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Q9Y5X1

- SNX9_HUMAN

UniProt

Q9Y5X1 - SNX9_HUMAN

Protein

Sorting nexin-9

Gene

SNX9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    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.9 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei286 – 2861Phosphatidylinositol 4,5-bisphosphate
    Binding sitei288 – 2881Phosphatidylinositol 4,5-bisphosphate
    Binding sitei313 – 3131Phosphatidylinositol 4,5-bisphosphate
    Binding sitei327 – 3271Phosphatidylinositol 4,5-bisphosphate

    GO - Molecular functioni

    1. 1-phosphatidylinositol binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. cleavage furrow formation Source: UniProtKB
    2. endocytosis Source: UniProtKB
    3. endosomal transport Source: UniProtKB
    4. intracellular protein transport Source: UniProtKB
    5. lipid tube assembly Source: UniProtKB
    6. mitotic cytokinesis Source: UniProtKB
    7. mitotic nuclear division Source: UniProtKB-KW
    8. positive regulation of GTPase activity Source: UniProtKB
    9. positive regulation of protein oligomerization Source: UniProtKB
    10. receptor-mediated endocytosis Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Endocytosis, Mitosis, Protein transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.
    SignaLinkiQ9Y5X1.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:SNX9
    Synonyms:SH3PX1, SH3PXD3A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:14973. SNX9.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. cytoplasmic membrane-bounded vesicle Source: UniProtKB
    4. cytoplasmic vesicle membrane Source: UniProtKB
    5. endosome Source: RefGenome
    6. extracellular vesicular exosome Source: UniProt
    7. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    8. plasma membrane Source: HPA
    9. ruffle Source: UniProtKB-SubCell
    10. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi287 – 2871Y → A: Abolishes membrane tubulation activity. Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-313. 1 Publication
    Mutagenesisi313 – 3131K → A: Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-287. 1 Publication
    Mutagenesisi363 – 3631K → E: Strongly reduced membrane binding. 1 Publication
    Mutagenesisi366 – 3672KR → EE: Loss of membrane binding.
    Mutagenesisi522 – 5221K → E: Abolishes membrane tubulation activity; when associated with E-528. 1 Publication
    Mutagenesisi528 – 5281K → E: Abolishes membrane tubulation activity; when associated with E-522. 1 Publication

    Organism-specific databases

    PharmGKBiPA37949.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 595595Sorting nexin-9PRO_0000213852Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei239 – 2391PhosphotyrosineBy similarity
    Modified residuei288 – 2881N6-acetyllysine1 Publication

    Post-translational modificationi

    Ubiquitinated by ITCH.1 Publication
    Phosphorylated on tyrosine residues by TNK2. Phosphorylation promotes its activity in the degradation of EGFR.

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y5X1.
    PaxDbiQ9Y5X1.
    PeptideAtlasiQ9Y5X1.
    PRIDEiQ9Y5X1.

    PTM databases

    PhosphoSiteiQ9Y5X1.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest levels in heart and placenta, and lowest levels in thymus and peripheral blood leukocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y5X1.
    BgeeiQ9Y5X1.
    CleanExiHS_SNX9.
    GenevestigatoriQ9Y5X1.

    Organism-specific databases

    HPAiHPA031410.

    Interactioni

    Subunit structurei

    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.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAM15Q134442EBI-77848,EBI-77818
    ATRAIDQ6UW562EBI-77848,EBI-723802
    DNM2P505702EBI-77848,EBI-346547
    espFB7UM884EBI-77848,EBI-2529480From a different organism.
    FASLGP480232EBI-77848,EBI-495538
    ITCHQ96J027EBI-77848,EBI-1564678
    SNX33Q8WV412EBI-77848,EBI-2481535
    SOS1Q078892EBI-77848,EBI-297487
    SOS2Q078902EBI-77848,EBI-298181
    TNK2Q17R135EBI-77848,EBI-457220From a different organism.
    UBCP0CG482EBI-77848,EBI-3390054
    WASLO004012EBI-77848,EBI-957615

    Protein-protein interaction databases

    BioGridi119535. 19 interactions.
    DIPiDIP-30997N.
    IntActiQ9Y5X1. 23 interactions.
    MINTiMINT-108846.
    STRINGi9606.ENSP00000376024.

    Structurei

    Secondary structure

    1
    595
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni167 – 1693
    Helixi215 – 2217
    Beta strandi232 – 2376
    Beta strandi240 – 2434
    Beta strandi252 – 2554
    Helixi257 – 2593
    Beta strandi260 – 2623
    Beta strandi263 – 2664
    Beta strandi271 – 2766
    Turni277 – 2793
    Beta strandi283 – 2864
    Helixi287 – 30115
    Turni302 – 3043
    Helixi324 – 33916
    Helixi344 – 3463
    Helixi348 – 3558
    Helixi359 – 37012
    Helixi376 – 3827
    Beta strandi383 – 3875
    Helixi392 – 42837
    Helixi430 – 45021
    Helixi455 – 4573
    Helixi458 – 48023
    Helixi482 – 4843
    Helixi486 – 50015
    Helixi503 – 51816
    Helixi520 – 5256
    Helixi531 – 59060

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ9Y5X1.
    SMRiQ9Y5X1. Positions 1-70, 214-595.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5X1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6262SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini250 – 361112PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini392 – 595204BARAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni201 – 21313Critical for tubulation activityAdd
    BLAST

    Domaini

    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.1 Publication

    Sequence similaritiesi

    Belongs to the sorting nexin family.Curated
    Contains 1 BAR domain.Curated
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiCOG5391.
    HOGENOMiHOG000261633.
    HOVERGENiHBG009996.
    InParanoidiQ9Y5X1.
    KOiK17923.
    OMAiDPWSAWN.
    OrthoDBiEOG7GTT36.
    PhylomeDBiQ9Y5X1.
    TreeFamiTF314082.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001683. Phox.
    IPR001452. SH3_domain.
    IPR028644. SNX9.
    IPR014536. Snx9_subfam.
    IPR019497. Sorting_nexin_WASP-bd-dom.
    [Graphical view]
    PANTHERiPTHR10555:SF14. PTHR10555:SF14. 1 hit.
    PfamiPF10456. BAR_3_WASP_bdg. 1 hit.
    PF00787. PX. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027744. Snx9. 1 hit.
    SMARTiSM00312. PX. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y5X1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATKARVMYD FAAEPGNNEL TVNEGEIITI TNPDVGGGWL EGRNIKGERG    50
    LVPTDYVEIL PSDGKDQFSC GNSVADQAFL DSLSASTAQA SSSAASNNHQ 100
    VGSGNDPWSA WSASKSGNWE SSEGWGAQPE GAGAQRNTNT PNNWDTAFGH 150
    PQAYQGPATG DDDDWDEDWD GPKSSSYFKD SESADAGGAQ RGNSRASSSS 200
    MKIPLNKFPG FAKPGTEQYL LAKQLAKPKE KIPIIVGDYG PMWVYPTSTF 250
    DCVVADPRKG SKMYGLKSYI EYQLTPTNTN RSVNHRYKHF DWLYERLLVK 300
    FGSAIPIPSL PDKQVTGRFE EEFIKMRMER LQAWMTRMCR HPVISESEVF 350
    QQFLNFRDEK EWKTGKRKAE RDELAGVMIF STMEPEAPDL DLVEIEQKCE 400
    AVGKFTKAMD DGVKELLTVG QEHWKRCTGP LPKEYQKIGK ALQSLATVFS 450
    SSGYQGETDL NDAITEAGKT YEEIASLVAE QPKKDLHFLM ECNHEYKGFL 500
    GCFPDIIGTH KGAIEKVKES DKLVATSKIT LQDKQNMVKR VSIMSYALQA 550
    EMNHFHSNRI YDYNSVIRLY LEQQVQFYET IAEKLRQALS RFPVM 595
    Length:595
    Mass (Da):66,592
    Last modified:November 1, 1999 - v1
    Checksum:i963892AC1A5A9227
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891Q → H in AAH05022. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS5253.1.
    RefSeqiNP_057308.1. NM_016224.4.
    UniGeneiHs.191213.

    Genome annotation databases

    EnsembliENST00000392185; ENSP00000376024; ENSG00000130340.
    GeneIDi51429.
    KEGGihsa:51429.
    UCSCiuc003qqv.1. human.

    Polymorphism databases

    DMDMi12643956.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS5253.1.
    RefSeqi NP_057308.1. NM_016224.4.
    UniGenei Hs.191213.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RAI X-ray 3.20 A/B 204-595 [» ]
    2RAJ X-ray 2.45 A 204-595 [» ]
    2RAK X-ray 3.00 A 204-595 [» ]
    3DYT X-ray 2.08 A 230-595 [» ]
    3DYU X-ray 4.10 A/B/C 230-595 [» ]
    3LGE X-ray 2.20 E/F/G/H 152-182 [» ]
    ProteinModelPortali Q9Y5X1.
    SMRi Q9Y5X1. Positions 1-70, 214-595.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119535. 19 interactions.
    DIPi DIP-30997N.
    IntActi Q9Y5X1. 23 interactions.
    MINTi MINT-108846.
    STRINGi 9606.ENSP00000376024.

    PTM databases

    PhosphoSitei Q9Y5X1.

    Polymorphism databases

    DMDMi 12643956.

    Proteomic databases

    MaxQBi Q9Y5X1.
    PaxDbi Q9Y5X1.
    PeptideAtlasi Q9Y5X1.
    PRIDEi Q9Y5X1.

    Protocols and materials databases

    DNASUi 51429.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392185 ; ENSP00000376024 ; ENSG00000130340 .
    GeneIDi 51429.
    KEGGi hsa:51429.
    UCSCi uc003qqv.1. human.

    Organism-specific databases

    CTDi 51429.
    GeneCardsi GC06P158153.
    HGNCi HGNC:14973. SNX9.
    HPAi HPA031410.
    MIMi 605952. gene.
    neXtProti NX_Q9Y5X1.
    PharmGKBi PA37949.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5391.
    HOGENOMi HOG000261633.
    HOVERGENi HBG009996.
    InParanoidi Q9Y5X1.
    KOi K17923.
    OMAi DPWSAWN.
    OrthoDBi EOG7GTT36.
    PhylomeDBi Q9Y5X1.
    TreeFami TF314082.

    Enzyme and pathway databases

    Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.
    SignaLinki Q9Y5X1.

    Miscellaneous databases

    ChiTaRSi SNX9. human.
    EvolutionaryTracei Q9Y5X1.
    GeneWikii SNX9.
    GenomeRNAii 51429.
    NextBioi 54991.
    PROi Q9Y5X1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5X1.
    Bgeei Q9Y5X1.
    CleanExi HS_SNX9.
    Genevestigatori Q9Y5X1.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    IPR001452. SH3_domain.
    IPR028644. SNX9.
    IPR014536. Snx9_subfam.
    IPR019497. Sorting_nexin_WASP-bd-dom.
    [Graphical view ]
    PANTHERi PTHR10555:SF14. PTHR10555:SF14. 1 hit.
    Pfami PF10456. BAR_3_WASP_bdg. 1 hit.
    PF00787. PX. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF027744. Snx9. 1 hit.
    SMARTi SM00312. PX. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiSNX9_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5X1
    Secondary accession number(s): Q9BSI7
    , Q9BVM1, Q9UJH6, Q9UP20
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3