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Sorting nexin-9 (SH3 and PX domain-containing protein 1) (Protein SDP1) (SH3 and PX domain-containing protein 3A)

 SNX9_HUMAN              Reviewed;         595 AA.
Q9Y5X1; Q9BSI7; Q9BVM1; Q9UJH6; Q9UP20;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
30-AUG-2017, entry version 161.
RecName: Full=Sorting nexin-9;
AltName: Full=SH3 and PX domain-containing protein 1;
Short=Protein SDP1;
AltName: Full=SH3 and PX domain-containing protein 3A;
Name=SNX9; Synonyms=SH3PX1, SH3PXD3A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11485546; DOI=10.1042/0264-6021:3580007;
Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
"A large family of endosome-localized proteins related to sorting
nexin 1.";
Biochem. J. 358:7-16(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADAM9 AND ADAM15, AND
TISSUE SPECIFICITY.
PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
"Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
two SH3 domain-containing proteins, endophilin I and SH3PX1.";
J. Biol. Chem. 274:31693-31699(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Zhang J.S., Smith D.I.;
"Identification of differentially expressed genes in matched prostate
cancer and normal epithelial cell lines.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 201-595.
Ramanathan G., Subramaniam V.N., Hong W.;
"Human SDP1.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, INTERACTION WITH TNK2, IDENTIFICATION IN A COMPLEX WITH TNK2
AND CLATHRIN HEAVY CHAIN, AND TYROSINE PHOSPHORYLATION.
PubMed=11799118; DOI=10.1074/jbc.M110329200;
Lin Q., Lo C.G., Cerione R.A., Yang W.;
"The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to
regulate epidermal growth factor receptor degradation.";
J. Biol. Chem. 277:10134-10138(2002).
[8]
FUNCTION, INTERACTION WITH DNM2 AND THE AP-2 COMPLEX, IDENTIFICATION
IN A COMPLEX WITH THE AP-2 COMPLEX; CLATHRIN AND DNM2, AND SUBCELLULAR
LOCATION.
PubMed=12952949; DOI=10.1074/jbc.M307334200;
Lundmark R., Carlsson S.R.;
"Sorting nexin 9 participates in clathrin-mediated endocytosis through
interactions with the core components.";
J. Biol. Chem. 278:46772-46781(2003).
[9]
INTERACTION WITH TNK2, AND SUBCELLULAR LOCATION.
PubMed=16137687; DOI=10.1016/j.febslet.2005.07.093;
Yeow-Fong L., Lim L., Manser E.;
"SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector
ACK1.";
FEBS Lett. 579:5040-5048(2005).
[10]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
AND INTERACTION WITH DNM1 AND DNM2.
PubMed=15703209; DOI=10.1091/mbc.E04-11-1016;
Soulet F., Yarar D., Leonard M., Schmid S.L.;
"SNX9 regulates dynamin assembly and is required for efficient
clathrin-mediated endocytosis.";
Mol. Biol. Cell 16:2058-2067(2005).
[11]
SUBUNIT, SUBCELLULAR LOCATION, AND TYROSINE PHOSPHORYLATION.
PubMed=16316319; DOI=10.1042/BJ20050576;
Childress C., Lin Q., Yang W.;
"Dimerization is required for SH3PX1 tyrosine phosphorylation in
response to epidermal growth factor signalling and interaction with
ACK2.";
Biochem. J. 394:693-698(2006).
[12]
FUNCTION, INTERACTION WITH WASL, SUBCELLULAR LOCATION, SUBUNIT, AND
PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE BINDING.
PubMed=17609109; DOI=10.1016/j.devcel.2007.04.014;
Yarar D., Waterman-Storer C.M., Schmid S.L.;
"SNX9 couples actin assembly to phosphoinositide signals and is
required for membrane remodeling during endocytosis.";
Dev. Cell 13:43-56(2007).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARP3; WASL AND
DNM2.
PubMed=18388313; DOI=10.1242/jcs.016709;
Shin N., Ahn N., Chang-Ileto B., Park J., Takei K., Ahn S.G.,
Kim S.A., Di Paolo G., Chang S.;
"SNX9 regulates tubular invagination of the plasma membrane through
interaction with actin cytoskeleton and dynamin 2.";
J. Cell Sci. 121:1252-1263(2008).
[14]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
INTERACTION WITH ITCH, AND UBIQUITINATION BY ITCH.
PubMed=20491914; DOI=10.1111/j.1742-4658.2010.07698.x;
Baumann C., Lindholm C.K., Rimoldi D., Levy F.;
"The E3 ubiquitin ligase Itch regulates sorting nexin 9 through an
unconventional substrate recognition domain.";
FEBS J. 277:2803-2814(2010).
[17]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=20427313; DOI=10.1242/jcs.064170;
Park J., Kim Y., Lee S., Park J.J., Park Z.Y., Sun W., Kim H.,
Chang S.;
"SNX18 shares a redundant role with SNX9 and modulates endocytic
trafficking at the plasma membrane.";
J. Cell Sci. 123:1742-1750(2010).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21048941; DOI=10.1371/journal.pone.0013763;
Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S.,
Teasdale R.D.;
"The SNX-PX-BAR family in macropinocytosis: the regulation of
macropinosome formation by SNX-PX-BAR proteins.";
PLoS ONE 5:E13763-E13763(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22718350; DOI=10.1242/jcs.105981;
Ma M.P., Chircop M.;
"SNX9, SNX18 and SNX33 are required for progression through and
completion of mitosis.";
J. Cell Sci. 125:4372-4382(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-121; SER-197;
SER-200 AND THR-216, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 204-595 IN COMPLEX WITH
PHOSPHATIDYLINOSITOL 3-PHOSPHATE, FUNCTION, SUBUNIT, DOMAIN,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-287; LYS-313; LYS-363;
366-LYS-ARG-367; LYS-522 AND LYS-528.
PubMed=17948057; DOI=10.1038/sj.emboj.7601889;
Pylypenko O., Lundmark R., Rasmuson E., Carlsson S.R., Rak A.;
"The PX-BAR membrane-remodeling unit of sorting nexin 9.";
EMBO J. 26:4788-4800(2007).
[24]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 230-595, AND SUBUNIT.
PubMed=18940612; DOI=10.1016/j.str.2008.07.016;
Wang Q., Kaan H.Y., Hooda R.N., Goh S.L., Sondermann H.;
"Structure and plasticity of Endophilin and Sorting Nexin 9.";
Structure 16:1574-1587(2008).
[25]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 152-182 IN COMPLEX WITH
ALDOA.
PubMed=20129922; DOI=10.1074/jbc.M109.092049;
Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.;
"Mechanism of aldolase control of sorting nexin 9 function in
endocytosis.";
J. Biol. Chem. 285:11983-11990(2010).
-!- 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}.
-!- SUBUNIT: Homodimer, and homooligomer. Heterodimer with SNX18.
Interacts with ITCH. Interacts (via SH3 domain) with TNK2, WASL
and ARP3. 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 ADAM9 and ADAM15 cytoplasmic tails.
{ECO:0000269|PubMed:10531379, ECO:0000269|PubMed:11799118,
ECO:0000269|PubMed:12952949, ECO:0000269|PubMed:15703209,
ECO:0000269|PubMed:16137687, ECO:0000269|PubMed:16316319,
ECO:0000269|PubMed:17609109, ECO:0000269|PubMed:17948057,
ECO:0000269|PubMed:18388313, ECO:0000269|PubMed:18940612,
ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20129922,
ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:20491914}.
-!- INTERACTION:
Q13444:ADAM15; NbExp=2; IntAct=EBI-77848, EBI-77818;
Q6UW56:ATRAID; NbExp=2; IntAct=EBI-77848, EBI-723802;
Q05193:DNM1; NbExp=2; IntAct=EBI-77848, EBI-713135;
P50570:DNM2; NbExp=4; IntAct=EBI-77848, EBI-346547;
B7UM88:espF (xeno); NbExp=4; IntAct=EBI-77848, EBI-2529480;
P48023:FASLG; NbExp=2; IntAct=EBI-77848, EBI-495538;
Q96J02:ITCH; NbExp=7; IntAct=EBI-77848, EBI-1564678;
Q98143:ORF21 (xeno); NbExp=2; IntAct=EBI-77848, EBI-2608563;
Q8WV41:SNX33; NbExp=2; IntAct=EBI-77848, EBI-2481535;
Q07889:SOS1; NbExp=2; IntAct=EBI-77848, EBI-297487;
Q07890:SOS2; NbExp=2; IntAct=EBI-77848, EBI-298181;
Q17R13:TNK2 (xeno); NbExp=5; IntAct=EBI-77848, EBI-457220;
P0CG48:UBC; NbExp=2; IntAct=EBI-77848, EBI-3390054;
O00401:WASL; NbExp=2; IntAct=EBI-77848, EBI-957615;
-!- 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.
-!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart
and placenta, and lowest levels in thymus and peripheral blood
leukocytes. {ECO:0000269|PubMed:10531379}.
-!- 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.
{ECO:0000269|PubMed:17948057}.
-!- PTM: Ubiquitinated by ITCH. {ECO:0000269|PubMed:20491914}.
-!- PTM: Phosphorylated on tyrosine residues by TNK2. Phosphorylation
promotes its activity in the degradation of EGFR.
-!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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EMBL; AF121859; AAD27832.1; -; mRNA.
EMBL; AF131214; AAF04473.1; -; mRNA.
EMBL; AF172847; AAL54871.1; -; mRNA.
EMBL; AL035634; CAI20465.1; -; Genomic_DNA.
EMBL; AL139330; CAI20465.1; JOINED; Genomic_DNA.
EMBL; AL391863; CAI20465.1; JOINED; Genomic_DNA.
EMBL; AL139330; CAI12979.1; -; Genomic_DNA.
EMBL; AL035634; CAI12979.1; JOINED; Genomic_DNA.
EMBL; AL391863; CAI12979.1; JOINED; Genomic_DNA.
EMBL; AL391863; CAI15180.1; -; Genomic_DNA.
EMBL; AL035634; CAI15180.1; JOINED; Genomic_DNA.
EMBL; AL139330; CAI15180.1; JOINED; Genomic_DNA.
EMBL; BC001084; AAH01084.3; -; mRNA.
EMBL; BC005022; AAH05022.1; -; mRNA.
EMBL; AF076957; AAD43001.1; -; mRNA.
CCDS; CCDS5253.1; -.
RefSeq; NP_057308.1; NM_016224.4.
UniGene; Hs.191213; -.
PDB; 2RAI; X-ray; 3.20 A; A/B=204-595.
PDB; 2RAJ; X-ray; 2.45 A; A=204-595.
PDB; 2RAK; X-ray; 3.00 A; A=204-595.
PDB; 3DYT; X-ray; 2.08 A; A=230-595.
PDB; 3DYU; X-ray; 4.10 A; A/B/C=230-595.
PDB; 3LGE; X-ray; 2.20 A; E/F/G/H=152-182.
PDBsum; 2RAI; -.
PDBsum; 2RAJ; -.
PDBsum; 2RAK; -.
PDBsum; 3DYT; -.
PDBsum; 3DYU; -.
PDBsum; 3LGE; -.
ProteinModelPortal; Q9Y5X1; -.
SMR; Q9Y5X1; -.
BioGrid; 119535; 49.
DIP; DIP-30997N; -.
IntAct; Q9Y5X1; 35.
MINT; MINT-108846; -.
STRING; 9606.ENSP00000376024; -.
iPTMnet; Q9Y5X1; -.
PhosphoSitePlus; Q9Y5X1; -.
DMDM; 12643956; -.
EPD; Q9Y5X1; -.
MaxQB; Q9Y5X1; -.
PaxDb; Q9Y5X1; -.
PeptideAtlas; Q9Y5X1; -.
PRIDE; Q9Y5X1; -.
DNASU; 51429; -.
Ensembl; ENST00000392185; ENSP00000376024; ENSG00000130340.
GeneID; 51429; -.
KEGG; hsa:51429; -.
UCSC; uc003qqv.3; human.
CTD; 51429; -.
DisGeNET; 51429; -.
GeneCards; SNX9; -.
HGNC; HGNC:14973; SNX9.
HPA; HPA031410; -.
HPA; HPA057203; -.
MIM; 605952; gene.
neXtProt; NX_Q9Y5X1; -.
OpenTargets; ENSG00000130340; -.
PharmGKB; PA37949; -.
eggNOG; KOG2528; Eukaryota.
eggNOG; ENOG410XPHZ; LUCA.
GeneTree; ENSGT00510000046469; -.
HOGENOM; HOG000261633; -.
HOVERGEN; HBG009996; -.
InParanoid; Q9Y5X1; -.
KO; K17923; -.
OMA; FAKPGME; -.
OrthoDB; EOG091G03D8; -.
PhylomeDB; Q9Y5X1; -.
TreeFam; TF314082; -.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SignaLink; Q9Y5X1; -.
SIGNOR; Q9Y5X1; -.
ChiTaRS; SNX9; human.
EvolutionaryTrace; Q9Y5X1; -.
GeneWiki; SNX9; -.
GenomeRNAi; 51429; -.
PRO; PR:Q9Y5X1; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000130340; -.
CleanEx; HS_SNX9; -.
ExpressionAtlas; Q9Y5X1; baseline and differential.
Genevisible; Q9Y5X1; HS.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0071933; F:Arp2/3 complex binding; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0036089; P:cleavage furrow formation; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
GO; GO:0060988; P:lipid tube assembly; IDA:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0032461; P:positive regulation of protein oligomerization; IDA:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
CDD; cd11898; SH3_SNX9; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR001683; Phox.
InterPro; IPR001452; SH3_domain.
InterPro; IPR028644; SNX9.
InterPro; IPR014536; Snx9_fam.
InterPro; IPR035558; SNX9_SH3.
InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
PANTHER; PTHR10555:SF181; PTHR10555:SF181; 1.
Pfam; PF10456; BAR_3_WASP_bdg; 1.
Pfam; PF00787; PX; 1.
Pfam; PF00018; SH3_1; 1.
PIRSF; PIRSF027744; Snx9; 1.
SMART; SM00312; PX; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50195; PX; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Cell division; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Endocytosis; Golgi apparatus; Lipid-binding; Membrane; Mitosis;
Phosphoprotein; Protein transport; Reference proteome; SH3 domain;
Transport; Ubl conjugation.
CHAIN 1 595 Sorting nexin-9.
/FTId=PRO_0000213852.
DOMAIN 1 62 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 250 361 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 392 595 BAR.
REGION 201 213 Critical for tubulation activity.
BINDING 286 286 Phosphatidylinositol 4,5-bisphosphate.
BINDING 288 288 Phosphatidylinositol 4,5-bisphosphate.
BINDING 313 313 Phosphatidylinositol 4,5-bisphosphate.
BINDING 327 327 Phosphatidylinositol 4,5-bisphosphate.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 216 216 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 239 239 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q91VH2}.
MOD_RES 288 288 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MUTAGEN 287 287 Y->A: Abolishes membrane tubulation
activity. Abolishes binding to
phosphatidylinositol 3-phosphate, but not
to phosphatidylinositol 4,5-bisphosphate;
when associated with A-313.
{ECO:0000269|PubMed:17948057}.
MUTAGEN 313 313 K->A: Abolishes binding to
phosphatidylinositol 3-phosphate, but not
to phosphatidylinositol 4,5-bisphosphate;
when associated with A-287.
{ECO:0000269|PubMed:17948057}.
MUTAGEN 363 363 K->E: Strongly reduced membrane binding.
{ECO:0000269|PubMed:17948057}.
MUTAGEN 366 367 KR->EE: Loss of membrane binding.
{ECO:0000269|PubMed:17948057}.
MUTAGEN 522 522 K->E: Abolishes membrane tubulation
activity; when associated with E-528.
{ECO:0000269|PubMed:17948057}.
MUTAGEN 528 528 K->E: Abolishes membrane tubulation
activity; when associated with E-522.
{ECO:0000269|PubMed:17948057}.
CONFLICT 89 89 Q -> H (in Ref. 5; AAH05022).
{ECO:0000305}.
TURN 167 169 {ECO:0000244|PDB:3LGE}.
HELIX 175 180 {ECO:0000244|PDB:3LGE}.
HELIX 215 221 {ECO:0000244|PDB:2RAJ}.
STRAND 232 237 {ECO:0000244|PDB:3DYT}.
STRAND 240 243 {ECO:0000244|PDB:3DYT}.
STRAND 252 255 {ECO:0000244|PDB:3DYT}.
HELIX 257 259 {ECO:0000244|PDB:3DYT}.
STRAND 260 262 {ECO:0000244|PDB:3DYT}.
STRAND 263 266 {ECO:0000244|PDB:2RAK}.
STRAND 271 276 {ECO:0000244|PDB:3DYT}.
TURN 277 279 {ECO:0000244|PDB:2RAJ}.
STRAND 283 286 {ECO:0000244|PDB:3DYT}.
HELIX 287 301 {ECO:0000244|PDB:3DYT}.
TURN 302 304 {ECO:0000244|PDB:3DYT}.
HELIX 324 339 {ECO:0000244|PDB:3DYT}.
HELIX 344 346 {ECO:0000244|PDB:3DYT}.
HELIX 348 355 {ECO:0000244|PDB:3DYT}.
HELIX 359 370 {ECO:0000244|PDB:3DYT}.
HELIX 376 382 {ECO:0000244|PDB:3DYT}.
STRAND 383 387 {ECO:0000244|PDB:3DYT}.
HELIX 392 428 {ECO:0000244|PDB:3DYT}.
HELIX 430 450 {ECO:0000244|PDB:3DYT}.
HELIX 455 457 {ECO:0000244|PDB:3DYT}.
HELIX 458 480 {ECO:0000244|PDB:3DYT}.
HELIX 482 484 {ECO:0000244|PDB:3DYT}.
HELIX 486 500 {ECO:0000244|PDB:3DYT}.
HELIX 503 518 {ECO:0000244|PDB:3DYT}.
HELIX 520 525 {ECO:0000244|PDB:3DYT}.
HELIX 531 590 {ECO:0000244|PDB:3DYT}.
SEQUENCE 595 AA; 66592 MW; 963892AC1A5A9227 CRC64;
MATKARVMYD FAAEPGNNEL TVNEGEIITI TNPDVGGGWL EGRNIKGERG LVPTDYVEIL
PSDGKDQFSC GNSVADQAFL DSLSASTAQA SSSAASNNHQ VGSGNDPWSA WSASKSGNWE
SSEGWGAQPE GAGAQRNTNT PNNWDTAFGH PQAYQGPATG DDDDWDEDWD GPKSSSYFKD
SESADAGGAQ RGNSRASSSS MKIPLNKFPG FAKPGTEQYL LAKQLAKPKE KIPIIVGDYG
PMWVYPTSTF DCVVADPRKG SKMYGLKSYI EYQLTPTNTN RSVNHRYKHF DWLYERLLVK
FGSAIPIPSL PDKQVTGRFE EEFIKMRMER LQAWMTRMCR HPVISESEVF QQFLNFRDEK
EWKTGKRKAE RDELAGVMIF STMEPEAPDL DLVEIEQKCE AVGKFTKAMD DGVKELLTVG
QEHWKRCTGP LPKEYQKIGK ALQSLATVFS SSGYQGETDL NDAITEAGKT YEEIASLVAE
QPKKDLHFLM ECNHEYKGFL GCFPDIIGTH KGAIEKVKES DKLVATSKIT LQDKQNMVKR
VSIMSYALQA EMNHFHSNRI YDYNSVIRLY LEQQVQFYET IAEKLRQALS RFPVM


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