Q9Y5X1 · SNX9_HUMAN
- ProteinSorting nexin-9
- GeneSNX9
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids595 (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. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 286 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 288 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 327 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSorting nexin-9
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y5X1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Cell membrane ; Peripheral membrane protein
Note: Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation. Colocalizes with the actin cytoskeleton at the cell membrane.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 287 | Abolishes membrane tubulation activity. Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-313. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 313 | Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-287. | ||||
Sequence: K → A | ||||||
Mutagenesis | 363 | Strongly reduced membrane binding. | ||||
Sequence: K → E | ||||||
Mutagenesis | 366-367 | Loss of membrane binding. | ||||
Sequence: KR → EE | ||||||
Mutagenesis | 522 | Abolishes membrane tubulation activity; when associated with E-528. | ||||
Sequence: K → E | ||||||
Mutagenesis | 528 | Abolishes membrane tubulation activity; when associated with E-522. | ||||
Sequence: K → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 527 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000213852 | 1-595 | UniProt | Sorting nexin-9 | |||
Sequence: MATKARVMYDFAAEPGNNELTVNEGEIITITNPDVGGGWLEGRNIKGERGLVPTDYVEILPSDGKDQFSCGNSVADQAFLDSLSASTAQASSSAASNNHQVGSGNDPWSAWSASKSGNWESSEGWGAQPEGAGAQRNTNTPNNWDTAFGHPQAYQGPATGDDDDWDEDWDGPKSSSYFKDSESADAGGAQRGNSRASSSSMKIPLNKFPGFAKPGTEQYLLAKQLAKPKEKIPIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWKTGKRKAERDELAGVMIFSTMEPEAPDLDLVEIEQKCEAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLATVFSSSGYQGETDLNDAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGTHKGAIEKVKESDKLVATSKITLQDKQNMVKRVSIMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALSRFPVM | |||||||
Modified residue | 116 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 121 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 183 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 197 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 197 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 200 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 200 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 216 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 219 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 239 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 239 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 288 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Ubiquitinated by ITCH.
Phosphorylated on tyrosine residues by TNK2. Phosphorylation promotes its activity in the degradation of EGFR.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed, with highest levels in heart and placenta, and lowest levels in thymus and peripheral blood leukocytes.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer, and homooligomer. Heterodimer with SNX18. Interacts with ITCH. Interacts (via SH3 domain) with TNK2, WASL and ACTR3. Identified in a complex with TNK2 and clathrin heavy chains. Identified in a complex with the AP-2 complex, clathrin and DNM2. Interacts (via SH3 domain) with DNM1 and DNM2. Identified in an oligomeric complex containing DNM1 and SNX9. Interacts with FCHSD1 (By similarity).
Interacts with ADAM9 and ADAM15 cytoplasmic tails
Interacts with ADAM9 and ADAM15 cytoplasmic tails
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y5X1 | ADAM15 Q13444 | 4 | EBI-77848, EBI-77818 | |
BINARY | Q9Y5X1 | ATRAID Q6UW56 | 2 | EBI-77848, EBI-723802 | |
BINARY | Q9Y5X1 | DNM1 Q05193 | 3 | EBI-77848, EBI-713135 | |
BINARY | Q9Y5X1 | DNM2 P50570 | 7 | EBI-77848, EBI-346547 | |
XENO | Q9Y5X1 | espF B7UM88 | 4 | EBI-77848, EBI-2529480 | |
BINARY | Q9Y5X1 | FASLG P48023 | 2 | EBI-77848, EBI-495538 | |
BINARY | Q9Y5X1 | ITCH Q96J02 | 7 | EBI-77848, EBI-1564678 | |
BINARY | Q9Y5X1 | OCRL Q01968 | 5 | EBI-77848, EBI-6148898 | |
XENO | Q9Y5X1 | ORF21 Q98143 | 2 | EBI-77848, EBI-2608563 | |
BINARY | Q9Y5X1 | SNX33 Q8WV41 | 2 | EBI-77848, EBI-2481535 | |
BINARY | Q9Y5X1 | SNX9 Q9Y5X1 | 5 | EBI-77848, EBI-77848 | |
BINARY | Q9Y5X1 | SOS1 Q07889 | 2 | EBI-77848, EBI-297487 | |
BINARY | Q9Y5X1 | SOS2 Q07890 | 2 | EBI-77848, EBI-298181 | |
XENO | Q9Y5X1 | TNK2 Q17R13 | 5 | EBI-77848, EBI-457220 | |
BINARY | Q9Y5X1 | UBC P0CG48 | 2 | EBI-77848, EBI-3390054 | |
BINARY | Q9Y5X1 | WAS P42768 | 2 | EBI-77848, EBI-346375 | |
BINARY | Q9Y5X1 | WASL O00401 | 2 | EBI-77848, EBI-957615 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-62 | SH3 | ||||
Sequence: MATKARVMYDFAAEPGNNELTVNEGEIITITNPDVGGGWLEGRNIKGERGLVPTDYVEILPS | ||||||
Compositional bias | 91-123 | Polar residues | ||||
Sequence: SSSAASNNHQVGSGNDPWSAWSASKSGNWESSE | ||||||
Region | 91-201 | Disordered | ||||
Sequence: SSSAASNNHQVGSGNDPWSAWSASKSGNWESSEGWGAQPEGAGAQRNTNTPNNWDTAFGHPQAYQGPATGDDDDWDEDWDGPKSSSYFKDSESADAGGAQRGNSRASSSSM | ||||||
Compositional bias | 132-149 | Polar residues | ||||
Sequence: AGAQRNTNTPNNWDTAFG | ||||||
Compositional bias | 176-201 | Polar residues | ||||
Sequence: SYFKDSESADAGGAQRGNSRASSSSM | ||||||
Region | 201-213 | Critical for tubulation activity | ||||
Sequence: MKIPLNKFPGFAK | ||||||
Domain | 250-361 | PX | ||||
Sequence: FDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVISESEVFQQFLNFRDEKE | ||||||
Domain | 392-595 | BAR | ||||
Sequence: LVEIEQKCEAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLATVFSSSGYQGETDLNDAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGTHKGAIEKVKESDKLVATSKITLQDKQNMVKRVSIMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALSRFPVM |
Domain
The PX domain mediates interaction with membranes enriched in phosphatidylinositol phosphate. Has high affinity for phosphatidylinositol 4,5-bisphosphate, but can also bind to membranes enriched in other phosphatidylinositol phosphates.
Sequence similarities
Belongs to the sorting nexin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length595
- Mass (Da)66,592
- Last updated1999-11-01 v1
- Checksum963892AC1A5A9227
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7P0T8D4 | A0A7P0T8D4_HUMAN | SNX9 | 591 | ||
A0A7P0T8C7 | A0A7P0T8C7_HUMAN | SNX9 | 632 | ||
A0A7P0T8M2 | A0A7P0T8M2_HUMAN | SNX9 | 270 | ||
A0A7P0T8L2 | A0A7P0T8L2_HUMAN | SNX9 | 122 | ||
A0A7P0T8S8 | A0A7P0T8S8_HUMAN | SNX9 | 625 | ||
A0A7P0T8Z2 | A0A7P0T8Z2_HUMAN | SNX9 | 628 | ||
A0A7P0T8Z7 | A0A7P0T8Z7_HUMAN | SNX9 | 499 | ||
A0A7P0TBD0 | A0A7P0TBD0_HUMAN | SNX9 | 47 | ||
A0A7P0TBI9 | A0A7P0TBI9_HUMAN | SNX9 | 577 | ||
A0A7P0Z4A2 | A0A7P0Z4A2_HUMAN | SNX9 | 585 | ||
A0A7P0Z4A5 | A0A7P0Z4A5_HUMAN | SNX9 | 588 | ||
A0A087WVE4 | A0A087WVE4_HUMAN | SNX9 | 63 | ||
A0A087WZW2 | A0A087WZW2_HUMAN | SNX9 | 84 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 89 | in Ref. 5; AAH05022 | ||||
Sequence: Q → H | ||||||
Compositional bias | 91-123 | Polar residues | ||||
Sequence: SSSAASNNHQVGSGNDPWSAWSASKSGNWESSE | ||||||
Compositional bias | 132-149 | Polar residues | ||||
Sequence: AGAQRNTNTPNNWDTAFG | ||||||
Compositional bias | 176-201 | Polar residues | ||||
Sequence: SYFKDSESADAGGAQRGNSRASSSSM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF121859 EMBL· GenBank· DDBJ | AAD27832.1 EMBL· GenBank· DDBJ | mRNA | ||
AF131214 EMBL· GenBank· DDBJ | AAF04473.1 EMBL· GenBank· DDBJ | mRNA | ||
AF172847 EMBL· GenBank· DDBJ | AAL54871.1 EMBL· GenBank· DDBJ | mRNA | ||
AL035634 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL139330 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL391863 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC001084 EMBL· GenBank· DDBJ | AAH01084.3 EMBL· GenBank· DDBJ | mRNA | ||
BC005022 EMBL· GenBank· DDBJ | AAH05022.1 EMBL· GenBank· DDBJ | mRNA | ||
AF076957 EMBL· GenBank· DDBJ | AAD43001.1 EMBL· GenBank· DDBJ | mRNA |