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Q13596

- SNX1_HUMAN

UniProt

Q13596 - SNX1_HUMAN

Protein

Sorting nexin-1

Gene

SNX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (16 Nov 2001)
      Previous versions | rss
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    Functioni

    May be involved in several stages of intracellular trafficking. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei186 – 1861Phosphatidylinositol 3-phosphateBy similarity
    Binding sitei188 – 1881Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei214 – 2141Phosphatidylinositol 3-phosphateBy similarity
    Binding sitei238 – 2381Phosphatidylinositol 3-phosphateBy similarity

    GO - Molecular functioni

    1. phosphatidylinositol binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. early endosome to Golgi transport Source: UniProtKB
    2. endocytosis Source: ProtInc
    3. intracellular protein transport Source: UniProtKB
    4. positive regulation of protein catabolic process Source: Ensembl

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sorting nexin-1
    Gene namesi
    Name:SNX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:11172. SNX1.

    Subcellular locationi

    Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatustrans-Golgi network membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. cytoplasmic membrane-bounded vesicle Source: RefGenome
    3. cytosol Source: Ensembl
    4. early endosome membrane Source: UniProtKB
    5. endosome membrane Source: UniProtKB
    6. Golgi apparatus Source: UniProtKB-SubCell
    7. intracellular membrane-bounded organelle Source: HPA
    8. retromer complex Source: InterPro

    Keywords - Cellular componenti

    Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi214 – 2141K → A: Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location. 2 Publications
    Mutagenesisi429 – 4313KKR → EEE: Loss of endosomal location.

    Organism-specific databases

    PharmGKBiPA36011.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 522522Sorting nexin-1PRO_0000213835Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321Phosphoserine1 Publication
    Modified residuei39 – 391Phosphoserine1 Publication
    Modified residuei188 – 1881Phosphoserine3 Publications
    Modified residuei237 – 2371N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13596.
    PaxDbiQ13596.
    PRIDEiQ13596.

    PTM databases

    PhosphoSiteiQ13596.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13596.
    BgeeiQ13596.
    CleanExiHS_SNX1.
    GenevestigatoriQ13596.

    Organism-specific databases

    HPAiHPA047373.
    HPA052761.

    Interactioni

    Subunit structurei

    Homodimer. Self-assembles into a complex of approximately 300 kDa By similarity. Interacts with HGS By similarity. Component of the retromer complex composed of VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts with SNX6.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi112525. 30 interactions.
    DIPiDIP-398N.
    IntActiQ13596. 10 interactions.
    MINTiMINT-4135098.
    STRINGi9606.ENSP00000369638.

    Structurei

    Secondary structure

    1
    522
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi173 – 1764
    Helixi187 – 19913
    Beta strandi202 – 2054
    Beta strandi210 – 2134
    Beta strandi216 – 2216
    Helixi234 – 25118
    Helixi253 – 2564
    Helixi259 – 2624
    Turni263 – 2664
    Helixi307 – 35650
    Helixi361 – 38525
    Helixi388 – 44053
    Helixi443 – 48341
    Turni484 – 4874
    Helixi489 – 51123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I4KNMR-A142-269[»]
    4FZSX-ray2.80A/B301-522[»]
    ProteinModelPortaliQ13596.
    SMRiQ13596. Positions 142-269, 305-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13596.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini143 – 272130PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini302 – 522221BARAdd
    BLAST

    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

    eggNOGiCOG5391.
    HOVERGENiHBG000618.
    InParanoidiQ13596.
    KOiK17917.
    OMAiEIAEWES.
    OrthoDBiEOG7HHWSB.
    PhylomeDBiQ13596.
    TreeFamiTF313698.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001683. Phox.
    IPR028660. SNX1.
    IPR005329. Sorting_nexin_N.
    IPR015404. Vps5_C.
    [Graphical view]
    PANTHERiPTHR10555:SF129. PTHR10555:SF129. 1 hit.
    PfamiPF00787. PX. 1 hit.
    PF03700. Sorting_nexin. 1 hit.
    PF09325. Vps5. 1 hit.
    [Graphical view]
    SMARTiSM00312. PX. 1 hit.
    [Graphical view]
    SUPFAMiSSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13596-1) [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

    MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA    50
    AVVSKHQSPK ITTSLLPINN GSKENGIHEE QDQEPQDLFA DATVELSLDS 100
    TQNNQKKVLA KTLISLPPQE ATNSSKPQPT YEELEEEEQE DQFDLTVGIT 150
    DPEKIGDGMN AYVAYKVTTQ TSLPLFRSKQ FAVKRRFSDF LGLYEKLSEK 200
    HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA ALERYLQRIV 250
    NHPTMLQDPD VREFLEKEEL PRAVGTQTLS GAGLLKMFNK ATDAVSKMTI 300
    KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTAQFAKS 350
    LAMLGSSEDN TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI 400
    RLLAIVRAAF DQRMKTWQRW QDAQATLQKK REAEARLLWA NKPDKLQQAK 450
    DEILEWESRV TQYERDFERI STVVRKEVIR FEKEKSKDFK NHVIKYLETL 500
    LYSQQQLAKY WEAFLPEAKA IS 522
    Length:522
    Mass (Da):59,070
    Last modified:November 16, 2001 - v3
    Checksum:i6AC8AA0A589513E3
    GO
    Isoform 1A (identifier: Q13596-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         91-155: Missing.

    Show »
    Length:457
    Mass (Da):51,813
    Checksum:i3F844B9E84C258C2
    GO
    Isoform 3 (identifier: Q13596-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         507-522: LAKYWEAFLPEAKAIS → AGEQLGIRSGILLTKKLPRYSKFFSTVHKFCAAASLWKWGFFLSAYLSYLF

    Note: No experimental confirmation available.

    Show »
    Length:557
    Mass (Da):63,082
    Checksum:iA03926548995DDA2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti117 – 1171P → S in AAC17182. (PubMed:9819414)Curated
    Sequence conflicti211 – 2111P → S in AAC17182. (PubMed:9819414)Curated
    Sequence conflicti211 – 2111P → S in AAC17183. (PubMed:9819414)Curated
    Sequence conflicti502 – 5021Y → C in BAC87312. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti115 – 1151S → Y.
    Corresponds to variant rs1049501 [ dbSNP | Ensembl ].
    VAR_052477
    Natural varianti466 – 4661D → N.
    Corresponds to variant rs1802376 [ dbSNP | Ensembl ].
    VAR_034507

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei91 – 15565Missing in isoform 1A. CuratedVSP_006189Add
    BLAST
    Alternative sequencei507 – 52216LAKYW…AKAIS → AGEQLGIRSGILLTKKLPRY SKFFSTVHKFCAAASLWKWG FFLSAYLSYLF in isoform 3. 1 PublicationVSP_044823Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53225 mRNA. Translation: AAA98672.1.
    AF065483 mRNA. Translation: AAC17182.1.
    AF065484 mRNA. Translation: AAC17183.1.
    BT006983 mRNA. Translation: AAP35629.1.
    AK128179 mRNA. Translation: BAC87312.1.
    AK291752 mRNA. Translation: BAF84441.1.
    AC021541 Genomic DNA. No translation available.
    AC100840 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77663.1.
    CH471082 Genomic DNA. Translation: EAW77665.1.
    BC000357 mRNA. Translation: AAH00357.1.
    CCDSiCCDS32266.1. [Q13596-1]
    CCDS32268.1. [Q13596-2]
    CCDS58371.1. [Q13596-3]
    PIRiG02522.
    RefSeqiNP_001229862.1. NM_001242933.1. [Q13596-3]
    NP_003090.2. NM_003099.4. [Q13596-1]
    NP_683758.1. NM_148955.3. [Q13596-2]
    UniGeneiHs.188634.

    Genome annotation databases

    EnsembliENST00000261889; ENSP00000261889; ENSG00000028528. [Q13596-3]
    ENST00000559844; ENSP00000453785; ENSG00000028528. [Q13596-1]
    ENST00000561026; ENSP00000453567; ENSG00000028528. [Q13596-2]
    GeneIDi6642.
    KEGGihsa:6642.
    UCSCiuc002amv.3. human. [Q13596-1]
    uc002amx.3. human. [Q13596-2]

    Polymorphism databases

    DMDMi17380569.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53225 mRNA. Translation: AAA98672.1 .
    AF065483 mRNA. Translation: AAC17182.1 .
    AF065484 mRNA. Translation: AAC17183.1 .
    BT006983 mRNA. Translation: AAP35629.1 .
    AK128179 mRNA. Translation: BAC87312.1 .
    AK291752 mRNA. Translation: BAF84441.1 .
    AC021541 Genomic DNA. No translation available.
    AC100840 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77663.1 .
    CH471082 Genomic DNA. Translation: EAW77665.1 .
    BC000357 mRNA. Translation: AAH00357.1 .
    CCDSi CCDS32266.1. [Q13596-1 ]
    CCDS32268.1. [Q13596-2 ]
    CCDS58371.1. [Q13596-3 ]
    PIRi G02522.
    RefSeqi NP_001229862.1. NM_001242933.1. [Q13596-3 ]
    NP_003090.2. NM_003099.4. [Q13596-1 ]
    NP_683758.1. NM_148955.3. [Q13596-2 ]
    UniGenei Hs.188634.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I4K NMR - A 142-269 [» ]
    4FZS X-ray 2.80 A/B 301-522 [» ]
    ProteinModelPortali Q13596.
    SMRi Q13596. Positions 142-269, 305-513.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112525. 30 interactions.
    DIPi DIP-398N.
    IntActi Q13596. 10 interactions.
    MINTi MINT-4135098.
    STRINGi 9606.ENSP00000369638.

    PTM databases

    PhosphoSitei Q13596.

    Polymorphism databases

    DMDMi 17380569.

    Proteomic databases

    MaxQBi Q13596.
    PaxDbi Q13596.
    PRIDEi Q13596.

    Protocols and materials databases

    DNASUi 6642.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261889 ; ENSP00000261889 ; ENSG00000028528 . [Q13596-3 ]
    ENST00000559844 ; ENSP00000453785 ; ENSG00000028528 . [Q13596-1 ]
    ENST00000561026 ; ENSP00000453567 ; ENSG00000028528 . [Q13596-2 ]
    GeneIDi 6642.
    KEGGi hsa:6642.
    UCSCi uc002amv.3. human. [Q13596-1 ]
    uc002amx.3. human. [Q13596-2 ]

    Organism-specific databases

    CTDi 6642.
    GeneCardsi GC15P064875.
    HGNCi HGNC:11172. SNX1.
    HPAi HPA047373.
    HPA052761.
    MIMi 601272. gene.
    neXtProti NX_Q13596.
    PharmGKBi PA36011.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5391.
    HOVERGENi HBG000618.
    InParanoidi Q13596.
    KOi K17917.
    OMAi EIAEWES.
    OrthoDBi EOG7HHWSB.
    PhylomeDBi Q13596.
    TreeFami TF313698.

    Miscellaneous databases

    ChiTaRSi SNX1. human.
    EvolutionaryTracei Q13596.
    GeneWikii SNX1.
    GenomeRNAii 6642.
    NextBioi 25881.
    PROi Q13596.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13596.
    Bgeei Q13596.
    CleanExi HS_SNX1.
    Genevestigatori Q13596.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    IPR028660. SNX1.
    IPR005329. Sorting_nexin_N.
    IPR015404. Vps5_C.
    [Graphical view ]
    PANTHERi PTHR10555:SF129. PTHR10555:SF129. 1 hit.
    Pfami PF00787. PX. 1 hit.
    PF03700. Sorting_nexin. 1 hit.
    PF09325. Vps5. 1 hit.
    [Graphical view ]
    SMARTi SM00312. PX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Enhanced degradation of EGF receptors by a sorting nexin, SNX1."
      Kurten R.C., Cadena D.L., Gill G.N.
      Science 272:1008-1010(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification of a family of sorting nexin molecules and characterization of their association with receptors."
      Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.
      Mol. Cell. Biol. 18:7278-7287(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, INTERACTION WITH VPS26A; VPS29; VPS35 AND SNX2.
    3. "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].
    4. "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 3).
      Tissue: Placenta and Testis.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Muscle.
    8. "The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation."
      Cozier G.E., Carlton J., McGregor A.H., Gleeson P.A., Teasdale R.D., Mellor H., Cullen P.J.
      J. Biol. Chem. 277:48730-48736(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214, INTERACTION WITH PHOSPHATIDYLINOSITIDES.
    9. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SNX2.
    10. "Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides."
      Carlton J., Bujny M., Peter B.J., Oorschot V.M., Rutherford A., Mellor H., Klumperman J., McMahon H.T., Cullen P.J.
      Curr. Biol. 14:1791-1800(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214 AND 429-LYS--ARG-431.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors."
      Rojas R., Kametaka S., Haft C.R., Bonifacino J.S.
      Mol. Cell. Biol. 27:1112-1124(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-39 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport."
      Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.
      Cell Res. 19:1334-1349(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNX6.
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Determinants of the endosomal localization of sorting nexin 1."
      Zhong Q., Watson M.J., Lazar C.S., Hounslow A.M., Waltho J.P., Gill G.N.
      Mol. Biol. Cell 16:2049-2057(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 142-269, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSNX1_HUMAN
    AccessioniPrimary (citable) accession number: Q13596
    Secondary accession number(s): A6NM19
    , A8K6T7, H0Y2M5, O60750, O60751, Q6ZRJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 16, 2001
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 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

    Miscellaneous

    Binds phosphatidylinositol 3-phosphate (PtdIns-3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2) in liposome-based assays. Can bind PtdIns(3,4,5)P3 in protein:lipid overlay assays, but not in liposome-based assays.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3