Q13873 · BMPR2_HUMAN
- ProteinBone morphogenetic protein receptor type-2
- GeneBMPR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1038 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6
Catalytic activity
- ATP + L-threonyl-[receptor-protein] = ADP + H+ + O-phospho-L-threonyl-[receptor-protein]
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 209-217 | ATP (UniProtKB | ChEBI) | ||||
Sequence: IGRGRYGAV | ||||||
Binding site | 230 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 280-282 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EYY | ||||||
Active site | 333 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 337-338 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RN | ||||||
Binding site | 351 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBone morphogenetic protein receptor type-2
- EC number
- Short namesBMP type-2 receptor; BMPR-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13873
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 27-150 | Extracellular | ||||
Sequence: SQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDET | ||||||
Transmembrane | 151-171 | Helical | ||||
Sequence: IIIALASVSVLAVLIVALCFG | ||||||
Topological domain | 172-1038 | Cytoplasmic | ||||
Sequence: YRMLTGDRKQGLHSMNMMEAAASEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGTCVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEIFMRCTDLFPGESVPEYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGMTTISEMPYPDETNLHTTNVAQSIGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEATGQQDFTQTANGQACLIPDVLPTQIYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGSKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRNHSVNSHAATTQYANGTVLSGQTTNIVTHRAQEMLQNQFIGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDVLAQGVPSTAADPGPSKPRRAQRPNSLDLSATNVLDGSSIQIGESTQDGKSGSGEKIKKRVKTPYSLKRWRPSTWVISTESLDCEVNNNGSNRAVHSKSSTAVYLAEGGTATTMVSKDIGMNCL |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Pulmonary hypertension, primary, 1 (PPH1)
- Note
- DescriptionA rare disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs.
- See alsoMIM:178600
Natural variants in PPH1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_013670 | 60 | C>Y | in PPH1; loss of function in BMP signaling pathway via SMAD proteins activation; does not localize to the cell surface; when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade; dbSNP:rs1085307172 | |
VAR_079588 | 64 | S>R | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_073041 | 67 | Y>C | in PPH1; significant decrease in nitric oxide synthesis by endothelial cells; dbSNP:rs1085307177 | |
VAR_079589 | 77 | I>L | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_033109 | 82 | Q>H | in PPH1; dbSNP:rs1085307185 | |
VAR_079590 | 84 | C>F | in PPH1; alters alternative splicing of BMPR2; dbSNP:rs1085307197 | |
VAR_079591 | 87 | H>Y | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_079592 | 92 | Q>L | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_079593 | 109 | Q>H | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_013671 | 117 | C>Y | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs1085307215 | |
VAR_013672 | 118 | C>W | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs137852743 | |
VAR_013673 | 123 | C>R | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs137852750 | |
VAR_013674 | 123 | C>S | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs137852750 | |
VAR_079594 | 138 | P>A | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_079595 | 162 | A>P | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_033110 | 182 | G>D | in PPH1; dbSNP:rs137852754 | |
VAR_079596 | 218-1038 | missing | in PPH1; changed localization to the plasma membrane | |
VAR_079597 | 248 | R>G | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_079598 | 264 | D>N | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_079599 | 298-1038 | missing | in PPH1; loss of localization to the plasma membrane; localized to the cytoplasm | |
VAR_079600 | 341 | V>M | in PPH1; uncertain significance; unchanged subcellular localization; dbSNP:rs767882551 | |
VAR_013676 | 347 | C>Y | in PPH1; does not localize to the cell surface; dbSNP:rs137852744 | |
VAR_013677 | 420 | C>R | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs1085307324 | |
VAR_079601 | 467 | K>R | in PPH1; uncertain significance; unchanged subcellular localization | |
VAR_013678 | 483 | C>R | in PPH1; sporadic; loss of function in BMP signaling pathway via SMAD proteins activation; does not localize to the cell surface; when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade; dbSNP:rs1085307354 | |
VAR_013679 | 485 | D>G | in PPH1; complete loss of function; no effect on localization to the cell surface; no effect on BMP4 binding; dbSNP:rs137852745 | |
VAR_013680 | 491 | R>Q | in PPH1; sporadic; no effect on localization to the cell surface; dbSNP:rs137852749 | |
VAR_013681 | 491 | R>W | in PPH1; loss of function in BMP signaling pathway via SMAD proteins activation; no effect on localization to the cell surface; no effect on BMP4 binding; when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade; dbSNP:rs137852746 | |
VAR_013682 | 512 | K>T | in PPH1; no effect on localization to the cell surface; no effect on BMP4 binding; when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade; dbSNP:rs1085307364 | |
VAR_013683 | 519 | N>K | in PPH1; no effect on localization to the cell surface; dbSNP:rs1085307365 | |
VAR_073042 | 863 | S>N | in PPH1; abnormal subcellular localization; significant increase in apoptosis of endothelial cells; significant decrease in proliferation of endothelial cells; significant decrease in nitric oxide synthesis by endothelial cells; significant increase in endothelin 1 synthesis by endothelial cells; dbSNP:rs1006246556 | |
VAR_033111 | 899 | R>P | in PPH1; leads to constitutive activation of the MAPK14 pathway; dbSNP:rs137852752 |
Pulmonary venoocclusive disease 1, autosomal dominant (PVOD1)
- Note
- DescriptionA disease characterized by widespread fibrous obstruction and intimal thickening of septal veins and preseptal venules, a low diffusing capacity for carbon monoxide, occult alveolar hemorrhage, and nodular ground-glass opacities, septal lines and lymph node enlargement showed by high-resolution computed tomography of the chest. It is frequently associated with pulmonary capillary dilatation and proliferation, and is a rare and devastating cause of pulmonary hypertension.
- See alsoMIM:265450
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_013670 | 60 | in PPH1; loss of function in BMP signaling pathway via SMAD proteins activation; does not localize to the cell surface; when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade; dbSNP:rs1085307172 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_079588 | 64 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: S → R | ||||||
Natural variant | VAR_073041 | 67 | in PPH1; significant decrease in nitric oxide synthesis by endothelial cells; dbSNP:rs1085307177 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_079589 | 77 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: I → L | ||||||
Natural variant | VAR_033109 | 82 | in PPH1; dbSNP:rs1085307185 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_079590 | 84 | in PPH1; alters alternative splicing of BMPR2; dbSNP:rs1085307197 | |||
Sequence: C → F | ||||||
Natural variant | VAR_079591 | 87 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: H → Y | ||||||
Natural variant | VAR_079592 | 92 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: Q → L | ||||||
Natural variant | VAR_079593 | 109 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: Q → H | ||||||
Natural variant | VAR_013671 | 117 | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs1085307215 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_013672 | 118 | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs137852743 | |||
Sequence: C → W | ||||||
Natural variant | VAR_013673 | 123 | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs137852750 | |||
Sequence: C → R | ||||||
Natural variant | VAR_013674 | 123 | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs137852750 | |||
Sequence: C → S | ||||||
Natural variant | VAR_079594 | 138 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: P → A | ||||||
Natural variant | VAR_079595 | 162 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: A → P | ||||||
Natural variant | VAR_033110 | 182 | in PPH1; dbSNP:rs137852754 | |||
Sequence: G → D | ||||||
Natural variant | VAR_079596 | 218-1038 | in PPH1; changed localization to the plasma membrane | |||
Sequence: Missing | ||||||
Natural variant | VAR_013675 | 224 | in dbSNP:rs754343081 | |||
Sequence: E → D | ||||||
Natural variant | VAR_079597 | 248 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: R → G | ||||||
Natural variant | VAR_079598 | 264 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: D → N | ||||||
Natural variant | VAR_079599 | 298-1038 | in PPH1; loss of localization to the plasma membrane; localized to the cytoplasm | |||
Sequence: Missing | ||||||
Natural variant | VAR_079600 | 341 | in PPH1; uncertain significance; unchanged subcellular localization; dbSNP:rs767882551 | |||
Sequence: V → M | ||||||
Natural variant | VAR_013676 | 347 | in PPH1; does not localize to the cell surface; dbSNP:rs137852744 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_013677 | 420 | in PPH1; loss of function in BMP signaling pathway; does not localize to the cell surface; dbSNP:rs1085307324 | |||
Sequence: C → R | ||||||
Natural variant | VAR_079601 | 467 | in PPH1; uncertain significance; unchanged subcellular localization | |||
Sequence: K → R | ||||||
Natural variant | VAR_013678 | 483 | in PPH1; sporadic; loss of function in BMP signaling pathway via SMAD proteins activation; does not localize to the cell surface; when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade; dbSNP:rs1085307354 | |||
Sequence: C → R | ||||||
Natural variant | VAR_013679 | 485 | in PPH1; complete loss of function; no effect on localization to the cell surface; no effect on BMP4 binding; dbSNP:rs137852745 | |||
Sequence: D → G | ||||||
Natural variant | VAR_013680 | 491 | in PPH1; sporadic; no effect on localization to the cell surface; dbSNP:rs137852749 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_013681 | 491 | in PPH1; loss of function in BMP signaling pathway via SMAD proteins activation; no effect on localization to the cell surface; no effect on BMP4 binding; when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade; dbSNP:rs137852746 | |||
Sequence: R → W | ||||||
Natural variant | VAR_013682 | 512 | in PPH1; no effect on localization to the cell surface; no effect on BMP4 binding; when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade; dbSNP:rs1085307364 | |||
Sequence: K → T | ||||||
Natural variant | VAR_013683 | 519 | in PPH1; no effect on localization to the cell surface; dbSNP:rs1085307365 | |||
Sequence: N → K | ||||||
Natural variant | VAR_019996 | 775 | unchanged subcellular localization; dbSNP:rs2228545 | |||
Sequence: S → N | ||||||
Natural variant | VAR_073042 | 863 | in PPH1; abnormal subcellular localization; significant increase in apoptosis of endothelial cells; significant decrease in proliferation of endothelial cells; significant decrease in nitric oxide synthesis by endothelial cells; significant increase in endothelin 1 synthesis by endothelial cells; dbSNP:rs1006246556 | |||
Sequence: S → N | ||||||
Natural variant | VAR_033111 | 899 | in PPH1; leads to constitutive activation of the MAPK14 pathway; dbSNP:rs137852752 | |||
Sequence: R → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,347 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, disulfide bond, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-26 | UniProt | |||||
Sequence: MTSSLQRPWRVPWLPWTILLVSTAAA | |||||||
Chain | PRO_0000024415 | 27-1038 | UniProt | Bone morphogenetic protein receptor type-2 | |||
Sequence: SQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDETIIIALASVSVLAVLIVALCFGYRMLTGDRKQGLHSMNMMEAAASEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGTCVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEIFMRCTDLFPGESVPEYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGMTTISEMPYPDETNLHTTNVAQSIGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEATGQQDFTQTANGQACLIPDVLPTQIYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGSKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRNHSVNSHAATTQYANGTVLSGQTTNIVTHRAQEMLQNQFIGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDVLAQGVPSTAADPGPSKPRRAQRPNSLDLSATNVLDGSSIQIGESTQDGKSGSGEKIKKRVKTPYSLKRWRPSTWVISTESLDCEVNNNGSNRAVHSKSSTAVYLAEGGTATTMVSKDIGMNCL | |||||||
Disulfide bond | 34↔66 | UniProt | |||||
Sequence: CAFKDPYQQDLGIGESRISHENGTILCSKGSTC | |||||||
Glycosylation | 55 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 60↔84 | UniProt | |||||
Sequence: CSKGSTCYGLWEKSKGDINLVKQGC | |||||||
Disulfide bond | 94↔117 | UniProt | |||||
Sequence: CHYEECVVTTTPPSIQNGTYRFCC | |||||||
Disulfide bond | 99↔116 | UniProt | |||||
Sequence: CVVTTTPPSIQNGTYRFC | |||||||
Glycosylation | 110 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 118↔123 | UniProt | |||||
Sequence: CSTDLC | |||||||
Glycosylation | 126 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 379 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 586 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 586 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 680 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 680 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 681 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 681 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 708 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 757 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 765 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 818 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 862 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 863 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 940 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with BMP4 (PubMed:29212066).
Interacts with SCUBE3 (PubMed:33308444).
Interacts with TSC22D1/TSC-22 (PubMed:21791611).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q13873 | C4bpa P08607 | 3 | EBI-527196, EBI-527325 | |
BINARY | Q13873 | GDF5 P43026 | 4 | EBI-527196, EBI-8571476 | |
XENO | Q13873 | Prkcb P68404 | 4 | EBI-527196, EBI-397048 | |
BINARY | Q13873 | PRKG1 Q13976 | 2 | EBI-527196, EBI-3952014 | |
BINARY | Q13873 | YWHAE P62258 | 2 | EBI-527196, EBI-356498 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 203-504 | Protein kinase | ||||
Sequence: LKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGTCVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEIFMRCTDLFPGESVPEYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAEL | ||||||
Region | 593-626 | Disordered | ||||
Sequence: QAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGM | ||||||
Compositional bias | 746-768 | Polar residues | ||||
Sequence: PKQQNLPKRPTSLPLNTKNSTKE | ||||||
Region | 746-770 | Disordered | ||||
Sequence: PKQQNLPKRPTSLPLNTKNSTKEPR | ||||||
Compositional bias | 872-897 | Basic and acidic residues | ||||
Sequence: RREQQAGHDEGVLDRLVDRRERPLEG | ||||||
Region | 872-972 | Disordered | ||||
Sequence: RREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDVLAQGVPSTAADPGPSKPRRAQRPNSLDLSATNVLDGSSIQIGESTQDGKSGSGEKIK | ||||||
Compositional bias | 898-918 | Polar residues | ||||
Sequence: GRTNSNNNNSNPCSEQDVLAQ | ||||||
Compositional bias | 937-964 | Polar residues | ||||
Sequence: RPNSLDLSATNVLDGSSIQIGESTQDGK |
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.
Q13873-1
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
- Length1,038
- Mass (Da)115,201
- Last updated2000-12-01 v2
- Checksum1389923CE574B913
Q13873-2
- Name2
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054441 | 530 | in isoform 2 | |||
Sequence: N → R | ||||||
Alternative sequence | VSP_054442 | 531-1038 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 746-768 | Polar residues | ||||
Sequence: PKQQNLPKRPTSLPLNTKNSTKE | ||||||
Sequence conflict | 828 | in Ref. 2; CAA88759 | ||||
Sequence: G → R | ||||||
Compositional bias | 872-897 | Basic and acidic residues | ||||
Sequence: RREQQAGHDEGVLDRLVDRRERPLEG | ||||||
Compositional bias | 898-918 | Polar residues | ||||
Sequence: GRTNSNNNNSNPCSEQDVLAQ | ||||||
Compositional bias | 937-964 | Polar residues | ||||
Sequence: RPNSLDLSATNVLDGSSIQIGESTQDGK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U25110 EMBL· GenBank· DDBJ | AAA86519.1 EMBL· GenBank· DDBJ | mRNA | ||
Z48923 EMBL· GenBank· DDBJ | CAA88759.1 EMBL· GenBank· DDBJ | mRNA | ||
D50516 EMBL· GenBank· DDBJ | BAA09094.1 EMBL· GenBank· DDBJ | mRNA | ||
U20165 EMBL· GenBank· DDBJ | AAC50105.1 EMBL· GenBank· DDBJ | mRNA | ||
AC009960 EMBL· GenBank· DDBJ | AAX76517.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC073410 EMBL· GenBank· DDBJ | AAX88941.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC064836 EMBL· GenBank· DDBJ | AAY24146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471063 EMBL· GenBank· DDBJ | EAW70309.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC052985 EMBL· GenBank· DDBJ | AAH52985.1 EMBL· GenBank· DDBJ | mRNA |