Q96RF0 · SNX18_HUMAN
- ProteinSorting nexin-18
- GeneSNX18
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids628 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis (PubMed:18411244, PubMed:20427313, PubMed:21048941, PubMed:22718350).
Required for efficient progress through mitosis and cytokinesis (PubMed:22718350).
Required for normal formation of the cleavage furrow at the end of mitosis (PubMed:22718350).
Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis (PubMed:20427313).
Plays a role in macropinocytosis (PubMed:21048941).
Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation (PubMed:18411244).
Stimulates the GTPase activity of DNM2 (PubMed:20427313).
Promotes DNM2 location at the plasma membrane (PubMed:20427313).
Together with DNM2, involved in autophagosome assembly by regulating trafficking from recycling endosomes of phospholipid scramblase ATG9A (PubMed:29437695).
Required for efficient progress through mitosis and cytokinesis (PubMed:22718350).
Required for normal formation of the cleavage furrow at the end of mitosis (PubMed:22718350).
Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis (PubMed:20427313).
Plays a role in macropinocytosis (PubMed:21048941).
Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation (PubMed:18411244).
Stimulates the GTPase activity of DNM2 (PubMed:20427313).
Promotes DNM2 location at the plasma membrane (PubMed:20427313).
Together with DNM2, involved in autophagosome assembly by regulating trafficking from recycling endosomes of phospholipid scramblase ATG9A (PubMed:29437695).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 312 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 314 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 352 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R |
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 | cytoplasmic side of plasma membrane | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | extracellular exosome | |
Cellular Component | plasma membrane | |
Cellular Component | recycling endosome membrane | |
Molecular Function | phosphatidylinositol binding | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Biological Process | cleavage furrow formation | |
Biological Process | endocytosis | |
Biological Process | endosomal transport | |
Biological Process | mitotic cytokinesis | |
Biological Process | plasma membrane tubulation | |
Biological Process | positive regulation of autophagosome assembly | |
Biological Process | positive regulation of GTPase activity | |
Biological Process | protein transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSorting nexin-18
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96RF0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endomembrane system ; Peripheral membrane protein
Endosome membrane ; Peripheral membrane protein
Recycling endosome membrane ; Peripheral membrane protein
Cell membrane ; Peripheral membrane protein
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Localized at sites of endocytosis at the cell membrane (PubMed:18411244).
Detected on newly formed macropinosomes (PubMed:21048941).
Partially colocalized with clathrin and dynamin at the cell membrane (PubMed:20427313).
Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation (PubMed:18411244).
Detected on newly formed macropinosomes (PubMed:21048941).
Partially colocalized with clathrin and dynamin at the cell membrane (PubMed:20427313).
Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation (PubMed:18411244).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052480 | 571 | in dbSNP:rs2548612 | |||
Sequence: E → D | ||||||
Natural variant | VAR_052481 | 593 | in dbSNP:rs13162502 | |||
Sequence: K → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 698 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).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000213866 | 1-628 | UniProt | Sorting nexin-18 | |||
Sequence: MALRARALYDFRSENPGEISLREHEVLSLCSEQDIEGWLEGVNSRGDRGLFPASYVQVIRAPEPGPAGDGGPGAPARYANVPPGGFEPLPVAPPASFKPPPDAFQALLQPQQAPPPSTFQPPGAGFPYGGGALQPSPQQLYGGYQASQGSDDDWDDEWDDSSTVADEPGALGSGAYPDLDGSSSAGVGAAGRYRLSTRSDLSLGSRGGSVPPQHHPSGPKSSATVSRNLNRFSTFVKSGGEAFVLGEASGFVKDGDKLCVVLGPYGPEWQENPYPFQCTIDDPTKQTKFKGMKSYISYKLVPTHTQVPVHRRYKHFDWLYARLAEKFPVISVPHLPEKQATGRFEEDFISKRRKGLIWWMNHMASHPVLAQCDVFQHFLTCPSSTDEKAWKQGKRKAEKDEMVGANFFLTLSTPPAAALDLQEVESKIDGFKCFTKKMDDSALQLNHTANEFARKQVTGFKKEYQKVGQSFRGLSQAFELDQQAFSVGLNQAIAFTGDAYDAIGELFAEQPRQDLDPVMDLLALYQGHLANFPDIIHVQKGKAWPLEQVIWSVLCRLKGATLTAVPLWVSESYSTGEEASRDVDAWVFSLECKLDCSTGSFLLEYLALGNEYSFSKVQRVPLMTVLSF | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 197 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 233 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Interaction
Subunit
Heterodimer with SNX9 (PubMed:20427313).
Interacts with ITCH (PubMed:20491914).
Interacts with dynamin-2 (DNM2), SYNJ1 and WASL (PubMed:20427313, PubMed:29437695).
Interacts with the AP-1 complex (PubMed:18411244).
Interacts with FCHSD1 (via the F-BAR domain) (By similarity).
Interacts with ITCH (PubMed:20491914).
Interacts with dynamin-2 (DNM2), SYNJ1 and WASL (PubMed:20427313, PubMed:29437695).
Interacts with the AP-1 complex (PubMed:18411244).
Interacts with FCHSD1 (via the F-BAR domain) (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96RF0 | ABI2 Q9NYB9-2 | 3 | EBI-298169, EBI-11096309 | |
BINARY | Q96RF0 | ADAM10 O14672 | 2 | EBI-298169, EBI-1536151 | |
BINARY | Q96RF0 | ADAM9 Q13443 | 2 | EBI-298169, EBI-77903 | |
BINARY | Q96RF0 | CPSF7 Q8N684-3 | 3 | EBI-298169, EBI-11523759 | |
BINARY | Q96RF0 | CYSRT1 A8MQ03 | 3 | EBI-298169, EBI-3867333 | |
BINARY | Q96RF0 | DPPA4 Q7L190 | 3 | EBI-298169, EBI-710457 | |
BINARY | Q96RF0 | GOLGA2 Q08379 | 3 | EBI-298169, EBI-618309 | |
BINARY | Q96RF0 | HSF2BP O75031 | 3 | EBI-298169, EBI-7116203 | |
BINARY | Q96RF0 | HSPB2 Q16082 | 3 | EBI-298169, EBI-739395 | |
BINARY | Q96RF0 | KHDRBS3 O75525 | 3 | EBI-298169, EBI-722504 | |
BINARY | Q96RF0 | KRTAP1-1 Q07627 | 3 | EBI-298169, EBI-11959885 | |
BINARY | Q96RF0 | KRTAP6-3 Q3LI67 | 3 | EBI-298169, EBI-22311199 | |
BINARY | Q96RF0 | MDFI Q99750 | 3 | EBI-298169, EBI-724076 | |
BINARY | Q96RF0 | MSS51 Q4VC12 | 3 | EBI-298169, EBI-11599933 | |
BINARY | Q96RF0 | PTPN21 Q16825 | 3 | EBI-298169, EBI-2860264 | |
BINARY | Q96RF0 | RAB11FIP5 Q9BXF6 | 3 | EBI-298169, EBI-1387068 | |
BINARY | Q96RF0 | ZBTB42 B2RXF5 | 3 | EBI-298169, EBI-12287587 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-61 | SH3 | ||||
Sequence: MALRARALYDFRSENPGEISLREHEVLSLCSEQDIEGWLEGVNSRGDRGLFPASYVQVIRA | ||||||
Region | 62-188 | Disordered | ||||
Sequence: PEPGPAGDGGPGAPARYANVPPGGFEPLPVAPPASFKPPPDAFQALLQPQQAPPPSTFQPPGAGFPYGGGALQPSPQQLYGGYQASQGSDDDWDDEWDDSSTVADEPGALGSGAYPDLDGSSSAGVG | ||||||
Compositional bias | 86-100 | Pro residues | ||||
Sequence: FEPLPVAPPASFKPP | ||||||
Region | 200-224 | Disordered | ||||
Sequence: DLSLGSRGGSVPPQHHPSGPKSSAT | ||||||
Domain | 276-386 | PX | ||||
Sequence: FQCTIDDPTKQTKFKGMKSYISYKLVPTHTQVPVHRRYKHFDWLYARLAEKFPVISVPHLPEKQATGRFEEDFISKRRKGLIWWMNHMASHPVLAQCDVFQHFLTCPSSTD | ||||||
Domain | 421-628 | BAR | ||||
Sequence: LQEVESKIDGFKCFTKKMDDSALQLNHTANEFARKQVTGFKKEYQKVGQSFRGLSQAFELDQQAFSVGLNQAIAFTGDAYDAIGELFAEQPRQDLDPVMDLLALYQGHLANFPDIIHVQKGKAWPLEQVIWSVLCRLKGATLTAVPLWVSESYSTGEEASRDVDAWVFSLECKLDCSTGSFLLEYLALGNEYSFSKVQRVPLMTVLSF |
Domain
The PX domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate.
Sequence similarities
Belongs to the sorting nexin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q96RF0-1
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
- Length628
- Mass (Da)68,894
- Last updated2008-11-25 v2
- ChecksumBE7B16835BA80F9C
Q96RF0-2
- Name2
- Differences from canonical
- 542-628: KAWPLEQVIWSVLCRLKGATLTAVPLWVSESYSTGEEASRDVDAWVFSLECKLDCSTGSFLLEYLALGNEYSFSKVQRVPLMTVLSF → ALTKVKESRRHVEEGKMEVQKADGIQDRCNTISFATLAEIHHFHQIRVRDFKSQMQHFLQQQIIFFQKVTQKLEEALHKYDSV
Q96RF0-3
- Name3
- Differences from canonical
- 592-628: Missing
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 32 | in Ref. 2; BAG65075 | ||||
Sequence: E → G | ||||||
Compositional bias | 86-100 | Pro residues | ||||
Sequence: FEPLPVAPPASFKPP | ||||||
Alternative sequence | VSP_035839 | 542-628 | in isoform 2 | |||
Sequence: KAWPLEQVIWSVLCRLKGATLTAVPLWVSESYSTGEEASRDVDAWVFSLECKLDCSTGSFLLEYLALGNEYSFSKVQRVPLMTVLSF → ALTKVKESRRHVEEGKMEVQKADGIQDRCNTISFATLAEIHHFHQIRVRDFKSQMQHFLQQQIIFFQKVTQKLEEALHKYDSV | ||||||
Alternative sequence | VSP_045476 | 592-628 | in isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF395536 EMBL· GenBank· DDBJ | AAK82415.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304195 EMBL· GenBank· DDBJ | BAG65075.1 EMBL· GenBank· DDBJ | mRNA | ||
AC091888 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471123 EMBL· GenBank· DDBJ | EAW54894.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC060791 EMBL· GenBank· DDBJ | AAH60791.1 EMBL· GenBank· DDBJ | mRNA | ||
BC067860 EMBL· GenBank· DDBJ | AAH67860.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117218 EMBL· GenBank· DDBJ | AAI17219.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117220 EMBL· GenBank· DDBJ | AAI17221.1 EMBL· GenBank· DDBJ | mRNA |