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O60749

- SNX2_HUMAN

UniProt

O60749 - SNX2_HUMAN

Protein

Sorting nexin-2

Gene

SNX2

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 127 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    May be involved in several stages of intracellular trafficking. 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).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei183 – 1831Phosphatidylinositol 3-phosphateBy similarity
    Binding sitei185 – 1851Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei211 – 2111Phosphatidylinositol 3-phosphateBy similarity
    Binding sitei235 – 2351Phosphatidylinositol 3-phosphateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. endocytosis Source: ProtInc
    2. intracellular protein transport Source: RefGenome

    Keywords - Biological processi

    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-2
    Alternative name(s):
    Transformation-related gene 9 protein
    Short name:
    TRG-9
    Gene namesi
    Name:SNX2
    ORF Names:TRG9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:11173. SNX2.

    Subcellular locationi

    Early endosome membrane 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. cytoplasmic membrane-bounded vesicle Source: RefGenome
    3. early endosome membrane Source: UniProtKB-SubCell
    4. endosome membrane Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. intracellular membrane-bounded organelle Source: HPA
    7. retromer complex Source: InterPro

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111K → A: Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location. 1 Publication

    Organism-specific databases

    PharmGKBiPA36012.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 519519Sorting nexin-2PRO_0000213838Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei119 – 1191Phosphoserine1 Publication
    Modified residuei185 – 1851Phosphoserine1 Publication
    Modified residuei277 – 2771Phosphoserine2 Publications
    Modified residuei469 – 4691N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60749.
    PaxDbiO60749.
    PeptideAtlasiO60749.
    PRIDEiO60749.

    PTM databases

    PhosphoSiteiO60749.

    Expressioni

    Gene expression databases

    ArrayExpressiO60749.
    BgeeiO60749.
    CleanExiHS_SNX2.
    GenevestigatoriO60749.

    Organism-specific databases

    HPAiHPA037400.

    Interactioni

    Subunit structurei

    Component of the retromer complex composed of VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts with FNBP1. Interacts with SNX6.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FNBP1Q96RU34EBI-1046690,EBI-1111248

    Protein-protein interaction databases

    BioGridi112526. 37 interactions.
    IntActiO60749. 16 interactions.
    MINTiMINT-5000817.
    STRINGi9606.ENSP00000368831.

    Structurei

    3D structure databases

    ProteinModelPortaliO60749.
    SMRiO60749. Positions 140-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini140 – 269130PXPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5391.
    HOVERGENiHBG000618.
    InParanoidiO60749.
    KOiK17917.
    OMAiCEEHTGL.
    OrthoDBiEOG7HHWSB.
    PhylomeDBiO60749.
    TreeFamiTF313698.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001683. Phox.
    IPR028653. SNX2.
    IPR005329. Sorting_nexin_N.
    IPR015404. Vps5_C.
    [Graphical view]
    PANTHERiPTHR10555:SF31. PTHR10555:SF31. 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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60749-1) [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

    MAAEREPPPL GDGKPTDFED LEDGEDLFTS TVSTLESSPS SPEPASLPAE    50
    DISANSNGPK PTEVVLDDDR EDLFAEATEE VSLDSPEREP ILSSEPSPAV 100
    TPVTPTTLIA PRIESKSMSA PVIFDRSREE IEEEANGDIF DIEIGVSDPE 150
    KVGDGMNAYM AYRVTTKTSL SMFSKSEFSV KRRFSDFLGL HSKLASKYLH 200
    VGYIVPPAPE KSIVGMTKVK VGKEDSSSTE FVEKRRAALE RYLQRTVKHP 250
    TLLQDPDLRQ FLESSELPRA VNTQALSGAG ILRMVNKAAD AVNKMTIKMN 300
    ESDAWFEEKQ QQFENLDQQL RKLHVSVEAL VCHRKELSAN TAAFAKSAAM 350
    LGNSEDHTAL SRALSQLAEV EEKIDQLHQE QAFADFYMFS ELLSDYIRLI 400
    AAVKGVFDHR MKCWQKWEDA QITLLKKREA EAKMMVANKP DKIQQAKNEI 450
    REWEAKVQQG ERDFEQISKT IRKEVGRFEK ERVKDFKTVI IKYLESLVQT 500
    QQQLIKYWEA FLPEAKAIA 519
    Length:519
    Mass (Da):58,471
    Last modified:May 30, 2006 - v2
    Checksum:i7DC07DFA523312B5
    GO
    Isoform 2 (identifier: O60749-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-117: Missing.

    Show »
    Length:402
    Mass (Da):46,098
    Checksum:i4CF80EFD3B9C160D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871E → A in AAQ02693. 1 PublicationCurated
    Sequence conflicti146 – 1461V → I in BAH12394. (PubMed:14702039)Curated
    Sequence conflicti331 – 3311V → F1 PublicationCurated
    Sequence conflicti331 – 3311V → F(PubMed:9819414)Curated
    Sequence conflicti384 – 3841A → S1 PublicationCurated
    Sequence conflicti384 – 3841A → S(PubMed:9819414)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 117117Missing in isoform 2. 1 PublicationVSP_054785Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF065482 mRNA. Translation: AAC17181.1.
    AF043453 mRNA. Translation: AAB99852.1.
    AY272044 mRNA. Translation: AAQ02693.1.
    BT009841 mRNA. Translation: AAP88843.1.
    AK023581 mRNA. Translation: BAG51206.1.
    AK293671 mRNA. Translation: BAG57115.1.
    AK296596 mRNA. Translation: BAH12394.1.
    AC008669 Genomic DNA. No translation available.
    AC093267 Genomic DNA. No translation available.
    CH471086 Genomic DNA. Translation: EAW48884.1.
    BC003382 mRNA. Translation: AAH03382.1.
    CCDSiCCDS34217.1. [O60749-1]
    CCDS64234.1. [O60749-2]
    RefSeqiNP_001265128.1. NM_001278199.1. [O60749-2]
    NP_003091.2. NM_003100.3. [O60749-1]
    UniGeneiHs.125352.
    Hs.713554.

    Genome annotation databases

    EnsembliENST00000379516; ENSP00000368831; ENSG00000205302. [O60749-1]
    ENST00000514949; ENSP00000421663; ENSG00000205302. [O60749-2]
    GeneIDi6643.
    KEGGihsa:6643.
    UCSCiuc003kte.4. human. [O60749-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF065482 mRNA. Translation: AAC17181.1 .
    AF043453 mRNA. Translation: AAB99852.1 .
    AY272044 mRNA. Translation: AAQ02693.1 .
    BT009841 mRNA. Translation: AAP88843.1 .
    AK023581 mRNA. Translation: BAG51206.1 .
    AK293671 mRNA. Translation: BAG57115.1 .
    AK296596 mRNA. Translation: BAH12394.1 .
    AC008669 Genomic DNA. No translation available.
    AC093267 Genomic DNA. No translation available.
    CH471086 Genomic DNA. Translation: EAW48884.1 .
    BC003382 mRNA. Translation: AAH03382.1 .
    CCDSi CCDS34217.1. [O60749-1 ]
    CCDS64234.1. [O60749-2 ]
    RefSeqi NP_001265128.1. NM_001278199.1. [O60749-2 ]
    NP_003091.2. NM_003100.3. [O60749-1 ]
    UniGenei Hs.125352.
    Hs.713554.

    3D structure databases

    ProteinModelPortali O60749.
    SMRi O60749. Positions 140-510.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112526. 37 interactions.
    IntActi O60749. 16 interactions.
    MINTi MINT-5000817.
    STRINGi 9606.ENSP00000368831.

    PTM databases

    PhosphoSitei O60749.

    Proteomic databases

    MaxQBi O60749.
    PaxDbi O60749.
    PeptideAtlasi O60749.
    PRIDEi O60749.

    Protocols and materials databases

    DNASUi 6643.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379516 ; ENSP00000368831 ; ENSG00000205302 . [O60749-1 ]
    ENST00000514949 ; ENSP00000421663 ; ENSG00000205302 . [O60749-2 ]
    GeneIDi 6643.
    KEGGi hsa:6643.
    UCSCi uc003kte.4. human. [O60749-1 ]

    Organism-specific databases

    CTDi 6643.
    GeneCardsi GC05P122110.
    HGNCi HGNC:11173. SNX2.
    HPAi HPA037400.
    MIMi 605929. gene.
    neXtProti NX_O60749.
    PharmGKBi PA36012.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5391.
    HOVERGENi HBG000618.
    InParanoidi O60749.
    KOi K17917.
    OMAi CEEHTGL.
    OrthoDBi EOG7HHWSB.
    PhylomeDBi O60749.
    TreeFami TF313698.

    Enzyme and pathway databases

    Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

    Miscellaneous databases

    ChiTaRSi SNX2. human.
    GeneWikii SNX2.
    GenomeRNAii 6643.
    NextBioi 25889.
    PROi O60749.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60749.
    Bgeei O60749.
    CleanExi HS_SNX2.
    Genevestigatori O60749.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    IPR028653. SNX2.
    IPR005329. Sorting_nexin_N.
    IPR015404. Vps5_C.
    [Graphical view ]
    PANTHERi PTHR10555:SF31. PTHR10555:SF31. 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. Kurten R.C., Leychkis Y., Wiley H.S., Gill G.N.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VPS26A; VPS29; VPS35 AND SNX1.
      Tissue: Placenta.
    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] (ISOFORM 1).
    3. "Identification of a human transforming gene."
      Kim J.W.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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: Cerebellum, Colon and Placenta.
    6. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. 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: Placenta.
    9. "The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia."
      Fuchs U., Rehkamp G.F., Haas O.A., Slany R., Koenig M., Bojesen S., Bohle R.M., Damm-Welk C., Ludwig W.-D., Harbott J., Borkhardt A.
      Proc. Natl. Acad. Sci. U.S.A. 98:8756-8761(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FNBP1.
    10. "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance."
      Fuchs U., Rehkamp G.F., Slany R., Follo M., Borkhardt A.
      FEBS Lett. 554:10-16(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FNBP1.
    11. "Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport."
      Carlton J.G., Bujny M.V., Peter B.J., Oorschot V.M., Rutherford A., Arkell R.S., Klumperman J., McMahon H.T., Cullen P.J.
      J. Cell Sci. 118:4527-4539(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-211, SUBCELLULAR LOCATION.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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.
    16. "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.
    17. "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-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSNX2_HUMAN
    AccessioniPrimary (citable) accession number: O60749
    Secondary accession number(s): B3KN44
    , B4DEK4, B7Z408, O43650, P82862, Q53XK8, Q597H6, Q9BTS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

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