O43166 · SI1L1_HUMAN
- ProteinSignal-induced proliferation-associated 1-like protein 1
- GeneSIPA1L1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1804 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity).
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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Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | cytoplasm | |
Cellular Component | dendritic spine | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic density | |
Molecular Function | ephrin receptor binding | |
Molecular Function | GTPase activator activity | |
Biological Process | actin cytoskeleton organization | |
Biological Process | activation of GTPase activity | |
Biological Process | ephrin receptor signaling pathway | |
Biological Process | regulation of axonogenesis | |
Biological Process | regulation of dendritic spine morphogenesis | |
Biological Process | regulation of GTPase activity | |
Biological Process | regulation of small GTPase mediated signal transduction | |
Biological Process | regulation of synaptic plasticity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSignal-induced proliferation-associated 1-like protein 1
- Short namesSIPA1-like protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43166
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_049152 | 56 | in dbSNP:rs12884638 | |||
Sequence: P → T | ||||||
Natural variant | VAR_035549 | 996 | in a breast cancer sample; somatic mutation | |||
Sequence: E → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,736 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000056746 | 1-1804 | UniProt | Signal-induced proliferation-associated 1-like protein 1 | |||
Sequence: MTSLKRSQTERPLATDRASVVGTDGTPKVHTDDFYMRRFRSQNGSLGSSVMAPVGPPRSEGSHHITSTPGVPKMGVRARIADWPPRKENIKESSRSSQEIETSSCLDSLSSKSSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTRPSENMDSRFLMPEAYPSSPRKALRRIRQRSNSDITISELDVDSFDECISPTYKTGPSLHREYGSTSSIDKQGTSGESFFDLLKGYKDDKSDRGPTPTKLSDFLITGGGKGSGFSLDVIDGPISQRENLRLFKEREKPLKRRSKSETGDSSIFRKLRNAKGEELGKSSDLEDNRSEDSVRPWTCPKCFAHYDVQSILFDLNEAIMNRHNVIKRRNTTTGASAAAVASLVSGPLSHSASFSSPMGSTEDLNSKGSLSMDQGDDKSNELVMSCPYFRNEIGGEGERKISLSKSNSGSFSGCESASFESTLSSHCTNAGVAVLEVPKENLVLHLDRVKRYIVEHVDLGAYYYRKFFYQKEHWNYFGADENLGPVAVSIRREKPDEMKENGSPYNYRIIFRTSELMTLRGSVLEDAIPSTAKHSTARGLPLKEVLEHVVPELNVQCLRLAFNTPKVTEQLMKLDEQGLNYQQKVGIMYCKAGQSTEEEMYNNESAGPAFEEFLQLLGERVRLKGFEKYRAQLDTKTDSTGTHSLYTTYKDYEIMFHVSTMLPYTPNNKQQLLRKRHIGNDIVTIVFQEPGAQPFSPKNIRSHFQHVFVIVRVHNPCSDSVCYSVAVTRSRDVPSFGPPIPKGVTFPKSNVFRDFLLAKVINAENAAHKSEKFRAMATRTRQEYLKDLAEKNVTNTPIDPSGKFPFISLASKKKEKSKPYPGAELSSMGAIVWAVRAEDYNKAMELDCLLGISNEFIVLIEQETKSVVFNCSCRDVIGWTSTDTSLKIFYERGECVSVGSFINIEEIKEIVKRLQFVSKGCESVEMTLRRNGLGQLGFHVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVIIPPHDDCTPRRSCSETYRMPVMEYKMNEGVSYEFKFPFRNNNKWQRNASKGPHSPQVPSQVQSPMTSRLNAGKGDGKMPPPERAANIPRSISSDGRPLERRLSPGSDIYVTVSSMALARSQCRNSPSNLSSSSDTGSVGGTYRQKSMPEGFGVSRRSPASIDRQNTQSDIGGSGKSTPSWQRSEDSIADQMAYSYRGPQDFNSFVLEQHEYTEPTCHLPAVSKVLPAFRESPSGRLMRQDPVVHLSPNKQGHSDSHYSSHSSSNTLSSNASSAHSDEKWYDGDRTESELNSYNYLQGTSADSGIDTTSYGPSHGSTASLGAATSSPRSGPGKEKVAPLWHSSSEVISMADRTLETESHGLDRKTESSLSLDIHSKSQAGSTPLTRENSTFSINDAASHTSTMSSRHSASPVVFTSARSSPKEELHPAAPSQLAPSFSSSSSSSSGPRSFYPRQGATSKYLIGWKKPEGTINSVGFMDTRKRHQSDGNEIAHTRLRASTRDLRASPKPTSKSTIEEDLKKLIDLESPTPESQKSFKFHALSSPQSPFPSTPTSRRALHRTLSDESIYNSQREHFFTSRASLLDQALPNDVLFSSTYPSLPKSLPLRRPSYTLGMKSLHGEFSASDSSLTDIQETRRQPMPDPGLMPLPDTAADLDWSNLVDAAKAYEVQRASFFAASDENHRPLSAASNSDQLEDQALAQMKPYSSSKDSSPTLASKVDQLEGMLKMLREDLKKEKEDKAHLQAEVQHLREDNLRLQEESQNASDKLKKFTEWVFNTIDMS | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 161 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 162 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 187 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 193 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 208 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 239 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 249 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 255 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 288 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 288 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1073 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1078 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1078 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1083 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1087 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1087 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1116 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1127 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1133 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1149 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1151 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1170 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1181 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1197 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1255 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1270 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1270 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1326 | UniProt | Phosphoserine; by PLK2 | ||||
Sequence: S | |||||||
Modified residue | 1330 | UniProt | Phosphothreonine; by PLK2 | ||||
Sequence: T | |||||||
Modified residue | 1349 | UniProt | Phosphoserine; by CDK5 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1366 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1366 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1388 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1390 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1390 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1391 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1391 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1393 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1412 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1412 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1431 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1431 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1433 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1438 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1442 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1443 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1454 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1508 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1528 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1528 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1549 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1549 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1551 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1551 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1554 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1554 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1564 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1565 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1565 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1568 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1568 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1572 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1573 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1576 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1583 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1585 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1585 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1588 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1601 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 1603 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1603 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1632 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1639 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1645 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1645 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1647 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1647 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1649 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1650 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1650 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1695 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1708 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1708 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1711 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1711 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1728 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1729 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1734 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1734 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2.
Phosphorylated at Ser-1349 by CDK5, creating a docking site for the POLO box domains of PLK2. Subsequently, PLK2 binds and phosphorylates SIPA1L1, leading to ubiquitination and degradation by the proteasome (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with the actin cytoskeleton (By similarity).
Interacts (via PDZ domain) with EPHA4 (via PDZ motif); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. Interacts with HPV E6
Interacts (via PDZ domain) with EPHA4 (via PDZ motif); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. Interacts with HPV E6
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O43166 | DLG4 P78352 | 2 | EBI-310678, EBI-80389 | |
BINARY | O43166 | SFN P31947 | 3 | EBI-310678, EBI-476295 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-157 | Disordered | ||||
Sequence: MTSLKRSQTERPLATDRASVVGTDGTPKVHTDDFYMRRFRSQNGSLGSSVMAPVGPPRSEGSHHITSTPGVPKMGVRARIADWPPRKENIKESSRSSQEIETSSCLDSLSSKSSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTRPSENMDSRFLMPE | ||||||
Compositional bias | 80-95 | Basic and acidic residues | ||||
Sequence: IADWPPRKENIKESSR | ||||||
Compositional bias | 96-144 | Polar residues | ||||
Sequence: SSQEIETSSCLDSLSSKSSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTR | ||||||
Region | 277-297 | Disordered | ||||
Sequence: EREKPLKRRSKSETGDSSIFR | ||||||
Region | 380-401 | Disordered | ||||
Sequence: ASFSSPMGSTEDLNSKGSLSMD | ||||||
Domain | 613-830 | Rap-GAP | ||||
Sequence: VGIMYCKAGQSTEEEMYNNESAGPAFEEFLQLLGERVRLKGFEKYRAQLDTKTDSTGTHSLYTTYKDYEIMFHVSTMLPYTPNNKQQLLRKRHIGNDIVTIVFQEPGAQPFSPKNIRSHFQHVFVIVRVHNPCSDSVCYSVAVTRSRDVPSFGPPIPKGVTFPKSNVFRDFLLAKVINAENAAHKSEKFRAMATRTRQEYLKDLAEKNVTNTPIDPSG | ||||||
Domain | 967-1045 | PDZ | ||||
Sequence: HVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVIIPPHDDCTPRRSCSETYRMPV | ||||||
Compositional bias | 1067-1093 | Polar residues | ||||
Sequence: KWQRNASKGPHSPQVPSQVQSPMTSRL | ||||||
Region | 1067-1128 | Disordered | ||||
Sequence: KWQRNASKGPHSPQVPSQVQSPMTSRLNAGKGDGKMPPPERAANIPRSISSDGRPLERRLSP | ||||||
Compositional bias | 1144-1166 | Polar residues | ||||
Sequence: SQCRNSPSNLSSSSDTGSVGGTY | ||||||
Region | 1144-1207 | Disordered | ||||
Sequence: SQCRNSPSNLSSSSDTGSVGGTYRQKSMPEGFGVSRRSPASIDRQNTQSDIGGSGKSTPSWQRS | ||||||
Compositional bias | 1182-1207 | Polar residues | ||||
Sequence: PASIDRQNTQSDIGGSGKSTPSWQRS | ||||||
Region | 1268-1306 | Disordered | ||||
Sequence: HLSPNKQGHSDSHYSSHSSSNTLSSNASSAHSDEKWYDG | ||||||
Compositional bias | 1270-1299 | Polar residues | ||||
Sequence: SPNKQGHSDSHYSSHSSSNTLSSNASSAHS | ||||||
Compositional bias | 1327-1349 | Polar residues | ||||
Sequence: GIDTTSYGPSHGSTASLGAATSS | ||||||
Region | 1327-1366 | Disordered | ||||
Sequence: GIDTTSYGPSHGSTASLGAATSSPRSGPGKEKVAPLWHSS | ||||||
Compositional bias | 1379-1393 | Basic and acidic residues | ||||
Sequence: TESHGLDRKTESSLS | ||||||
Region | 1379-1475 | Disordered | ||||
Sequence: TESHGLDRKTESSLSLDIHSKSQAGSTPLTRENSTFSINDAASHTSTMSSRHSASPVVFTSARSSPKEELHPAAPSQLAPSFSSSSSSSSGPRSFYP | ||||||
Compositional bias | 1394-1440 | Polar residues | ||||
Sequence: LDIHSKSQAGSTPLTRENSTFSINDAASHTSTMSSRHSASPVVFTSA | ||||||
Compositional bias | 1455-1475 | Polar residues | ||||
Sequence: QLAPSFSSSSSSSSGPRSFYP | ||||||
Compositional bias | 1505-1524 | Basic and acidic residues | ||||
Sequence: RHQSDGNEIAHTRLRASTRD | ||||||
Region | 1505-1536 | Disordered | ||||
Sequence: RHQSDGNEIAHTRLRASTRDLRASPKPTSKST | ||||||
Coiled coil | 1735-1795 | |||||
Sequence: PTLASKVDQLEGMLKMLREDLKKEKEDKAHLQAEVQHLREDNLRLQEESQNASDKLKKFTE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O43166-1
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
- SynonymsE6TP1 beta
- Length1,804
- Mass (Da)200,029
- Last updated2006-10-03 v4
- Checksum91AB6AB4E7F47B2F
O43166-2
- Name2
- SynonymsE6TP1 alpha
- Differences from canonical
- 1216-1236: Missing
O43166-3
- Name3
- Differences from canonical
- 1216-1236: Missing
- 1728-1728: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 80-95 | Basic and acidic residues | ||||
Sequence: IADWPPRKENIKESSR | ||||||
Compositional bias | 96-144 | Polar residues | ||||
Sequence: SSQEIETSSCLDSLSSKSSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTR | ||||||
Compositional bias | 1067-1093 | Polar residues | ||||
Sequence: KWQRNASKGPHSPQVPSQVQSPMTSRL | ||||||
Compositional bias | 1144-1166 | Polar residues | ||||
Sequence: SQCRNSPSNLSSSSDTGSVGGTY | ||||||
Compositional bias | 1182-1207 | Polar residues | ||||
Sequence: PASIDRQNTQSDIGGSGKSTPSWQRS | ||||||
Alternative sequence | VSP_010917 | 1216-1236 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 1270-1299 | Polar residues | ||||
Sequence: SPNKQGHSDSHYSSHSSSNTLSSNASSAHS | ||||||
Compositional bias | 1327-1349 | Polar residues | ||||
Sequence: GIDTTSYGPSHGSTASLGAATSS | ||||||
Compositional bias | 1379-1393 | Basic and acidic residues | ||||
Sequence: TESHGLDRKTESSLS | ||||||
Sequence conflict | 1387 | in Ref. 4; AK122930 | ||||
Sequence: K → R | ||||||
Compositional bias | 1394-1440 | Polar residues | ||||
Sequence: LDIHSKSQAGSTPLTRENSTFSINDAASHTSTMSSRHSASPVVFTSA | ||||||
Compositional bias | 1455-1475 | Polar residues | ||||
Sequence: QLAPSFSSSSSSSSGPRSFYP | ||||||
Compositional bias | 1505-1524 | Basic and acidic residues | ||||
Sequence: RHQSDGNEIAHTRLRASTRD | ||||||
Sequence conflict | 1722 | in Ref. 2; BAA23712 | ||||
Sequence: A → P | ||||||
Alternative sequence | VSP_054774 | 1728 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 1730 | in Ref. 2; BAA23712 | ||||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF090989 EMBL· GenBank· DDBJ | AAD12543.1 EMBL· GenBank· DDBJ | mRNA | ||
AF090990 EMBL· GenBank· DDBJ | AAD12544.1 EMBL· GenBank· DDBJ | mRNA | ||
AB007900 EMBL· GenBank· DDBJ | BAA23712.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK122930 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AC004974 EMBL· GenBank· DDBJ | AAC83179.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC004900 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC004968 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC005476 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC005994 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL391735 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |