SNX15_HUMAN
ID SNX15_HUMAN Reviewed; 342 AA.
AC Q9NRS6; E5KQS6; Q9NRS5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Sorting nexin-15;
GN Name=SNX15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=20843780; DOI=10.1093/nar/gkq750;
RA Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
RA Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M.,
RA Speed T.P., Scharfe C.;
RT "Identification of rare DNA variants in mitochondrial disorders with
RT improved array-based sequencing.";
RL Nucleic Acids Res. 39:44-58(2011).
RN [3]
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 vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP 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 [8]
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., Buerckstuemmer T.,
RA 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-227, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Overexpression of SNX15 disrupts the normal trafficking of
CC proteins from the plasma membrane to recycling endosomes or the TGN.
CC {ECO:0000269|PubMed:11085978}.
CC -!- SUBUNIT: Homodimer. Interacts with SNX1, SNX2 and SNX4.
CC {ECO:0000269|PubMed:11085978}.
CC -!- INTERACTION:
CC Q9NRS6; Q15041: ARL6IP1; NbExp=4; IntAct=EBI-725924, EBI-714543;
CC Q9NRS6; Q9UI14: RABAC1; NbExp=4; IntAct=EBI-725924, EBI-712367;
CC Q9NRS6; Q96HR9: REEP6; NbExp=5; IntAct=EBI-725924, EBI-750345;
CC Q9NRS6; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-725924, EBI-14065960;
CC Q9NRS6; Q9NQC3: RTN4; NbExp=4; IntAct=EBI-725924, EBI-715945;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11085978}. Membrane
CC {ECO:0000269|PubMed:11085978}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11085978}; Cytoplasmic side
CC {ECO:0000269|PubMed:11085978}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:11085978}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11085978}; Cytoplasmic side
CC {ECO:0000269|PubMed:11085978}.
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. {ECO:0000269|PubMed:11085978}.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF175267; AAF89955.1; -; mRNA.
DR EMBL; AF175268; AAF89956.1; -; mRNA.
DR EMBL; HQ205586; ADP91255.1; -; Genomic_DNA.
DR EMBL; HQ205587; ADP91257.1; -; Genomic_DNA.
DR EMBL; HQ205588; ADP91259.1; -; Genomic_DNA.
DR EMBL; HQ205589; ADP91261.1; -; Genomic_DNA.
DR EMBL; HQ205590; ADP91263.1; -; Genomic_DNA.
DR EMBL; HQ205591; ADP91265.1; -; Genomic_DNA.
DR EMBL; HQ205592; ADP91267.1; -; Genomic_DNA.
DR EMBL; HQ205593; ADP91269.1; -; Genomic_DNA.
DR EMBL; HQ205594; ADP91271.1; -; Genomic_DNA.
DR EMBL; HQ205595; ADP91273.1; -; Genomic_DNA.
DR EMBL; HQ205596; ADP91275.1; -; Genomic_DNA.
DR EMBL; HQ205597; ADP91277.1; -; Genomic_DNA.
DR EMBL; HQ205598; ADP91279.1; -; Genomic_DNA.
DR EMBL; HQ205599; ADP91281.1; -; Genomic_DNA.
DR EMBL; HQ205600; ADP91283.1; -; Genomic_DNA.
DR EMBL; HQ205601; ADP91285.1; -; Genomic_DNA.
DR EMBL; HQ205602; ADP91287.1; -; Genomic_DNA.
DR EMBL; HQ205603; ADP91289.1; -; Genomic_DNA.
DR EMBL; HQ205604; ADP91291.1; -; Genomic_DNA.
DR EMBL; HQ205605; ADP91293.1; -; Genomic_DNA.
DR EMBL; HQ205606; ADP91295.1; -; Genomic_DNA.
DR EMBL; HQ205607; ADP91297.1; -; Genomic_DNA.
DR EMBL; HQ205608; ADP91299.1; -; Genomic_DNA.
DR EMBL; HQ205609; ADP91301.1; -; Genomic_DNA.
DR EMBL; HQ205610; ADP91303.1; -; Genomic_DNA.
DR EMBL; HQ205611; ADP91305.1; -; Genomic_DNA.
DR EMBL; HQ205612; ADP91307.1; -; Genomic_DNA.
DR EMBL; HQ205613; ADP91309.1; -; Genomic_DNA.
DR EMBL; HQ205614; ADP91311.1; -; Genomic_DNA.
DR EMBL; HQ205615; ADP91313.1; -; Genomic_DNA.
DR EMBL; HQ205616; ADP91315.1; -; Genomic_DNA.
DR EMBL; HQ205617; ADP91317.1; -; Genomic_DNA.
DR EMBL; HQ205618; ADP91319.1; -; Genomic_DNA.
DR EMBL; HQ205619; ADP91321.1; -; Genomic_DNA.
DR EMBL; HQ205620; ADP91323.1; -; Genomic_DNA.
DR EMBL; HQ205621; ADP91325.1; -; Genomic_DNA.
DR EMBL; HQ205622; ADP91327.1; -; Genomic_DNA.
DR EMBL; HQ205623; ADP91329.1; -; Genomic_DNA.
DR EMBL; HQ205624; ADP91331.1; -; Genomic_DNA.
DR EMBL; HQ205625; ADP91333.1; -; Genomic_DNA.
DR EMBL; BT006631; AAP35277.1; -; mRNA.
DR EMBL; AP000436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009897; AAH09897.1; -; mRNA.
DR EMBL; BC012767; AAH12767.1; -; mRNA.
DR EMBL; BC014520; AAH14520.1; -; mRNA.
DR CCDS; CCDS8089.1; -. [Q9NRS6-1]
DR CCDS; CCDS8090.1; -. [Q9NRS6-2]
DR RefSeq; NP_037438.2; NM_013306.4. [Q9NRS6-1]
DR RefSeq; NP_680086.2; NM_147777.3. [Q9NRS6-2]
DR PDB; 6ECM; X-ray; 2.35 A; A=1-126.
DR PDB; 6MBI; X-ray; 2.83 A; A=1-126.
DR PDBsum; 6ECM; -.
DR PDBsum; 6MBI; -.
DR AlphaFoldDB; Q9NRS6; -.
DR SMR; Q9NRS6; -.
DR BioGRID; 118955; 14.
DR IntAct; Q9NRS6; 9.
DR MINT; Q9NRS6; -.
DR STRING; 9606.ENSP00000366452; -.
DR iPTMnet; Q9NRS6; -.
DR PhosphoSitePlus; Q9NRS6; -.
DR BioMuta; SNX15; -.
DR DMDM; 13124562; -.
DR EPD; Q9NRS6; -.
DR jPOST; Q9NRS6; -.
DR MassIVE; Q9NRS6; -.
DR MaxQB; Q9NRS6; -.
DR PaxDb; Q9NRS6; -.
DR PeptideAtlas; Q9NRS6; -.
DR PRIDE; Q9NRS6; -.
DR ProteomicsDB; 15302; -.
DR ProteomicsDB; 82421; -. [Q9NRS6-1]
DR ProteomicsDB; 82422; -. [Q9NRS6-2]
DR Antibodypedia; 29586; 234 antibodies from 30 providers.
DR DNASU; 29907; -.
DR Ensembl; ENST00000352068.5; ENSP00000316410.5; ENSG00000110025.13. [Q9NRS6-2]
DR Ensembl; ENST00000377244.8; ENSP00000366452.3; ENSG00000110025.13. [Q9NRS6-1]
DR GeneID; 29907; -.
DR KEGG; hsa:29907; -.
DR MANE-Select; ENST00000377244.8; ENSP00000366452.3; NM_013306.5; NP_037438.2.
DR UCSC; uc001ock.4; human. [Q9NRS6-1]
DR CTD; 29907; -.
DR GeneCards; SNX15; -.
DR HGNC; HGNC:14978; SNX15.
DR HPA; ENSG00000110025; Low tissue specificity.
DR MIM; 605964; gene.
DR neXtProt; NX_Q9NRS6; -.
DR OpenTargets; ENSG00000110025; -.
DR PharmGKB; PA37953; -.
DR VEuPathDB; HostDB:ENSG00000110025; -.
DR eggNOG; KOG0603; Eukaryota.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00940000160125; -.
DR InParanoid; Q9NRS6; -.
DR OMA; YRFFTVT; -.
DR PhylomeDB; Q9NRS6; -.
DR TreeFam; TF323964; -.
DR PathwayCommons; Q9NRS6; -.
DR SignaLink; Q9NRS6; -.
DR BioGRID-ORCS; 29907; 23 hits in 1082 CRISPR screens.
DR GeneWiki; SNX15; -.
DR GenomeRNAi; 29907; -.
DR Pharos; Q9NRS6; Tdark.
DR PRO; PR:Q9NRS6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NRS6; protein.
DR Bgee; ENSG00000110025; Expressed in bone marrow cell and 100 other tissues.
DR ExpressionAtlas; Q9NRS6; baseline and differential.
DR Genevisible; Q9NRS6; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Lipid-binding; Membrane; Methylation; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..342
FT /note="Sorting nexin-15"
FT /id="PRO_0000213862"
FT DOMAIN 1..130
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 265..342
FT /note="MIT"
FT REGION 245..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q91WE1"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 222..308
FT /note="EGAAPSPTHVAELATMEVESARLDQEPWEPGGQEEEEDGEGGPTPAYLSQAT
FT ELITQALRDEKAGAYAAALQGYRDGVHVLLQGVPS -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11085978"
FT /id="VSP_006193"
FT VARIANT 334
FT /note="R -> C (in dbSNP:rs495820)"
FT /id="VAR_052478"
FT CONFLICT 221
FT /note="Missing (in Ref. 1; AAF89956)"
FT /evidence="ECO:0000305"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:6ECM"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:6ECM"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:6ECM"
FT HELIX 52..73
FT /evidence="ECO:0007829|PDB:6ECM"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:6ECM"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6ECM"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6ECM"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:6ECM"
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
