Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15036

- SNX17_HUMAN

UniProt

Q15036 - SNX17_HUMAN

Protein

Sorting nexin-17

Gene

SNX17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)).6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361Phosphatidylinositol 3-phosphateBy similarity
    Binding sitei38 – 381Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei62 – 621Phosphatidylinositol 3-phosphateBy similarity
    Binding sitei75 – 751Phosphatidylinositol 3-phosphateBy similarity

    GO - Molecular functioni

    1. low-density lipoprotein particle receptor binding Source: UniProtKB
    2. phosphatidylinositol binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB
    5. receptor binding Source: UniProtKB

    GO - Biological processi

    1. cholesterol catabolic process Source: UniProtKB
    2. endosomal transport Source: UniProtKB
    3. intracellular protein transport Source: UniProtKB
    4. receptor-mediated endocytosis Source: Ensembl
    5. regulation of endocytosis Source: UniProtKB
    6. signal transduction Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    SignaLinkiQ15036.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sorting nexin-17
    Gene namesi
    Name:SNX17
    Synonyms:KIAA0064
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:14979. SNX17.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. cytosol Source: UniProtKB
    5. early endosome Source: UniProtKB
    6. endosome Source: MGI
    7. endosome membrane Source: MGI
    8. Golgi apparatus Source: UniProtKB
    9. intracellular membrane-bounded organelle Source: HPA
    10. membrane Source: UniProtKB
    11. protein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi62 – 621K → A: No association with endosomes. 1 Publication

    Organism-specific databases

    PharmGKBiPA37954.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Sorting nexin-17PRO_0000213865Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei407 – 4071Phosphoserine1 Publication
    Modified residuei409 – 4091PhosphoserineBy similarity
    Modified residuei415 – 4151Phosphoserine2 Publications
    Modified residuei421 – 4211Phosphoserine2 Publications
    Modified residuei437 – 4371Phosphoserine2 Publications
    Modified residuei440 – 4401Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15036.
    PaxDbiQ15036.
    PeptideAtlasiQ15036.
    PRIDEiQ15036.

    PTM databases

    PhosphoSiteiQ15036.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15036.
    BgeeiQ15036.
    CleanExiHS_SNX17.
    GenevestigatoriQ15036.

    Organism-specific databases

    HPAiHPA043867.

    Interactioni

    Subunit structurei

    Monomer. Interacts with APP (via cytoplasmic YXNPXY motif). Interacts with KIF1B By similarity. Interacts with the C-termini of P-selectin, PTC, LDLR, VLDLR, LRP1 and LRP8. Interacts with KRIT1 (via N-terminus). Interacts with HRAS. Interacts with ITGB1 and ITGB5 (via NPxY motif).By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163333EBI-1752620,EBI-389883
    PLCG1P191742EBI-1752620,EBI-79387

    Protein-protein interaction databases

    BioGridi115128. 9 interactions.
    DIPiDIP-52265N.
    IntActiQ15036. 10 interactions.
    MINTiMINT-1188067.
    STRINGi9606.ENSP00000233575.

    Structurei

    Secondary structure

    1
    470
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Beta strandi20 – 278
    Beta strandi30 – 367
    Helixi37 – 5115
    Turni53 – 553
    Helixi69 – 8820
    Helixi90 – 945
    Helixi96 – 10914
    Beta strandi116 – 1238
    Beta strandi128 – 1347
    Helixi139 – 15012
    Helixi154 – 1596
    Beta strandi160 – 1678
    Beta strandi173 – 1786
    Helixi185 – 1906
    Beta strandi197 – 2037
    Helixi208 – 2103
    Helixi211 – 2144
    Helixi218 – 23316
    Beta strandi236 – 2383
    Helixi241 – 25313
    Helixi256 – 2638
    Turni268 – 2703
    Beta strandi277 – 2837
    Beta strandi286 – 2938
    Beta strandi296 – 3005
    Beta strandi310 – 3145
    Helixi315 – 3173
    Beta strandi318 – 3258
    Beta strandi346 – 35510
    Beta strandi358 – 3658
    Helixi369 – 38719

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FOGX-ray2.80A1-108[»]
    3LUIX-ray1.80A/B/C1-112[»]
    4GXBX-ray1.80A111-388[»]
    ProteinModelPortaliQ15036.
    SMRiQ15036. Positions 1-109, 112-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15036.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 109109PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini115 – 20692Ras-associatingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni115 – 432318FERM-likeAdd
    BLAST
    Regioni270 – 432163PTB-like F3 moduleAdd
    BLAST

    Domaini

    The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)). Required for association with endosomes.1 Publication
    The PTB-like F3 module within the FERM-like domain mediates cargo recognition via their NPxY sequences, while the F1 module (Ras-associating) is responsible for interaction with membrane-bound HRAS.1 Publication

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG290558.
    HOGENOMiHOG000007722.
    HOVERGENiHBG061207.
    InParanoidiQ15036.
    KOiK17929.
    OMAiKKIFTLT.
    OrthoDBiEOG70CR71.
    PhylomeDBiQ15036.
    TreeFamiTF318398.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001683. Phox.
    IPR000159. Ras-assoc.
    IPR028666. SNX17.
    [Graphical view]
    PANTHERiPTHR12431:SF16. PTHR12431:SF16. 1 hit.
    PfamiPF00787. PX. 1 hit.
    [Graphical view]
    SMARTiSM00312. PX. 1 hit.
    [Graphical view]
    SUPFAMiSSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    PS50200. RA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15036-1) [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

    MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE    50
    YGANVLPAFP PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS 100
    FLRRAQQETQ QVPTEEVSLE VLLSNGQKVL VNVLTSDQTE DVLEAVAAKL 150
    DLPDDLIGYF SLFLVREKED GAFSFVRKLQ EFELPYVSVT SLRSQEYKIV 200
    LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIERGWILVT KEQHRQLKSL 250
    QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ 300
    LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGSTSSPGRG RGEVRLELAF 350
    EYLMSKDRLQ WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV 400
    GGTLRRSDSQ QAVKSPPLLE SPDATRESMV KLSSKLSAVS LRGIGSPSTD 450
    ASASDVHGNF AFEGIGDEDL 470
    Length:470
    Mass (Da):52,901
    Last modified:November 1, 1996 - v1
    Checksum:iB1C8650CB8AFB5EE
    GO
    Isoform 2 (identifier: Q15036-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         22-46: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:445
    Mass (Da):49,999
    Checksum:iA2D07008B80114CE
    GO

    Sequence cautioni

    The sequence BAA06542.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti429 – 4291M → V in BAD96263. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei22 – 4625Missing in isoform 2. 1 PublicationVSP_044935Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31764 mRNA. Translation: BAA06542.2. Different initiation.
    AJ404855, AJ404856 Genomic DNA. Translation: CAC12897.1.
    BT007167 mRNA. Translation: AAP35831.1.
    AK298869 mRNA. Translation: BAG60989.1.
    CR457081 mRNA. Translation: CAG33362.1.
    AK222543 mRNA. Translation: BAD96263.1.
    AC074117 Genomic DNA. Translation: AAY14844.1.
    BC002524 mRNA. Translation: AAH02524.1.
    BC002610 mRNA. Translation: AAH02610.1.
    BC014620 mRNA. Translation: AAH14620.1.
    BC050590 mRNA. Translation: AAH50590.1.
    CCDSiCCDS1750.1. [Q15036-1]
    CCDS58704.1. [Q15036-2]
    RefSeqiNP_001253989.1. NM_001267060.1. [Q15036-2]
    NP_055563.1. NM_014748.3. [Q15036-1]
    UniGeneiHs.278569.

    Genome annotation databases

    EnsembliENST00000233575; ENSP00000233575; ENSG00000115234. [Q15036-1]
    ENST00000537606; ENSP00000439208; ENSG00000115234. [Q15036-2]
    GeneIDi9784.
    KEGGihsa:9784.
    UCSCiuc002rkg.2. human. [Q15036-1]
    uc010ylp.2. human.

    Polymorphism databases

    DMDMi3123050.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31764 mRNA. Translation: BAA06542.2 . Different initiation.
    AJ404855 , AJ404856 Genomic DNA. Translation: CAC12897.1 .
    BT007167 mRNA. Translation: AAP35831.1 .
    AK298869 mRNA. Translation: BAG60989.1 .
    CR457081 mRNA. Translation: CAG33362.1 .
    AK222543 mRNA. Translation: BAD96263.1 .
    AC074117 Genomic DNA. Translation: AAY14844.1 .
    BC002524 mRNA. Translation: AAH02524.1 .
    BC002610 mRNA. Translation: AAH02610.1 .
    BC014620 mRNA. Translation: AAH14620.1 .
    BC050590 mRNA. Translation: AAH50590.1 .
    CCDSi CCDS1750.1. [Q15036-1 ]
    CCDS58704.1. [Q15036-2 ]
    RefSeqi NP_001253989.1. NM_001267060.1. [Q15036-2 ]
    NP_055563.1. NM_014748.3. [Q15036-1 ]
    UniGenei Hs.278569.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FOG X-ray 2.80 A 1-108 [» ]
    3LUI X-ray 1.80 A/B/C 1-112 [» ]
    4GXB X-ray 1.80 A 111-388 [» ]
    ProteinModelPortali Q15036.
    SMRi Q15036. Positions 1-109, 112-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115128. 9 interactions.
    DIPi DIP-52265N.
    IntActi Q15036. 10 interactions.
    MINTi MINT-1188067.
    STRINGi 9606.ENSP00000233575.

    PTM databases

    PhosphoSitei Q15036.

    Polymorphism databases

    DMDMi 3123050.

    Proteomic databases

    MaxQBi Q15036.
    PaxDbi Q15036.
    PeptideAtlasi Q15036.
    PRIDEi Q15036.

    Protocols and materials databases

    DNASUi 9784.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233575 ; ENSP00000233575 ; ENSG00000115234 . [Q15036-1 ]
    ENST00000537606 ; ENSP00000439208 ; ENSG00000115234 . [Q15036-2 ]
    GeneIDi 9784.
    KEGGi hsa:9784.
    UCSCi uc002rkg.2. human. [Q15036-1 ]
    uc010ylp.2. human.

    Organism-specific databases

    CTDi 9784.
    GeneCardsi GC02P027593.
    HGNCi HGNC:14979. SNX17.
    HPAi HPA043867.
    MIMi 605963. gene.
    neXtProti NX_Q15036.
    PharmGKBi PA37954.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290558.
    HOGENOMi HOG000007722.
    HOVERGENi HBG061207.
    InParanoidi Q15036.
    KOi K17929.
    OMAi KKIFTLT.
    OrthoDBi EOG70CR71.
    PhylomeDBi Q15036.
    TreeFami TF318398.

    Enzyme and pathway databases

    SignaLinki Q15036.

    Miscellaneous databases

    ChiTaRSi SNX17. human.
    EvolutionaryTracei Q15036.
    GeneWikii SNX17.
    GenomeRNAii 9784.
    NextBioi 36842.
    PROi Q15036.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15036.
    Bgeei Q15036.
    CleanExi HS_SNX17.
    Genevestigatori Q15036.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    IPR000159. Ras-assoc.
    IPR028666. SNX17.
    [Graphical view ]
    PANTHERi PTHR12431:SF16. PTHR12431:SF16. 1 hit.
    Pfami PF00787. PX. 1 hit.
    [Graphical view ]
    SMARTi SM00312. PX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    PS50200. RA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "Genomic structure of the KIAA064 gene."
      Wightman P.J., Bonthron D.T.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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] (ISOFORM 1).
    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] (ISOFORM 2).
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adipose tissue.
    7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Lymph, Muscle, Placenta and Testis.
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-11.
      Tissue: Platelet.
    10. "A new member of the sorting nexin family interacts with the C-terminus of P-selectin."
      Florian V., Schlueter T., Bohnensack R.
      Biochem. Biophys. Res. Commun. 281:1045-1050(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH P-SELECTIN.
    11. "Sorting motifs in the intracellular domain of the low density lipoprotein receptor interact with a novel domain of sorting nexin-17."
      Burden J.J., Sun X.-M., Garcia Garcia A.B., Soutar A.K.
      J. Biol. Chem. 279:16237-16245(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LDLR, MUTAGENESIS OF LYS-62, SUBCELLULAR LOCATION.
    12. "Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin."
      Williams R., Schlueter T., Roberts M.S., Knauth P., Bohnensack R., Cutler D.F.
      Mol. Biol. Cell 15:3095-3105(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    13. "Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking."
      Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V., Schreckenberger S., Hahn H., Bohnensack R.
      J. Mol. Biol. 347:813-825(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH P-SELECTIN; LRP1 AND PTC, FUNCTION.
    14. "Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1."
      Czubayko M., Knauth P., Schluter T., Florian V., Bohnensack R.
      Biochem. Biophys. Res. Commun. 345:1264-1272(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KRIT1.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-421; SER-437 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Polarized traffic of LRP1 involves AP1B and SNX17 operating on Y-dependent sorting motifs in different pathways."
      Donoso M., Cancino J., Lee J., van Kerkhof P., Retamal C., Bu G., Gonzalez A., Caceres A., Marzolo M.P.
      Mol. Biol. Cell 20:481-497(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LRP1.
    17. "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-407; SER-415 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways."
      Steinberg F., Heesom K.J., Bass M.D., Cullen P.J.
      J. Cell Biol. 197:219-230(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ITGB1 AND ITGB5.
    22. "Crystal structure of the PX domain of sorting nexin-17 (SNX17)."
      Structural genomics consortium (SGC)
      Submitted (JAN-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-108.
    23. "Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases."
      Ghai R., Mobli M., Norwood S.J., Bugarcic A., Teasdale R.D., King G.F., Collins B.M.
      Proc. Natl. Acad. Sci. U.S.A. 108:7763-7768(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112, FUNCTION, SUBCELLULAR LOCATION, DOMAIN FERM-LIKE REGION, SUBUNIT, INTERACTION WITH HRAS.

    Entry informationi

    Entry nameiSNX17_HUMAN
    AccessioniPrimary (citable) accession number: Q15036
    Secondary accession number(s): B4DQM7, Q53HN7, Q6IAS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 145 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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