O08838 · AMPH_RAT
- ProteinAmphiphysin
- GeneAmph
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids683 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton (By similarity).
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 | axon terminus | |
Cellular Component | cytoskeleton | |
Cellular Component | extrinsic component of synaptic vesicle membrane | |
Cellular Component | glutamatergic synapse | |
Cellular Component | leading edge membrane | |
Cellular Component | photoreceptor ribbon synapse | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic endocytic zone | |
Cellular Component | presynapse | |
Cellular Component | presynaptic endocytic zone | |
Cellular Component | synapse | |
Cellular Component | synaptic vesicle | |
Cellular Component | terminal bouton | |
Molecular Function | phosphatase binding | |
Molecular Function | phospholipid binding | |
Molecular Function | protein-containing complex binding | |
Biological Process | learning | |
Biological Process | positive regulation of endocytosis | |
Biological Process | synaptic vesicle endocytosis |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAmphiphysin
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO08838
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000192949 | 1-683 | Amphiphysin | |||
Sequence: MADIKTGIFAKNVQKRLNRAQEKVLQKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGDQHADKAFSIQGAPSDSGPLRIAKTPSPPEEASPLPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVPPLPKVTPTKELQQENIINFFEDNFVPEINVTTPSQNEVLEVKKEETLLDLDFDPFKPDVTPAGSAAATHSPMSQTLPWDLWTTSTDLVQPASGGSFNDFTQPQDTSLFTMQTDQNMAETEQALPTEPQAEEPPTTAAAPTAGLDLGLEMEEPKEEAAIPPGTDAGETVGTEGSTGEEAEAEKAALPAGEGESPEGAKIDVESTELASSESPQAAELEAGAPQEKVIPSVVIEPASNHEGEEHQETTTGTETREATEDVAPQGPAGEKQELATEPTPLDSQAATPAPAGAVDASLSAGDAAQELPPGFLYKVETLHDFEAANSDELTLQRGDVVLVVPSDSEADQDAGWLVGVKESDWLQYRDLATYKGLFPENFTRHLE | ||||||
Modified residue | 252 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 260 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 262 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 268 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 272 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 276 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 280 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 496 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 626 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Heterodimer with BIN1 (PubMed:9341169).
Binds SH3GLB1 (By similarity).
Interacts with REPS1 and SGIP1 (By similarity).
Binds AP2A2 (PubMed:10380931, PubMed:10430869).
Interacts with AP2B1 (PubMed:16516836, PubMed:16903783).
Interacts with DNM1 and SYNJ1 (PubMed:9341169).
Binds SH3GLB1 (By similarity).
Interacts with REPS1 and SGIP1 (By similarity).
Binds AP2A2 (PubMed:10380931, PubMed:10430869).
Interacts with AP2B1 (PubMed:16516836, PubMed:16903783).
Interacts with DNM1 and SYNJ1 (PubMed:9341169).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O08838 | Bin1 O08839 | 2 | EBI-80080, EBI-80095 | |
BINARY | O08838 | Dnm1 P21575 | 3 | EBI-80080, EBI-80070 | |
BINARY | O08838 | Dnm2 P39052 | 2 | EBI-80080, EBI-349613 | |
XENO | O08838 | Necap1 Q9CR95 | 8 | EBI-80080, EBI-7592476 | |
XENO | O08838 | SRGAP3 O43295 | 3 | EBI-80080, EBI-368166 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil, domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 10-83 | |||||
Sequence: AKNVQKRLNRAQEKVLQKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHE | ||||||
Domain | 24-240 | BAR | ||||
Sequence: VLQKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGDQHAD | ||||||
Coiled coil | 144-191 | |||||
Sequence: DYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNVDLQEEL | ||||||
Region | 244-312 | Disordered | ||||
Sequence: SIQGAPSDSGPLRIAKTPSPPEEASPLPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVPPLPKVTPT | ||||||
Compositional bias | 287-309 | Pro residues | ||||
Sequence: APVRPRSPSQTRKGPPVPPLPKV | ||||||
Region | 421-443 | Disordered | ||||
Sequence: AETEQALPTEPQAEEPPTTAAAP | ||||||
Region | 455-599 | Disordered | ||||
Sequence: EPKEEAAIPPGTDAGETVGTEGSTGEEAEAEKAALPAGEGESPEGAKIDVESTELASSESPQAAELEAGAPQEKVIPSVVIEPASNHEGEEHQETTTGTETREATEDVAPQGPAGEKQELATEPTPLDSQAATPAPAGAVDASLS | ||||||
Compositional bias | 539-555 | Basic and acidic residues | ||||
Sequence: SNHEGEEHQETTTGTET | ||||||
Domain | 610-683 | SH3 | ||||
Sequence: GFLYKVETLHDFEAANSDELTLQRGDVVLVVPSDSEADQDAGWLVGVKESDWLQYRDLATYKGLFPENFTRHLE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length683
- Mass (Da)74,878
- Last updated1997-07-01 v1
- Checksum7FEA4A9E5A1F6631
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2K5Z4 | A0A0G2K5Z4_RAT | Amph | 680 | ||
F1LPP0 | F1LPP0_RAT | Amph | 656 | ||
A0A0G2JX32 | A0A0G2JX32_RAT | Amph | 817 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 287-309 | Pro residues | ||||
Sequence: APVRPRSPSQTRKGPPVPPLPKV | ||||||
Compositional bias | 539-555 | Basic and acidic residues | ||||
Sequence: SNHEGEEHQETTTGTET |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y13381 EMBL· GenBank· DDBJ | CAA73808.1 EMBL· GenBank· DDBJ | mRNA |