SNX8_HUMAN
ID SNX8_HUMAN Reviewed; 465 AA.
AC Q9Y5X2; A4D207; Q96I67;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Sorting nexin-8;
GN Name=SNX8;
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].
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Lung;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452 AND SER-456, AND
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19782049; DOI=10.1016/j.bbrc.2009.09.076;
RA Dyve A.B., Bergan J., Utskarpen A., Sandvig K.;
RT "Sorting nexin 8 regulates endosome-to-Golgi transport.";
RL Biochem. Biophys. Res. Commun. 390:109-114(2009).
RN [7]
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 [8]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-147.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. May play a role in intracellular protein transport from
CC early endosomes to the trans-Golgi network.
CC {ECO:0000269|PubMed:19782049}.
CC -!- INTERACTION:
CC Q9Y5X2; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-1752557, EBI-714543;
CC Q9Y5X2; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-1752557, EBI-725606;
CC Q9Y5X2; P16333: NCK1; NbExp=2; IntAct=EBI-1752557, EBI-389883;
CC Q9Y5X2; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-1752557, EBI-712367;
CC Q9Y5X2; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-1752557, EBI-14065960;
CC Q9Y5X2; Q9Y5X2: SNX8; NbExp=2; IntAct=EBI-1752557, EBI-1752557;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:19782049}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19782049}; Cytoplasmic side
CC {ECO:0000269|PubMed:19782049}. Note=Colocalizes with retromer
CC components.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF121858; AAD27831.1; -; mRNA.
DR EMBL; CH236953; EAL23950.1; -; Genomic_DNA.
DR EMBL; CH471144; EAW87235.1; -; Genomic_DNA.
DR EMBL; BC007785; AAH07785.2; -; mRNA.
DR EMBL; BC021565; AAH21565.1; -; mRNA.
DR CCDS; CCDS5331.1; -.
DR RefSeq; NP_037453.1; NM_013321.3.
DR AlphaFoldDB; Q9Y5X2; -.
DR SMR; Q9Y5X2; -.
DR BioGRID; 118939; 32.
DR IntAct; Q9Y5X2; 22.
DR MINT; Q9Y5X2; -.
DR STRING; 9606.ENSP00000222990; -.
DR GlyGen; Q9Y5X2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5X2; -.
DR PhosphoSitePlus; Q9Y5X2; -.
DR BioMuta; SNX8; -.
DR DMDM; 10720288; -.
DR EPD; Q9Y5X2; -.
DR jPOST; Q9Y5X2; -.
DR MassIVE; Q9Y5X2; -.
DR MaxQB; Q9Y5X2; -.
DR PaxDb; Q9Y5X2; -.
DR PeptideAtlas; Q9Y5X2; -.
DR PRIDE; Q9Y5X2; -.
DR ProteomicsDB; 86527; -.
DR Antibodypedia; 24341; 290 antibodies from 28 providers.
DR DNASU; 29886; -.
DR Ensembl; ENST00000222990.8; ENSP00000222990.3; ENSG00000106266.11.
DR GeneID; 29886; -.
DR KEGG; hsa:29886; -.
DR MANE-Select; ENST00000222990.8; ENSP00000222990.3; NM_013321.4; NP_037453.1.
DR UCSC; uc003slw.3; human.
DR CTD; 29886; -.
DR DisGeNET; 29886; -.
DR GeneCards; SNX8; -.
DR HGNC; HGNC:14972; SNX8.
DR HPA; ENSG00000106266; Low tissue specificity.
DR MIM; 614905; gene.
DR neXtProt; NX_Q9Y5X2; -.
DR OpenTargets; ENSG00000106266; -.
DR PharmGKB; PA37948; -.
DR VEuPathDB; HostDB:ENSG00000106266; -.
DR eggNOG; KOG2273; Eukaryota.
DR GeneTree; ENSGT00460000041594; -.
DR HOGENOM; CLU_042580_0_0_1; -.
DR InParanoid; Q9Y5X2; -.
DR OMA; YLENKMV; -.
DR OrthoDB; 793604at2759; -.
DR PhylomeDB; Q9Y5X2; -.
DR TreeFam; TF314082; -.
DR PathwayCommons; Q9Y5X2; -.
DR SignaLink; Q9Y5X2; -.
DR BioGRID-ORCS; 29886; 21 hits in 1082 CRISPR screens.
DR ChiTaRS; SNX8; human.
DR GenomeRNAi; 29886; -.
DR Pharos; Q9Y5X2; Tbio.
DR PRO; PR:Q9Y5X2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y5X2; protein.
DR Bgee; ENSG00000106266; Expressed in stromal cell of endometrium and 120 other tissues.
DR ExpressionAtlas; Q9Y5X2; baseline and differential.
DR Genevisible; Q9Y5X2; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:UniProtKB.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR CDD; cd06866; PX_SNX8_Mvp1p_like; 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; IPR028662; SNX8/Mvp1.
DR InterPro; IPR035704; SNX8/Mvp1_PX.
DR InterPro; IPR045734; Snx8_BAR_dom.
DR PANTHER; PTHR46571; PTHR46571; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF19566; Snx8_BAR_dom; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Endosome; Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..465
FT /note="Sorting nexin-8"
FT /id="PRO_0000213851"
FT DOMAIN 73..181
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
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 135
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 148
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 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 147
FT /note="A -> G (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036259"
SQ SEQUENCE 465 AA; 52569 MW; 90C5EDB761C31E88 CRC64;
MTGRAMDPLP AAAVGAAAEA EADEEADPPA SDLPTPQAIE PQAIVQQVPA PSRMQMPQGN
PLLLSHTLQE LLARDTVQVE LIPEKKGLFL KHVEYEVSSQ RFKSSVYRRY NDFVVFQEML
LHKFPYRMVP ALPPKRMLGA DREFIEARRR ALKRFVNLVA RHPLFSEDVV LKLFLSFSGS
DVQNKLKESA QCVGDEFLNC KLATRAKDFL PADIQAQFAI SRELIRNIYN SFHKLRDRAE
RIASRAIDNA ADLLIFGKEL SAIGSDTTPL PSWAALNSST WGSLKQALKG LSVEFALLAD
KAAQQGKQEE NDVVEKLNLF LDLLQSYKDL CERHEKGVLH KHQRALHKYS LMKRQMMSAT
AQNREPESVE QLESRIVEQE NAIQTMELRN YFSLYCLHQE TQLIHVYLPL TSHILRAFVN
SQIQGHKEMS KVWNDLRPKL SCLFAGPHST LTPPCSPPED GLCPH
