Q9H223 · EHD4_HUMAN
- ProteinEH domain-containing protein 4
- GeneEHD4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids541 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 68-75 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GQYSTGKT | ||||||
Binding site | 223 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 261 | ATP (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 492 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 494 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 496 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 498 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 503 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | early endosome | |
Cellular Component | early endosome membrane | |
Cellular Component | endocytic vesicle | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | recycling endosome membrane | |
Molecular Function | ATP binding | |
Molecular Function | cadherin binding | |
Molecular Function | calcium ion binding | |
Molecular Function | GTP binding | |
Molecular Function | nucleic acid binding | |
Biological Process | cellular response to growth factor stimulus | |
Biological Process | cilium assembly | |
Biological Process | endocytic recycling | |
Biological Process | endocytosis | |
Biological Process | pinocytosis | |
Biological Process | positive regulation of peptidyl-tyrosine phosphorylation | |
Biological Process | protein homooligomerization | |
Biological Process | protein localization to plasma membrane | |
Biological Process | regulation of endocytosis |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEH domain-containing protein 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H223
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Early endosome membrane ; Peripheral membrane protein
Recycling endosome membrane ; Peripheral membrane protein
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053070 | 154 | in dbSNP:rs11549015 | |||
Sequence: V → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 562 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 modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000146114 | 1-541 | UniProt | EH domain-containing protein 4 | |||
Sequence: MFSWMGRQAGGRERAGGADAVQTVTGGLRSLYLRKVLPLEEAYRFHEFHSPALEDADFENKPMILLVGQYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMYGETEGSTPGNALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISVIDSPGILSGEKQRISRGYDFCQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVINTPEVLRVYIGSFWAQPLQNTDNRRLFEAEAQDLFRDIQSLPQKAAVRKLNDLIKRARLAKVHAYIISYLKKEMPSVFGKENKKRELISRLPEIYIQLQREYQISAGDFPEVKAMQEQLENYDFTKFHSLKPKLIEAVDNMLSNKISPLMNLISQEETSTPTQLVQGGAFDGTTEGPFNQGYGEGAKEGADEEEWVVAKDKPVYDELFYTLSPINGKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKLDGYELPSSLPPHLVPPSHRKSLPKAD | |||||||
Modified residue (large scale data) | 157 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 162 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 376 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 451 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 459 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 459 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 482 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in pancreas and heart.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homooligomer, and heterooligomer with EHD1, EHD2 and EHD3.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H223 | MICALL1 Q8N3F8 | 2 | EBI-1050573, EBI-1056885 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 58-289 | Dynamin-type G | ||||
Sequence: FENKPMILLVGQYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMYGETEGSTPGNALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISVIDSPGILSGEKQRISRGYDFCQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVINTPEVLRVYIGSFWAQPLQNTDNRRLFEAEAQDLFRDIQSLP | ||||||
Region | 68-75 | G1 motif | ||||
Sequence: GQYSTGKT | ||||||
Region | 94-95 | G2 motif | ||||
Sequence: EP | ||||||
Region | 156-159 | G3 motif | ||||
Sequence: DSPG | ||||||
Region | 222-225 | G4 motif | ||||
Sequence: NKAD | ||||||
Region | 246 | G5 motif | ||||
Sequence: V | ||||||
Domain | 447-535 | EH | ||||
Sequence: DKPVYDELFYTLSPINGKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKLDGYELPSSLPPHLVPPSHRK | ||||||
Domain | 479-514 | EF-hand | ||||
Sequence: LPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIK |
Domain
The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins.
Sequence similarities
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. EHD subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length541
- Mass (Da)61,175
- Last updated2001-03-01 v1
- Checksum72DDE551829B7BF5
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 297 | in Ref. 2; AAG28784 | ||||
Sequence: L → I | ||||||
Sequence conflict | 421-433 | in Ref. 2; AAG28784 | ||||
Sequence: TEGPFNQGYGEGA → PRAPSTRATGRVP | ||||||
Sequence conflict | 439 | in Ref. 2; AAG28784 | ||||
Sequence: E → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF323924 EMBL· GenBank· DDBJ | AAK11599.1 EMBL· GenBank· DDBJ | mRNA | ||
AF307137 EMBL· GenBank· DDBJ | AAG28784.1 EMBL· GenBank· DDBJ | mRNA | ||
AF454953 EMBL· GenBank· DDBJ | AAL51079.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006287 EMBL· GenBank· DDBJ | AAH06287.1 EMBL· GenBank· DDBJ | mRNA | ||
BC051823 EMBL· GenBank· DDBJ | AAH51823.1 EMBL· GenBank· DDBJ | mRNA | ||
AF181265 EMBL· GenBank· DDBJ | AAF40472.1 EMBL· GenBank· DDBJ | mRNA |