ID SNX9_HUMAN Reviewed; 595 AA.
AC Q9Y5X1; Q9BSI7; Q9BVM1; Q9UJH6; Q9UP20;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 203.
DE RecName: Full=Sorting nexin-9;
DE AltName: Full=SH3 and PX domain-containing protein 1;
DE Short=Protein SDP1;
DE AltName: Full=SH3 and PX domain-containing protein 3A;
GN Name=SNX9; Synonyms=SH3PX1, SH3PXD3A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11485546; DOI=10.1042/0264-6021:3580007;
RA Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
RT "A large family of endosome-localized proteins related to sorting nexin
RT 1.";
RL Biochem. J. 358:7-16(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADAM9 AND ADAM15, AND TISSUE
RP SPECIFICITY.
RX PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
RA Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
RT "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two
RT SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL J. Biol. Chem. 274:31693-31699(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang J.S., Smith D.I.;
RT "Identification of differentially expressed genes in matched prostate
RT cancer and normal epithelial cell lines.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 201-595.
RA Ramanathan G., Subramaniam V.N., Hong W.;
RT "Human SDP1.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, INTERACTION WITH TNK2, IDENTIFICATION IN A COMPLEX WITH TNK2 AND
RP CLATHRIN HEAVY CHAIN, AND TYROSINE PHOSPHORYLATION.
RX PubMed=11799118; DOI=10.1074/jbc.m110329200;
RA Lin Q., Lo C.G., Cerione R.A., Yang W.;
RT "The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate
RT epidermal growth factor receptor degradation.";
RL J. Biol. Chem. 277:10134-10138(2002).
RN [8]
RP FUNCTION, INTERACTION WITH DNM2 AND THE AP-2 COMPLEX, IDENTIFICATION IN A
RP COMPLEX WITH THE AP-2 COMPLEX; CLATHRIN AND DNM2, AND SUBCELLULAR LOCATION.
RX PubMed=12952949; DOI=10.1074/jbc.m307334200;
RA Lundmark R., Carlsson S.R.;
RT "Sorting nexin 9 participates in clathrin-mediated endocytosis through
RT interactions with the core components.";
RL J. Biol. Chem. 278:46772-46781(2003).
RN [9]
RP INTERACTION WITH TNK2, AND SUBCELLULAR LOCATION.
RX PubMed=16137687; DOI=10.1016/j.febslet.2005.07.093;
RA Yeow-Fong L., Lim L., Manser E.;
RT "SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector
RT ACK1.";
RL FEBS Lett. 579:5040-5048(2005).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH DNM1 AND DNM2.
RX PubMed=15703209; DOI=10.1091/mbc.e04-11-1016;
RA Soulet F., Yarar D., Leonard M., Schmid S.L.;
RT "SNX9 regulates dynamin assembly and is required for efficient clathrin-
RT mediated endocytosis.";
RL Mol. Biol. Cell 16:2058-2067(2005).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TYROSINE PHOSPHORYLATION.
RX PubMed=16316319; DOI=10.1042/bj20050576;
RA Childress C., Lin Q., Yang W.;
RT "Dimerization is required for SH3PX1 tyrosine phosphorylation in response
RT to epidermal growth factor signalling and interaction with ACK2.";
RL Biochem. J. 394:693-698(2006).
RN [12]
RP FUNCTION, INTERACTION WITH WASL, SUBCELLULAR LOCATION, SUBUNIT, AND
RP PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE BINDING.
RX PubMed=17609109; DOI=10.1016/j.devcel.2007.04.014;
RA Yarar D., Waterman-Storer C.M., Schmid S.L.;
RT "SNX9 couples actin assembly to phosphoinositide signals and is required
RT for membrane remodeling during endocytosis.";
RL Dev. Cell 13:43-56(2007).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ACTR3; WASL AND DNM2.
RX PubMed=18388313; DOI=10.1242/jcs.016709;
RA Shin N., Ahn N., Chang-Ileto B., Park J., Takei K., Ahn S.G., Kim S.A.,
RA Di Paolo G., Chang S.;
RT "SNX9 regulates tubular invagination of the plasma membrane through
RT interaction with actin cytoskeleton and dynamin 2.";
RL J. Cell Sci. 121:1252-1263(2008).
RN [14]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP INTERACTION WITH ITCH, AND UBIQUITINATION BY ITCH.
RX PubMed=20491914; DOI=10.1111/j.1742-4658.2010.07698.x;
RA Baumann C., Lindholm C.K., Rimoldi D., Levy F.;
RT "The E3 ubiquitin ligase Itch regulates sorting nexin 9 through an
RT unconventional substrate recognition domain.";
RL FEBS J. 277:2803-2814(2010).
RN [17]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20427313; DOI=10.1242/jcs.064170;
RA Park J., Kim Y., Lee S., Park J.J., Park Z.Y., Sun W., Kim H., Chang S.;
RT "SNX18 shares a redundant role with SNX9 and modulates endocytic
RT trafficking at the plasma membrane.";
RL J. Cell Sci. 123:1742-1750(2010).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21048941; DOI=10.1371/journal.pone.0013763;
RA Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S., Teasdale R.D.;
RT "The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome
RT formation by SNX-PX-BAR proteins.";
RL PLoS ONE 5:E13763-E13763(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22718350; DOI=10.1242/jcs.105981;
RA Ma M.P., Chircop M.;
RT "SNX9, SNX18 and SNX33 are required for progression through and completion
RT of mitosis.";
RL J. Cell Sci. 125:4372-4382(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-121; SER-197;
RP SER-200 AND THR-216, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 204-595 IN COMPLEX WITH
RP PHOSPHATIDYLINOSITOL 3-PHOSPHATE, FUNCTION, SUBUNIT, DOMAIN, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF TYR-287; LYS-313; LYS-363; 366-LYS-ARG-367;
RP LYS-522 AND LYS-528.
RX PubMed=17948057; DOI=10.1038/sj.emboj.7601889;
RA Pylypenko O., Lundmark R., Rasmuson E., Carlsson S.R., Rak A.;
RT "The PX-BAR membrane-remodeling unit of sorting nexin 9.";
RL EMBO J. 26:4788-4800(2007).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 230-595, AND SUBUNIT.
RX PubMed=18940612; DOI=10.1016/j.str.2008.07.016;
RA Wang Q., Kaan H.Y., Hooda R.N., Goh S.L., Sondermann H.;
RT "Structure and plasticity of Endophilin and Sorting Nexin 9.";
RL Structure 16:1574-1587(2008).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 152-182 IN COMPLEX WITH ALDOA.
RX PubMed=20129922; DOI=10.1074/jbc.m109.092049;
RA Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.;
RT "Mechanism of aldolase control of sorting nexin 9 function in
RT endocytosis.";
RL J. Biol. Chem. 285:11983-11990(2010).
CC -!- FUNCTION: Involved in endocytosis and intracellular vesicle
CC trafficking, both during interphase and at the end of mitosis. Required
CC for efficient progress through mitosis and cytokinesis. Required for
CC normal formation of the cleavage furrow at the end of mitosis. Plays a
CC role in endocytosis via clathrin-coated pits, but also clathrin-
CC independent, actin-dependent fluid-phase endocytosis. Plays a role in
CC macropinocytosis. Promotes internalization of TNFR. Promotes
CC degradation of EGFR after EGF signaling. Stimulates the GTPase activity
CC of DNM1. Promotes DNM1 oligomerization. Promotes activation of the
CC Arp2/3 complex by WASL, and thereby plays a role in the reorganization
CC of the F-actin cytoskeleton. Binds to membranes enriched in
CC phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation.
CC Has lower affinity for membranes enriched in phosphatidylinositol 3-
CC phosphate. {ECO:0000269|PubMed:11799118, ECO:0000269|PubMed:12952949,
CC ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:17609109,
CC ECO:0000269|PubMed:17948057, ECO:0000269|PubMed:18388313,
CC ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:21048941,
CC ECO:0000269|PubMed:22718350}.
CC -!- SUBUNIT: Homodimer, and homooligomer. Heterodimer with SNX18. Interacts
CC with ITCH. Interacts (via SH3 domain) with TNK2, WASL and ACTR3.
CC Identified in a complex with TNK2 and clathrin heavy chains. Identified
CC in a complex with the AP-2 complex, clathrin and DNM2. Interacts (via
CC SH3 domain) with DNM1 and DNM2. Identified in an oligomeric complex
CC containing DNM1 and SNX9. Interacts with FCHSD1 (By similarity).
CC Interacts with ADAM9 and ADAM15 cytoplasmic tails.
CC {ECO:0000250|UniProtKB:Q91VH2, ECO:0000269|PubMed:10531379,
CC ECO:0000269|PubMed:11799118, ECO:0000269|PubMed:12952949,
CC ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:16137687,
CC ECO:0000269|PubMed:16316319, ECO:0000269|PubMed:17609109,
CC ECO:0000269|PubMed:17948057, ECO:0000269|PubMed:18388313,
CC ECO:0000269|PubMed:18940612, ECO:0000269|PubMed:19807924,
CC ECO:0000269|PubMed:20129922, ECO:0000269|PubMed:20427313,
CC ECO:0000269|PubMed:20491914}.
CC -!- INTERACTION:
CC Q9Y5X1; Q13444: ADAM15; NbExp=4; IntAct=EBI-77848, EBI-77818;
CC Q9Y5X1; Q6UW56: ATRAID; NbExp=2; IntAct=EBI-77848, EBI-723802;
CC Q9Y5X1; Q05193: DNM1; NbExp=2; IntAct=EBI-77848, EBI-713135;
CC Q9Y5X1; P50570: DNM2; NbExp=4; IntAct=EBI-77848, EBI-346547;
CC Q9Y5X1; P48023: FASLG; NbExp=2; IntAct=EBI-77848, EBI-495538;
CC Q9Y5X1; Q96J02: ITCH; NbExp=7; IntAct=EBI-77848, EBI-1564678;
CC Q9Y5X1; Q01968: OCRL; NbExp=5; IntAct=EBI-77848, EBI-6148898;
CC Q9Y5X1; Q8WV41: SNX33; NbExp=2; IntAct=EBI-77848, EBI-2481535;
CC Q9Y5X1; Q9Y5X1: SNX9; NbExp=5; IntAct=EBI-77848, EBI-77848;
CC Q9Y5X1; Q07889: SOS1; NbExp=2; IntAct=EBI-77848, EBI-297487;
CC Q9Y5X1; Q07890: SOS2; NbExp=2; IntAct=EBI-77848, EBI-298181;
CC Q9Y5X1; P0CG48: UBC; NbExp=2; IntAct=EBI-77848, EBI-3390054;
CC Q9Y5X1; P42768: WAS; NbExp=2; IntAct=EBI-77848, EBI-346375;
CC Q9Y5X1; O00401: WASL; NbExp=2; IntAct=EBI-77848, EBI-957615;
CC Q9Y5X1; B7UM88: espF; Xeno; NbExp=4; IntAct=EBI-77848, EBI-2529480;
CC Q9Y5X1; Q98143: ORF21; Xeno; NbExp=2; IntAct=EBI-77848, EBI-2608563;
CC Q9Y5X1; Q17R13: TNK2; Xeno; NbExp=5; IntAct=EBI-77848, EBI-457220;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi
CC apparatus, trans-Golgi network. Cell projection, ruffle. Cytoplasm.
CC Note=Localized at sites of endocytosis at the cell membrane. Detected
CC on newly formed macropinosomes. Transiently recruited to clathrin-
CC coated pits at a late stage of clathrin-coated vesicle formation.
CC Colocalizes with the actin cytoskeleton at the cell membrane.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and
CC placenta, and lowest levels in thymus and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:10531379}.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol phosphate. Has high affinity for
CC phosphatidylinositol 4,5-bisphosphate, but can also bind to membranes
CC enriched in other phosphatidylinositol phosphates.
CC {ECO:0000269|PubMed:17948057}.
CC -!- PTM: Ubiquitinated by ITCH. {ECO:0000269|PubMed:20491914}.
CC -!- PTM: Phosphorylated on tyrosine residues by TNK2. Phosphorylation
CC promotes its activity in the degradation of EGFR.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF121859; AAD27832.1; -; mRNA.
DR EMBL; AF131214; AAF04473.1; -; mRNA.
DR EMBL; AF172847; AAL54871.1; -; mRNA.
DR EMBL; AL035634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001084; AAH01084.3; -; mRNA.
DR EMBL; BC005022; AAH05022.1; -; mRNA.
DR EMBL; AF076957; AAD43001.1; -; mRNA.
DR CCDS; CCDS5253.1; -.
DR RefSeq; NP_057308.1; NM_016224.4.
DR PDB; 2RAI; X-ray; 3.20 A; A/B=204-595.
DR PDB; 2RAJ; X-ray; 2.45 A; A=204-595.
DR PDB; 2RAK; X-ray; 3.00 A; A=204-595.
DR PDB; 3DYT; X-ray; 2.08 A; A=230-595.
DR PDB; 3DYU; X-ray; 4.10 A; A/B/C=230-595.
DR PDB; 3LGE; X-ray; 2.20 A; E/F/G/H=152-182.
DR PDB; 7OJ9; NMR; -; A=1-64.
DR PDBsum; 2RAI; -.
DR PDBsum; 2RAJ; -.
DR PDBsum; 2RAK; -.
DR PDBsum; 3DYT; -.
DR PDBsum; 3DYU; -.
DR PDBsum; 3LGE; -.
DR PDBsum; 7OJ9; -.
DR AlphaFoldDB; Q9Y5X1; -.
DR SMR; Q9Y5X1; -.
DR BioGRID; 119535; 135.
DR DIP; DIP-30997N; -.
DR IntAct; Q9Y5X1; 76.
DR MINT; Q9Y5X1; -.
DR STRING; 9606.ENSP00000376024; -.
DR GlyGen; Q9Y5X1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5X1; -.
DR MetOSite; Q9Y5X1; -.
DR PhosphoSitePlus; Q9Y5X1; -.
DR BioMuta; SNX9; -.
DR DMDM; 12643956; -.
DR EPD; Q9Y5X1; -.
DR jPOST; Q9Y5X1; -.
DR MassIVE; Q9Y5X1; -.
DR MaxQB; Q9Y5X1; -.
DR PaxDb; 9606-ENSP00000376024; -.
DR PeptideAtlas; Q9Y5X1; -.
DR ProteomicsDB; 86526; -.
DR Pumba; Q9Y5X1; -.
DR Antibodypedia; 33429; 468 antibodies from 33 providers.
DR DNASU; 51429; -.
DR Ensembl; ENST00000392185.8; ENSP00000376024.3; ENSG00000130340.17.
DR Ensembl; ENST00000679814.1; ENSP00000506326.1; ENSG00000130340.17.
DR GeneID; 51429; -.
DR KEGG; hsa:51429; -.
DR MANE-Select; ENST00000392185.8; ENSP00000376024.3; NM_016224.5; NP_057308.1.
DR UCSC; uc003qqv.3; human.
DR AGR; HGNC:14973; -.
DR CTD; 51429; -.
DR DisGeNET; 51429; -.
DR GeneCards; SNX9; -.
DR HGNC; HGNC:14973; SNX9.
DR HPA; ENSG00000130340; Low tissue specificity.
DR MIM; 605952; gene.
DR neXtProt; NX_Q9Y5X1; -.
DR OpenTargets; ENSG00000130340; -.
DR PharmGKB; PA37949; -.
DR VEuPathDB; HostDB:ENSG00000130340; -.
DR eggNOG; KOG2528; Eukaryota.
DR GeneTree; ENSGT00940000156557; -.
DR HOGENOM; CLU_021494_2_0_1; -.
DR InParanoid; Q9Y5X1; -.
DR OMA; FDSAPMR; -.
DR OrthoDB; 5401713at2759; -.
DR PhylomeDB; Q9Y5X1; -.
DR TreeFam; TF314082; -.
DR PathwayCommons; Q9Y5X1; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q9Y5X1; -.
DR SIGNOR; Q9Y5X1; -.
DR BioGRID-ORCS; 51429; 13 hits in 1163 CRISPR screens.
DR ChiTaRS; SNX9; human.
DR EvolutionaryTrace; Q9Y5X1; -.
DR GeneWiki; SNX9; -.
DR GenomeRNAi; 51429; -.
DR Pharos; Q9Y5X1; Tbio.
DR PRO; PR:Q9Y5X1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y5X1; Protein.
DR Bgee; ENSG00000130340; Expressed in cartilage tissue and 185 other cell types or tissues.
DR ExpressionAtlas; Q9Y5X1; baseline and differential.
DR Genevisible; Q9Y5X1; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0036089; P:cleavage furrow formation; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0060988; P:lipid tube assembly; IDA:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR CDD; cd07668; BAR_SNX9; 1.
DR CDD; cd07285; PX_SNX9; 1.
DR CDD; cd11898; SH3_SNX9; 1.
DR DisProt; DP02304; -.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037425; SNX9_BAR.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR037426; SNX9_PX.
DR InterPro; IPR035558; SNX9_SH3.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827; SORTING NEXIN; 1.
DR PANTHER; PTHR45827:SF2; SORTING NEXIN-9; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cell membrane;
KW Cell projection; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW Golgi apparatus; Lipid-binding; Membrane; Mitosis; Phosphoprotein;
KW Protein transport; Reference proteome; SH3 domain; Transport;
KW Ubl conjugation.
FT CHAIN 1..595
FT /note="Sorting nexin-9"
FT /id="PRO_0000213852"
FT DOMAIN 1..62
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 250..361
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 392..595
FT /note="BAR"
FT REGION 91..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..213
FT /note="Critical for tubulation activity"
FT COMPBIAS 91..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000269|PubMed:17948057,
FT ECO:0007744|PDB:2RAK"
FT BINDING 288
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000269|PubMed:17948057,
FT ECO:0007744|PDB:2RAK"
FT BINDING 327
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000269|PubMed:17948057,
FT ECO:0007744|PDB:2RAK"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91VH2"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 287
FT /note="Y->A: Abolishes membrane tubulation activity.
FT Abolishes binding to phosphatidylinositol 3-phosphate, but
FT not to phosphatidylinositol 4,5-bisphosphate; when
FT associated with A-313."
FT /evidence="ECO:0000269|PubMed:17948057"
FT MUTAGEN 313
FT /note="K->A: Abolishes binding to phosphatidylinositol 3-
FT phosphate, but not to phosphatidylinositol 4,5-
FT bisphosphate; when associated with A-287."
FT /evidence="ECO:0000269|PubMed:17948057"
FT MUTAGEN 363
FT /note="K->E: Strongly reduced membrane binding."
FT /evidence="ECO:0000269|PubMed:17948057"
FT MUTAGEN 366..367
FT /note="KR->EE: Loss of membrane binding."
FT /evidence="ECO:0000269|PubMed:17948057"
FT MUTAGEN 522
FT /note="K->E: Abolishes membrane tubulation activity; when
FT associated with E-528."
FT /evidence="ECO:0000269|PubMed:17948057"
FT MUTAGEN 528
FT /note="K->E: Abolishes membrane tubulation activity; when
FT associated with E-522."
FT /evidence="ECO:0000269|PubMed:17948057"
FT CONFLICT 89
FT /note="Q -> H (in Ref. 5; AAH05022)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7OJ9"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:7OJ9"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:7OJ9"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:7OJ9"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:7OJ9"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:7OJ9"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7OJ9"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3LGE"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:3LGE"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:2RAJ"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3DYT"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:3DYT"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3DYT"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3DYT"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:2RAK"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:3DYT"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:2RAJ"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:3DYT"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 324..339
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 376..382
FT /evidence="ECO:0007829|PDB:3DYT"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 392..428
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 430..450
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 458..480
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 486..500
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 503..518
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 520..525
FT /evidence="ECO:0007829|PDB:3DYT"
FT HELIX 531..590
FT /evidence="ECO:0007829|PDB:3DYT"
SQ 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
//
