Q80VP1 · EPN1_MOUSE
- ProteinEpsin-1
- GeneEpn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids575 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity).
Regulates receptor-mediated endocytosis (By similarity).
Regulates receptor-mediated endocytosis (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 25 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 30 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 63 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 73 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: H |
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 | clathrin vesicle coat | |
Cellular Component | clathrin-coated pit | |
Cellular Component | cytosol | |
Cellular Component | endosome | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Cellular Component | postsynapse | |
Cellular Component | postsynaptic membrane | |
Cellular Component | presynapse | |
Cellular Component | presynaptic membrane | |
Cellular Component | Schaffer collateral - CA1 synapse | |
Molecular Function | clathrin adaptor activity | |
Molecular Function | clathrin binding | |
Molecular Function | molecular sequestering activity | |
Molecular Function | phospholipid binding | |
Molecular Function | transmembrane transporter binding | |
Biological Process | clathrin coat assembly | |
Biological Process | embryonic organ development | |
Biological Process | endocytosis | |
Biological Process | female pregnancy | |
Biological Process | in utero embryonic development | |
Biological Process | membrane fission | |
Biological Process | negative regulation of sprouting angiogenesis | |
Biological Process | Notch signaling pathway | |
Biological Process | positive regulation of clathrin coat assembly |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEpsin-1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80VP1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000074514 | 1-575 | Epsin-1 | |||
Sequence: MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL | ||||||
Modified residue | 382 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 418 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 419 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 420 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 434 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 446 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 453 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 459 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 463 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 469 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 472 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 493 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 533 | Omega-N-methylarginine | ||||
Sequence: R |
Post-translational modification
Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation.
Ubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Monomer. Binds clathrin and ZBTB16/ZNF145 (By similarity).
Binds ubiquitinated proteins (By similarity).
Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis (By similarity).
Interacts with AP2B1 (By similarity).
Interacts with UBQLN2 (By similarity).
Interacts with ITSN1. Interacts with AP2A1 and AP2A2. Interacts with REPS2; the interaction is direct (By similarity).
Interacts with EPS15; the interaction is direct (By similarity).
Interacts with ENTREP1 (By similarity).
Binds ubiquitinated proteins (By similarity).
Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis (By similarity).
Interacts with AP2B1 (By similarity).
Interacts with UBQLN2 (By similarity).
Interacts with ITSN1. Interacts with AP2A1 and AP2A2. Interacts with REPS2; the interaction is direct (By similarity).
Interacts with EPS15; the interaction is direct (By similarity).
Interacts with ENTREP1 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, repeat, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-144 | ENTH | ||||
Sequence: NIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER | ||||||
Region | 150-186 | Disordered | ||||
Sequence: TKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEEL | ||||||
Domain | 183-202 | UIM 1 | ||||
Sequence: EEELQLQLALAMSKEEADQP | ||||||
Domain | 208-227 | UIM 2 | ||||
Sequence: EDDVQLQLALSLSREEHDKE | ||||||
Domain | 233-252 | UIM 3 | ||||
Sequence: GDDLRLQMAIEESKRETGGK | ||||||
Region | 264-575 | Disordered | ||||
Sequence: FTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL | ||||||
Repeat | 274-276 | 1 | ||||
Sequence: DPW | ||||||
Region | 274-379 | 8 X 3 AA repeats of D-P-W | ||||
Sequence: DPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPW | ||||||
Repeat | 294-296 | 2 | ||||
Sequence: DPW | ||||||
Repeat | 306-308 | 3 | ||||
Sequence: DPW | ||||||
Repeat | 319-321 | 4 | ||||
Sequence: DPW | ||||||
Repeat | 332-334 | 5 | ||||
Sequence: DPW | ||||||
Repeat | 349-351 | 6 | ||||
Sequence: DPW | ||||||
Repeat | 367-369 | 7 | ||||
Sequence: DPW | ||||||
Repeat | 377-379 | 8 | ||||
Sequence: DPW | ||||||
Motif | 401-410 | [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif | ||||
Sequence: DEFSDFDRLR | ||||||
Compositional bias | 455-469 | Pro residues | ||||
Sequence: PPAATPTPTPPTRKT | ||||||
Repeat | 501-503 | 1 | ||||
Sequence: NPF | ||||||
Region | 501-573 | 3 X 3 AA repeats of N-P-F | ||||
Sequence: NPFLPSGAPPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPF | ||||||
Compositional bias | 506-520 | Pro residues | ||||
Sequence: SGAPPTGPSVTNPFQ | ||||||
Repeat | 517-519 | 2 | ||||
Sequence: NPF | ||||||
Compositional bias | 537-575 | Pro residues | ||||
Sequence: VPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL | ||||||
Repeat | 571-573 | 3 | ||||
Sequence: NPF |
Domain
The NPF repeat domain is involved in EPS15 binding.
The DPW repeat domain is involved in AP2A2 and clathrin binding.
The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1.
Sequence similarities
Belongs to the epsin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q80VP1-1
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
- Length575
- Mass (Da)60,212
- Last updated2006-11-28 v3
- Checksum70B8011EB3AE5C4C
Q80VP1-2
- Name2
- Differences from canonical
- 392-392: A → AA
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_009153 | 392 | in isoform 2 | |||
Sequence: A → AA | ||||||
Compositional bias | 455-469 | Pro residues | ||||
Sequence: PPAATPTPTPPTRKT | ||||||
Compositional bias | 506-520 | Pro residues | ||||
Sequence: SGAPPTGPSVTNPFQ | ||||||
Compositional bias | 537-575 | Pro residues | ||||
Sequence: VPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC046962 EMBL· GenBank· DDBJ | AAH46962.2 EMBL· GenBank· DDBJ | mRNA | ||
BC067206 EMBL· GenBank· DDBJ | AAH67206.1 EMBL· GenBank· DDBJ | mRNA | ||
BC099682 EMBL· GenBank· DDBJ | AAH99682.1 EMBL· GenBank· DDBJ | mRNA | ||
AF057285 EMBL· GenBank· DDBJ | AAC97475.1 EMBL· GenBank· DDBJ | mRNA |