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Q9Y5X1 (SNX9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sorting nexin-9
Alternative name(s):
SH3 and PX domain-containing protein 1
Short name=Protein SDP1
SH3 and PX domain-containing protein 3A
Gene names
Name:SNX9
Synonyms:SH3PX1, SH3PXD3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.17 Ref.18 Ref.20 Ref.21

Subunit structure

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. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.21 Ref.22

Subcellular location

Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleclathrin-coated vesicle. Golgi apparatustrans-Golgi network. Cell projectionruffle. 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 Ref.20 Ref.21

Tissue specificity

Widely expressed, with highest levels in heart and placenta, and lowest levels in thymus and peripheral blood leukocytes. Ref.2

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. Ref.21

Post-translational modification

Ubiquitinated by ITCH. Ref.16

Phosphorylated on tyrosine residues by TNK2. Phosphorylation promotes its activity in the degradation of EGFR. Ref.7 Ref.11

Sequence similarities

Belongs to the sorting nexin family.

Contains 1 BAR domain.

Contains 1 PX (phox homology) domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Endocytosis
Mitosis
Protein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
   DomainSH3 domain
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcleavage furrow formation

Inferred from mutant phenotype Ref.20. Source: UniProtKB

endocytosis

Inferred from mutant phenotype Ref.20. Source: UniProtKB

endosomal transport

Inferred from mutant phenotype Ref.20. Source: UniProtKB

intracellular protein transport

Inferred from mutant phenotype Ref.10. Source: UniProtKB

lipid tube assembly

Inferred from direct assay Ref.21. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cytokinesis

Inferred from mutant phenotype Ref.20. Source: UniProtKB

positive regulation of GTPase activity

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of protein oligomerization

Inferred from direct assay Ref.10. Source: UniProtKB

receptor-mediated endocytosis

Inferred from mutant phenotype Ref.10. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

clathrin-coated vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic membrane-bounded vesicle

Inferred from direct assay Ref.10Ref.20. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from direct assay Ref.21. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_function1-phosphatidylinositol binding

Inferred from direct assay Ref.21. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.21. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 595595Sorting nexin-9
PRO_0000213852

Regions

Domain1 – 6262SH3
Domain250 – 361112PX
Domain392 – 595204BAR
Region201 – 21313Critical for tubulation activity

Sites

Binding site2861Phosphatidylinositol 4,5-bisphosphate
Binding site2881Phosphatidylinositol 4,5-bisphosphate
Binding site3131Phosphatidylinositol 4,5-bisphosphate
Binding site3271Phosphatidylinositol 4,5-bisphosphate

Amino acid modifications

Modified residue2391Phosphotyrosine By similarity
Modified residue2881N6-acetyllysine Ref.15

Experimental info

Mutagenesis2871Y → A: Abolishes membrane tubulation activity. Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-313. Ref.21
Mutagenesis3131K → A: Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-287. Ref.21
Mutagenesis3631K → E: Strongly reduced membrane binding. Ref.21
Mutagenesis366 – 3672KR → EE: Loss of membrane binding.
Mutagenesis5221K → E: Abolishes membrane tubulation activity; when associated with E-528. Ref.21
Mutagenesis5281K → E: Abolishes membrane tubulation activity; when associated with E-522. Ref.21
Sequence conflict891Q → H in AAH05022. Ref.5

Secondary structure

.................................................. 595
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y5X1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 963892AC1A5A9227

FASTA59566,592
        10         20         30         40         50         60 
MATKARVMYD FAAEPGNNEL TVNEGEIITI TNPDVGGGWL EGRNIKGERG LVPTDYVEIL 

        70         80         90        100        110        120 
PSDGKDQFSC GNSVADQAFL DSLSASTAQA SSSAASNNHQ VGSGNDPWSA WSASKSGNWE 

       130        140        150        160        170        180 
SSEGWGAQPE GAGAQRNTNT PNNWDTAFGH PQAYQGPATG DDDDWDEDWD GPKSSSYFKD 

       190        200        210        220        230        240 
SESADAGGAQ RGNSRASSSS MKIPLNKFPG FAKPGTEQYL LAKQLAKPKE KIPIIVGDYG 

       250        260        270        280        290        300 
PMWVYPTSTF DCVVADPRKG SKMYGLKSYI EYQLTPTNTN RSVNHRYKHF DWLYERLLVK 

       310        320        330        340        350        360 
FGSAIPIPSL PDKQVTGRFE EEFIKMRMER LQAWMTRMCR HPVISESEVF QQFLNFRDEK 

       370        380        390        400        410        420 
EWKTGKRKAE RDELAGVMIF STMEPEAPDL DLVEIEQKCE AVGKFTKAMD DGVKELLTVG 

       430        440        450        460        470        480 
QEHWKRCTGP LPKEYQKIGK ALQSLATVFS SSGYQGETDL NDAITEAGKT YEEIASLVAE 

       490        500        510        520        530        540 
QPKKDLHFLM ECNHEYKGFL GCFPDIIGTH KGAIEKVKES DKLVATSKIT LQDKQNMVKR 

       550        560        570        580        590 
VSIMSYALQA EMNHFHSNRI YDYNSVIRLY LEQQVQFYET IAEKLRQALS RFPVM 

« Hide

References

« Hide 'large scale' references
[1]"A large family of endosome-localized proteins related to sorting nexin 1."
Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.
Biochem. J. 358:7-16(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1."
Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.
J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADAM9 AND ADAM15, TISSUE SPECIFICITY.
[3]"Identification of differentially expressed genes in matched prostate cancer and normal epithelial cell lines."
Zhang J.S., Smith D.I.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney and Skin.
[6]"Human SDP1."
Ramanathan G., Subramaniam V.N., Hong W.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 201-595.
[7]"The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation."
Lin Q., Lo C.G., Cerione R.A., Yang W.
J. Biol. Chem. 277:10134-10138(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TNK2, IDENTIFICATION IN A COMPLEX WITH TNK2 AND CLATHRIN HEAVY CHAIN, TYROSINE PHOSPHORYLATION.
[8]"Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components."
Lundmark R., Carlsson S.R.
J. Biol. Chem. 278:46772-46781(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNM2 AND THE AP-2 COMPLEX, IDENTIFICATION IN A COMPLEX WITH THE AP-2 COMPLEX; CLATHRIN AND DNM2, SUBCELLULAR LOCATION.
[9]"SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector ACK1."
Yeow-Fong L., Lim L., Manser E.
FEBS Lett. 579:5040-5048(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNK2, SUBCELLULAR LOCATION.
[10]"SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis."
Soulet F., Yarar D., Leonard M., Schmid S.L.
Mol. Biol. Cell 16:2058-2067(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DNM1 AND DNM2.
[11]"Dimerization is required for SH3PX1 tyrosine phosphorylation in response to epidermal growth factor signalling and interaction with ACK2."
Childress C., Lin Q., Yang W.
Biochem. J. 394:693-698(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, TYROSINE PHOSPHORYLATION.
[12]"SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis."
Yarar D., Waterman-Storer C.M., Schmid S.L.
Dev. Cell 13:43-56(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH WASL, SUBCELLULAR LOCATION, SUBUNIT, PHOSPHATIDYLINOSITOL 4,5-BISPHOSPATE BINDING.
[13]"SNX9 regulates tubular invagination of the plasma membrane through interaction with actin cytoskeleton and dynamin 2."
Shin N., Ahn N., Chang-Ileto B., Park J., Takei K., Ahn S.G., Kim S.A., Di Paolo G., Chang S.
J. Cell Sci. 121:1252-1263(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARP3; WASL AND DNM2.
[14]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"The E3 ubiquitin ligase Itch regulates sorting nexin 9 through an unconventional substrate recognition domain."
Baumann C., Lindholm C.K., Rimoldi D., Levy F.
FEBS J. 277:2803-2814(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITCH, UBIQUITINATION BY ITCH.
[17]"SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane."
Park J., Kim Y., Lee S., Park J.J., Park Z.Y., Sun W., Kim H., Chang S.
J. Cell Sci. 123:1742-1750(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[18]"The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome formation by SNX-PX-BAR proteins."
Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S., Teasdale R.D.
PLoS ONE 5:E13763-E13763(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"SNX9, SNX18 and SNX33 are required for progression through and completion of mitosis."
Ma M.P., Chircop M.
J. Cell Sci. 125:4372-4382(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[21]"The PX-BAR membrane-remodeling unit of sorting nexin 9."
Pylypenko O., Lundmark R., Rasmuson E., Carlsson S.R., Rak A.
EMBO J. 26:4788-4800(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 204-595 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE, FUNCTION, SUBUNIT, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-287; LYS-313; LYS-363; 366-LYS-ARG-367; LYS-522 AND LYS-528.
[22]"Structure and plasticity of Endophilin and Sorting Nexin 9."
Wang Q., Kaan H.Y., Hooda R.N., Goh S.L., Sondermann H.
Structure 16:1574-1587(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 230-595, SUBUNIT.
[23]"Mechanism of aldolase control of sorting nexin 9 function in endocytosis."
Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.
J. Biol. Chem. 285:11983-11990(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 152-182 IN COMPLEX WITH ALDOA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF121859 mRNA. Translation: AAD27832.1.
AF131214 mRNA. Translation: AAF04473.1.
AF172847 mRNA. Translation: AAL54871.1.
AL035634, AL139330, AL391863 Genomic DNA. Translation: CAI20465.1.
AL139330, AL035634, AL391863 Genomic DNA. Translation: CAI12979.1.
AL391863, AL035634, AL139330 Genomic DNA. Translation: CAI15180.1.
BC001084 mRNA. Translation: AAH01084.3.
BC005022 mRNA. Translation: AAH05022.1.
AF076957 mRNA. Translation: AAD43001.1.
RefSeqNP_057308.1. NM_016224.4.
UniGeneHs.191213.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RAIX-ray3.20A/B204-595[»]
2RAJX-ray2.45A204-595[»]
2RAKX-ray3.00A204-595[»]
3DYTX-ray2.08A230-595[»]
3DYUX-ray4.10A/B/C230-595[»]
3LGEX-ray2.20E/F/G/H152-182[»]
ProteinModelPortalQ9Y5X1.
SMRQ9Y5X1. Positions 1-70, 214-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119535. 20 interactions.
DIPDIP-30997N.
IntActQ9Y5X1. 21 interactions.
MINTMINT-108846.
STRING9606.ENSP00000376024.

PTM databases

PhosphoSiteQ9Y5X1.

Polymorphism databases

DMDM12643956.

Proteomic databases

PaxDbQ9Y5X1.
PeptideAtlasQ9Y5X1.
PRIDEQ9Y5X1.

Protocols and materials databases

DNASU51429.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392185; ENSP00000376024; ENSG00000130340.
GeneID51429.
KEGGhsa:51429.
UCSCuc003qqv.1. human.

Organism-specific databases

CTD51429.
GeneCardsGC06P158153.
HGNCHGNC:14973. SNX9.
HPAHPA031410.
MIM605952. gene.
neXtProtNX_Q9Y5X1.
PharmGKBPA37949.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5391.
HOGENOMHOG000261633.
HOVERGENHBG009996.
InParanoidQ9Y5X1.
KOK17923.
OMADPWSAWN.
OrthoDBEOG7GTT36.
PhylomeDBQ9Y5X1.
TreeFamTF314082.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
SignaLinkQ9Y5X1.

Gene expression databases

ArrayExpressQ9Y5X1.
BgeeQ9Y5X1.
CleanExHS_SNX9.
GenevestigatorQ9Y5X1.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR001683. Phox.
IPR001452. SH3_domain.
IPR028644. SNX9.
IPR014536. Snx9_subfam.
IPR019497. Sorting_nexin_WASP-bd-dom.
[Graphical view]
PANTHERPTHR10555:SF14. PTHR10555:SF14. 1 hit.
PfamPF10456. BAR_3_WASP_bdg. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFPIRSF027744. Snx9. 1 hit.
SMARTSM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNX9. human.
EvolutionaryTraceQ9Y5X1.
GeneWikiSNX9.
GenomeRNAi51429.
NextBio54991.
PROQ9Y5X1.
SOURCESearch...

Entry information

Entry nameSNX9_HUMAN
AccessionPrimary (citable) accession number: Q9Y5X1
Secondary accession number(s): Q9BSI7 expand/collapse secondary AC list , Q9BVM1, Q9UJH6, Q9UP20
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM