Q9NS56 · TOPRS_HUMAN
- ProteinE3 ubiquitin-protein ligase Topors
- GeneTOPORS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1045 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as an E3 ubiquitin-protein ligase and as an E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA damage-induced cell death through IKBKE sumoylation.
Catalytic activity
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase Topors
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NS56
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Targeted to PML nuclear bodies upon DNA damage.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Retinitis pigmentosa 31 (RP31)
- Note
- DescriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
- See alsoMIM:609923
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 76 | No effect on sumoylation. | ||||
Sequence: K → R | ||||||
Mutagenesis | 98 | Loss of phosphorylation but no effect on E3 ubiquitin-protein ligase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 98 | Increase in E3 ubiquitin-protein ligase activity and increased binding to UBE2D1. No effect on SUMO1-protein ligase activity. | ||||
Sequence: S → D | ||||||
Mutagenesis | 131 | Abrogates E3 ubiquitin-protein ligase activity. | ||||
Sequence: W → A | ||||||
Natural variant | VAR_037629 | 154 | in dbSNP:rs17855104 | |||
Sequence: A → T | ||||||
Mutagenesis | 301 | No effect on sumoylation. | ||||
Sequence: K → R | ||||||
Mutagenesis | 485 | No effect on sumoylation. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_037630 | 517 | in dbSNP:rs17855103 | |||
Sequence: E → K | ||||||
Mutagenesis | 560 | Strongly reduces sumoylation. | ||||
Sequence: K → R | ||||||
Mutagenesis | 718 | Loss of phosphorylation by PLK1 and increases in p53/TP53 stability. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_037631 | 749 | in dbSNP:rs17857515 | |||
Sequence: N → D | ||||||
Natural variant | VAR_037632 | 812 | in dbSNP:rs36034138 | |||
Sequence: P → R | ||||||
Mutagenesis | 921 | No effect on sumoylation. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,149 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), cross-link, modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000232626 | 1-1045 | UniProt | E3 ubiquitin-protein ligase Topors | |||
Sequence: MGSQPPLGSPLSREEGEAPPPAPASEGRRRSRRVRLRGSCRHRPSFLGCRELAASAPARPAPASSEIMASAAKEFKMDNFSPKAGTSKLQQTVPADASPDSKCPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCKQPFDSIFHSVRAEDDFKEYVLRPSYNGSFVTPDRRFRYRTTLTRERNASVYSPSGPVNRRTTTPPDSGVLFEGLGISTRPRDVEIPQFMRQIAVRRPTTADERSLRKIQEQDIINFRRTLYRAGARVRNIEDGGRYRDISAEFFRRNPACLHRLVPWLKRELTVLFGAHGSLVNIVQHIIMSNVTRYDLESQAFVSDLRPFLLNRTEHFIHEFISFARSPFNMAAFDQHANYDCPAPSYEEGSHSDSSVITISPDEAETQELDINVATVSQAPWDDETPGPSYSSSEQVHVTMSSLLNTSDSSDEELVTGGATSQIQGVQTNDDLNNDSDDSSDNCVIVGFVKPLAERTPELVELSSDSEDLGSYEKMETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNLNSSVRGDRVYSPYNHRHRKRGRSRSSDSRSQSRSGHDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKRSRTRDSSWSRRSQTLSLSSESTSRSRSRSSDHGKRRSRSRNRDRYYLRNNYGSRYKWEYTYYSRNKDRDGYESSYRRRTLSRAHYSRQSSSPEFRVQSFSERTNARKKNNHSERKYYYYERHRSRSLSSNRSRTASTGTDRVRNEKPGGKRKYKTRHLEGTNEVAQPSREFASKAKDSHYQKSSSKLDGNYKNESDTFSDSRSSDRETKHKRRKRKTRSLSVEIVYEGKATDTTKHHKKKKKKHKKKHKKHHGDNASRSPVVITIDSDSDKDSEVKEDTECDNSGPQDPLQNEFLAPSLEPFETKDVVTIEAEFGVLDKECDIATLSNNLNNANKTVDNIPPLAASVEQTLDVREESTFVSDLENQPSNIVSLQTEPSRQLPSPRTSLMSVCLGRDCDMS | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 73 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 76 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 83 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 88 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 98 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 159 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 173 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 191 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 194 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 203 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 249 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 491 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 498 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 499 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 560 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 569 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 577 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 585 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 585 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 701 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 718 | UniProt | Phosphoserine; by PLK1 | ||||
Sequence: S | |||||||
Modified residue | 734 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 734 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 735 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 736 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 819 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 837 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 864 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 864 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 866 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 866 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 912 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 912 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 914 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 914 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1028 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-98 regulates the E3 ubiquitin-protein ligase activity but not the SUMO1-protein ligase activity. Phosphorylation at Ser-718 increases the E3 ubiquitin-protein ligase activity versus the SUMO1-protein ligase activity resulting in increased p53/TP53 ubiquitination and degradation.
Sumoylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at highest levels in testis and at lower levels in adrenal gland, bone marrow, brain, colon, heart, kidney, liver, muscle, ovary, pancreas, placenta, prostate, skeletal muscle, skin, small intestine, spleen, stomach, testis, thymus, thyroid and uterus. Expressed in the alveolar epithelium of the lung. Expression is commonly decreased in colon adenocarcinomas and lung cancers.
Induction
By genotoxic agents such as cisplatin and camptothecin.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PARK7/DJ-1 (By similarity).
Interacts with TOP1. Interacts with p53/TP53; can both ubiquitinate and sumoylate p53/TP53. Interacts with the SUMO1 conjugating enzyme UBE2I. Interacts with SUMO1. Interacts with NKX3-1; polyubiquitinates NKX3-1 and induces its proteasomal degradation. Interacts with SIN3A; sumoylates SIN3A. Interacts with IKBKE; induced by DNA damage
Interacts with TOP1. Interacts with p53/TP53; can both ubiquitinate and sumoylate p53/TP53. Interacts with the SUMO1 conjugating enzyme UBE2I. Interacts with SUMO1. Interacts with NKX3-1; polyubiquitinates NKX3-1 and induces its proteasomal degradation. Interacts with SIN3A; sumoylates SIN3A. Interacts with IKBKE; induced by DNA damage
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9NS56 | Rep68 P03132 | 3 | EBI-1996473, EBI-7387242 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-35 | Disordered | ||||
Sequence: MGSQPPLGSPLSREEGEAPPPAPASEGRRRSRRVR | ||||||
Region | 1-195 | E3 ubiquitin-protein ligase activity | ||||
Sequence: MGSQPPLGSPLSREEGEAPPPAPASEGRRRSRRVRLRGSCRHRPSFLGCRELAASAPARPAPASSEIMASAAKEFKMDNFSPKAGTSKLQQTVPADASPDSKCPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCKQPFDSIFHSVRAEDDFKEYVLRPSYNGSFVTPDRRFRYRTTLTRERNASVYSP | ||||||
Region | 51-374 | Required for DNA-binding | ||||
Sequence: ELAASAPARPAPASSEIMASAAKEFKMDNFSPKAGTSKLQQTVPADASPDSKCPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCKQPFDSIFHSVRAEDDFKEYVLRPSYNGSFVTPDRRFRYRTTLTRERNASVYSPSGPVNRRTTTPPDSGVLFEGLGISTRPRDVEIPQFMRQIAVRRPTTADERSLRKIQEQDIINFRRTLYRAGARVRNIEDGGRYRDISAEFFRRNPACLHRLVPWLKRELTVLFGAHGSLVNIVQHIIMSNVTRYDLESQAFVSDLRPFLLNRTEHFIHEFISFARSPFNMAAFDQHANY | ||||||
Zinc finger | 103-142 | RING-type | ||||
Sequence: CPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCK | ||||||
Region | 437-574 | Required for sumoylation and localization to discrete nuclear foci | ||||
Sequence: SLLNTSDSSDEELVTGGATSQIQGVQTNDDLNNDSDDSSDNCVIVGFVKPLAERTPELVELSSDSEDLGSYEKMETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNL | ||||||
Region | 437-654 | Interaction with SUMO1 | ||||
Sequence: SLLNTSDSSDEELVTGGATSQIQGVQTNDDLNNDSDDSSDNCVIVGFVKPLAERTPELVELSSDSEDLGSYEKMETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNLNSSVRGDRVYSPYNHRHRKRGRSRSSDSRSQSRSGHDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKRSRTRDSSWS | ||||||
Region | 442-475 | Disordered | ||||
Sequence: SDSSDEELVTGGATSQIQGVQTNDDLNNDSDDSS | ||||||
Region | 456-731 | Interaction with p53/TP53 | ||||
Sequence: SQIQGVQTNDDLNNDSDDSSDNCVIVGFVKPLAERTPELVELSSDSEDLGSYEKMETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNLNSSVRGDRVYSPYNHRHRKRGRSRSSDSRSQSRSGHDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKRSRTRDSSWSRRSQTLSLSSESTSRSRSRSSDHGKRRSRSRNRDRYYLRNNYGSRYKWEYTYYSRNKDRDGYESSYRRRTLSRAHYS | ||||||
Region | 456-882 | Interaction with TOP1 | ||||
Sequence: SQIQGVQTNDDLNNDSDDSSDNCVIVGFVKPLAERTPELVELSSDSEDLGSYEKMETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNLNSSVRGDRVYSPYNHRHRKRGRSRSSDSRSQSRSGHDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKRSRTRDSSWSRRSQTLSLSSESTSRSRSRSSDHGKRRSRSRNRDRYYLRNNYGSRYKWEYTYYSRNKDRDGYESSYRRRTLSRAHYSRQSSSPEFRVQSFSERTNARKKNNHSERKYYYYERHRSRSLSSNRSRTASTGTDRVRNEKPGGKRKYKTRHLEGTNEVAQPSREFASKAKDSHYQKSSSKLDGNYKNESDTFSDSRSSDRETKHKRRKRKTRSLSVEIVYEGKATDTTKHH | ||||||
Region | 511-692 | Disordered | ||||
Sequence: ETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNLNSSVRGDRVYSPYNHRHRKRGRSRSSDSRSQSRSGHDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKRSRTRDSSWSRRSQTLSLSSESTSRSRSRSSDHGKRRSRSRNRDRYYL | ||||||
Compositional bias | 516-540 | Polar residues | ||||
Sequence: QEQEQSYSSGDSDVSRCSSPHSVLG | ||||||
Compositional bias | 542-567 | Basic and acidic residues | ||||
Sequence: DEQINKGHCDSSTRIKSKKEEKRSTS | ||||||
Compositional bias | 568-582 | Polar residues | ||||
Sequence: LSSPRNLNSSVRGDR | ||||||
Compositional bias | 610-645 | Basic residues | ||||
Sequence: HDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKR | ||||||
Compositional bias | 653-669 | Polar residues | ||||
Sequence: WSRRSQTLSLSSESTSR | ||||||
Region | 713-936 | Disordered | ||||
Sequence: RDGYESSYRRRTLSRAHYSRQSSSPEFRVQSFSERTNARKKNNHSERKYYYYERHRSRSLSSNRSRTASTGTDRVRNEKPGGKRKYKTRHLEGTNEVAQPSREFASKAKDSHYQKSSSKLDGNYKNESDTFSDSRSSDRETKHKRRKRKTRSLSVEIVYEGKATDTTKHHKKKKKKHKKKHKKHHGDNASRSPVVITIDSDSDKDSEVKEDTECDNSGPQDPLQ | ||||||
Compositional bias | 729-744 | Polar residues | ||||
Sequence: HYSRQSSSPEFRVQSF | ||||||
Compositional bias | 745-772 | Basic and acidic residues | ||||
Sequence: SERTNARKKNNHSERKYYYYERHRSRSL | ||||||
Compositional bias | 783-804 | Basic and acidic residues | ||||
Sequence: GTDRVRNEKPGGKRKYKTRHLE | ||||||
Compositional bias | 838-852 | Basic and acidic residues | ||||
Sequence: NESDTFSDSRSSDRE | ||||||
Region | 854-917 | Interaction with UBE2I | ||||
Sequence: KHKRRKRKTRSLSVEIVYEGKATDTTKHHKKKKKKHKKKHKKHHGDNASRSPVVITIDSDSDKD | ||||||
Compositional bias | 879-899 | Basic residues | ||||
Sequence: TKHHKKKKKKHKKKHKKHHGD | ||||||
Compositional bias | 910-928 | Basic and acidic residues | ||||
Sequence: IDSDSDKDSEVKEDTECDN |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9NS56-1
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.
- Name1
- SynonymsLUN-1
- Length1,045
- Mass (Da)119,198
- Last updated2000-10-01 v1
- Checksum3DA635FDB5C83B77
Q9NS56-2
- Name2
- SynonymsLUN-2
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_017916 | 1-65 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017917 | 66 | in isoform 2 | |||
Sequence: E → M | ||||||
Sequence conflict | 124-125 | in Ref. 5; AAC98530 | ||||
Sequence: CF → K | ||||||
Sequence conflict | 257 | in Ref. 1; AAD23379 | ||||
Sequence: N → S | ||||||
Sequence conflict | 308 | in Ref. 1; AAD23379 | ||||
Sequence: F → S | ||||||
Compositional bias | 516-540 | Polar residues | ||||
Sequence: QEQEQSYSSGDSDVSRCSSPHSVLG | ||||||
Compositional bias | 542-567 | Basic and acidic residues | ||||
Sequence: DEQINKGHCDSSTRIKSKKEEKRSTS | ||||||
Compositional bias | 568-582 | Polar residues | ||||
Sequence: LSSPRNLNSSVRGDR | ||||||
Compositional bias | 610-645 | Basic residues | ||||
Sequence: HDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKR | ||||||
Compositional bias | 653-669 | Polar residues | ||||
Sequence: WSRRSQTLSLSSESTSR | ||||||
Compositional bias | 729-744 | Polar residues | ||||
Sequence: HYSRQSSSPEFRVQSF | ||||||
Compositional bias | 745-772 | Basic and acidic residues | ||||
Sequence: SERTNARKKNNHSERKYYYYERHRSRSL | ||||||
Compositional bias | 783-804 | Basic and acidic residues | ||||
Sequence: GTDRVRNEKPGGKRKYKTRHLE | ||||||
Compositional bias | 838-852 | Basic and acidic residues | ||||
Sequence: NESDTFSDSRSSDRE | ||||||
Compositional bias | 879-899 | Basic residues | ||||
Sequence: TKHHKKKKKKHKKKHKKHHGD | ||||||
Compositional bias | 910-928 | Basic and acidic residues | ||||
Sequence: IDSDSDKDSEVKEDTECDN | ||||||
Sequence conflict | 922 | in Ref. 1; AAD23379 | ||||
Sequence: E → G | ||||||
Sequence conflict | 1040 | in Ref. 1; AAD23379 | ||||
Sequence: R → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF098300 EMBL· GenBank· DDBJ | AAD23379.1 EMBL· GenBank· DDBJ | mRNA | ||
AB045732 EMBL· GenBank· DDBJ | BAB03714.1 EMBL· GenBank· DDBJ | mRNA | ||
AB045733 EMBL· GenBank· DDBJ | BAB03715.1 EMBL· GenBank· DDBJ | mRNA | ||
AL353671 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC060884 EMBL· GenBank· DDBJ | AAH60884.1 EMBL· GenBank· DDBJ | mRNA | ||
U82939 EMBL· GenBank· DDBJ | AAC98530.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |