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Q9Y5X3

- SNX5_HUMAN

UniProt

Q9Y5X3 - SNX5_HUMAN

Protein

Sorting nexin-5

Gene

SNX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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.2 Publications

    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

    Enzyme and pathway databases

    ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sorting nexin-5
    Gene namesi
    Name:SNX5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:14969. SNX5.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37945.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 404403Sorting nexin-5PRO_0000213844Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei275 – 2751N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y5X3.
    PaxDbiQ9Y5X3.
    PRIDEiQ9Y5X3.

    PTM databases

    PhosphoSiteiQ9Y5X3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y5X3.
    BgeeiQ9Y5X3.
    CleanExiHS_SNX5.
    GenevestigatoriQ9Y5X3.

    Organism-specific databases

    HPAiCAB020679.

    Interactioni

    Subunit structurei

    Interacts with SNX1; this promotes location at the endosome membrane.2 Publications

    Protein-protein interaction databases

    BioGridi118022. 23 interactions.
    IntActiQ9Y5X3. 17 interactions.
    MINTiMINT-2823978.
    STRINGi9606.ENSP00000366988.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SYSX-ray2.40C257-265[»]
    ProteinModelPortaliQ9Y5X3.
    SMRiQ9Y5X3. Positions 20-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5X3.

    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.
    HOVERGENiHBG000716.
    InParanoidiQ9Y5X3.
    KOiK17920.
    OMAiIKDSCAK.
    OrthoDBiEOG7X0VH4.
    PhylomeDBiQ9Y5X3.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y5X3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH    50
    TKTTLPTFQS PEFSVTRQHE DFVWLHDTLI ETTDYAGLII PPAPTKPDFD 100
    GPREKMQKLG EGEGSMTKEE FAKMKQELEA EYLAVFKKTV SSHEVFLQRL 150
    SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK EMFGGFFKSV VKSADEVLFT 200
    GVKEVDDFFE QEKNFLINYY NRIKDSCVKA DKMTRSHKNV ADDYIHTAAC 250
    LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML 300
    NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE AHQQECCQKF 350
    EQLSESAKEE LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL 400
    FKNN 404
    Length:404
    Mass (Da):46,816
    Last modified:November 1, 1999 - v1
    Checksum:i87A85620AF827EC6
    GO
    Isoform 2 (identifier: Q9Y5X3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         18-126: LRSVSVDLNV...TKEEFAKMKQ → VRSSQPQTPG...FFLKLSSASW
         127-404: Missing.

    Show »
    Length:126
    Mass (Da):13,349
    Checksum:iF04391B429CE2D7A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti279 – 2791V → L(PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei18 – 126109LRSVS…AKMKQ → VRSSQPQTPGRAALRAPGSL HSFPCASIGRGCSPPSPARE APVRPGRPLSLVFTEGCPGE SLWMSRILLGQNQRRGTLAP AQAPVPSGLGEMISGDPGMF FLKLSSASW in isoform 2. 2 PublicationsVSP_056386Add
    BLAST
    Alternative sequencei127 – 404278Missing in isoform 2. 2 PublicationsVSP_056387Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF121855 mRNA. Translation: AAD27828.1.
    BT007191 mRNA. Translation: AAP35855.1.
    AK001793 mRNA. Translation: BAA91914.1.
    AK123903 mRNA. Translation: BAG53980.1.
    AL121585 Genomic DNA. Translation: CAC00471.1.
    BC000100 mRNA. No translation available.
    CH471133 Genomic DNA. Translation: EAX10264.1.
    CH471133 Genomic DNA. Translation: EAX10265.1.
    CH471133 Genomic DNA. Translation: EAX10266.1.
    CH471133 Genomic DNA. Translation: EAX10268.1.
    BC093623 mRNA. Translation: AAH93623.1.
    BC093980 mRNA. Translation: AAH93980.1.
    BC143274 mRNA. Translation: AAI43275.1.
    CCDSiCCDS13130.1.
    RefSeqiNP_055241.1. NM_014426.3.
    NP_689413.1. NM_152227.2.
    UniGeneiHs.316890.

    Genome annotation databases

    EnsembliENST00000377759; ENSP00000366988; ENSG00000089006.
    ENST00000377768; ENSP00000366998; ENSG00000089006.
    ENST00000606557; ENSP00000475510; ENSG00000089006.
    GeneIDi27131.
    KEGGihsa:27131.
    UCSCiuc002wqc.3. human.

    Polymorphism databases

    DMDMi10720289.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF121855 mRNA. Translation: AAD27828.1 .
    BT007191 mRNA. Translation: AAP35855.1 .
    AK001793 mRNA. Translation: BAA91914.1 .
    AK123903 mRNA. Translation: BAG53980.1 .
    AL121585 Genomic DNA. Translation: CAC00471.1 .
    BC000100 mRNA. No translation available.
    CH471133 Genomic DNA. Translation: EAX10264.1 .
    CH471133 Genomic DNA. Translation: EAX10265.1 .
    CH471133 Genomic DNA. Translation: EAX10266.1 .
    CH471133 Genomic DNA. Translation: EAX10268.1 .
    BC093623 mRNA. Translation: AAH93623.1 .
    BC093980 mRNA. Translation: AAH93980.1 .
    BC143274 mRNA. Translation: AAI43275.1 .
    CCDSi CCDS13130.1.
    RefSeqi NP_055241.1. NM_014426.3.
    NP_689413.1. NM_152227.2.
    UniGenei Hs.316890.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SYS X-ray 2.40 C 257-265 [» ]
    ProteinModelPortali Q9Y5X3.
    SMRi Q9Y5X3. Positions 20-174.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118022. 23 interactions.
    IntActi Q9Y5X3. 17 interactions.
    MINTi MINT-2823978.
    STRINGi 9606.ENSP00000366988.

    PTM databases

    PhosphoSitei Q9Y5X3.

    Polymorphism databases

    DMDMi 10720289.

    Proteomic databases

    MaxQBi Q9Y5X3.
    PaxDbi Q9Y5X3.
    PRIDEi Q9Y5X3.

    Protocols and materials databases

    DNASUi 27131.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377759 ; ENSP00000366988 ; ENSG00000089006 .
    ENST00000377768 ; ENSP00000366998 ; ENSG00000089006 .
    ENST00000606557 ; ENSP00000475510 ; ENSG00000089006 .
    GeneIDi 27131.
    KEGGi hsa:27131.
    UCSCi uc002wqc.3. human.

    Organism-specific databases

    CTDi 27131.
    GeneCardsi GC20M017870.
    HGNCi HGNC:14969. SNX5.
    HPAi CAB020679.
    MIMi 605937. gene.
    neXtProti NX_Q9Y5X3.
    PharmGKBi PA37945.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255198.
    HOVERGENi HBG000716.
    InParanoidi Q9Y5X3.
    KOi K17920.
    OMAi IKDSCAK.
    OrthoDBi EOG7X0VH4.
    PhylomeDBi Q9Y5X3.
    TreeFami TF313698.

    Enzyme and pathway databases

    Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

    Miscellaneous databases

    ChiTaRSi SNX5. human.
    EvolutionaryTracei Q9Y5X3.
    GeneWikii SNX5.
    GenomeRNAii 27131.
    NextBioi 49854.
    PROi Q9Y5X3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5X3.
    Bgeei Q9Y5X3.
    CleanExi HS_SNX5.
    Genevestigatori Q9Y5X3.

    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. "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] (ISOFORM 1), SUBCELLULAR LOCATION.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Ovarian carcinoma.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Brain and Placenta.
    7. "Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation."
      Merino-Trigo A., Kerr M.C., Houghton F., Lindberg A., Mitchell C., Teasdale R.D., Gleeson P.A.
      J. Cell Sci. 117:6413-6424(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL 3,4-BISPHOSPHATE BINDING.
    8. "Visualisation of macropinosome maturation by the recruitment of sorting nexins."
      Kerr M.C., Lindsay M.R., Luetterforst R., Hamilton N., Simpson F., Parton R.G., Gleeson P.A., Teasdale R.D.
      J. Cell Sci. 119:3967-3980(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNX1, SUBCELLULAR LOCATION.
    9. "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.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 257-265 IN COMPLEX WITH HLA CLASS I HISTOCOMPATIBILITY COMPLEX.

    Entry informationi

    Entry nameiSNX5_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5X3
    Secondary accession number(s): B7ZKN3
    , D3DW26, Q52LC4, Q7KZN0, Q9BWP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 124 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

    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.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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