SNX6_HUMAN
ID SNX6_HUMAN Reviewed; 406 AA.
AC Q9UNH7; C0H5W9; Q9Y449;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Sorting nexin-6;
DE AltName: Full=TRAF4-associated factor 2;
DE Contains:
DE RecName: Full=Sorting nexin-6, N-terminally processed;
GN Name=SNX6;
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), AND SUBCELLULAR LOCATION.
RX PubMed=11485546; DOI=10.1042/0264-6021:3580007;
RA Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
RT "A large family of endosome-localized proteins related to sorting nexin
RT 1.";
RL Biochem. J. 358:7-16(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Toji S., Yano M., Kobayasi A., Tamai K.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 SUBCELLULAR LOCATION, INTERACTION WITH PIM1, AND PHOSPHORYLATION BY PIM1.
RX PubMed=11591366; DOI=10.1016/s0014-5793(01)02881-2;
RA Ishibashi Y., Maita H., Yano M., Koike N., Tamai K., Ariga H.,
RA Iguchi-Ariga S.M.;
RT "Pim-1 translocates sorting nexin 6/TRAF4-associated factor 2 from
RT cytoplasm to nucleus.";
RL FEBS Lett. 506:33-38(2001).
RN [7]
RP CHARACTERIZATION, AND SUBUNIT.
RX PubMed=11279102; DOI=10.1074/jbc.m100606200;
RA Parks W.T., Frank D.B., Huff C., Haft C.R., Martin J., Meng X.,
RA de Caestecker M.P., McNally J.G., Reddi A., Taylor S.I., Roberts A.B.,
RA Wang T., Lechleider R.J.;
RT "Sorting nexin 6, a novel SNX, interacts with the transforming growth
RT factor-beta family of receptor serine-threonine kinases.";
RL J. Biol. Chem. 276:19332-19339(2001).
RN [8]
RP FUNCTION, INTERACTION WITH SNX1, AND SUBCELLULAR LOCATION.
RX PubMed=17148574; DOI=10.1242/jcs.03302;
RA Wassmer T., Attar N., Bujny M.V., Oakley J., Traer C.J., Cullen P.J.;
RT "A loss-of-function screen reveals SNX5 and SNX6 as potential components of
RT the mammalian retromer.";
RL J. Cell Sci. 120:45-54(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP 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 [10]
RP FUNCTION, INTERACTION WITH DCTN1; SNX1 AND SNX2, MUTAGENESIS OF ARG-68;
RP GLN-69 AND ARG-97, AND SUBCELLULAR LOCATION.
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 [11]
RP INTERACTION WITH SNX1; SNX2; VPS26A; VPS29; VPS35 AND DCTN1.
RX PubMed=19619496; DOI=10.1016/j.devcel.2009.04.016;
RA Wassmer T., Attar N., Harterink M., van Weering J.R., Traer C.J.,
RA Oakley J., Goud B., Stephens D.J., Verkade P., Korswagen H.C., Cullen P.J.;
RT "The retromer coat complex coordinates endosomal sorting and dynein-
RT mediated transport, with carrier recognition by the trans-Golgi network.";
RL Dev. Cell 17:110-122(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BACE1.
RX PubMed=20354142; DOI=10.1096/fj.09-146357;
RA Okada H., Zhang W., Peterhoff C., Hwang J.C., Nixon R.A., Ryu S.H.,
RA Kim T.W.;
RT "Proteomic identification of sorting nexin 6 as a negative regulator of
RT BACE1-mediated APP processing.";
RL FASEB J. 24:2783-2794(2010).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BRMS1.
RX PubMed=20830743; DOI=10.1002/jcb.22874;
RA Rivera J., Megias D., Bravo J.;
RT "Sorting nexin 6 interacts with breast cancer metastasis suppressor-1 and
RT promotes transcriptional repression.";
RL J. Cell. Biochem. 111:1464-1472(2010).
RN [14]
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 [15]
RP FUNCTION, INTERACTION WITH SNX1 AND SNX2, AND DOMAIN.
RX PubMed=23085988; DOI=10.1038/emboj.2012.283;
RA van Weering J.R., Sessions R.B., Traer C.J., Kloer D.P., Bhatia V.K.,
RA Stamou D., Carlsson S.R., Hurley J.H., Cullen P.J.;
RT "Molecular basis for SNX-BAR-mediated assembly of distinct endosomal
RT sorting tubules.";
RL EMBO J. 31:4466-4480(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-194, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [19]
RP FUNCTION, AND INTERACTION WITH PIP5K1C.
RX PubMed=24610942; DOI=10.1242/jcs.132423;
RA Schill N.J., Hedman A.C., Choi S., Anderson R.A.;
RT "Isoform 5 of PIPKIgamma regulates the endosomal trafficking and
RT degradation of E-cadherin.";
RL J. Cell Sci. 127:2189-2203(2014).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP 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).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in several stages of intracellular trafficking.
CC Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or
CC phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as
CC component of the retromer membrane-deforming SNX-BAR subcomplex
CC (PubMed:19935774). The SNX-BAR retromer mediates retrograde transport
CC of cargo proteins from endosomes to the trans-Golgi network (TGN) and
CC is involved in endosome-to-plasma membrane transport for cargo protein
CC recycling. The SNX-BAR subcomplex functions to deform the donor
CC membrane into a tubular profile called endosome-to-TGN transport
CC carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane
CC remodeling activity (PubMed:23085988). Involved in retrograde endosome-
CC to-TGN transport of lysosomal enzyme receptor IGF2R (PubMed:17148574).
CC May function as link between transport vesicles and dynactin
CC (Probable). Negatively regulates retrograde transport of BACE1 from the
CC cell surface to the trans-Golgi network (PubMed:20354142). Involved in
CC E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated
CC E-cadherin degradation (PubMed:24610942). In association with GIT1
CC involved in EGFR degradation. Promotes lysosomal degradation of CDKN1B
CC (By similarity). May contribute to transcription regulation (Probable).
CC {ECO:0000250|UniProtKB:Q6P8X1, ECO:0000269|PubMed:17148574,
CC ECO:0000269|PubMed:19935774, ECO:0000269|PubMed:20354142,
CC ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:24610942,
CC ECO:0000303|PubMed:19935774, ECO:0000303|PubMed:20830743, ECO:0000305}.
CC -!- SUBUNIT: Forms heterodimers with BAR domain-containing sorting nexins
CC SNX1 and SNX2 (PubMed:23085988). The heterodimers are proposed to self-
CC assemble into helical arrays on the membrane to stabilize and expand
CC local membrane curvature underlying endosomal tubule formation. Thought
CC to be a component of the originally described retromer complex (also
CC called SNX-BAR retromer) which is a pentamer containing the
CC heterotrimeric retromer cargo-selective complex (CSC), also described
CC as vacuolar protein sorting subcomplex (VPS), and a heterodimeric
CC membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or
CC SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR
CC subcomplexes associate with low affinity (Probable). Interacts with
CC SNX1, SNX2, VPS26A, VPS29, VPS35, CDKN1B, TGFB receptors, BACE1, BRMS1,
CC PIP5K1C isoform 3. Interacts with DCTN1; the association with DCTN1 is
CC involved in movement of retromer-c ontaining vesicles toward the TGN
CC (PubMed:11279102, PubMed:17148574, PubMed:19935774, PubMed:19619496,
CC PubMed:20354142, PubMed:20830743, PubMed:23085988, PubMed:24610942).
CC Interacts with CDKN1B and GIT1 (By similarity). Interacts with PIM1;
CC translocating SNX6 to the nucleus (PubMed:11591366).
CC {ECO:0000250|UniProtKB:Q6P8X1, ECO:0000269|PubMed:11279102,
CC ECO:0000269|PubMed:11591366, ECO:0000269|PubMed:17148574,
CC ECO:0000269|PubMed:19619496, ECO:0000269|PubMed:19935774,
CC ECO:0000269|PubMed:20354142, ECO:0000269|PubMed:20830743,
CC ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:24610942}.
CC -!- INTERACTION:
CC Q9UNH7; P05067: APP; NbExp=3; IntAct=EBI-949294, EBI-77613;
CC Q9UNH7; P56817: BACE1; NbExp=2; IntAct=EBI-949294, EBI-2433139;
CC Q9UNH7; Q14203: DCTN1; NbExp=2; IntAct=EBI-949294, EBI-724352;
CC Q9UNH7; Q13596: SNX1; NbExp=6; IntAct=EBI-949294, EBI-2822329;
CC Q9UNH7; O60749: SNX2; NbExp=7; IntAct=EBI-949294, EBI-1046690;
CC Q9UNH7; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-949294, EBI-11523345;
CC Q9UNH7; P0DJI4: incE; Xeno; NbExp=8; IntAct=EBI-949294, EBI-22303778;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:11485546,
CC ECO:0000269|PubMed:17148574, ECO:0000269|PubMed:19935774}. Early
CC endosome membrane {ECO:0000269|PubMed:19935774,
CC ECO:0000303|PubMed:11485546}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11485546}; Cytoplasmic side {ECO:0000305}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:20354142}. Cytoplasm
CC {ECO:0000269|PubMed:20830743}. Nucleus {ECO:0000269|PubMed:11591366,
CC ECO:0000269|PubMed:20830743}. Note=Interaction with SNX1 or SNX2
CC promotes location at endosome membranes (PubMed:19935774). Only a minor
CC proportion is seen in the nucleus. {ECO:0000269|PubMed:19935774}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNH7-2; Sequence=VSP_044824;
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-
CC bisphosphate. {ECO:0000250|UniProtKB:B1H267}.
CC -!- DOMAIN: The BAR domain is able to sense membrane curvature upon
CC dimerization. Membrane remodeling seems to implicate insertion of an
CC amphipathic helix (AH) in the membrane (Probable).
CC {ECO:0000303|PubMed:23085988}.
CC -!- PTM: In vitro phosphorylated by PIM1; not affecting PIM1-dependent
CC nuclear translocation (PubMed:11591366). {ECO:0000269|PubMed:11591366}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24202.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF121856; AAD27829.1; -; mRNA.
DR EMBL; U83194; AAD24202.1; ALT_INIT; mRNA.
DR EMBL; AL445363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65913.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65915.1; -; Genomic_DNA.
DR EMBL; BC001798; AAH01798.1; -; mRNA.
DR CCDS; CCDS41942.1; -. [Q9UNH7-1]
DR CCDS; CCDS9648.1; -. [Q9UNH7-2]
DR RefSeq; NP_067072.3; NM_021249.4. [Q9UNH7-2]
DR RefSeq; NP_689419.2; NM_152233.3. [Q9UNH7-1]
DR AlphaFoldDB; Q9UNH7; -.
DR SMR; Q9UNH7; -.
DR BioGRID; 121852; 192.
DR CORUM; Q9UNH7; -.
DR DIP; DIP-37549N; -.
DR IntAct; Q9UNH7; 54.
DR MINT; Q9UNH7; -.
DR STRING; 9606.ENSP00000355217; -.
DR GlyGen; Q9UNH7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UNH7; -.
DR MetOSite; Q9UNH7; -.
DR PhosphoSitePlus; Q9UNH7; -.
DR SwissPalm; Q9UNH7; -.
DR BioMuta; SNX6; -.
DR DMDM; 10720285; -.
DR OGP; Q9UNH7; -.
DR REPRODUCTION-2DPAGE; IPI00298111; -.
DR EPD; Q9UNH7; -.
DR jPOST; Q9UNH7; -.
DR MassIVE; Q9UNH7; -.
DR MaxQB; Q9UNH7; -.
DR PaxDb; Q9UNH7; -.
DR PeptideAtlas; Q9UNH7; -.
DR PRIDE; Q9UNH7; -.
DR ProteomicsDB; 7568; -.
DR ProteomicsDB; 85296; -. [Q9UNH7-1]
DR Antibodypedia; 23146; 312 antibodies from 28 providers.
DR DNASU; 58533; -.
DR Ensembl; ENST00000362031.10; ENSP00000355217.5; ENSG00000129515.20. [Q9UNH7-1]
DR Ensembl; ENST00000396526.7; ENSP00000379779.3; ENSG00000129515.20. [Q9UNH7-2]
DR GeneID; 58533; -.
DR KEGG; hsa:58533; -.
DR MANE-Select; ENST00000362031.10; ENSP00000355217.5; NM_152233.4; NP_689419.3.
DR UCSC; uc001wse.2; human. [Q9UNH7-1]
DR CTD; 58533; -.
DR DisGeNET; 58533; -.
DR GeneCards; SNX6; -.
DR HGNC; HGNC:14970; SNX6.
DR HPA; ENSG00000129515; Low tissue specificity.
DR MIM; 606098; gene.
DR neXtProt; NX_Q9UNH7; -.
DR OpenTargets; ENSG00000129515; -.
DR PharmGKB; PA37946; -.
DR VEuPathDB; HostDB:ENSG00000129515; -.
DR eggNOG; KOG1660; Eukaryota.
DR GeneTree; ENSGT00940000154940; -.
DR InParanoid; Q9UNH7; -.
DR OrthoDB; 1009572at2759; -.
DR PhylomeDB; Q9UNH7; -.
DR TreeFam; TF313698; -.
DR PathwayCommons; Q9UNH7; -.
DR SignaLink; Q9UNH7; -.
DR BioGRID-ORCS; 58533; 51 hits in 1080 CRISPR screens.
DR ChiTaRS; SNX6; human.
DR GenomeRNAi; 58533; -.
DR Pharos; Q9UNH7; Tbio.
DR PRO; PR:Q9UNH7; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UNH7; protein.
DR Bgee; ENSG00000129515; Expressed in left ventricle myocardium and 187 other tissues.
DR ExpressionAtlas; Q9UNH7; baseline and differential.
DR Genevisible; Q9UNH7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:HPA.
DR GO; GO:0005764; C:lysosome; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030904; C:retromer complex; IDA:UniProtKB.
DR GO; GO:0030905; C:retromer, tubulation complex; NAS:ParkinsonsUK-UCL.
DR GO; GO:0097422; C:tubular endosome; IDA:UniProtKB.
DR GO; GO:0034452; F:dynactin binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:HGNC-UCL.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; NAS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:ARUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR CDD; cd07292; PX_SNX6; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042136; PX_SNX6.
DR InterPro; IPR014637; SNX5/SNX6/SNX32.
DR InterPro; IPR028657; SNX6.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR45850:SF4; PTHR45850:SF4; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR PIRSF; PIRSF036924; Snx5_Snx6; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; Lipid-binding; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..406
FT /note="Sorting nexin-6"
FT /id="PRO_0000423277"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..406
FT /note="Sorting nexin-6, N-terminally processed"
FT /id="PRO_0000213846"
FT DOMAIN 26..173
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 203..406
FT /note="BAR"
FT /evidence="ECO:0000305"
FT REGION 2..179
FT /note="Interaction with PIM1"
FT /evidence="ECO:0000269|PubMed:11591366"
FT REGION 182..199
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000303|PubMed:23085988"
FT BINDING 41..47
FT /ligand="phosphatidylinositol bisphosphate"
FT /ligand_id="ChEBI:CHEBI:83191"
FT /evidence="ECO:0000250|UniProtKB:B1H267"
FT BINDING 100..106
FT /ligand="phosphatidylinositol bisphosphate"
FT /ligand_id="ChEBI:CHEBI:83191"
FT /evidence="ECO:0000250|UniProtKB:B1H267"
FT BINDING 114..117
FT /ligand="phosphatidylinositol bisphosphate"
FT /ligand_id="ChEBI:CHEBI:83191"
FT /evidence="ECO:0000250|UniProtKB:B1H267"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylmethionine; in Sorting nexin-6, N-terminally
FT processed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044824"
FT MUTAGEN 68
FT /note="R->A: Reduces interaction with SNX1. Abolishes
FT location at endosome membranes."
FT /evidence="ECO:0000269|PubMed:19935774"
FT MUTAGEN 69
FT /note="Q->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:19935774"
FT MUTAGEN 97
FT /note="R->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:19935774"
SQ SEQUENCE 406 AA; 46649 MW; E3659DB19C59E1BB CRC64;
MMEGLDDGPD FLSEEDRGLK AINVDLQSDA ALQVDISDAL SERDKVKFTV HTKSSLPNFK
QNEFSVVRQH EEFIWLHDSF VENEDYAGYI IPPAPPRPDF DASREKLQKL GEGEGSMTKE
EFTKMKQELE AEYLAIFKKT VAMHEVFLCR VAAHPILRRD LNFHVFLEYN QDLSVRGKNK
KEKLEDFFKN MVKSADGVIV SGVKDVDDFF EHERTFLLEY HNRVKDASAK SDRMTRSHKS
AADDYNRIGS SLYALGTQDS TDICKFFLKV SELFDKTRKI EARVSADEDL KLSDLLKYYL
RESQAAKDLL YRRSRSLVDY ENANKALDKA RAKNKDVLQA ETSQQLCCQK FEKISESAKQ
ELIDFKTRRV AAFRKNLVEL AELELKHAKG NLQLLQNCLA VLNGDT
