.1. [Q969M7-7] CCDS63176.1. [Q969M7-6] CCDS63177.1. [Q969M7-3] |
NCBI Reference Sequences More...RefSeqi | NP_001265234.1. NM_001278305.1. [Q969M7-1] NP_001265235.1. NM_001278306.1. [Q969M7-7] NP_001265236.1. NM_001278307.1. [Q969M7-3] NP_001265237.1. NM_001278308.1. [Q969M7-6] NP_542409.1. NM_080678.2. [Q969M7-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.471785. |
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 |
2EDI | NMR | - | A | 26-185 | [»] | |
3FN1 | X-ray | 2.50 | B | 21-185 | [»] | |
4GBA | X-ray | 2.40 | F/G | 1-25 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q969M7. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q969M7. | |||||
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 | 126682. 15 interactors. |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q969M7. |
Protein interaction database and analysis system More...IntActi | Q969M7. 9 interactors. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000272930. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q969M7. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q969M7. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | UBE2F. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74751725. |
Proteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | Q969M7. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q969M7. |
PeptideAtlas More...PeptideAtlasi | Q969M7. |
PRoteomics IDEntifications database More...PRIDEi | Q969M7. |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 140739. |
Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000272930; ENSP00000272930; ENSG00000184182. [Q969M7-1] ENST00000409633; ENSP00000387299; ENSG00000184182. [Q969M7-6] ENST00000409953; ENSP00000386680; ENSG00000184182. [Q969M7-7] ENST00000414443; ENSP00000399183; ENSG00000184182. [Q969M7-3] ENST00000433241; ENSP00000393515; ENSG00000184182. [Q969M7-4] ENST00000441728; ENSP00000409749; ENSG00000184182. [Q969M7-5] ENST00000612130; ENSP00000478474; ENSG00000184182. [Q969M7-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 140739. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:140739. |
UCSC genome browser More...UCSCi | uc002vxk.4. human. [Q969M7-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 140739. |
DisGeNET More...DisGeNETi | 140739. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000184182.18. |
GeneCards: human genes, protein and diseases More...GeneCardsi | UBE2F. |
Human Gene Nomenclature Database More...HGNCi | HGNC:12480. UBE2F. |
Human Protein Atlas More...HPAi | HPA037444. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 617700. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q969M7. |
Open Targets More...OpenTargetsi | ENSG00000184182. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA37130. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0420. Eukaryota. ENOG410XS81. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00630000089859. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233456. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG098591. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q969M7. |
KEGG Orthology (KO) More...KOi | K10687. |
Identification of Orthologs from Complete Genome Data More...OMAi | WHPNISE. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0N8A. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q969M7. |
TreeFam database of animal gene trees More...TreeFami | TF101125. |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00885. |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-8951664. Neddylation. R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q969M7. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | UBE2F. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q969M7. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 140739. |
Protein Ontology More...PROi | PR:Q969M7. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000184182. |
CleanEx database of gene expression profiles More...CleanExi | HS_UBE2F. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q969M7. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q969M7. HS. |
Family and domain databases
Conserved Domains Database More...CDDi | cd00195. UBCc. 1 hit. |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.10.110.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00179. UQ_con. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54495. SSF54495. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 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 | UBE2F_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 | Q969M7Primary (citable) accession number: Q969M7 Secondary accession number(s): A8K1Z8 , B4DDT9, B4DFI1, B4DMK3, B4DZU2, B8ZZG2, C9J212, H9KVB9 | |
<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: | December 12, 2006 |
Last sequence update: | December 1, 2001 | |
Last modified: | March 28, 2018 | |
This is version 138 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. |