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Q9D8U8

- SNX5_MOUSE

UniProt

Q9D8U8 - SNX5_MOUSE

Protein

Sorting nexin-5

Gene

Snx5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    May be involved in several stages of intracellular trafficking. Plays a role in macropinocytosis. Plays a role in the internalization of EGFR after EGF stimulation By similarity.By similarity

    GO - Molecular functioni

    1. phosphatidylinositol binding Source: UniProtKB

    GO - Biological processi

    1. intracellular protein transport Source: RefGenome
    2. pinocytosis Source: UniProtKB

    Keywords - Biological processi

    Endocytosis, Protein transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sorting nexin-5
    Gene namesi
    Name:Snx5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1916428. Snx5.

    Subcellular locationi

    Early endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasm 1 Publication. Cell projectionphagocytic cup 1 Publication. Cell projectionruffle By similarity
    Note: Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2). Targeted to membrane ruffles in response to EGFR stimulation By similarity. Detected on macropinosomes.By similarity

    GO - Cellular componenti

    1. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    2. early endosome membrane Source: UniProtKB-SubCell
    3. endosome Source: RefGenome
    4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    5. extrinsic component of endosome membrane Source: UniProtKB
    6. macropinocytic cup Source: UniProtKB
    7. phagocytic cup Source: UniProtKB-SubCell
    8. ruffle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 404403Sorting nexin-5PRO_0000213845Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei275 – 2751N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9D8U8.
    PaxDbiQ9D8U8.
    PRIDEiQ9D8U8.

    PTM databases

    PhosphoSiteiQ9D8U8.

    Expressioni

    Tissue specificityi

    Detected in macrophages (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9D8U8.
    BgeeiQ9D8U8.
    CleanExiMM_SNX5.
    GenevestigatoriQ9D8U8.

    Interactioni

    Subunit structurei

    Interacts with SNX1; this promotes location at the endosome membrane.By similarity

    Protein-protein interaction databases

    IntActiQ9D8U8. 1 interaction.
    MINTiMINT-1751142.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D8U8.
    SMRiQ9D8U8. Positions 20-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 172148PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini202 – 404203BARAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 467Phosphatidylinositol bisphosphate bindingBy similarity
    Regioni99 – 1057Phosphatidylinositol bisphosphate bindingBy similarity
    Regioni113 – 1164Phosphatidylinositol bisphosphate bindingBy similarity

    Domaini

    The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG255198.
    GeneTreeiENSGT00740000115413.
    HOGENOMiHOG000231691.
    HOVERGENiHBG000716.
    InParanoidiQ9D8U8.
    KOiK17920.
    OMAiIKDSCAK.
    OrthoDBiEOG7X0VH4.
    PhylomeDBiQ9D8U8.
    TreeFamiTF313698.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001683. Phox.
    IPR028654. SNX5.
    IPR014637. SNX5/SNX6/SNX32.
    IPR015404. Vps5_C.
    [Graphical view]
    PANTHERiPTHR10555:SF6. PTHR10555:SF6. 1 hit.
    PfamiPF00787. PX. 1 hit.
    PF09325. Vps5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
    SMARTiSM00312. PX. 1 hit.
    [Graphical view]
    SUPFAMiSSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9D8U8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVPELLEQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH    50
    TKTTLSTFQS PEFSVTRQHE DFVWLHDTLT ETTDYAGLII PPAPTKPDFD 100
    GPREKMQKLG EGEGSMTKEE FAKMKQELEA EYLAVFKKTV STHEVFLQRL 150
    SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK EMFGGFFKSV VKSADEVLFS 200
    GVKEVDDFFE QEKNFLINYY NRIKDSCAKA DKMTRSHKNV ADDYIHTAAC 250
    LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML 300
    NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE THQQECCQKF 350
    EQLSESAKEE LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL 400
    FKNN 404
    Length:404
    Mass (Da):46,797
    Last modified:June 1, 2001 - v1
    Checksum:iC24D8C78F753FAFC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK007676 mRNA. Translation: BAB25180.1.
    AK029463 mRNA. Translation: BAC26460.1.
    AK031873 mRNA. Translation: BAC27587.1.
    AK049129 mRNA. Translation: BAC33558.1.
    AK159904 mRNA. Translation: BAE35468.1.
    AK169786 mRNA. Translation: BAE41365.1.
    BC002242 mRNA. Translation: AAH02242.1.
    CCDSiCCDS16815.1.
    RefSeqiNP_001186117.1. NM_001199188.1.
    NP_077187.1. NM_024225.5.
    UniGeneiMm.273379.

    Genome annotation databases

    EnsembliENSMUST00000028909; ENSMUSP00000028909; ENSMUSG00000027423.
    ENSMUST00000110030; ENSMUSP00000105657; ENSMUSG00000027423.
    GeneIDi69178.
    KEGGimmu:69178.
    UCSCiuc008mqq.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK007676 mRNA. Translation: BAB25180.1 .
    AK029463 mRNA. Translation: BAC26460.1 .
    AK031873 mRNA. Translation: BAC27587.1 .
    AK049129 mRNA. Translation: BAC33558.1 .
    AK159904 mRNA. Translation: BAE35468.1 .
    AK169786 mRNA. Translation: BAE41365.1 .
    BC002242 mRNA. Translation: AAH02242.1 .
    CCDSi CCDS16815.1.
    RefSeqi NP_001186117.1. NM_001199188.1.
    NP_077187.1. NM_024225.5.
    UniGenei Mm.273379.

    3D structure databases

    ProteinModelPortali Q9D8U8.
    SMRi Q9D8U8. Positions 20-174.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9D8U8. 1 interaction.
    MINTi MINT-1751142.

    PTM databases

    PhosphoSitei Q9D8U8.

    Proteomic databases

    MaxQBi Q9D8U8.
    PaxDbi Q9D8U8.
    PRIDEi Q9D8U8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028909 ; ENSMUSP00000028909 ; ENSMUSG00000027423 .
    ENSMUST00000110030 ; ENSMUSP00000105657 ; ENSMUSG00000027423 .
    GeneIDi 69178.
    KEGGi mmu:69178.
    UCSCi uc008mqq.3. mouse.

    Organism-specific databases

    CTDi 27131.
    MGIi MGI:1916428. Snx5.

    Phylogenomic databases

    eggNOGi NOG255198.
    GeneTreei ENSGT00740000115413.
    HOGENOMi HOG000231691.
    HOVERGENi HBG000716.
    InParanoidi Q9D8U8.
    KOi K17920.
    OMAi IKDSCAK.
    OrthoDBi EOG7X0VH4.
    PhylomeDBi Q9D8U8.
    TreeFami TF313698.

    Miscellaneous databases

    ChiTaRSi SNX5. mouse.
    NextBioi 328774.
    PROi Q9D8U8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D8U8.
    Bgeei Q9D8U8.
    CleanExi MM_SNX5.
    Genevestigatori Q9D8U8.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    IPR028654. SNX5.
    IPR014637. SNX5/SNX6/SNX32.
    IPR015404. Vps5_C.
    [Graphical view ]
    PANTHERi PTHR10555:SF6. PTHR10555:SF6. 1 hit.
    Pfami PF00787. PX. 1 hit.
    PF09325. Vps5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036924. Snx5_Snx6. 1 hit.
    SMARTi SM00312. PX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Head, Medulla oblongata, Pancreas and Thymus.
    2. "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].
    3. "A role for SNX5 in the regulation of macropinocytosis."
      Lim J.P., Wang J.T., Kerr M.C., Teasdale R.D., Gleeson P.A.
      BMC Cell Biol. 9:58-58(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiSNX5_MOUSE
    AccessioniPrimary (citable) accession number: Q9D8U8
    Secondary accession number(s): Q543N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    The selectivity for particular phosphatidylinositol lipids is under debate. According to one report (PubMed:19553671), the rat protein binds exclusively to phosphatidylinositol 4,5-bisphosphate, while the human protein has been reported (PubMed:15561769) to bind to phosphatidylinositol 3,4-bisphosphate and also to phosphatidylinositol 3-phosphate.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3