UniProtKB - Q9UBE0 (SAE1_HUMAN)
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- BLAST>sp|Q9UBE0|SAE1_HUMAN SUMO-activating enzyme subunit 1 OS=Homo sapiens OX=9606 GN=SAE1 PE=1 SV=1 MVEKEEAGGGISEEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGV KGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPE SFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEHEFVEEKTK VAKVSQGVEDGPDTKRAKLDSSETTMVKKKVVFCPVKEALEVDWSSEKAKAALKRTTSDY FLLQVLLKFRTDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPDLLPEDFVRYCFSEMA PVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKGNGIVECLGPK
- Align
SUMO-activating enzyme subunit 1
SAE1
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.1"In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2."
Okuma T., Honda R., Ichikawa G., Tsumagari N., Yasuda H.
Biochem. Biophys. Res. Commun. 254:693-698(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DIMERIZATION, FUNCTION. - Ref.2"Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex."
Gong L., Li B., Millas S., Yeh E.T.H.
FEBS Lett. 448:185-189(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DIMERIZATION, FUNCTION. - Ref.3"Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1."
Desterro J.M.P., Rodriguez M.S., Kemp G.D., Hay R.T.
J. Biol. Chem. 274:10618-10624(1999) [PubMed] [Europe PMC] [Abstract] - Ref.11"Expression and regulation of the mammalian SUMO-1 E1 enzyme."
Azuma Y., Tan S.-H., Cavenagh M.M., Ainsztein A.M., Saitoh H., Dasso M.
FASEB J. 15:1825-1827(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DIMERIZATION, FUNCTION. - Ref.12"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9."
Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T.
J. Biol. Chem. 276:35368-35374(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.20"Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."
Lois L.M., Lima C.D.
EMBO J. 24:439-451(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UBA2; SUMO1 AND ATP, FUNCTION. - Ref.21"Active site remodelling accompanies thioester bond formation in the SUMO E1."
Olsen S.K., Capili A.D., Lu X., Tan D.S., Lima C.D.
Nature 463:906-912(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH UBA2 AND SUMO1, FUNCTION, MUTAGENESIS OF ARG-21 AND 24-ARG--TRP-26.
<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 sumoylation
This protein is involved in the pathway protein sumoylation, which is part of Protein modification.View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.
<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-dependent protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- enzyme activator 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 C-terminus binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein heterodimerization activity Source: CAFA <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
- small protein activating enzyme binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ubiquitin activating enzyme 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
- positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCLInferred from high throughput mutant phenotypei
- protein sumoylation 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 ubiquitination 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>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 | Ligase |
| Biological process | Ubl conjugation pathway |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3065676 SUMO is conjugated to E1 (UBA2:SAE1) R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9) |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00886 |
<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: SUMO-activating enzyme subunit 1Alternative name(s): Ubiquitin-like 1-activating enzyme E1A Cleaved into the following chain: |
| <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:SAE1 Synonyms:AOS1, SUA1, UBLE1A |
| <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:ENSG00000142230.11 |
Human Gene Nomenclature Database More...HGNCi | HGNC:30660 SAE1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 613294 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UBE0 |
<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
Nucleus
- Nucleus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Expression and regulation of the mammalian SUMO-1 E1 enzyme."
Azuma Y., Tan S.-H., Cavenagh M.M., Ainsztein A.M., Saitoh H., Dasso M.
FASEB J. 15:1825-1827(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DIMERIZATION, FUNCTION.
- Nucleus 1 Publication
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKBInferred from high throughput direct assayi
- SUMO activating enzyme 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
Other locations
- cytoplasm Source: GO_Central
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
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
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 21 | R → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 24 – 26 | RLW → AAA: Abolishes ATP-dependent activation of SUMO proteins. 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
| 3 |
Organism-specific databases
DisGeNET More...DisGeNETi | 10055 |
Open Targets More...OpenTargetsi | ENSG00000142230 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA162402387 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1615388 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SAE1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 42559897 |
<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_0000194966 | 1 – 346 | SUMO-activating enzyme subunit 1Add BLAST | 346 | |
| <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 | Removed; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000423290 | 2 – 346 | SUMO-activating enzyme subunit 1, N-terminally processedAdd BLAST | 345 |
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-acetylmethionineCombined 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 | 2 | N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 12 | 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 | 198 | 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>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, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UBE0 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9UBE0 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UBE0 |
PeptideAtlas More...PeptideAtlasi | Q9UBE0 |
PRoteomics IDEntifications database More...PRIDEi | Q9UBE0 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 83952 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UBE0 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UBE0 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q9UBE0 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Expression and regulation of the mammalian SUMO-1 E1 enzyme."
Azuma Y., Tan S.-H., Cavenagh M.M., Ainsztein A.M., Saitoh H., Dasso M.
FASEB J. 15:1825-1827(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DIMERIZATION, FUNCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000142230 |
CleanEx database of gene expression profiles More...CleanExi | HS_SAE1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UBE0 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UBE0 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA041906 HPA043552 |
<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.20"Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."
Lois L.M., Lima C.D.
EMBO J. 24:439-451(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UBA2; SUMO1 AND ATP, FUNCTION. - Ref.21"Active site remodelling accompanies thioester bond formation in the SUMO E1."
Olsen S.K., Capili A.D., Lu X., Tan D.S., Lima C.D.
Nature 463:906-912(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH UBA2 AND SUMO1, FUNCTION, MUTAGENESIS OF ARG-21 AND 24-ARG--TRP-26.
<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 |
|---|---|---|---|---|
| UBA2 | Q9UBT2 | 12 | EBI-743154,EBI-718569 | |
| UBE2I | P63279 | 2 | EBI-743154,EBI-80168 |
<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-dependent protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein C-terminus binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein heterodimerization activity Source: CAFA <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
- small protein activating enzyme binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115366, 60 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-2161 SUMO activating enzyme complex CPX-3042 activated SUMO1-E1 ligase complex CPX-3044 activated SUMO2-E1 ligase complex CPX-3045 activated SUMO3-E1 ligase complex CPX-3076 activated SUMO4-E1 ligase complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UBE0 |
Database of interacting proteins More...DIPi | DIP-34587N |
Protein interaction database and analysis system More...IntActi | Q9UBE0, 30 interactors |
Molecular INTeraction database More...MINTi | Q9UBE0 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000270225 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q9UBE0 |
<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 | 13 – 26 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <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 | 28 – 35 | 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 | 38 – 42 | 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 | 46 – 58 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 61 – 66 | 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 | 73 – 75 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 76 – 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 | 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 | 91 – 101 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 106 – 111 | 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 | 115 – 117 | 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 | 120 – 123 | 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 | 127 – 133 | 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 | 136 – 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 | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 152 – 160 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 162 – 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 | 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 | 170 – 177 | 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 | 206 – 212 | 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 | 216 – 219 | 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 | 227 – 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 | 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 | 239 – 252 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <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 | 253 – 255 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 259 – 261 | 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 | 262 – 278 | 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 | 17 | |
| <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 | 279 – 281 | 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 | 284 – 286 | 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 | 289 – 293 | 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 | 296 – 298 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 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 | 300 – 319 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 327 – 332 | 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 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 | 333 – 336 | 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 | 337 – 341 | 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 |
3D structure databases
Database of protein disorder More...DisProti | DP00485 |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UBE0 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UBE0 |
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 | Q9UBE0 |
<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
<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 | KOG2014 Eukaryota COG0476 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000075007 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000172217 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG080782 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UBE0 |
KEGG Orthology (KO) More...KOi | K10684 |
Identification of Orthologs from Complete Genome Data More...OMAi | SYCFSEM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DZ1 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UBE0 |
TreeFam database of animal gene trees More...TreeFami | TF315037 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000594 ThiF_NAD_FAD-bd IPR035985 Ubiquitin-activating_enz IPR000011 UBQ/SUMO-activ_enz_E1-like |
Pfam protein domain database More...Pfami | View protein in Pfam PF00899 ThiF, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01849 UBIQUITINACT |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF69572 SSF69572, 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 (3)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 3 <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
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE
60 70 80 90 100
IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ
110 120 130 140 150
NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS
160 170 180 190 200
IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD
210 220 230 240 250
SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQVLLKFR
260 270 280 290 300
TDKGRDPSSD TYEEDSELLL QIRNDVLDSL GISPDLLPED FVRYCFSEMA
310 320 330 340
PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPK
The sequence of this isoform differs from the canonical sequence as follows:
245-266: VLLKFRTDKGRDPSSDTYEEDS → GTASPRWPQCVRWLEGFWHRKL
267-346: Missing.
10 20 30 40 50
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE
60 70 80 90 100
IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ
110 120 130 140 150
NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS
160 170 180 190 200
IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD
210 220 230 240 250
SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQGTASPR
260
WPQCVRWLEG FWHRKL
The sequence of this isoform differs from the canonical sequence as follows:
245-299: VLLKFRTDKG...DFVRYCFSEM → GPVSAGPSSQ...PTCIPCPLPS
300-346: Missing.
10 20 30 40 50
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE
60 70 80 90 100
IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ
110 120 130 140 150
NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS
160 170 180 190 200
IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD
210 220 230 240 250
SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQGPVSAG
260 270 280 290
PSSQQLLLLR WHEGEWDCGV PWPQVNSRFG SPRDANCSMP TCIPCPLPS
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 | 115 | I → M in BAG51064 (Ref. 6) Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 158 | V → A in AAF29104 (PubMed:11042152).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 178 – 180 | KTK → ETD in AAF29104 (PubMed:11042152).Curated | 3 | |
| <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 | 186 | Q → H in AAF29104 (PubMed:11042152).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 273 | R → G in AAD12785 (PubMed:9920803).Curated | 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_045372 | 245 – 299 | VLLKF…CFSEM → GPVSAGPSSQQLLLLRWHEG EWDCGVPWPQVNSRFGSPRD ANCSMPTCIPCPLPS 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
| 55 | |
| <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_045373 | 245 – 266 | VLLKF…YEEDS → GTASPRWPQCVRWLEGFWHR KL in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 22 | |
| <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_045374 | 267 – 346 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 80 | |
| <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_045375 | 300 – 346 | Missing 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
| 47 |
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 | AF090385 mRNA Translation: AAD12785.2 AF046025 mRNA Translation: AAD23902.2 AF110956 mRNA Translation: AAD24433.1 AF161489 mRNA Translation: AAF29104.1 AL560234 mRNA No translation available. BT007290 mRNA Translation: AAP35954.1 AK021978 mRNA Translation: BAG51064.1 AK315624 mRNA Translation: BAG37992.1 AC008532 Genomic DNA No translation available. AC008755 Genomic DNA No translation available. CH471126 Genomic DNA Translation: EAW57461.1 CH471126 Genomic DNA Translation: EAW57463.1 BC000344 mRNA Translation: AAH00344.1 BC003611 mRNA Translation: AAH03611.1 BC018271 mRNA Translation: AAH18271.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12696.1 [Q9UBE0-1] CCDS54284.1 [Q9UBE0-2] CCDS54285.1 [Q9UBE0-3] |
NCBI Reference Sequences More...RefSeqi | NP_001139185.1, NM_001145713.1 [Q9UBE0-3] NP_001139186.1, NM_001145714.1 [Q9UBE0-2] NP_005491.1, NM_005500.2 [Q9UBE0-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.515500 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000270225; ENSP00000270225; ENSG00000142230 [Q9UBE0-1] ENST00000392776; ENSP00000440818; ENSG00000142230 [Q9UBE0-2] ENST00000413379; ENSP00000416557; ENSG00000142230 [Q9UBE0-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10055 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10055 |
UCSC genome browser More...UCSCi | uc002pgc.4 human [Q9UBE0-1] |
<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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9UBE0 | SUMO-activating enzyme subunit 1 | 346 | |||
| SUMO-1 activating enzyme subunit 1, isoform CRA_b | 346 | ||||
| SAE1 isoform 9 | 346 | ||||
| SUMO1 activating enzyme subunit 1 | 346 | ||||
| SAE1 isoform 9 | 346 | ||||
| +11 | |||||
| Q9UBE0-2 | SAE1 isoform 11 | 266 | |||
| SUMO1 activating enzyme subunit 1 | 266 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9UBE0 | SUMO-activating enzyme subunit 1 | 346 | |||
| SUMO-1 activating enzyme subunit 1, isoform CRA_b | 346 | ||||
| SAE1 isoform 9 | 346 | ||||
| SUMO1 activating enzyme subunit 1 | 346 | ||||
| UPI00048DFF52 | 382 | ||||
| +42 | |||||
| Q9UBE0-2 | SAE1 isoform 11 | 266 | |||
| SUMO1 activating enzyme subunit 1 | 266 | ||||
| UPI0007625584 | 332 | ||||
| SUMO-activating enzyme subunit 1 isoform c | 266 | ||||
| SAE1 isoform 11 | 266 | ||||
| Q9UBE0-3 | UPI0005F4FCD2 | 361 | |||
| SUMO1 activating enzyme subunit 1 | 299 | ||||
| SAE1 isoform 4 | 299 | ||||
| SUMO1 activating enzyme subunit 1 | 299 | ||||
| SUMO1 activating enzyme subunit 1 | 299 | ||||
| +6 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9UBE0 | SUMO-activating enzyme subunit 1 | 346 | |||
| SUMO-1 activating enzyme subunit 1, isoform CRA_b | 346 | ||||
| SAE1 isoform 9 | 346 | ||||
| SUMO1 activating enzyme subunit 1 | 346 | ||||
| UPI00048DFF52 | 382 | ||||
| +248 | |||||
| Q9UBE0-2 | UPI000A30DA10 | 343 | |||
| SUMO-activating enzyme subunit 1 (Fragment) | 116 | ||||
| SUMO1 activating enzyme subunit 1 | 340 | ||||
| UPI0009A3BEEC | 344 | ||||
| SUMO1 activating enzyme subunit 1 | 345 | ||||
| +42 | |||||
<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 | AF090385 mRNA Translation: AAD12785.2 AF046025 mRNA Translation: AAD23902.2 AF110956 mRNA Translation: AAD24433.1 AF161489 mRNA Translation: AAF29104.1 AL560234 mRNA No translation available. BT007290 mRNA Translation: AAP35954.1 AK021978 mRNA Translation: BAG51064.1 AK315624 mRNA Translation: BAG37992.1 AC008532 Genomic DNA No translation available. AC008755 Genomic DNA No translation available. CH471126 Genomic DNA Translation: EAW57461.1 CH471126 Genomic DNA Translation: EAW57463.1 BC000344 mRNA Translation: AAH00344.1 BC003611 mRNA Translation: AAH03611.1 BC018271 mRNA Translation: AAH18271.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12696.1 [Q9UBE0-1] CCDS54284.1 [Q9UBE0-2] CCDS54285.1 [Q9UBE0-3] |
NCBI Reference Sequences More...RefSeqi | NP_001139185.1, NM_001145713.1 [Q9UBE0-3] NP_001139186.1, NM_001145714.1 [Q9UBE0-2] NP_005491.1, NM_005500.2 [Q9UBE0-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.515500 |
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 |
| 1Y8Q | X-ray | 2.25 | A/C | 1-346 | [»] | |
| 1Y8R | X-ray | 2.75 | A/D | 1-346 | [»] | |
| 3KYC | X-ray | 2.45 | A | 1-346 | [»] | |
| 3KYD | X-ray | 2.61 | A | 1-346 | [»] | |
Database of protein disorder More...DisProti | DP00485 | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UBE0 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UBE0 | |||||
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 | 115366, 60 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-2161 SUMO activating enzyme complex CPX-3042 activated SUMO1-E1 ligase complex CPX-3044 activated SUMO2-E1 ligase complex CPX-3045 activated SUMO3-E1 ligase complex CPX-3076 activated SUMO4-E1 ligase complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UBE0 |
Database of interacting proteins More...DIPi | DIP-34587N |
Protein interaction database and analysis system More...IntActi | Q9UBE0, 30 interactors |
Molecular INTeraction database More...MINTi | Q9UBE0 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000270225 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q9UBE0 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1615388 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UBE0 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UBE0 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q9UBE0 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SAE1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 42559897 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UBE0 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9UBE0 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UBE0 |
PeptideAtlas More...PeptideAtlasi | Q9UBE0 |
PRoteomics IDEntifications database More...PRIDEi | Q9UBE0 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 83952 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 10055 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000270225; ENSP00000270225; ENSG00000142230 [Q9UBE0-1] ENST00000392776; ENSP00000440818; ENSG00000142230 [Q9UBE0-2] ENST00000413379; ENSP00000416557; ENSG00000142230 [Q9UBE0-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10055 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10055 |
UCSC genome browser More...UCSCi | uc002pgc.4 human [Q9UBE0-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 10055 |
DisGeNET More...DisGeNETi | 10055 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000142230.11 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SAE1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:30660 SAE1 |
Human Protein Atlas More...HPAi | HPA041906 HPA043552 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 613294 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UBE0 |
Open Targets More...OpenTargetsi | ENSG00000142230 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA162402387 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2014 Eukaryota COG0476 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000075007 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000172217 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG080782 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UBE0 |
KEGG Orthology (KO) More...KOi | K10684 |
Identification of Orthologs from Complete Genome Data More...OMAi | SYCFSEM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DZ1 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UBE0 |
TreeFam database of animal gene trees More...TreeFami | TF315037 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00886 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3065676 SUMO is conjugated to E1 (UBA2:SAE1) R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9) |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SAE1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UBE0 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SAE1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 10055 |
Protein Ontology More...PROi | PR:Q9UBE0 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000142230 |
CleanEx database of gene expression profiles More...CleanExi | HS_SAE1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UBE0 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UBE0 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000594 ThiF_NAD_FAD-bd IPR035985 Ubiquitin-activating_enz IPR000011 UBQ/SUMO-activ_enz_E1-like |
Pfam protein domain database More...Pfami | View protein in Pfam PF00899 ThiF, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01849 UBIQUITINACT |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF69572 SSF69572, 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 | SAE1_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 | Q9UBE0Primary (citable) accession number: Q9UBE0 Secondary accession number(s): B2RDP5 , B3KMQ2, F5GXX7, G3XAK6, O95717, Q9P020 | |
| <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: | February 16, 2004 |
| Last sequence update: | May 1, 2000 | |
| Last modified: | July 18, 2018 | |
| This is version 167 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
