P09619 · PGFRB_HUMAN
- ProteinPlatelet-derived growth factor receptor beta
- GenePDGFRB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1106 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Activity regulation
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 527-528 | Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein | ||||
Sequence: SL | ||||||
Site | 527-528 | Breakpoint for translocation to form TRIP11-PDGFRB | ||||
Sequence: SL | ||||||
Site | 558-559 | Breakpoint for translocation to form the CEP85L-PDGFRB fusion protein | ||||
Sequence: KK | ||||||
Binding site | 606-614 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGSGAFGQV | ||||||
Binding site | 634 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 826 | Proton acceptor | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePlatelet-derived growth factor receptor beta
- EC number
- Short namesPDGF-R-beta; PDGFR-beta
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP09619
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 33-532 | Extracellular | ||||
Sequence: LVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGTLQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVVPHSLPFKV | ||||||
Transmembrane | 533-553 | Helical | ||||
Sequence: VVISAILALVVLTIISLIILI | ||||||
Topological domain | 554-1106 | Cytoplasmic | ||||
Sequence: MLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Myeloproliferative disorder chronic with eosinophilia (MPE)
- Note
- DescriptionA hematologic disorder characterized by malignant eosinophils proliferation.
- See alsoMIM:131440
Leukemia, acute myelogenous (AML)
- Note
- DescriptionA subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.
- See alsoMIM:601626
Leukemia, juvenile myelomonocytic (JMML)
- Note
- DescriptionAn aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages.
- See alsoMIM:607785
Basal ganglia calcification, idiopathic, 4 (IBGC4)
- Note
- DescriptionA form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas.
- See alsoMIM:615007
Natural variants in IBGC4
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_069320 | 658 | L>P | in IBGC4; no effect on protein abundance; loss of PDGF beta receptor activity; dbSNP:rs397509381 | |
VAR_069321 | 987 | R>W | in IBGC4; decreased protein abundance; no effect on receptor activity; decreased PDGF signaling pathway; dbSNP:rs397509382 | |
VAR_075395 | 1071 | E>V | in IBGC4; no effect on protein abundance; no effect on receptor activity; decreased PDGF signaling pathway |
Myofibromatosis, infantile 1 (IMF1)
- Note
- DescriptionA rare mesenchymal disorder characterized by the development of benign tumors in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about half of the patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life. Visceral lesions are associated with high morbidity and mortality.
- See alsoMIM:228550
Natural variants in IMF1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_069925 | 561 | R>C | in IMF1; dbSNP:rs367543286 | |
VAR_069926 | 660 | P>T | in IMF1; dbSNP:rs144050370 |
Kosaki overgrowth syndrome (KOGS)
- Note
- DescriptionA syndrome characterized by somatic overgrowth, distinctive facial features, hyperelastic and fragile skin, and progressive neurologic deterioration with white matter lesions on brain imaging.
- See alsoMIM:616592
Natural variants in KOGS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_075865 | 584 | P>R | in KOGS; dbSNP:rs863224946 |
Premature aging syndrome, Penttinen type (PENTT)
- Note
- DescriptionA syndrome characterized by a prematurely aged appearance with lipoatrophy, epidermal and dermal atrophy along with hypertrophic lesions that resemble scars, thin hair, proptosis, underdeveloped cheekbones, and marked acro-osteolysis.
- See alsoMIM:601812
Natural variants in PENTT
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_075866 | 665 | V>A | in PENTT; gain of function in protein tyrosine kinase activity; shows ligand-independent constitutive signaling; dbSNP:rs1554108211 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_034377 | 29 | in dbSNP:rs17110944 | |||
Sequence: I → F | ||||||
Natural variant | VAR_035125 | 180 | in dbSNP:rs17853027 | |||
Sequence: S → F | ||||||
Natural variant | VAR_042027 | 282 | in dbSNP:rs34586048 | |||
Sequence: E → K | ||||||
Natural variant | VAR_049717 | 345 | in dbSNP:rs2229558 | |||
Sequence: P → S | ||||||
Natural variant | VAR_042028 | 485 | in dbSNP:rs41287110 | |||
Sequence: E → K | ||||||
Natural variant | VAR_069925 | 561 | in IMF1; dbSNP:rs367543286 | |||
Sequence: R → C | ||||||
Mutagenesis | 579 | Loss of kinase activity; when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 581 | Loss of kinase activity; when associated with F-579. No effect on interaction with GRB10. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_075865 | 584 | in KOGS; dbSNP:rs863224946 | |||
Sequence: P → R | ||||||
Natural variant | VAR_042029 | 589 | in a gastric adenocarcinoma sample; somatic mutation | |||
Sequence: Y → H | ||||||
Mutagenesis | 634 | Loss of kinase activity. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. | ||||
Sequence: K → A or R | ||||||
Natural variant | VAR_069320 | 658 | in IBGC4; no effect on protein abundance; loss of PDGF beta receptor activity; dbSNP:rs397509381 | |||
Sequence: L → P | ||||||
Natural variant | VAR_069926 | 660 | in IMF1; dbSNP:rs144050370 | |||
Sequence: P → T | ||||||
Natural variant | VAR_075866 | 665 | in PENTT; gain of function in protein tyrosine kinase activity; shows ligand-independent constitutive signaling; dbSNP:rs1554108211 | |||
Sequence: V → A | ||||||
Mutagenesis | 716 | No effect neither on interaction with GRB10 and RASA1 nor on phosphatidylinositol 3-kinase activity. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_042030 | 718 | in dbSNP:rs35322465 | |||
Sequence: N → Y | ||||||
Mutagenesis | 740 | Strongly reduces up-regulation of cell proliferation; when associated with F-751. Strongly decreases phosphatidylinositol 3-kinase activity. No effect on interaction with GRB10 and RASA1. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 751 | Strongly reduces up-regulation of cell proliferation; when associated with F-740. Abolishes phosphatidylinositol 3-kinase activity and interaction with NCK1, and slightly reduces interaction with RASA1. No effect on interaction with GRB10. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 763 | No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 771 | Loss of interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 775 | No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 778 | Strongly reduces expression levels. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 857 | Reduces kinase activity. No effect on interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_042031 | 882 | in a breast infiltrating ductal carcinoma sample; somatic mutation | |||
Sequence: T → I | ||||||
Natural variant | VAR_069321 | 987 | in IBGC4; decreased protein abundance; no effect on receptor activity; decreased PDGF signaling pathway; dbSNP:rs397509382 | |||
Sequence: R → W | ||||||
Mutagenesis | 1009 | No effect on interaction with GRB10. Abolishes interaction with PLCG1; when associated with F-1021. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1021 | Strongly reduces up-regulation of cell proliferation. Abolishes interaction with PLCG1; when associated with F-1009. No effect on interaction with GRB10. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_075395 | 1071 | in IBGC4; no effect on protein abundance; no effect on receptor activity; decreased PDGF signaling pathway | |||
Sequence: E → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,005 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-32 | UniProt | |||||
Sequence: MRLPGAMPALALKGELLLLSLLLLLEPQISQG | |||||||
Chain | PRO_0000016757 | 33-1106 | UniProt | Platelet-derived growth factor receptor beta | |||
Sequence: LVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGTLQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVVPHSLPFKVVVISAILALVVLTIISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL | |||||||
Glycosylation | 45 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 54↔100 | UniProt | |||||
Sequence: CSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFC | |||||||
Glycosylation | 89 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 103 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 149↔190 | UniProt | |||||
Sequence: CRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYIC | |||||||
Glycosylation | 215 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 230 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 235↔291 | UniProt | |||||
Sequence: CIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTC | |||||||
Glycosylation | 292 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 307 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 354 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 371 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 436↔508 | UniProt | |||||
Sequence: CRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRC | |||||||
Glycosylation | 468 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 479 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 562 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 579 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 581 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 683 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 686 | UniProt | Phosphotyrosine; by ABL1 and ABL2 | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 712 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 716 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 740 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 748 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 751 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 763 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 771 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 775 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 778 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 857 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 934 | UniProt | Phosphotyrosine; by ABL1 and ABL2 | ||||
Sequence: Y | |||||||
Modified residue | 970 | UniProt | Phosphotyrosine; by ABL1 and ABL2 | ||||
Sequence: Y | |||||||
Modified residue | 1009 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue | 1021 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-120 | Ig-like C2-type 1 | ||||
Sequence: LVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFV | ||||||
Domain | 129-210 | Ig-like C2-type 2 | ||||
Sequence: PNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQ | ||||||
Domain | 214-309 | Ig-like C2-type 3 | ||||
Sequence: INVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINIT | ||||||
Domain | 331-403 | Ig-like C2-type 4 | ||||
Sequence: HRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDA | ||||||
Domain | 416-524 | Ig-like C2-type 5 | ||||
Sequence: PVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVV | ||||||
Domain | 600-962 | Protein kinase | ||||
Sequence: LVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLL | ||||||
Region | 1019-1106 | Disordered | ||||
Sequence: NDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL | ||||||
Compositional bias | 1041-1063 | Polar residues | ||||
Sequence: SPSLASSTLNEVNTSSTISCDSP | ||||||
Compositional bias | 1066-1080 | Acidic residues | ||||
Sequence: PQDEPEPEPQLELQV |
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.
P09619-1
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
- Length1,106
- Mass (Da)123,968
- Last updated1989-07-01 v1
- Checksum038C15E531D6E89D
P09619-2
- Name2
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 241 | in Ref. 2; AAA36427 | ||||
Sequence: E → D | ||||||
Alternative sequence | VSP_056008 | 311-336 | in isoform 2 | |||
Sequence: VESGYVRLLGEVGTLQFAELHRSRTL → RAATCGSWERWAHYNLLSCIGAGHCR | ||||||
Alternative sequence | VSP_056009 | 337-1106 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1041-1063 | Polar residues | ||||
Sequence: SPSLASSTLNEVNTSSTISCDSP | ||||||
Compositional bias | 1066-1080 | Acidic residues | ||||
Sequence: PQDEPEPEPQLELQV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J03278 EMBL· GenBank· DDBJ | AAA60049.1 EMBL· GenBank· DDBJ | mRNA | ||
M21616 EMBL· GenBank· DDBJ | AAA36427.1 EMBL· GenBank· DDBJ | mRNA | ||
EU826595 EMBL· GenBank· DDBJ | ACF47631.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005895 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC011382 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC032224 EMBL· GenBank· DDBJ | AAH32224.1 EMBL· GenBank· DDBJ | mRNA | ||
U33172 EMBL· GenBank· DDBJ | AAC51675.1 EMBL· GenBank· DDBJ | Genomic DNA |