Full text data of SNX2
SNX2
[Confidence: low (only semi-automatic identification from reviews)]
Sorting nexin-2 (Transformation-related gene 9 protein; TRG-9)
Sorting nexin-2 (Transformation-related gene 9 protein; TRG-9)
UniProt
O60749
ID SNX2_HUMAN Reviewed; 519 AA.
AC O60749; B3KN44; O43650; P82862; Q53XK8; Q597H6; Q9BTS8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Sorting nexin-2;
DE AltName: Full=Transformation-related gene 9 protein;
DE Short=TRG-9;
GN Name=SNX2; ORFNames=TRG9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VPS26A; VPS29; VPS35
RP AND SNX1.
RC TISSUE=Placenta;
RA Kurten R.C., Leychkis Y., Wiley H.S., Gill G.N.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9819414;
RA Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.;
RT "Identification of a family of sorting nexin molecules and
RT characterization of their association with receptors.";
RL Mol. Cell. Biol. 18:7278-7287(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human transforming gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH FNBP1.
RX PubMed=11438682; DOI=10.1073/pnas.121433898;
RA Fuchs U., Rehkamp G.F., Haas O.A., Slany R., Koenig M., Bojesen S.,
RA Bohle R.M., Damm-Welk C., Ludwig W.-D., Harbott J., Borkhardt A.;
RT "The human formin-binding protein 17 (FBP17) interacts with sorting
RT nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous
RT leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8756-8761(2001).
RN [9]
RP INTERACTION WITH FNBP1.
RX PubMed=14596906; DOI=10.1016/S0014-5793(03)01063-9;
RA Fuchs U., Rehkamp G.F., Slany R., Follo M., Borkhardt A.;
RT "The formin-binding protein 17, FBP17, binds via a TNKS binding motif
RT to tankyrase, a protein involved in telomere maintenance.";
RL FEBS Lett. 554:10-16(2003).
RN [10]
RP FUNCTION, MUTAGENESIS OF LYS-211, AND SUBCELLULAR LOCATION.
RX PubMed=16179610; DOI=10.1242/jcs.02568;
RA Carlton J.G., Bujny M.V., Peter B.J., Oorschot V.M., Rutherford A.,
RA Arkell R.S., Klumperman J., McMahon H.T., Cullen P.J.;
RT "Sorting nexin-2 is associated with tubular elements of the early
RT endosome, but is not essential for retromer-mediated endosome-to-TGN
RT transport.";
RL J. Cell Sci. 118:4527-4539(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17101778; DOI=10.1128/MCB.00156-06;
RA Rojas R., Kametaka S., Haft C.R., Bonifacino J.S.;
RT "Interchangeable but essential functions of SNX1 and SNX2 in the
RT association of retromer with endosomes and the trafficking of mannose
RT 6-phosphate receptors.";
RL Mol. Cell. Biol. 27:1112-1124(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-185, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP INTERACTION WITH SNX6.
RX PubMed=19935774; DOI=10.1038/cr.2009.130;
RA Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.;
RT "The retromer component SNX6 interacts with dynactin p150(Glued) and
RT mediates endosome-to-TGN transport.";
RL Cell Res. 19:1334-1349(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-469, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Component of the retromer complex, a complex required
CC to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from
CC endosomes to the trans-Golgi network. Interacts with membranes
CC containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or
CC phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC -!- SUBUNIT: Component of the retromer complex composed of VPS26
CC (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts with
CC FNBP1. Interacts with SNX6.
CC -!- INTERACTION:
CC Q96RU3:FNBP1; NbExp=4; IntAct=EBI-1046690, EBI-1111248;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR EMBL; AF065482; AAC17181.1; -; mRNA.
DR EMBL; AF043453; AAB99852.1; -; mRNA.
DR EMBL; AY272044; AAQ02693.1; -; mRNA.
DR EMBL; BT009841; AAP88843.1; -; mRNA.
DR EMBL; AK023581; BAG51206.1; -; mRNA.
DR EMBL; CH471086; EAW48884.1; -; Genomic_DNA.
DR EMBL; BC003382; AAH03382.1; -; mRNA.
DR RefSeq; NP_001265128.1; NM_001278199.1.
DR RefSeq; NP_003091.2; NM_003100.3.
DR UniGene; Hs.125352; -.
DR UniGene; Hs.713554; -.
DR ProteinModelPortal; O60749; -.
DR SMR; O60749; 140-499.
DR IntAct; O60749; 16.
DR MINT; MINT-5000817; -.
DR STRING; 9606.ENSP00000368831; -.
DR PhosphoSite; O60749; -.
DR PaxDb; O60749; -.
DR PeptideAtlas; O60749; -.
DR PRIDE; O60749; -.
DR DNASU; 6643; -.
DR Ensembl; ENST00000379516; ENSP00000368831; ENSG00000205302.
DR GeneID; 6643; -.
DR KEGG; hsa:6643; -.
DR UCSC; uc003kte.4; human.
DR CTD; 6643; -.
DR GeneCards; GC05P122110; -.
DR HGNC; HGNC:11173; SNX2.
DR HPA; HPA037400; -.
DR MIM; 605929; gene.
DR neXtProt; NX_O60749; -.
DR PharmGKB; PA36012; -.
DR eggNOG; COG5391; -.
DR HOVERGEN; HBG000618; -.
DR InParanoid; O60749; -.
DR OMA; ITYKMDE; -.
DR OrthoDB; EOG7HHWSB; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; SNX2; human.
DR GeneWiki; SNX2; -.
DR GenomeRNAi; 6643; -.
DR NextBio; 25889; -.
DR PRO; PR:O60749; -.
DR ArrayExpress; O60749; -.
DR Bgee; O60749; -.
DR CleanEx; HS_SNX2; -.
DR Genevestigator; O60749; -.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
DR InterPro; IPR005329; Sorting_nexin_N.
DR InterPro; IPR015404; Vps5_C.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF03700; Sorting_nexin; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1 519 Sorting nexin-2.
FT /FTId=PRO_0000213838.
FT DOMAIN 140 269 PX.
FT BINDING 183 183 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 185 185 Phosphatidylinositol 3-phosphate; via
FT amide nitrogen and carbonyl oxygen (By
FT similarity).
FT BINDING 211 211 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 235 235 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT MOD_RES 119 119 Phosphoserine.
FT MOD_RES 185 185 Phosphoserine.
FT MOD_RES 277 277 Phosphoserine.
FT MOD_RES 469 469 N6-acetyllysine.
FT MUTAGEN 211 211 K->A: Abolishes phosphatidylinositol
FT phosphate binding. Abolishes endosomal
FT location.
FT CONFLICT 87 87 E -> A (in Ref. 3; AAQ02693).
FT CONFLICT 331 331 V -> F (in Ref. 1 and 2).
FT CONFLICT 384 384 A -> S (in Ref. 1 and 2).
SQ SEQUENCE 519 AA; 58471 MW; 7DC07DFA523312B5 CRC64;
MAAEREPPPL GDGKPTDFED LEDGEDLFTS TVSTLESSPS SPEPASLPAE DISANSNGPK
PTEVVLDDDR EDLFAEATEE VSLDSPEREP ILSSEPSPAV TPVTPTTLIA PRIESKSMSA
PVIFDRSREE IEEEANGDIF DIEIGVSDPE KVGDGMNAYM AYRVTTKTSL SMFSKSEFSV
KRRFSDFLGL HSKLASKYLH VGYIVPPAPE KSIVGMTKVK VGKEDSSSTE FVEKRRAALE
RYLQRTVKHP TLLQDPDLRQ FLESSELPRA VNTQALSGAG ILRMVNKAAD AVNKMTIKMN
ESDAWFEEKQ QQFENLDQQL RKLHVSVEAL VCHRKELSAN TAAFAKSAAM LGNSEDHTAL
SRALSQLAEV EEKIDQLHQE QAFADFYMFS ELLSDYIRLI AAVKGVFDHR MKCWQKWEDA
QITLLKKREA EAKMMVANKP DKIQQAKNEI REWEAKVQQG ERDFEQISKT IRKEVGRFEK
ERVKDFKTVI IKYLESLVQT QQQLIKYWEA FLPEAKAIA
//
ID SNX2_HUMAN Reviewed; 519 AA.
AC O60749; B3KN44; O43650; P82862; Q53XK8; Q597H6; Q9BTS8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Sorting nexin-2;
DE AltName: Full=Transformation-related gene 9 protein;
DE Short=TRG-9;
GN Name=SNX2; ORFNames=TRG9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VPS26A; VPS29; VPS35
RP AND SNX1.
RC TISSUE=Placenta;
RA Kurten R.C., Leychkis Y., Wiley H.S., Gill G.N.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9819414;
RA Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.;
RT "Identification of a family of sorting nexin molecules and
RT characterization of their association with receptors.";
RL Mol. Cell. Biol. 18:7278-7287(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human transforming gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH FNBP1.
RX PubMed=11438682; DOI=10.1073/pnas.121433898;
RA Fuchs U., Rehkamp G.F., Haas O.A., Slany R., Koenig M., Bojesen S.,
RA Bohle R.M., Damm-Welk C., Ludwig W.-D., Harbott J., Borkhardt A.;
RT "The human formin-binding protein 17 (FBP17) interacts with sorting
RT nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous
RT leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8756-8761(2001).
RN [9]
RP INTERACTION WITH FNBP1.
RX PubMed=14596906; DOI=10.1016/S0014-5793(03)01063-9;
RA Fuchs U., Rehkamp G.F., Slany R., Follo M., Borkhardt A.;
RT "The formin-binding protein 17, FBP17, binds via a TNKS binding motif
RT to tankyrase, a protein involved in telomere maintenance.";
RL FEBS Lett. 554:10-16(2003).
RN [10]
RP FUNCTION, MUTAGENESIS OF LYS-211, AND SUBCELLULAR LOCATION.
RX PubMed=16179610; DOI=10.1242/jcs.02568;
RA Carlton J.G., Bujny M.V., Peter B.J., Oorschot V.M., Rutherford A.,
RA Arkell R.S., Klumperman J., McMahon H.T., Cullen P.J.;
RT "Sorting nexin-2 is associated with tubular elements of the early
RT endosome, but is not essential for retromer-mediated endosome-to-TGN
RT transport.";
RL J. Cell Sci. 118:4527-4539(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17101778; DOI=10.1128/MCB.00156-06;
RA Rojas R., Kametaka S., Haft C.R., Bonifacino J.S.;
RT "Interchangeable but essential functions of SNX1 and SNX2 in the
RT association of retromer with endosomes and the trafficking of mannose
RT 6-phosphate receptors.";
RL Mol. Cell. Biol. 27:1112-1124(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-185, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP INTERACTION WITH SNX6.
RX PubMed=19935774; DOI=10.1038/cr.2009.130;
RA Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.;
RT "The retromer component SNX6 interacts with dynactin p150(Glued) and
RT mediates endosome-to-TGN transport.";
RL Cell Res. 19:1334-1349(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-469, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Component of the retromer complex, a complex required
CC to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from
CC endosomes to the trans-Golgi network. Interacts with membranes
CC containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or
CC phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC -!- SUBUNIT: Component of the retromer complex composed of VPS26
CC (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts with
CC FNBP1. Interacts with SNX6.
CC -!- INTERACTION:
CC Q96RU3:FNBP1; NbExp=4; IntAct=EBI-1046690, EBI-1111248;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR EMBL; AF065482; AAC17181.1; -; mRNA.
DR EMBL; AF043453; AAB99852.1; -; mRNA.
DR EMBL; AY272044; AAQ02693.1; -; mRNA.
DR EMBL; BT009841; AAP88843.1; -; mRNA.
DR EMBL; AK023581; BAG51206.1; -; mRNA.
DR EMBL; CH471086; EAW48884.1; -; Genomic_DNA.
DR EMBL; BC003382; AAH03382.1; -; mRNA.
DR RefSeq; NP_001265128.1; NM_001278199.1.
DR RefSeq; NP_003091.2; NM_003100.3.
DR UniGene; Hs.125352; -.
DR UniGene; Hs.713554; -.
DR ProteinModelPortal; O60749; -.
DR SMR; O60749; 140-499.
DR IntAct; O60749; 16.
DR MINT; MINT-5000817; -.
DR STRING; 9606.ENSP00000368831; -.
DR PhosphoSite; O60749; -.
DR PaxDb; O60749; -.
DR PeptideAtlas; O60749; -.
DR PRIDE; O60749; -.
DR DNASU; 6643; -.
DR Ensembl; ENST00000379516; ENSP00000368831; ENSG00000205302.
DR GeneID; 6643; -.
DR KEGG; hsa:6643; -.
DR UCSC; uc003kte.4; human.
DR CTD; 6643; -.
DR GeneCards; GC05P122110; -.
DR HGNC; HGNC:11173; SNX2.
DR HPA; HPA037400; -.
DR MIM; 605929; gene.
DR neXtProt; NX_O60749; -.
DR PharmGKB; PA36012; -.
DR eggNOG; COG5391; -.
DR HOVERGEN; HBG000618; -.
DR InParanoid; O60749; -.
DR OMA; ITYKMDE; -.
DR OrthoDB; EOG7HHWSB; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; SNX2; human.
DR GeneWiki; SNX2; -.
DR GenomeRNAi; 6643; -.
DR NextBio; 25889; -.
DR PRO; PR:O60749; -.
DR ArrayExpress; O60749; -.
DR Bgee; O60749; -.
DR CleanEx; HS_SNX2; -.
DR Genevestigator; O60749; -.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
DR InterPro; IPR005329; Sorting_nexin_N.
DR InterPro; IPR015404; Vps5_C.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF03700; Sorting_nexin; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1 519 Sorting nexin-2.
FT /FTId=PRO_0000213838.
FT DOMAIN 140 269 PX.
FT BINDING 183 183 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 185 185 Phosphatidylinositol 3-phosphate; via
FT amide nitrogen and carbonyl oxygen (By
FT similarity).
FT BINDING 211 211 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 235 235 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT MOD_RES 119 119 Phosphoserine.
FT MOD_RES 185 185 Phosphoserine.
FT MOD_RES 277 277 Phosphoserine.
FT MOD_RES 469 469 N6-acetyllysine.
FT MUTAGEN 211 211 K->A: Abolishes phosphatidylinositol
FT phosphate binding. Abolishes endosomal
FT location.
FT CONFLICT 87 87 E -> A (in Ref. 3; AAQ02693).
FT CONFLICT 331 331 V -> F (in Ref. 1 and 2).
FT CONFLICT 384 384 A -> S (in Ref. 1 and 2).
SQ SEQUENCE 519 AA; 58471 MW; 7DC07DFA523312B5 CRC64;
MAAEREPPPL GDGKPTDFED LEDGEDLFTS TVSTLESSPS SPEPASLPAE DISANSNGPK
PTEVVLDDDR EDLFAEATEE VSLDSPEREP ILSSEPSPAV TPVTPTTLIA PRIESKSMSA
PVIFDRSREE IEEEANGDIF DIEIGVSDPE KVGDGMNAYM AYRVTTKTSL SMFSKSEFSV
KRRFSDFLGL HSKLASKYLH VGYIVPPAPE KSIVGMTKVK VGKEDSSSTE FVEKRRAALE
RYLQRTVKHP TLLQDPDLRQ FLESSELPRA VNTQALSGAG ILRMVNKAAD AVNKMTIKMN
ESDAWFEEKQ QQFENLDQQL RKLHVSVEAL VCHRKELSAN TAAFAKSAAM LGNSEDHTAL
SRALSQLAEV EEKIDQLHQE QAFADFYMFS ELLSDYIRLI AAVKGVFDHR MKCWQKWEDA
QITLLKKREA EAKMMVANKP DKIQQAKNEI REWEAKVQQG ERDFEQISKT IRKEVGRFEK
ERVKDFKTVI IKYLESLVQT QQQLIKYWEA FLPEAKAIA
//
MIM
605929
*RECORD*
*FIELD* NO
605929
*FIELD* TI
*605929 SORTING NEXIN 2; SNX2
*FIELD* TX
DESCRIPTION
SNX2 is a member of the sorting nexin family of molecules that contain
read morean approximately 100-amino acid region termed the phox homology (PX)
domain (Haft et al., 1998).
CLONING
By database searching with the sequence of sorting nexin-1 (SNX1;
601272), Haft et al. (1998) obtained several human EST clones,
determined their nucleotide sequences, and constructed full-length cDNAS
corresponding to an isoform of SNX1 (SNX1A), SNX2, SNX3 (605930), and
SNX4 (605931). The SNX2 cDNA encodes a deduced 519-amino acid protein
that shares 63% sequence identity with SNX1. Northern blot analysis
detected SNX2 transcripts of approximately 3.1 and 2.4 kb in all tissues
tested, with highest expression in spleen, heart, skeletal muscle, and
peripheral leukocytes, and low expression in kidney, liver, and brain.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SNX2
gene to chromosome 5q23 (TMAP stSG21976).
GENE FUNCTION
By Western blot analysis, Haft et al. (1998) showed that SNX1, SNX1A,
SNX2, and SNX4 are associated predominantly with membranes, whereas SNX3
is found mainly in the cytosol. SNX2 is able to oligomerize with itself
and forms heteromeric complexes with SNX1, SNX1A, and SNX4, but not with
SNX3. When expressed in COS-7 cells, epitope-tagged SNX1, SNX1A, SNX2,
and SNX4 coimmunoprecipitated with receptor tyrosine kinases for EGF
(131550), platelet-derived growth factor (see 173490), and insulin
(147670). They also associated with the long isoform of the leptin
receptor (601007) but not with the short and medium isoforms. Based on
the functions of their yeast homologs, Haft et al. (1998) suggested that
mammalian sorting nexins function in intracellular trafficking of
proteins to various organelles.
The cell surface receptor CED1 (107770) mediates apoptotic cell
recognition by phagocytic cells, enabling cell corpse clearance in C.
elegans. Chen et al. (2010) found that the C. elegans intracellular
protein sorting complex, retromer, was required for cell corpse
clearance by mediating the recycling of CED1. The mammalian retromer
complex contains sorting nexins 1 and 2 (C. elegans homolog snx1) and
5/6 (605937, 606098) (C. elegans homolog snx6). Retromer was recruited
to the surfaces of phagosomes containing cell corpses, and its loss of
function caused defective cell corpse removal. The retromer probably
acted through direct interaction with CED1 in the cell corpse
recognition pathway. In the absence of retromer function, CED1
associated with lysosomes and failed to recycle from phagosomes and
cytosol to the plasma membrane. Thus, Chen et al. (2010) concluded that
retromer is an essential mediator of apoptotic cell clearance by
regulating phagocytic receptor(s) during cell corpse engulfment.
*FIELD* RF
1. Chen, D.; Xiao, H.; Zhang, K.; Wang, B.; Gao, Z.; Jian, Y.; Qi,
X.; Sun, J.; Miao, L.; Yang, C.: Retromer is required for apoptotic
cell clearance by phagocytic receptor recycling. Science 327: 1261-1264,
2010.
2. Haft, C. R.; de la Luz Sierra, M.; Barr, V. A.; Haft, D. H.; Taylor,
S. I.: Identification of a family of sorting nexin molecules and
characterization of their association with receptors. Molec. Cell.
Biol. 18: 7278-7287, 1998.
*FIELD* CN
Ada Hamosh - updated: 4/22/2010
*FIELD* CD
Carol A. Bocchini: 5/14/2001
*FIELD* ED
alopez: 04/26/2010
terry: 4/22/2010
carol: 10/19/2009
mcapotos: 5/16/2001
carol: 5/15/2001
*RECORD*
*FIELD* NO
605929
*FIELD* TI
*605929 SORTING NEXIN 2; SNX2
*FIELD* TX
DESCRIPTION
SNX2 is a member of the sorting nexin family of molecules that contain
read morean approximately 100-amino acid region termed the phox homology (PX)
domain (Haft et al., 1998).
CLONING
By database searching with the sequence of sorting nexin-1 (SNX1;
601272), Haft et al. (1998) obtained several human EST clones,
determined their nucleotide sequences, and constructed full-length cDNAS
corresponding to an isoform of SNX1 (SNX1A), SNX2, SNX3 (605930), and
SNX4 (605931). The SNX2 cDNA encodes a deduced 519-amino acid protein
that shares 63% sequence identity with SNX1. Northern blot analysis
detected SNX2 transcripts of approximately 3.1 and 2.4 kb in all tissues
tested, with highest expression in spleen, heart, skeletal muscle, and
peripheral leukocytes, and low expression in kidney, liver, and brain.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SNX2
gene to chromosome 5q23 (TMAP stSG21976).
GENE FUNCTION
By Western blot analysis, Haft et al. (1998) showed that SNX1, SNX1A,
SNX2, and SNX4 are associated predominantly with membranes, whereas SNX3
is found mainly in the cytosol. SNX2 is able to oligomerize with itself
and forms heteromeric complexes with SNX1, SNX1A, and SNX4, but not with
SNX3. When expressed in COS-7 cells, epitope-tagged SNX1, SNX1A, SNX2,
and SNX4 coimmunoprecipitated with receptor tyrosine kinases for EGF
(131550), platelet-derived growth factor (see 173490), and insulin
(147670). They also associated with the long isoform of the leptin
receptor (601007) but not with the short and medium isoforms. Based on
the functions of their yeast homologs, Haft et al. (1998) suggested that
mammalian sorting nexins function in intracellular trafficking of
proteins to various organelles.
The cell surface receptor CED1 (107770) mediates apoptotic cell
recognition by phagocytic cells, enabling cell corpse clearance in C.
elegans. Chen et al. (2010) found that the C. elegans intracellular
protein sorting complex, retromer, was required for cell corpse
clearance by mediating the recycling of CED1. The mammalian retromer
complex contains sorting nexins 1 and 2 (C. elegans homolog snx1) and
5/6 (605937, 606098) (C. elegans homolog snx6). Retromer was recruited
to the surfaces of phagosomes containing cell corpses, and its loss of
function caused defective cell corpse removal. The retromer probably
acted through direct interaction with CED1 in the cell corpse
recognition pathway. In the absence of retromer function, CED1
associated with lysosomes and failed to recycle from phagosomes and
cytosol to the plasma membrane. Thus, Chen et al. (2010) concluded that
retromer is an essential mediator of apoptotic cell clearance by
regulating phagocytic receptor(s) during cell corpse engulfment.
*FIELD* RF
1. Chen, D.; Xiao, H.; Zhang, K.; Wang, B.; Gao, Z.; Jian, Y.; Qi,
X.; Sun, J.; Miao, L.; Yang, C.: Retromer is required for apoptotic
cell clearance by phagocytic receptor recycling. Science 327: 1261-1264,
2010.
2. Haft, C. R.; de la Luz Sierra, M.; Barr, V. A.; Haft, D. H.; Taylor,
S. I.: Identification of a family of sorting nexin molecules and
characterization of their association with receptors. Molec. Cell.
Biol. 18: 7278-7287, 1998.
*FIELD* CN
Ada Hamosh - updated: 4/22/2010
*FIELD* CD
Carol A. Bocchini: 5/14/2001
*FIELD* ED
alopez: 04/26/2010
terry: 4/22/2010
carol: 10/19/2009
mcapotos: 5/16/2001
carol: 5/15/2001