P04412 · EGFR_DROME
- ProteinEpidermal growth factor receptor
- GeneEgfr
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1426 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor tyrosine kinase, binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:22140578, PubMed:23579691, PubMed:8070664, PubMed:9882502).
Known ligands include spitz, gurken, vein and giant-lens (PubMed:19718021, PubMed:20723758, PubMed:22140578, PubMed:9882502).
Transduces the signal through the ras-raf-MAPK pathway (PubMed:9094709).
Critical for the proliferation of imaginal tissues, and for the determination of both the antero-posterior and dorso-ventral polarities of the oocyte (PubMed:23579691, PubMed:34411095, PubMed:9882502).
In the embryo, plays a role in the establishment of ventral cell fates, maintenance of amnioserosa and ventral neuroectodermal cells, germ band retraction, cell fate specification in the central nervous system, and production and repair of the cuticle (PubMed:22140578, PubMed:23029159, PubMed:23579691, PubMed:9094709).
During dorsal closure (DC) functions with the dpp- and ACK-signaling pathways to regulate expression of the myosin zip in the embryonic epidermis and amnioserosa (AS), and thus coordinate the progression of epidermal cell shape changes required for correct DC (PubMed:23579691).
In the embryonic epidermis, functions by negatively regulating dpp and consequently the dpp-dependent expression of the myosin zip (PubMed:23579691).
In the AS, negatively regulates the production/ and or secretion of a diffusible signal which, is produced by the ACK-signaling pathway, and acts in the AS and epidermal cells to promote zip expression (PubMed:23579691).
Also required in the AS to inhibit or delay apoptosis, and consequently slow the rate of DC (PubMed:23579691).
Therefore functions at multiple levels to negatively regulate morphogenesis during DC, suggesting that it acts as a general brake mechanism for adjusting the rate of dorsal closure to ensure that closure proceeds smoothly and without loss of epidermal integrity (PubMed:23579691).
During oogenesis, one of two tyrosine kinase chemoattractant receptors (Egfr and Pvr), that function in the border cells (BC) to detect guidance cues from the oocyte and transduce this information to the guidance pathway that regulate the collective migration of the BC cluster through the nurse cells to the oocyte (PubMed:24855950).
Known ligands include spitz, gurken, vein and giant-lens (PubMed:19718021, PubMed:20723758, PubMed:22140578, PubMed:9882502).
Transduces the signal through the ras-raf-MAPK pathway (PubMed:9094709).
Critical for the proliferation of imaginal tissues, and for the determination of both the antero-posterior and dorso-ventral polarities of the oocyte (PubMed:23579691, PubMed:34411095, PubMed:9882502).
In the embryo, plays a role in the establishment of ventral cell fates, maintenance of amnioserosa and ventral neuroectodermal cells, germ band retraction, cell fate specification in the central nervous system, and production and repair of the cuticle (PubMed:22140578, PubMed:23029159, PubMed:23579691, PubMed:9094709).
During dorsal closure (DC) functions with the dpp- and ACK-signaling pathways to regulate expression of the myosin zip in the embryonic epidermis and amnioserosa (AS), and thus coordinate the progression of epidermal cell shape changes required for correct DC (PubMed:23579691).
In the embryonic epidermis, functions by negatively regulating dpp and consequently the dpp-dependent expression of the myosin zip (PubMed:23579691).
In the AS, negatively regulates the production/ and or secretion of a diffusible signal which, is produced by the ACK-signaling pathway, and acts in the AS and epidermal cells to promote zip expression (PubMed:23579691).
Also required in the AS to inhibit or delay apoptosis, and consequently slow the rate of DC (PubMed:23579691).
Therefore functions at multiple levels to negatively regulate morphogenesis during DC, suggesting that it acts as a general brake mechanism for adjusting the rate of dorsal closure to ensure that closure proceeds smoothly and without loss of epidermal integrity (PubMed:23579691).
During oogenesis, one of two tyrosine kinase chemoattractant receptors (Egfr and Pvr), that function in the border cells (BC) to detect guidance cues from the oocyte and transduce this information to the guidance pathway that regulate the collective migration of the BC cluster through the nurse cells to the oocyte (PubMed:24855950).
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEpidermal growth factor receptor
- EC number
- Short namesEgfr
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP04412
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 31-868 | Extracellular | ||||
Sequence: ARDRYARQNNRQRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKICIGTKSRLSVPSNKEHHYRNLRDRYTNCTYVDGNLKLTWLPNENLDLSFLDNIREVTGYILISHVDVKKVVFPKLQIIRGRTLFSLSVEEEKYALFVTYSKMYTLEIPDLRDVLNGQVGFHNNYNLCHMRTIQWSEIVSNGTDAYYNYDFTAPERECPKCHESCTHGCWGEGPKNCQKFSKLTCSPQCAGGRCYGPKPRECCHLFCAGGCTGPTQKDCIACKNFFDEAVSKEECPPMRKYNPTTYVLETNPEGKYAYGATCVKECPGHLLRDNGACVRSCPQDKMDKGGECVPCNGPCPKTCPGVTVLHAGNIDSFRNCTVIDGNIRILDQTFSGFQDVYANYTMGPRYIPLDPERREVFSTVKEITGYLNIEGTHPQFRNLSYFRNLETIHGRQLMESMFAALAIVKSSLYSLEMRNLKQISSGSVVIQHNRDLCYVSNIRWPAIQKEPEQKVWVNENLRADLCEKNGTICSDQCNEDGCWGAGTDQCLTCKNFNFNGTCIADCGYISNAYKFDNRTCKICHPECRTCNGAGADHCQECVHVRDGQHCVSECPKNKYNDRGVCRECHATCDGCTGPKDTIGIGACTTCNLAIINNDATVKRCLLKDDKCPDGYFWEYVHPQEQGSLKPLAGRAVCRKCHPLCELCTNYGYHEQVCSKCTHYKRREQCETECPADHYTDEEQRECFQRHPECNGCTGPGADDCKSCRNFKLFDANETGPYVNSTMFNCTSKCPLEMRHVNYQYTAIGPYCAASPPRSSKITANLDVN | ||||||
Transmembrane | 869-889 | Helical | ||||
Sequence: MIFIITGAVLVPTICILCVVT | ||||||
Topological domain | 890-1426 | Cytoplasmic | ||||
Sequence: YICRQKQKAKKETVKMTMALSGCEDSEPLRPSNIGANLCKLRIVKDAELRKGGVLGMGAFGRVYKGVWVPEGENVKIPVAIKELLKSTGAESSEEFLREAYIMASEEHVNLLKLLAVCMSSQMMLITQLMPLGCLLDYVRNNRDKIGSKALLNWSTQIAKGMSYLEEKRLVHRDLAARNVLVQTPSLVKITDFGLAKLLSSDSNEYKAAGGKMPIKWLALECIRNRVFTSKSDVWAFGVTIWELLTFGQRPHENIPAKDIPDLIEVGLKLEQPEICSLDIYCTLLSCWHLDAAMRPTFKQLTTVFAEFARDPGRYLAIPGDKFTRLPAYTSQDEKDLIRKLAPTTDGSEAIAKPDDYLQPKAAPGPSHRTDCTDEMPKLNRYCKDPSNKNSSTGDDERDSSAREVGVGNLRLDLPVDEDDYLMPTCQPGPNNNNNMNNPNQNNMAAVGVAAGYMDLIGVPVSVDNPEYLLNAQTLGVGESPIPTQTIGIPVMGGPGTMEVKVPMPGSEPTSSDHEYYNDTQRELQPLHRNRNTETRV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryonic wound healing defects. RNAi-mediated knockdown in tracheal cells results in defective gas-filling lumen in terminal branches (PubMed:23029159).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 101 | Increased binding to spitz; when associated with A-101; A-358 and S-369. | ||||
Sequence: I → A | ||||||
Mutagenesis | 131 | Increased binding to spitz; when associated with A-131; A-358 and S-369. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 341 | In dim-arm; Does not form dimers even in the presence of spitz; when associated with A-342; D-344; E-346; A-347 and D-348. | ||||
Sequence: Y → E | ||||||
Mutagenesis | 342 | In dim-arm; Does not form dimers even in the presence of spitz; when associated with E-341; D-344; E-346; A-347 and D-348. | ||||
Sequence: N → A | ||||||
Mutagenesis | 344 | >D: In dim-arm; Does not form dimers even in the presence of spitz; when associated with E-341; A-342; E-346; A-347 and D-348. | ||||
Sequence: T → D | ||||||
Mutagenesis | 346 | In dim-arm; Does not form dimers even in the presence of spitz; when associated with E-341; A-342; D-344; A-347 and D-348. | ||||
Sequence: Y → E | ||||||
Mutagenesis | 347 | In dim-arm; Does not form dimers even in the presence of Spitz; when associated with E-341; A-342; D-344; E-346 and D-348. | ||||
Sequence: V → A | ||||||
Mutagenesis | 348 | In dim-arm; Does not form dimers even in the presence of spitz; when associated with E-341; A-342; D-344; E-346 and A-347. | ||||
Sequence: L → D | ||||||
Mutagenesis | 358 | Reduced dissociation and increased binding to spitz; when associated with S-369. Increased binding to spitz; when associated with A-101; A-131 and S-369. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 369 | Reduced dissociation and increased binding to spitz; when associated with A-358. Increased binding to spitz; when associated with A-101; A-131 and A-358. | ||||
Sequence: H → S | ||||||
Mutagenesis | 592-1426 | Slightly reduced affinity for spitz. | ||||
Sequence: Missing | ||||||
Mutagenesis | 646 | In tether; No effect on binding to spitz; when associated with A-649 and A-658. | ||||
Sequence: D → A | ||||||
Mutagenesis | 649 | In tether; No effect on binding to spitz; when associated with A-646 and A-658. | ||||
Sequence: H → A | ||||||
Mutagenesis | 658 | In tether; No effect on binding to spitz; when associated with A-646 and A-649. | ||||
Sequence: K → A | ||||||
Mutagenesis | 688-1426 | Forms dimers in presence of spitz. Forms weak dimers in the absence of spitz. | ||||
Sequence: Missing | ||||||
Mutagenesis | 793 | In EGFR-ELP-1. | ||||
Sequence: C → R | ||||||
Mutagenesis | 936 | In EGFR-ELP-B1 and EGFR-ELP-B1RB1. | ||||
Sequence: A → T | ||||||
Mutagenesis | 1058 | In EGFR-ELP-B1RB1. | ||||
Sequence: R → Q | ||||||
Mutagenesis | 1095 | Weak interaction with EGFRAP; when associated with F-1204; F-1218; F-1246; F-1271; F-1310; F-1342. Very weak interaction with EGFRAP; when associated with F-1204; F-1218; F-1246; F-1271; F-1310; F-1342 and 1405-F-F-1406. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1135 | In EGFR-2W74. | ||||
Sequence: T → I | ||||||
Mutagenesis | 1156 | In EGFR-2C82. | ||||
Sequence: G → S | ||||||
Mutagenesis | 1162 | In EGFR-1F26. | ||||
Sequence: P → L | ||||||
Mutagenesis | 1166 | In EGFR-2L65. | ||||
Sequence: S → L | ||||||
Mutagenesis | 1204 | Weak interaction with EGFRAP; when associated with F-1095; F-1218; F-1246; F-1271; F-1310; F-1342. Very weak interaction with EGFRAP; when associated with F-1095; F-1218; F-1246; F-1271; F-1310; F-1342 and 1405-F-F-1406. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1210-1216 | In EGFR-2X51. | ||||
Sequence: DKFTRLP → EKVHPAA | ||||||
Mutagenesis | 1218 | Weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1246; F-1271; F-1310; F-1342. Very weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1246; F-1271; F-1310; F-1342 and 1405-F-F-1406. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1246 | Weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1218; F-1271; F-1310; F-1342. Very weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1218; F-1271; F-1310; F-1342 and 1405-F-F-1406. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1271 | Cbl-mediated ubiquitination, in response to high levels of Egfr ligand spi, is impaired resulting in reduced interaction with Graf and thus decreased GEEC-mediated endocytosis and degradation. Weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1218; F-1246; F-1310; F-1342. Very weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1218; F-1246; F-1310; F-1342 and 1405-F-F-1406. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1310 | Weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1218; F-1246; F-1271; F-1342. Very weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1218; F-1246; F-1271; F-1342 and 1405-F-F-1406. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1357 | No effect on interaction with EGFRAP. Decreased interaction with EGFRAP; when associated with 1405-F-F-1406. Very weak interaction with EGFRAP; when associated with F-1095; F-1204; F-1218; F-1246; F-1271; F-1310. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1405-1406 | Decreased interaction with EGFRAP; when associated with F-1357. | ||||
Sequence: YY → FF |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MLLRRRNGPCPFPLLLLLLAHCICIWPASA | ||||||
Chain | PRO_0000016676 | 31-1426 | Epidermal growth factor receptor | |||
Sequence: ARDRYARQNNRQRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKICIGTKSRLSVPSNKEHHYRNLRDRYTNCTYVDGNLKLTWLPNENLDLSFLDNIREVTGYILISHVDVKKVVFPKLQIIRGRTLFSLSVEEEKYALFVTYSKMYTLEIPDLRDVLNGQVGFHNNYNLCHMRTIQWSEIVSNGTDAYYNYDFTAPERECPKCHESCTHGCWGEGPKNCQKFSKLTCSPQCAGGRCYGPKPRECCHLFCAGGCTGPTQKDCIACKNFFDEAVSKEECPPMRKYNPTTYVLETNPEGKYAYGATCVKECPGHLLRDNGACVRSCPQDKMDKGGECVPCNGPCPKTCPGVTVLHAGNIDSFRNCTVIDGNIRILDQTFSGFQDVYANYTMGPRYIPLDPERREVFSTVKEITGYLNIEGTHPQFRNLSYFRNLETIHGRQLMESMFAALAIVKSSLYSLEMRNLKQISSGSVVIQHNRDLCYVSNIRWPAIQKEPEQKVWVNENLRADLCEKNGTICSDQCNEDGCWGAGTDQCLTCKNFNFNGTCIADCGYISNAYKFDNRTCKICHPECRTCNGAGADHCQECVHVRDGQHCVSECPKNKYNDRGVCRECHATCDGCTGPKDTIGIGACTTCNLAIINNDATVKRCLLKDDKCPDGYFWEYVHPQEQGSLKPLAGRAVCRKCHPLCELCTNYGYHEQVCSKCTHYKRREQCETECPADHYTDEEQRECFQRHPECNGCTGPGADDCKSCRNFKLFDANETGPYVNSTMFNCTSKCPLEMRHVNYQYTAIGPYCAASPPRSSKITANLDVNMIFIITGAVLVPTICILCVVTYICRQKQKAKKETVKMTMALSGCEDSEPLRPSNIGANLCKLRIVKDAELRKGGVLGMGAFGRVYKGVWVPEGENVKIPVAIKELLKSTGAESSEEFLREAYIMASEEHVNLLKLLAVCMSSQMMLITQLMPLGCLLDYVRNNRDKIGSKALLNWSTQIAKGMSYLEEKRLVHRDLAARNVLVQTPSLVKITDFGLAKLLSSDSNEYKAAGGKMPIKWLALECIRNRVFTSKSDVWAFGVTIWELLTFGQRPHENIPAKDIPDLIEVGLKLEQPEICSLDIYCTLLSCWHLDAAMRPTFKQLTTVFAEFARDPGRYLAIPGDKFTRLPAYTSQDEKDLIRKLAPTTDGSEAIAKPDDYLQPKAAPGPSHRTDCTDEMPKLNRYCKDPSNKNSSTGDDERDSSAREVGVGNLRLDLPVDEDDYLMPTCQPGPNNNNNMNNPNQNNMAAVGVAAGYMDLIGVPVSVDNPEYLLNAQTLGVGESPIPTQTIGIPVMGGPGTMEVKVPMPGSEPTSSDHEYYNDTQRELQPLHRNRNTETRV | ||||||
Glycosylation | 128 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 241 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 419 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 443 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 482 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 569 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 599 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 617 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 816 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 823 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 828 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 902 | Phosphothreonine; by PKC | ||||
Sequence: T | ||||||
Modified residue | 1310 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y |
Post-translational modification
Ubiquitination by Cbl in response to high spi, promotes its interaction with Graf and thus facilitates its GPI-enriched endocytic compartment (GEEC) mediated endocytosis and its subsequent degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed in embryos. In larvae, uniform expression is seen in wing disks, genital disk, anlagen of testis and ovary, and brain cortex. In eye-antenna disk, highest expression is anterior to morphogenetic furrow, levels remain high in photoreceptor precursor cells. This pattern is reversed in posterior eye disk. In adults expression is high in brain cortex and thoracic and abdominal ganglia.
Gene expression databases
Interaction
Subunit
Homodimer (PubMed:19718021, PubMed:20723758).
Binding of the ligand spitz triggers homodimerization of the receptor however, it is able to form dimers, albeit weakly, in the absence of spitz (PubMed:19718021, PubMed:20723758).
Interacts (when phosphorylated on tyrosine residues) with Vav (via SH2 domain) (PubMed:10781813).
Interacts (when ubiquitinated) with Graf (PubMed:28993397).
May interact (when phosphorylated) with EGFRAP (via SH2 domain) (PubMed:34411095).
Binding of the ligand spitz triggers homodimerization of the receptor however, it is able to form dimers, albeit weakly, in the absence of spitz (PubMed:19718021, PubMed:20723758).
Interacts (when phosphorylated on tyrosine residues) with Vav (via SH2 domain) (PubMed:10781813).
Interacts (when ubiquitinated) with Graf (PubMed:28993397).
May interact (when phosphorylated) with EGFRAP (via SH2 domain) (PubMed:34411095).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P04412 | kek1 P91643 | 2 | EBI-197863, EBI-6896313 | |
BINARY | P04412 | spi Q01083 | 4 | EBI-197863, EBI-91342 | |
BINARY | P04412-1 | Egfr P04412-1 | 4 | EBI-15802052, EBI-15802052 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 938-1198 | Protein kinase | ||||
Sequence: LRKGGVLGMGAFGRVYKGVWVPEGENVKIPVAIKELLKSTGAESSEEFLREAYIMASEEHVNLLKLLAVCMSSQMMLITQLMPLGCLLDYVRNNRDKIGSKALLNWSTQIAKGMSYLEEKRLVHRDLAARNVLVQTPSLVKITDFGLAKLLSSDSNEYKAAGGKMPIKWLALECIRNRVFTSKSDVWAFGVTIWELLTFGQRPHENIPAKDIPDLIEVGLKLEQPEICSLDIYCTLLSCWHLDAAMRPTFKQLTTVFAEFA | ||||||
Region | 1232-1297 | Disordered | ||||
Sequence: PTTDGSEAIAKPDDYLQPKAAPGPSHRTDCTDEMPKLNRYCKDPSNKNSSTGDDERDSSAREVGVG | ||||||
Compositional bias | 1279-1293 | Basic and acidic residues | ||||
Sequence: NSSTGDDERDSSARE |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P04412-1
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.
- NameType I
- Length1,426
- Mass (Da)159,718
- Last updated1998-12-15 v3
- Checksum4D424C3C99DA4AF4
P04412-2
- NameType II
- Differences from canonical
- 1-101: MLLRRRNGPCPFPLLLLLLAHCICIWPASAARDRYARQNNRQRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKI → MMIISMWMSISRGLWDSSSILSVLLILACMASITTSSSVSNAGYVDNGNMKV
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q8MLW0 | Q8MLW0_DROME | Egfr | 1377 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002897 | 1-101 | in isoform Type II | |||
Sequence: MLLRRRNGPCPFPLLLLLLAHCICIWPASAARDRYARQNNRQRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKI → MMIISMWMSISRGLWDSSSILSVLLILACMASITTSSSVSNAGYVDNGNMKV | ||||||
Sequence conflict | 137 | in Ref. 5 and 6 | ||||
Sequence: K → E | ||||||
Sequence conflict | 329-331 | in Ref. 5 and 6 | ||||
Sequence: AVS → GVC | ||||||
Sequence conflict | 458 | in Ref. 5 and 6 | ||||
Sequence: R → L | ||||||
Sequence conflict | 789 | in Ref. 5 and 6 | ||||
Sequence: R → C | ||||||
Sequence conflict | 959 | in Ref. 8; CAA26157 | ||||
Sequence: P → A | ||||||
Sequence conflict | 995 | in Ref. 5 and 6 | ||||
Sequence: E → V | ||||||
Sequence conflict | 1072-1080 | in Ref. 3, 4 and 9 | ||||
Sequence: QTPSLVKIT → RLLAGEDH | ||||||
Sequence conflict | 1097-1098 | in Ref. 9; CAA05747 | ||||
Sequence: AA → I | ||||||
Sequence conflict | 1118 | in Ref. 9; CAA05747 | ||||
Sequence: T → R | ||||||
Sequence conflict | 1242 | in Ref. 5 and 6 | ||||
Sequence: K → E | ||||||
Sequence conflict | 1265 | in Ref. 5 and 6 | ||||
Sequence: M → I | ||||||
Compositional bias | 1279-1293 | Basic and acidic residues | ||||
Sequence: NSSTGDDERDSSARE | ||||||
Sequence conflict | 1287 | in Ref. 5 and 6 | ||||
Sequence: R → T | ||||||
Sequence conflict | 1325 | in Ref. 6; AAF46732 | ||||
Sequence: M → I | ||||||
Sequence conflict | 1383 | in Ref. 5 and 6 | ||||
Sequence: G → V | ||||||
Sequence conflict | 1412-1426 | in Ref. 3 and 4 | ||||
Sequence: ELQPLHRNRNTETRV → SCSHASKPQHGDEGVGSSRVGAIANEEGESCQVPLEAMRYAFAGCYLR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF052754 EMBL· GenBank· DDBJ | AAC08536.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF052753 EMBL· GenBank· DDBJ | AAC08536.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF052754 EMBL· GenBank· DDBJ | AAC08535.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF052752 EMBL· GenBank· DDBJ | AAC08535.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K03054 EMBL· GenBank· DDBJ | AAA51462.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K03417 EMBL· GenBank· DDBJ | AAA51460.1 EMBL· GenBank· DDBJ | mRNA | ||
K03416 EMBL· GenBank· DDBJ | AAA50965.1 EMBL· GenBank· DDBJ | mRNA | ||
AF109077 EMBL· GenBank· DDBJ | AAD26134.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109078 EMBL· GenBank· DDBJ | AAD26132.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109082 EMBL· GenBank· DDBJ | AAD26132.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109078 EMBL· GenBank· DDBJ | AAD26133.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109084 EMBL· GenBank· DDBJ | AAD26133.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109079 EMBL· GenBank· DDBJ | AAD26130.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109081 EMBL· GenBank· DDBJ | AAD26130.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109079 EMBL· GenBank· DDBJ | AAD26131.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109083 EMBL· GenBank· DDBJ | AAD26131.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF109080 EMBL· GenBank· DDBJ | AAD26135.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF46732.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X02293 EMBL· GenBank· DDBJ | CAA26157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ002912 EMBL· GenBank· DDBJ | CAA05747.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X78920 EMBL· GenBank· DDBJ | CAA55523.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X78918 EMBL· GenBank· DDBJ | CAA55521.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X78919 EMBL· GenBank· DDBJ | CAA55522.1 EMBL· GenBank· DDBJ | Genomic DNA |