Q9H201 · EPN3_HUMAN
- ProteinEpsin-3
- GeneEPN3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids632 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 8 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
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
Aspect | Term | |
---|---|---|
Cellular Component | clathrin vesicle coat | |
Cellular Component | clathrin-coated pit | |
Cellular Component | clathrin-coated vesicle | |
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | endosome | |
Cellular Component | extracellular exosome | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | clathrin binding | |
Molecular Function | EH domain binding | |
Molecular Function | phospholipid binding | |
Biological Process | endocytosis |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEpsin-3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H201
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_059973 | 544 | in dbSNP:rs4794159 | |||
Sequence: P → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 852 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000074519 | 1-632 | UniProt | Epsin-3 | |||
Sequence: MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGIGIGSGQLGFSRRYGEDYSRSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEELQLQLALAMSREEAEKPVPPASHRDEDLQLQLALRLSRQEHEKEVRSWQGDGSPMANGAGAVVHHQRDREPEREERKEEEKLKTSQSSILDLADIFVPALAPPSTHCSADPWDIPGFRPNTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPWGASLETSDTPGGASTFDPFAKPPESTETKEGLEQALPSGKPSSPVELDLFGDPSPSSKQNGTKEPDALDLGILGEALTQPSKEARACRTPESFLGPSASSLVNLDSLVKAPQVAKTRNPFLTGLSAPSPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPLPLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNPFL | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 163 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 191 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 192 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 264 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 264 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 393 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 449 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 495 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-144 | ENTH | ||||
Sequence: NIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQER | ||||||
Region | 172-214 | Disordered | ||||
Sequence: YGEDYSRSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEELQL | ||||||
Compositional bias | 178-212 | Polar residues | ||||
Sequence: RSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEEL | ||||||
Domain | 209-228 | UIM 1 | ||||
Sequence: EEELQLQLALAMSREEAEKP | ||||||
Domain | 236-255 | UIM 2 | ||||
Sequence: DEDLQLQLALRLSRQEHEKE | ||||||
Region | 257-296 | Disordered | ||||
Sequence: RSWQGDGSPMANGAGAVVHHQRDREPEREERKEEEKLKTS | ||||||
Compositional bias | 274-296 | Basic and acidic residues | ||||
Sequence: VHHQRDREPEREERKEEEKLKTS | ||||||
Repeat | 321-323 | 1 | ||||
Sequence: DPW | ||||||
Region | 321-406 | 5 X 3 AA repeats of [DE]-P-W | ||||
Sequence: DPWDIPGFRPNTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPW | ||||||
Region | 326-501 | Disordered | ||||
Sequence: PGFRPNTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPWGASLETSDTPGGASTFDPFAKPPESTETKEGLEQALPSGKPSSPVELDLFGDPSPSSKQNGTKEPDALDLGILGEALTQPSKEARACRTPESFLG | ||||||
Compositional bias | 331-371 | Polar residues | ||||
Sequence: NTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSE | ||||||
Repeat | 344-346 | 2 | ||||
Sequence: DPW | ||||||
Repeat | 371-373 | 3 | ||||
Sequence: EPW | ||||||
Repeat | 387-389 | 4 | ||||
Sequence: DPW | ||||||
Repeat | 404-406 | 5 | ||||
Sequence: DPW | ||||||
Repeat | 524-526 | 1 | ||||
Sequence: NPF | ||||||
Region | 524-631 | 3 X 3 AA repeats of N-P-F | ||||
Sequence: NPFLTGLSAPSPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPLPLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNPF | ||||||
Region | 525-560 | Disordered | ||||
Sequence: PFLTGLSAPSPTNPFGAGEPGRPTLNQMRTGSPALG | ||||||
Repeat | 537-539 | 2 | ||||
Sequence: NPF | ||||||
Region | 604-632 | Disordered | ||||
Sequence: AFAPQPLLPTPSSAGPRPPPPQTGTNPFL | ||||||
Compositional bias | 612-632 | Pro residues | ||||
Sequence: PTPSSAGPRPPPPQTGTNPFL | ||||||
Repeat | 629-631 | 3 | ||||
Sequence: NPF |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9H201-1
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
- Length632
- Mass (Da)68,222
- Last updated2001-03-01 v1
- Checksum13940F2FBD6215D0
Q9H201-2
- Name2
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 178-212 | Polar residues | ||||
Sequence: RSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEEL | ||||||
Alternative sequence | VSP_009158 | 188-208 | in isoform 2 | |||
Sequence: SSSSSPRYTSDLEQARPQTSG → CPASDVRGRGTAAAAGPRHEP | ||||||
Alternative sequence | VSP_009159 | 209-632 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 274-296 | Basic and acidic residues | ||||
Sequence: VHHQRDREPEREERKEEEKLKTS | ||||||
Compositional bias | 331-371 | Polar residues | ||||
Sequence: NTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSE | ||||||
Sequence conflict | 375 | in Ref. 2; BAF85666 | ||||
Sequence: R → K | ||||||
Sequence conflict | 396 | in Ref. 2; BAA91378 | ||||
Sequence: H → Y | ||||||
Sequence conflict | 417 | in Ref. 2; BAF85666 | ||||
Sequence: G → S | ||||||
Compositional bias | 612-632 | Pro residues | ||||
Sequence: PTPSSAGPRPPPPQTGTNPFL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF324241 EMBL· GenBank· DDBJ | AAG45223.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000785 EMBL· GenBank· DDBJ | BAA91378.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291658 EMBL· GenBank· DDBJ | BAF84347.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292977 EMBL· GenBank· DDBJ | BAF85666.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94607.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001038 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC051365 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC077722 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |