Q96D09 · GASP2_HUMAN
- ProteinG-protein coupled receptor-associated sorting protein 2
- GeneGPRASP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids838 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May play a role in regulation of a variety of G-protein coupled receptors.
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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | amyloid-beta binding | |
Molecular Function | G protein-coupled receptor binding | |
Biological Process | hematopoietic stem cell homeostasis |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameG-protein coupled receptor-associated sorting protein 2
- Short namesGASP-2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96D09
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Deafness, X-linked, 7 (DFNX7)
- Note
- DescriptionA congenital form of bilateral mixed or conductive hearing loss, which is progressive in some patients. Additional clinical features include ear anomalies and facial dysmorphism with bilateral ptosis.
- See alsoMIM:301018
Natural variants in DFNX7
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081645 | 573 | A>N | in DFNX7; requires 2 nucleotide substitutions |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_049265 | 173 | in dbSNP:rs6616421 | |||
Sequence: R → S | ||||||
Natural variant | VAR_081645 | 573 | in DFNX7; requires 2 nucleotide substitutions | |||
Sequence: A → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 835 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000239053 | 1-838 | UniProt | G-protein coupled receptor-associated sorting protein 2 | |||
Sequence: MTGAEIEPSAQAKPEKKAGEEVIAGPERENDVPLVVRPKVRTQATTGARPKTETKSVPAARPKTEAQAMSGARPKTEVQVMGGARPKTEAQGITGARPKTDARAVGGARSKTDAKAIPGARPKDEAQAWAQSEFGTEAVSQAEGVSQTNAVAWPLATAESGSVTKSKGLSMDRELVNVDAETFPGTQGQKGIQPWFGPGEETNMGSWCYSRPRAREEASNESGFWSADETSTASSFWTGEETSVRSWPREESNTRSRHRAKHQTNPRSRPRSKQEAYVDSWSGSEDEASNPFSFWVGENTNNLFRPRVREEANIRSKLRTNREDCFESESEDEFYKQSWVLPGEEANSRFRHRDKEDPNTALKLRAQKDVDSDRVKQEPRFEEEVIIGSWFWAEKEASLEGGASAICESEPGTEEGAIGGSAYWAEEKSSLGAVAREEAKPESEEEAIFGSWFWDRDEACFDLNPCPVYKVSDRFRDAAEELNASSRPQTWDEVTVEFKPGLFHGVGFRSTSPFGIPEEASEMLEAKPKNLELSPEGEEQESLLQPDQPSPEFTFQYDPSYRSVREIREHLRARESAESESWSCSCIQCELKIGSEEFEEFLLLMDKIRDPFIHEISKIAMGMRSASQFTRDFIRDSGVVSLIETLLNYPSSRVRTSFLENMIHMAPPYPNLNMIETFICQVCEETLAHSVDSLEQLTGIRMLRHLTMTIDYHTLIANYMSGFLSLLTTANARTKFHVLKMLLNLSENPAVAKKLFSAKALSIFVGLFNIEETNDNIQIVIKMFQNISNIIKSGKMSLIDDDFSLEPLISAFREFEELAKQLQAQIDNQNDPEVGQQS | |||||||
Modified residue | 282 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 282 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 284 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 284 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 512 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 550 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with cytoplasmic tails of a variety of G-protein coupled receptors such as muscarinic acetylcholine receptor M1/CHRM1 and calcitonin receptor/CALCR.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-122 | Disordered | ||||
Sequence: MTGAEIEPSAQAKPEKKAGEEVIAGPERENDVPLVVRPKVRTQATTGARPKTETKSVPAARPKTEAQAMSGARPKTEVQVMGGARPKTEAQGITGARPKTDARAVGGARSKTDAKAIPGARP | ||||||
Compositional bias | 10-35 | Basic and acidic residues | ||||
Sequence: AQAKPEKKAGEEVIAGPERENDVPLV | ||||||
Region | 218-292 | Disordered | ||||
Sequence: ASNESGFWSADETSTASSFWTGEETSVRSWPREESNTRSRHRAKHQTNPRSRPRSKQEAYVDSWSGSEDEASNPF | ||||||
Compositional bias | 223-242 | Polar residues | ||||
Sequence: GFWSADETSTASSFWTGEET | ||||||
Compositional bias | 244-258 | Basic and acidic residues | ||||
Sequence: VRSWPREESNTRSRH | ||||||
Compositional bias | 275-292 | Polar residues | ||||
Sequence: EAYVDSWSGSEDEASNPF | ||||||
Region | 349-368 | Disordered | ||||
Sequence: RFRHRDKEDPNTALKLRAQK | ||||||
Region | 531-552 | Disordered | ||||
Sequence: LELSPEGEEQESLLQPDQPSPE |
Sequence similarities
Belongs to the GPRASP family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length838
- Mass (Da)93,773
- Last updated2001-12-01 v1
- Checksum2D30515916B7EACE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 10-35 | Basic and acidic residues | ||||
Sequence: AQAKPEKKAGEEVIAGPERENDVPLV | ||||||
Compositional bias | 223-242 | Polar residues | ||||
Sequence: GFWSADETSTASSFWTGEET | ||||||
Compositional bias | 244-258 | Basic and acidic residues | ||||
Sequence: VRSWPREESNTRSRH | ||||||
Compositional bias | 275-292 | Polar residues | ||||
Sequence: EAYVDSWSGSEDEASNPF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL035427 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471190 EMBL· GenBank· DDBJ | EAW54727.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471190 EMBL· GenBank· DDBJ | EAW54728.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471190 EMBL· GenBank· DDBJ | EAW54729.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC013576 EMBL· GenBank· DDBJ | AAH13576.1 EMBL· GenBank· DDBJ | mRNA | ||
BC036772 EMBL· GenBank· DDBJ | AAH36772.1 EMBL· GenBank· DDBJ | mRNA | ||
AK092981 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |