O60292 · SI1L3_HUMAN
- ProteinSignal-induced proliferation-associated 1-like protein 3
- GeneSIPA1L3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1781 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217).
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 | apical part of cell | |
Cellular Component | apical plasma membrane | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular space | |
Cellular Component | Golgi apparatus | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | stress fiber | |
Cellular Component | tricellular tight junction | |
Molecular Function | GTPase activator activity | |
Biological Process | cytoskeleton organization | |
Biological Process | epithelial cell morphogenesis | |
Biological Process | establishment of epithelial cell polarity | |
Biological Process | eye development | |
Biological Process | hematopoietic progenitor cell differentiation | |
Biological Process | regulation of small GTPase mediated signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSignal-induced proliferation-associated 1-like protein 3
- Short namesSIPA1-like protein 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60292
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected in tricellular junctions. Colocalizes with apical F-actin.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cataract 45 (CTRCT45)
- Note
- DescriptionAn opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function.
- See alsoMIM:616851
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_075045 | 148 | found in a patient with bilateral congenital cataracts; uncertain significance; lack of normal basal actin stress fiber formation; absence of SIPA1L3 and F-actin colocalization; dbSNP:rs138476311 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_025476 | 1371 | in dbSNP:rs2304133 | |||
Sequence: G → S | ||||||
Natural variant | VAR_025477 | 1450 | in dbSNP:rs3745945 | |||
Sequence: P → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,186 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), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000056752 | 1-1781 | UniProt | Signal-induced proliferation-associated 1-like protein 3 | |||
Sequence: MTTYRAIPSDGVDLAASCGARVGDVLPGPHTGDYAPLGFWAQNGSMSQPLGESPATATATATATTRPSPTTPAMPKMGVRARVADWPPKREALREHSNPSPSQDTDGTKATKMAHSMRSIQNGQPPTSTPASSGSKAFHRLSRRRSKDVEFQDGWPRSPGRAFLPLRHRSSSEITLSECDAEDAGEPRGARHTGALPLFREYGSTSSIDVQGMPEQSFFDILNEFRSEQPDARGCQALTELLRADPGPHLMGGGGGAKGDSHNGQPAKDSLLPLQPTKEKEKARKKPARGLGGGDTVDSSIFRKLRSSKPEGEAGRSPGEADEGRSPPEASRPWVCQKSFAHFDVQSMLFDLNEAAANRVSVSQRRNTTTGASAASAASAMASLTASRAHSLGGLDPAFTSTEDLNCKENLEQDLGDDNSNDLLLSCPHFRNEIGGECERNVSFSRASVGSPSSGEGHLAEPALSAYRTNASISVLEVPKEQQRTQSRPRQYSIEHVDLGARYYQDYFVGKEHANYFGVDEKLGPVAVSIKREKLEDHKEHGPQYQYRIIFRTRELITLRGSILEDATPTATKHGTGRGLPLKDALEYVIPELNIHCLRLALNTPKVTEQLLKLDEQGLCRKHKVGILYCKAGQSSEEEMYNNEEAGPAFEEFLSLIGEKVCLKGFTKYAAQLDVKTDSTGTHSLYTMYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGNDIVTIIFQEPGALPFTPKNIRSHFQHVFIIVRVHNPCTDNVCYSMAVTRSKDAPPFGPPIPSGTTFRKSDVFRDFLLAKVINAENAAHKSDKFHTMATRTRQEYLKDLAENCVSNTPIDSTGKFNLISLTSKKKEKTKARAGAEQHSAGAIAWRVVAQDYAQGVEIDCILGISNEFVVLLDLRTKEVVFNCYCGDVIGWTPDSSTLKIFYGRGDHIFLQATEGSVEDIREIVQRLKVMTSGWETVDMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSVTVKVVIIPPFEDGTPRRGWPETYDMNTSEPKTEQESITPGGRPPYRSNAPWQWSGPASHNSLPASKWATPTTPGHAQSLSRPLKQTPIVPFRESQPLHSKRPVSFPETPYTVSPAGADRVPPYRQPSGSFSTPGSATYVRYKPSPERYTAAPHPLLSLDPHFSHDGTSSGDSSSGGLTSQESTMERQKPEPLWHVPAQARLSAIAGSSGNKHPSRQDAAGKDSPNRHSKGEPQYSSHSSSNTLSSNASSSHSDDRWFDPLDPLEPEQDPLSKGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAGQSKGYRPKLYSSGSSTPTGLAGGSRDPPRQPSDMGSRVGYPAQVYKTASAETPRPSQLAQPSPFQLSASVPKSFFSKQPVRNKHPTGWKRTEEPPPRPLPFSDPKKQVDTNTKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPEQERDTGQSPQKGLQRTLSDESLCSGRREPSFASPAGLEPGLPSDVLFTSTCAFPSSTLPARRQHQHPHPPVGPGATPAAGSGFPEKKSTISASELSLADGRDRPLRRLDPGLMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDIPPAHSPVHSHLSLERGPPTPRTTPTMSEEPPLDLTGKVYQLEVMLKQLHTDLQKEKQDKVVLQSEVASLRQNNQRLQEESQAASEQLRKFAEIFCREKKEL | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 100 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 100 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 146 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 158 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 326 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 391 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 401 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1109 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1135 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1139 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1141 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1144 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1158 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1316 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1364 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1381 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1382 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1386 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1387 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1387 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1440 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1448 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1531 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1534 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1542 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1544 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1547 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1547 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1559 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1617 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1619 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1619 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1622 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1677 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1677 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1685 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1699 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1699 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1702 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1703 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1703 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1705 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1707 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O60292 | SFN P31947 | 4 | EBI-2559690, EBI-476295 | |
BINARY | O60292 | YWHAZ P63104 | 6 | EBI-2559690, EBI-347088 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 45-71 | Polar residues | ||||
Sequence: SMSQPLGESPATATATATATTRPSPTT | ||||||
Region | 45-166 | Disordered | ||||
Sequence: SMSQPLGESPATATATATATTRPSPTTPAMPKMGVRARVADWPPKREALREHSNPSPSQDTDGTKATKMAHSMRSIQNGQPPTSTPASSGSKAFHRLSRRRSKDVEFQDGWPRSPGRAFLPL | ||||||
Compositional bias | 83-97 | Basic and acidic residues | ||||
Sequence: VADWPPKREALREHS | ||||||
Compositional bias | 98-136 | Polar residues | ||||
Sequence: NPSPSQDTDGTKATKMAHSMRSIQNGQPPTSTPASSGSK | ||||||
Region | 239-332 | Disordered | ||||
Sequence: TELLRADPGPHLMGGGGGAKGDSHNGQPAKDSLLPLQPTKEKEKARKKPARGLGGGDTVDSSIFRKLRSSKPEGEAGRSPGEADEGRSPPEASR | ||||||
Compositional bias | 274-291 | Basic and acidic residues | ||||
Sequence: LQPTKEKEKARKKPARGL | ||||||
Compositional bias | 302-327 | Basic and acidic residues | ||||
Sequence: FRKLRSSKPEGEAGRSPGEADEGRSP | ||||||
Domain | 611-828 | Rap-GAP | ||||
Sequence: LLKLDEQGLCRKHKVGILYCKAGQSSEEEMYNNEEAGPAFEEFLSLIGEKVCLKGFTKYAAQLDVKTDSTGTHSLYTMYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGNDIVTIIFQEPGALPFTPKNIRSHFQHVFIIVRVHNPCTDNVCYSMAVTRSKDAPPFGPPIPSGTTFRKSDVFRDFLLAKVINAENAAHKSDKFHTMATRTRQEYLKDL | ||||||
Domain | 966-1042 | PDZ | ||||
Sequence: DMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSVTVKVVIIPPFE | ||||||
Region | 1046-1112 | Disordered | ||||
Sequence: PRRGWPETYDMNTSEPKTEQESITPGGRPPYRSNAPWQWSGPASHNSLPASKWATPTTPGHAQSLSR | ||||||
Compositional bias | 1082-1112 | Polar residues | ||||
Sequence: WQWSGPASHNSLPASKWATPTTPGHAQSLSR | ||||||
Region | 1124-1221 | Disordered | ||||
Sequence: ESQPLHSKRPVSFPETPYTVSPAGADRVPPYRQPSGSFSTPGSATYVRYKPSPERYTAAPHPLLSLDPHFSHDGTSSGDSSSGGLTSQESTMERQKPE | ||||||
Compositional bias | 1193-1217 | Polar residues | ||||
Sequence: FSHDGTSSGDSSSGGLTSQESTMER | ||||||
Region | 1236-1565 | Disordered | ||||
Sequence: AGSSGNKHPSRQDAAGKDSPNRHSKGEPQYSSHSSSNTLSSNASSSHSDDRWFDPLDPLEPEQDPLSKGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAGQSKGYRPKLYSSGSSTPTGLAGGSRDPPRQPSDMGSRVGYPAQVYKTASAETPRPSQLAQPSPFQLSASVPKSFFSKQPVRNKHPTGWKRTEEPPPRPLPFSDPKKQVDTNTKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPEQERDTGQSPQKGLQRTLSDESLCSGRREPSFASPAGLEP | ||||||
Compositional bias | 1260-1284 | Polar residues | ||||
Sequence: KGEPQYSSHSSSNTLSSNASSSHSD | ||||||
Compositional bias | 1302-1324 | Polar residues | ||||
Sequence: SKGGSSDSGIDTTLYTSSPSCMS | ||||||
Compositional bias | 1378-1392 | Polar residues | ||||
Sequence: PKLYSSGSSTPTGLA | ||||||
Compositional bias | 1420-1451 | Polar residues | ||||
Sequence: SAETPRPSQLAQPSPFQLSASVPKSFFSKQPV | ||||||
Compositional bias | 1496-1523 | Basic and acidic residues | ||||
Sequence: LRDLRSPRKNYKSTIEDDLKKLIIMDNL | ||||||
Compositional bias | 1527-1546 | Polar residues | ||||
Sequence: QERDTGQSPQKGLQRTLSDE | ||||||
Region | 1583-1636 | Disordered | ||||
Sequence: TLPARRQHQHPHPPVGPGATPAAGSGFPEKKSTISASELSLADGRDRPLRRLDP | ||||||
Region | 1685-1712 | Disordered | ||||
Sequence: SPVHSHLSLERGPPTPRTTPTMSEEPPL | ||||||
Coiled coil | 1720-1774 | |||||
Sequence: QLEVMLKQLHTDLQKEKQDKVVLQSEVASLRQNNQRLQEESQAASEQLRKFAEIF |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,781
- Mass (Da)194,610
- Last updated2006-03-07 v3
- Checksum6A91F43B5BC3E175
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 45-71 | Polar residues | ||||
Sequence: SMSQPLGESPATATATATATTRPSPTT | ||||||
Compositional bias | 83-97 | Basic and acidic residues | ||||
Sequence: VADWPPKREALREHS | ||||||
Compositional bias | 98-136 | Polar residues | ||||
Sequence: NPSPSQDTDGTKATKMAHSMRSIQNGQPPTSTPASSGSK | ||||||
Compositional bias | 274-291 | Basic and acidic residues | ||||
Sequence: LQPTKEKEKARKKPARGL | ||||||
Compositional bias | 302-327 | Basic and acidic residues | ||||
Sequence: FRKLRSSKPEGEAGRSPGEADEGRSP | ||||||
Compositional bias | 1082-1112 | Polar residues | ||||
Sequence: WQWSGPASHNSLPASKWATPTTPGHAQSLSR | ||||||
Compositional bias | 1193-1217 | Polar residues | ||||
Sequence: FSHDGTSSGDSSSGGLTSQESTMER | ||||||
Compositional bias | 1260-1284 | Polar residues | ||||
Sequence: KGEPQYSSHSSSNTLSSNASSSHSD | ||||||
Compositional bias | 1302-1324 | Polar residues | ||||
Sequence: SKGGSSDSGIDTTLYTSSPSCMS | ||||||
Compositional bias | 1378-1392 | Polar residues | ||||
Sequence: PKLYSSGSSTPTGLA | ||||||
Compositional bias | 1420-1451 | Polar residues | ||||
Sequence: SAETPRPSQLAQPSPFQLSASVPKSFFSKQPV | ||||||
Compositional bias | 1496-1523 | Basic and acidic residues | ||||
Sequence: LRDLRSPRKNYKSTIEDDLKKLIIMDNL | ||||||
Compositional bias | 1527-1546 | Polar residues | ||||
Sequence: QERDTGQSPQKGLQRTLSDE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY168880 EMBL· GenBank· DDBJ | AAO12531.1 EMBL· GenBank· DDBJ | mRNA | ||
AB011117 EMBL· GenBank· DDBJ | BAA25471.2 EMBL· GenBank· DDBJ | mRNA | ||
AC011465 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC011479 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |