Full text data of SNX15
SNX15
[Confidence: low (only semi-automatic identification from reviews)]
Sorting nexin-15
Sorting nexin-15
UniProt
Q9NRS6
ID SNX15_HUMAN Reviewed; 342 AA.
AC Q9NRS6; Q9NRS5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Sorting nexin-15;
GN Name=SNX15;
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Parathyroid;
RX PubMed=11085978; DOI=10.1074/jbc.M004671200;
RA Phillips S.A., Barr V.A., Haft D.H., Taylor S.I., Haft C.R.;
RT "Identification and characterization of snx15, a novel sorting nexin
RT involved in protein trafficking.";
RL J. Biol. Chem. 276:5074-5084(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lymph;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
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 [6]
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).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Overexpression of SNX15 disrupts the normal
CC trafficking of proteins from the plasma membrane to recycling
CC endosomes or the TGN.
CC -!- SUBUNIT: Homodimer. Interacts with SNX1, SNX2 and SNX4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasmic vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRS6-1; Sequence=Displayed;
CC Name=2; Synonyms=SNX15A;
CC IsoId=Q9NRS6-2; Sequence=VSP_006193;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched
CC in phosphatidylinositol 3-phosphate (By similarity).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC -!- SIMILARITY: Contains 1 MIT domain.
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF175267; AAF89955.1; -; mRNA.
DR EMBL; AF175268; AAF89956.1; -; mRNA.
DR EMBL; BT006631; AAP35277.1; -; mRNA.
DR EMBL; BC009897; AAH09897.1; -; mRNA.
DR EMBL; BC012767; AAH12767.1; -; mRNA.
DR EMBL; BC014520; AAH14520.1; -; mRNA.
DR RefSeq; NP_037438.2; NM_013306.4.
DR RefSeq; NP_680086.2; NM_147777.3.
DR UniGene; Hs.80132; -.
DR ProteinModelPortal; Q9NRS6; -.
DR IntAct; Q9NRS6; 5.
DR MINT; MINT-1380453; -.
DR STRING; 9606.ENSP00000301886; -.
DR PhosphoSite; Q9NRS6; -.
DR DMDM; 13124562; -.
DR PaxDb; Q9NRS6; -.
DR PRIDE; Q9NRS6; -.
DR DNASU; 29907; -.
DR Ensembl; ENST00000377244; ENSP00000366452; ENSG00000110025.
DR GeneID; 29907; -.
DR KEGG; hsa:29907; -.
DR UCSC; uc001oci.4; human.
DR CTD; 29907; -.
DR GeneCards; GC11P064782; -.
DR HGNC; HGNC:14978; SNX15.
DR HPA; HPA038955; -.
DR MIM; 605964; gene.
DR neXtProt; NX_Q9NRS6; -.
DR PharmGKB; PA37953; -.
DR eggNOG; NOG245612; -.
DR HOGENOM; HOG000154362; -.
DR HOVERGEN; HBG066336; -.
DR InParanoid; Q9NRS6; -.
DR OMA; ERLDQEP; -.
DR OrthoDB; EOG7B31NH; -.
DR PhylomeDB; Q9NRS6; -.
DR GeneWiki; SNX15; -.
DR GenomeRNAi; 29907; -.
DR NextBio; 52486; -.
DR PRO; PR:Q9NRS6; -.
DR ArrayExpress; Q9NRS6; -.
DR Bgee; Q9NRS6; -.
DR CleanEx; HS_SNX15; -.
DR Genevestigator; Q9NRS6; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0008565; F:protein transporter activity; NAS:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR007330; MIT.
DR InterPro; IPR001683; Phox.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Lipid-binding; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT CHAIN 1 342 Sorting nexin-15.
FT /FTId=PRO_0000213862.
FT DOMAIN 1 130 PX.
FT DOMAIN 265 342 MIT.
FT BINDING 51 51 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 53 53 Phosphatidylinositol 3-phosphate; via
FT amide nitrogen and carbonyl oxygen (By
FT similarity).
FT BINDING 87 87 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 96 96 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT MOD_RES 227 227 Phosphoserine.
FT VAR_SEQ 221 308 EEGAAPSPTHVAELATMEVESARLDQEPWEPGGQEEEEDGE
FT GGPTPAYLSQATELITQALRDEKAGAYAAALQGYRDGVHVL
FT LQGVPS -> G (in isoform 2).
FT /FTId=VSP_006193.
FT VARIANT 334 334 R -> C (in dbSNP:rs495820).
FT /FTId=VAR_052478.
SQ SEQUENCE 342 AA; 38291 MW; 33F64A79EAF6BBDC CRC64;
MSRQAKDDFL RHYTVSDPRT HPKGYTEYKV TAQFISKKDP EDVKEVVVWK RYSDFRKLHG
DLAYTHRNLF RRLEEFPAFP RAQVFGRFEA SVIEERRKGA EDLLRFTVHI PALNNSPQLK
EFFRGGEVTR PLEVSRDLHI LPPPLIPTPP PDDPRLSQLL PAERRGLEEL EVPVDPPPSS
PAQEALDLLF NCESTEEASG SPARGPLTEA ELALFDPFSK EEGAAPSPTH VAELATMEVE
SARLDQEPWE PGGQEEEEDG EGGPTPAYLS QATELITQAL RDEKAGAYAA ALQGYRDGVH
VLLQGVPSDP LPARQEGVKK KAAEYLKRAE EILRLHLSQL PP
//
ID SNX15_HUMAN Reviewed; 342 AA.
AC Q9NRS6; Q9NRS5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Sorting nexin-15;
GN Name=SNX15;
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Parathyroid;
RX PubMed=11085978; DOI=10.1074/jbc.M004671200;
RA Phillips S.A., Barr V.A., Haft D.H., Taylor S.I., Haft C.R.;
RT "Identification and characterization of snx15, a novel sorting nexin
RT involved in protein trafficking.";
RL J. Biol. Chem. 276:5074-5084(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lymph;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
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 [6]
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).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Overexpression of SNX15 disrupts the normal
CC trafficking of proteins from the plasma membrane to recycling
CC endosomes or the TGN.
CC -!- SUBUNIT: Homodimer. Interacts with SNX1, SNX2 and SNX4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasmic vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRS6-1; Sequence=Displayed;
CC Name=2; Synonyms=SNX15A;
CC IsoId=Q9NRS6-2; Sequence=VSP_006193;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched
CC in phosphatidylinositol 3-phosphate (By similarity).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC -!- SIMILARITY: Contains 1 MIT domain.
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF175267; AAF89955.1; -; mRNA.
DR EMBL; AF175268; AAF89956.1; -; mRNA.
DR EMBL; BT006631; AAP35277.1; -; mRNA.
DR EMBL; BC009897; AAH09897.1; -; mRNA.
DR EMBL; BC012767; AAH12767.1; -; mRNA.
DR EMBL; BC014520; AAH14520.1; -; mRNA.
DR RefSeq; NP_037438.2; NM_013306.4.
DR RefSeq; NP_680086.2; NM_147777.3.
DR UniGene; Hs.80132; -.
DR ProteinModelPortal; Q9NRS6; -.
DR IntAct; Q9NRS6; 5.
DR MINT; MINT-1380453; -.
DR STRING; 9606.ENSP00000301886; -.
DR PhosphoSite; Q9NRS6; -.
DR DMDM; 13124562; -.
DR PaxDb; Q9NRS6; -.
DR PRIDE; Q9NRS6; -.
DR DNASU; 29907; -.
DR Ensembl; ENST00000377244; ENSP00000366452; ENSG00000110025.
DR GeneID; 29907; -.
DR KEGG; hsa:29907; -.
DR UCSC; uc001oci.4; human.
DR CTD; 29907; -.
DR GeneCards; GC11P064782; -.
DR HGNC; HGNC:14978; SNX15.
DR HPA; HPA038955; -.
DR MIM; 605964; gene.
DR neXtProt; NX_Q9NRS6; -.
DR PharmGKB; PA37953; -.
DR eggNOG; NOG245612; -.
DR HOGENOM; HOG000154362; -.
DR HOVERGEN; HBG066336; -.
DR InParanoid; Q9NRS6; -.
DR OMA; ERLDQEP; -.
DR OrthoDB; EOG7B31NH; -.
DR PhylomeDB; Q9NRS6; -.
DR GeneWiki; SNX15; -.
DR GenomeRNAi; 29907; -.
DR NextBio; 52486; -.
DR PRO; PR:Q9NRS6; -.
DR ArrayExpress; Q9NRS6; -.
DR Bgee; Q9NRS6; -.
DR CleanEx; HS_SNX15; -.
DR Genevestigator; Q9NRS6; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0008565; F:protein transporter activity; NAS:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR007330; MIT.
DR InterPro; IPR001683; Phox.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Lipid-binding; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT CHAIN 1 342 Sorting nexin-15.
FT /FTId=PRO_0000213862.
FT DOMAIN 1 130 PX.
FT DOMAIN 265 342 MIT.
FT BINDING 51 51 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 53 53 Phosphatidylinositol 3-phosphate; via
FT amide nitrogen and carbonyl oxygen (By
FT similarity).
FT BINDING 87 87 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 96 96 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT MOD_RES 227 227 Phosphoserine.
FT VAR_SEQ 221 308 EEGAAPSPTHVAELATMEVESARLDQEPWEPGGQEEEEDGE
FT GGPTPAYLSQATELITQALRDEKAGAYAAALQGYRDGVHVL
FT LQGVPS -> G (in isoform 2).
FT /FTId=VSP_006193.
FT VARIANT 334 334 R -> C (in dbSNP:rs495820).
FT /FTId=VAR_052478.
SQ SEQUENCE 342 AA; 38291 MW; 33F64A79EAF6BBDC CRC64;
MSRQAKDDFL RHYTVSDPRT HPKGYTEYKV TAQFISKKDP EDVKEVVVWK RYSDFRKLHG
DLAYTHRNLF RRLEEFPAFP RAQVFGRFEA SVIEERRKGA EDLLRFTVHI PALNNSPQLK
EFFRGGEVTR PLEVSRDLHI LPPPLIPTPP PDDPRLSQLL PAERRGLEEL EVPVDPPPSS
PAQEALDLLF NCESTEEASG SPARGPLTEA ELALFDPFSK EEGAAPSPTH VAELATMEVE
SARLDQEPWE PGGQEEEEDG EGGPTPAYLS QATELITQAL RDEKAGAYAA ALQGYRDGVH
VLLQGVPSDP LPARQEGVKK KAAEYLKRAE EILRLHLSQL PP
//
MIM
605964
*RECORD*
*FIELD* NO
605964
*FIELD* TI
*605964 SORTING NEXIN 15; SNX15
*FIELD* TX
SNX15 is a member of the sorting nexin family of phox homology domain
read more(PX)-containing proteins that are homologous to yeast proteins involved
in protein trafficking (Phillips et al., 2001).
CLONING
By EST database searching with a consensus sequence for the PX domain of
several SNX molecules, followed by nested PCR on brain, lung, and liver
cDNA libraries, Phillips et al. (2001) obtained a full-length SNX15
cDNA. SNX15 encodes a deduced 342-amino acid protein as well as a
256-amino acid splice variant, designated SNX15A. SNX15 contains a
124-amino acid PX domain in the N terminus and a novel 73-amino acid
domain in the C terminus, which the authors designated the ESP domain.
SNX15A is identical to SNX15 except that it lacks 86 amino acids within
its C terminus, including a large portion of the ESP domain. Northern
blot analysis detected ubiquitous expression of an approximately 2-kb
SNX15 transcript, with highest expression in skeletal muscle, heart,
brain, kidney, spleen, thymus, and small intestine. Screening of 8
tissues by PCR detected SNX15 expression in lung, liver, skeletal
muscle, prostate, pancreas, and adult and fetal brain, and SNX15A
expression in adult brain, liver, and placenta. Although predicted to be
a soluble protein, both endogenous and overexpressed SNX15 were found on
membranes and in the cytosol.
MAPPING
Phillips et al. (2001) determined that SNX15 is identical to a clone
identified as an expressed gene on chromosome 11q13 by Guru et al.
(1997).
GENE FUNCTION
Using cotransfection experiments, Phillips et al. (2001) showed that
SNX15 associates with itself as well as with SNX1 (601272), SNX2
(605929), SNX4 (605931), and platelet-derived growth factor receptor
(PDGFR; see 173490). Its PX domain is required for its membrane
association and for its association with PDGFR. No association of SNX15
with receptors for epidermal growth factor (131550) or insulin (147670)
was found, but overexpression of SNX15 led to a decrease in the
processing of insulin and hepatocyte growth factor receptors (164860) to
their mature subunits. Immunofluorescence studies showed that
overexpression of SNX15 resulted in mislocalization of furin (136950),
the endoprotease responsible for cleavage of insulin and hepatocyte
growth factor receptors.
*FIELD* RF
1. Guru, S. C.; Agarwal, S. K.; Manickam, P.; Olufemi, S.-E.; Crabtree,
J. S.; Weisemann, J. M.; Kester, M. B.; Kim, Y. S.; Wang, Y.; Emmert-Buck,
M. R.; Liotta, L. A.; Spiegel, A. M.; Boguski, M. S.; Roe, B. A.;
Collins, F. S.; Marx, S. J.; Burns, L.; Chandrasekharappa, S. C.:
A transcript map for the 2.8-Mb region containing the multiple endocrine
neoplasia type 1 locus. Genome Res. 7: 725-735, 1997.
2. Phillips, S. A.; Barr, V. A.; Haft, D. H.; Taylor, S. I.; Haft,
C. R.: Identification and characterization of SNX15, a novel sorting
nexin involved in protein trafficking. J. Biol. Chem. 276: 5074-5084,
2001.
*FIELD* CD
Carol A. Bocchini: 5/24/2001
*FIELD* ED
carol: 10/19/2009
carol: 5/24/2001
mcapotos: 5/24/2001
carol: 5/24/2001
*RECORD*
*FIELD* NO
605964
*FIELD* TI
*605964 SORTING NEXIN 15; SNX15
*FIELD* TX
SNX15 is a member of the sorting nexin family of phox homology domain
read more(PX)-containing proteins that are homologous to yeast proteins involved
in protein trafficking (Phillips et al., 2001).
CLONING
By EST database searching with a consensus sequence for the PX domain of
several SNX molecules, followed by nested PCR on brain, lung, and liver
cDNA libraries, Phillips et al. (2001) obtained a full-length SNX15
cDNA. SNX15 encodes a deduced 342-amino acid protein as well as a
256-amino acid splice variant, designated SNX15A. SNX15 contains a
124-amino acid PX domain in the N terminus and a novel 73-amino acid
domain in the C terminus, which the authors designated the ESP domain.
SNX15A is identical to SNX15 except that it lacks 86 amino acids within
its C terminus, including a large portion of the ESP domain. Northern
blot analysis detected ubiquitous expression of an approximately 2-kb
SNX15 transcript, with highest expression in skeletal muscle, heart,
brain, kidney, spleen, thymus, and small intestine. Screening of 8
tissues by PCR detected SNX15 expression in lung, liver, skeletal
muscle, prostate, pancreas, and adult and fetal brain, and SNX15A
expression in adult brain, liver, and placenta. Although predicted to be
a soluble protein, both endogenous and overexpressed SNX15 were found on
membranes and in the cytosol.
MAPPING
Phillips et al. (2001) determined that SNX15 is identical to a clone
identified as an expressed gene on chromosome 11q13 by Guru et al.
(1997).
GENE FUNCTION
Using cotransfection experiments, Phillips et al. (2001) showed that
SNX15 associates with itself as well as with SNX1 (601272), SNX2
(605929), SNX4 (605931), and platelet-derived growth factor receptor
(PDGFR; see 173490). Its PX domain is required for its membrane
association and for its association with PDGFR. No association of SNX15
with receptors for epidermal growth factor (131550) or insulin (147670)
was found, but overexpression of SNX15 led to a decrease in the
processing of insulin and hepatocyte growth factor receptors (164860) to
their mature subunits. Immunofluorescence studies showed that
overexpression of SNX15 resulted in mislocalization of furin (136950),
the endoprotease responsible for cleavage of insulin and hepatocyte
growth factor receptors.
*FIELD* RF
1. Guru, S. C.; Agarwal, S. K.; Manickam, P.; Olufemi, S.-E.; Crabtree,
J. S.; Weisemann, J. M.; Kester, M. B.; Kim, Y. S.; Wang, Y.; Emmert-Buck,
M. R.; Liotta, L. A.; Spiegel, A. M.; Boguski, M. S.; Roe, B. A.;
Collins, F. S.; Marx, S. J.; Burns, L.; Chandrasekharappa, S. C.:
A transcript map for the 2.8-Mb region containing the multiple endocrine
neoplasia type 1 locus. Genome Res. 7: 725-735, 1997.
2. Phillips, S. A.; Barr, V. A.; Haft, D. H.; Taylor, S. I.; Haft,
C. R.: Identification and characterization of SNX15, a novel sorting
nexin involved in protein trafficking. J. Biol. Chem. 276: 5074-5084,
2001.
*FIELD* CD
Carol A. Bocchini: 5/24/2001
*FIELD* ED
carol: 10/19/2009
carol: 5/24/2001
mcapotos: 5/24/2001
carol: 5/24/2001