SNX9
entrez
51429
canonical
uniprot
Q9Y5X1
canonical
ensembl
ENSG00000130340
resolver
ensp
ENSP00000376024
resolver
ensp
ENSP00000506326
resolver
enst
ENST00000392185
resolver
enst
ENST00000679814
resolver
genesymbol
SNX9
resolver
genesymbol_syn
SH3PX1
resolver
genesymbol_syn
SH3PXD3A
resolver
hgnc
HGNC:14973
resolver
uniprot
Q9BSI7
resolver
uniprot
Q9BVM1
resolver
uniprot
Q9UJH6
resolver
uniprot
Q9UP20
resolver
uniprot_entry
SNX9_HUMAN
resolver
uniprot_sec
Q9BSI7
resolver
uniprot_sec
Q9BVM1
resolver
uniprot_sec
Q9UJH6
resolver
uniprot_sec
Q9UP20
resolver
amino_acid_sequence
MATKARVMYDFAAEPGNNELTVNEGEIITITNPDVGGGWLEGRNIKGERGLVPTDYVEILPSDGKDQFSCGNSVADQAFLDSLSASTAQASSSAASNNHQVGSGNDPWSAWSASKSGNWESSEGWGAQPEGAGAQRNTNTPNNWDTAFGHPQAYQGPATGDDDDWDEDWDGPKSSSYFKDSESADAGGAQRGNSRASSSSMKIPLNKFPGFAKPGTEQYLLAKQLAKPKEKIPIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWKTGKRKAERDELAGVMIFSTMEPEAPDLDLVEIEQKCEAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLATVFSSSGYQGETDLNDAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGTHKGAIEKVKESDKLVATSKITLQDKQNMVKRVSIMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALSRFPVM
uniprot
proteins
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. {ECO:0000269|PubMed:11799118, ECO:0000269|PubMed:12952949, ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:17609109, ECO:0000269|PubMed:17948057, ECO:0000269|PubMed:18388313, ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:22718350}.
uniprot
proteins
mass_dalton
66592
uniprot
proteins
mutagenesis
MUTAGEN 287; /note="Y->A: Abolishes membrane tubulation activity. Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-313."; /evidence="ECO:0000269|PubMed:17948057"; MUTAGEN 313; /note="K->A: Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-287."; /evidence="ECO:0000269|PubMed:17948057"; MUTAGEN 363; /note="K->E: Strongly reduced membrane binding."; /evidence="ECO:0000269|PubMed:17948057"; MUTAGEN 366..367; /note="KR->EE: Loss of membrane binding."; /evidence="ECO:0000269|PubMed:17948057"; MUTAGEN 522; /note="K->E: Abolishes membrane tubulation activity; when associated with E-528."; /evidence="ECO:0000269|PubMed:17948057"; MUTAGEN 528; /note="K->E: Abolishes membrane tubulation activity; when associated with E-522."; /evidence="ECO:0000269|PubMed:17948057
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by ITCH. {ECO:0000269|PubMed:20491914}.; PTM: Phosphorylated on tyrosine residues by TNK2. Phosphorylation promotes its activity in the degradation of EGFR.
uniprot
proteins
protein_family
Sorting nexin family
uniprot
proteins
pubmed
10531379
uniprot
proteins
pubmed
11485546
uniprot
proteins
pubmed
11799118
uniprot
proteins
pubmed
12952949
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15703209
uniprot
proteins
pubmed
16137687
uniprot
proteins
pubmed
16316319
uniprot
proteins
pubmed
17609109
uniprot
proteins
pubmed
17948057
uniprot
proteins
pubmed
18388313
uniprot
proteins
pubmed
18940612
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19807924
uniprot
proteins
pubmed
20129922
uniprot
proteins
pubmed
20427313
uniprot
proteins
pubmed
20491914
uniprot
proteins
pubmed
21048941
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22718350
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
595
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network. Cell projection, ruffle. Cytoplasm. 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.
uniprot
proteins