SNX16_HUMAN
ID SNX16_HUMAN Reviewed; 344 AA.
AC P57768; A8K4D8; Q658L0; Q8N4U3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Sorting nexin-16;
GN Name=SNX16;
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] (ISOFORM 1).
RA Hanson B.J., Hong W.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Esophagus;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN PX, MUTAGENESIS OF TYR-145,
RP AND TISSUE SPECIFICITY.
RX PubMed=12813048; DOI=10.1074/jbc.m300143200;
RA Hanson B.J., Hong W.;
RT "Evidence for a role of SNX16 in regulating traffic between the early and
RT later endosomal compartments.";
RL J. Biol. Chem. 278:34617-34630(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-144.
RX PubMed=15951806; DOI=10.1038/ncb1269;
RA Le Blanc I., Luyet P.P., Pons V., Ferguson C., Emans N., Petiot A.,
RA Mayran N., Demaurex N., Faure J., Sadoul R., Parton R.G., Gruenberg J.;
RT "Endosome-to-cytosol transport of viral nucleocapsids.";
RL Nat. Cell Biol. 7:653-664(2005).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
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 [12]
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. Plays a role in protein transport from early to late
CC endosomes. Plays a role in protein transport to the lysosome. Promotes
CC degradation of EGFR after EGF signaling. Plays a role in intracellular
CC transport of vesicular stomatitis virus nucleocapsids from the endosome
CC to the cytoplasm. {ECO:0000269|PubMed:12813048,
CC ECO:0000269|PubMed:15951806}.
CC -!- SUBUNIT: Homooligomer. Interacts with EGFR (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Late endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm {ECO:0000250}. Lysosome
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P57768-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57768-2; Sequence=VSP_042944;
CC -!- TISSUE SPECIFICITY: Detected in placenta, lung, liver,heart and
CC pancreas. {ECO:0000269|PubMed:12813048}.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 3-phosphate. {ECO:0000269|PubMed:12813048}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF305779; AAG25676.1; -; mRNA.
DR EMBL; AK290903; BAF83592.1; -; mRNA.
DR EMBL; AL833763; CAH56235.1; -; mRNA.
DR EMBL; AC087349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW87108.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW87109.1; -; Genomic_DNA.
DR EMBL; BC033630; AAH33630.1; -; mRNA.
DR CCDS; CCDS6234.1; -. [P57768-1]
DR CCDS; CCDS6235.1; -. [P57768-2]
DR RefSeq; NP_071416.2; NM_022133.3. [P57768-1]
DR RefSeq; NP_690049.1; NM_152836.2. [P57768-1]
DR RefSeq; NP_690050.1; NM_152837.2. [P57768-2]
DR PDB; 5GW0; X-ray; 3.30 A; A/B/C/D/E/F=100-278.
DR PDB; 5GW1; X-ray; 3.35 A; A/B/C/D/E/F/G/H=100-278.
DR PDBsum; 5GW0; -.
DR PDBsum; 5GW1; -.
DR AlphaFoldDB; P57768; -.
DR SMR; P57768; -.
DR BioGRID; 122051; 18.
DR IntAct; P57768; 6.
DR STRING; 9606.ENSP00000379621; -.
DR iPTMnet; P57768; -.
DR PhosphoSitePlus; P57768; -.
DR BioMuta; SNX16; -.
DR DMDM; 116242795; -.
DR EPD; P57768; -.
DR jPOST; P57768; -.
DR MassIVE; P57768; -.
DR MaxQB; P57768; -.
DR PaxDb; P57768; -.
DR PeptideAtlas; P57768; -.
DR PRIDE; P57768; -.
DR ProteomicsDB; 57030; -. [P57768-1]
DR ProteomicsDB; 57031; -. [P57768-2]
DR Antibodypedia; 12573; 139 antibodies from 29 providers.
DR DNASU; 64089; -.
DR Ensembl; ENST00000345957.9; ENSP00000322652.4; ENSG00000104497.15. [P57768-1]
DR Ensembl; ENST00000353788.8; ENSP00000322631.4; ENSG00000104497.15. [P57768-2]
DR Ensembl; ENST00000396330.6; ENSP00000379621.2; ENSG00000104497.15. [P57768-1]
DR GeneID; 64089; -.
DR KEGG; hsa:64089; -.
DR MANE-Select; ENST00000345957.9; ENSP00000322652.4; NM_152836.3; NP_690049.1.
DR UCSC; uc003ycn.4; human. [P57768-1]
DR CTD; 64089; -.
DR DisGeNET; 64089; -.
DR GeneCards; SNX16; -.
DR HGNC; HGNC:14980; SNX16.
DR HPA; ENSG00000104497; Low tissue specificity.
DR MIM; 614903; gene.
DR neXtProt; NX_P57768; -.
DR OpenTargets; ENSG00000104497; -.
DR PharmGKB; PA134972049; -.
DR VEuPathDB; HostDB:ENSG00000104497; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00390000005651; -.
DR HOGENOM; CLU_069154_0_0_1; -.
DR InParanoid; P57768; -.
DR OMA; ENHETCW; -.
DR OrthoDB; 1094695at2759; -.
DR PhylomeDB; P57768; -.
DR TreeFam; TF324116; -.
DR PathwayCommons; P57768; -.
DR SignaLink; P57768; -.
DR BioGRID-ORCS; 64089; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; SNX16; human.
DR GenomeRNAi; 64089; -.
DR Pharos; P57768; Tbio.
DR PRO; PR:P57768; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P57768; protein.
DR Bgee; ENSG00000104497; Expressed in sperm and 179 other tissues.
DR ExpressionAtlas; P57768; baseline and differential.
DR Genevisible; P57768; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; IMP:UniProtKB.
DR CDD; cd07276; PX_SNX16; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR037911; SNX16_PX.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Endosome;
KW Lipid-binding; Lysosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..344
FT /note="Sorting nexin-16"
FT /id="PRO_0000213863"
FT DOMAIN 105..218
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..278
FT /evidence="ECO:0000255"
FT COMPBIAS 13..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
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:0000305"
FT BINDING 146
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 184
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 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C080"
FT VAR_SEQ 126..154
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_042944"
FT VARIANT 98
FT /note="P -> L (in dbSNP:rs16919654)"
FT /id="VAR_052479"
FT MUTAGEN 144
FT /note="R->A: Abolishes binding to membranes enriched in
FT phosphatidylinositol 3-phosphate."
FT /evidence="ECO:0000269|PubMed:15951806"
FT MUTAGEN 145
FT /note="Y->A: Abolishes binding to phosphatidylinositol 3-
FT phosphate."
FT /evidence="ECO:0000269|PubMed:12813048"
FT CONFLICT 308..311
FT /note="LDEE -> WMR (in Ref. 1; AAG25676)"
FT /evidence="ECO:0000305"
FT STRAND 108..136
FT /evidence="ECO:0007829|PDB:5GW0"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:5GW0"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:5GW0"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5GW1"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5GW0"
FT HELIX 178..197
FT /evidence="ECO:0007829|PDB:5GW0"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:5GW0"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:5GW0"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5GW1"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:5GW0"
FT HELIX 233..276
FT /evidence="ECO:0007829|PDB:5GW0"
SQ SEQUENCE 344 AA; 39167 MW; 213744E94B5B3BB8 CRC64;
MATPYVPVPM PIGNSASSFT TNRNQRSSSF GSVSTSSNSS KGQLEDSNMG NFKQTSVPDQ
MDNTSSVCSS PLIRTKFTGT ASSIEYSTRP RDTEEQNPET VNWEDRPSTP TILGYEVMEE
RAKFTVYKIL VKKTPEESWV VFRRYTDFSR LNDKLKEMFP GFRLALPPKR WFKDNYNADF
LEDRQLGLQA FLQNLVAHKD IANCLAVREF LCLDDPPGPF DSLEESRAFC ETLEETNYRL
QKELLEKQKE MESLKKLLSE KQLHIDTLEN RIRTLSLEPE ESLDVSETEG EQILKVESSA
LEVDQDVLDE ESRADNKPCL SFSEPENAVS EIEVAEVAYD AEED
