Full text data of SNX8
SNX8
[Confidence: low (only semi-automatic identification from reviews)]
Sorting nexin-8
Sorting nexin-8
UniProt
Q9Y5X2
ID SNX8_HUMAN Reviewed; 465 AA.
AC Q9Y5X2; A4D207; Q96I67;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Sorting nexin-8;
GN Name=SNX8;
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].
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
RT nexin 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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS SPECTROMETRY.
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.,
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).
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT 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
CC from early endosomes to the trans-Golgi network.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-1752557, EBI-1752557;
CC P16333:NCK1; NbExp=2; IntAct=EBI-1752557, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Colocalizes with retromer
CC components.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
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; 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 RefSeq; NP_037453.1; NM_013321.2.
DR UniGene; Hs.584900; -.
DR ProteinModelPortal; Q9Y5X2; -.
DR SMR; Q9Y5X2; 92-330.
DR IntAct; Q9Y5X2; 10.
DR MINT; MINT-3087539; -.
DR STRING; 9606.ENSP00000222990; -.
DR PhosphoSite; Q9Y5X2; -.
DR DMDM; 10720288; -.
DR PaxDb; Q9Y5X2; -.
DR PRIDE; Q9Y5X2; -.
DR DNASU; 29886; -.
DR Ensembl; ENST00000222990; ENSP00000222990; ENSG00000106266.
DR GeneID; 29886; -.
DR KEGG; hsa:29886; -.
DR UCSC; uc003slw.3; human.
DR CTD; 29886; -.
DR GeneCards; GC07M002261; -.
DR HGNC; HGNC:14972; SNX8.
DR MIM; 614905; gene.
DR neXtProt; NX_Q9Y5X2; -.
DR PharmGKB; PA37948; -.
DR eggNOG; COG5391; -.
DR HOGENOM; HOG000252992; -.
DR HOVERGEN; HBG017827; -.
DR InParanoid; Q9Y5X2; -.
DR OMA; MMSATVQ; -.
DR OrthoDB; EOG77128D; -.
DR PhylomeDB; Q9Y5X2; -.
DR GenomeRNAi; 29886; -.
DR NextBio; 52423; -.
DR PRO; PR:Q9Y5X2; -.
DR ArrayExpress; Q9Y5X2; -.
DR Bgee; Q9Y5X2; -.
DR CleanEx; HS_SNX8; -.
DR Genevestigator; Q9Y5X2; -.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
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 Complete proteome; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT CHAIN 1 465 Sorting nexin-8.
FT /FTId=PRO_0000213851.
FT DOMAIN 73 181 PX.
FT BINDING 109 109 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 135 135 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 148 148 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT MOD_RES 452 452 Phosphothreonine.
FT MOD_RES 456 456 Phosphoserine.
FT VARIANT 147 147 A -> G (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=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
//
ID SNX8_HUMAN Reviewed; 465 AA.
AC Q9Y5X2; A4D207; Q96I67;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Sorting nexin-8;
GN Name=SNX8;
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].
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
RT nexin 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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS SPECTROMETRY.
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.,
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).
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT 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
CC from early endosomes to the trans-Golgi network.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-1752557, EBI-1752557;
CC P16333:NCK1; NbExp=2; IntAct=EBI-1752557, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Colocalizes with retromer
CC components.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
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; 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 RefSeq; NP_037453.1; NM_013321.2.
DR UniGene; Hs.584900; -.
DR ProteinModelPortal; Q9Y5X2; -.
DR SMR; Q9Y5X2; 92-330.
DR IntAct; Q9Y5X2; 10.
DR MINT; MINT-3087539; -.
DR STRING; 9606.ENSP00000222990; -.
DR PhosphoSite; Q9Y5X2; -.
DR DMDM; 10720288; -.
DR PaxDb; Q9Y5X2; -.
DR PRIDE; Q9Y5X2; -.
DR DNASU; 29886; -.
DR Ensembl; ENST00000222990; ENSP00000222990; ENSG00000106266.
DR GeneID; 29886; -.
DR KEGG; hsa:29886; -.
DR UCSC; uc003slw.3; human.
DR CTD; 29886; -.
DR GeneCards; GC07M002261; -.
DR HGNC; HGNC:14972; SNX8.
DR MIM; 614905; gene.
DR neXtProt; NX_Q9Y5X2; -.
DR PharmGKB; PA37948; -.
DR eggNOG; COG5391; -.
DR HOGENOM; HOG000252992; -.
DR HOVERGEN; HBG017827; -.
DR InParanoid; Q9Y5X2; -.
DR OMA; MMSATVQ; -.
DR OrthoDB; EOG77128D; -.
DR PhylomeDB; Q9Y5X2; -.
DR GenomeRNAi; 29886; -.
DR NextBio; 52423; -.
DR PRO; PR:Q9Y5X2; -.
DR ArrayExpress; Q9Y5X2; -.
DR Bgee; Q9Y5X2; -.
DR CleanEx; HS_SNX8; -.
DR Genevestigator; Q9Y5X2; -.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
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 Complete proteome; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT CHAIN 1 465 Sorting nexin-8.
FT /FTId=PRO_0000213851.
FT DOMAIN 73 181 PX.
FT BINDING 109 109 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 135 135 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 148 148 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT MOD_RES 452 452 Phosphothreonine.
FT MOD_RES 456 456 Phosphoserine.
FT VARIANT 147 147 A -> G (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=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
//
MIM
614905
*RECORD*
*FIELD* NO
614905
*FIELD* TI
*614905 SORTING NEXIN 8; SNX8
*FIELD* TX
DESCRIPTION
SNX8 belongs to a large family of proteins characterized by the presence
read moreof an SNX-type phox (see 608512) homology (PX) domain with conserved
arg-arg-tyr-X-asp/glu and pro-pro-X-pro-X-lys motifs. SNX family members
are predicted to be involved in the sorting of endosomes (Teasdale et
al., 2001).
CLONING
By searching databases for sequences similar to yeast Snx1 (601272),
Teasdale et al. (2001) identified human SNX8. The deduced protein has a
171-amino acid SNX-PH domain in its N-terminal half and a coiled-coil
domain in its C-terminal half.
Using confocal microscopy, Dyve et al. (2009) found that
fluorescence-tagged SNX8 partly colocalized with the endosome marker
EEA1 (605070) in punctate vesicular structures in transfected HeLa
cells. It also partly colocalized with the retromer components SNX1,
VPS35 (601501), SNX2 (605929), and VPS26 (VPS26A; 605506).
GENE FUNCTION
By knockdown of SNX8 in HeLa cells, Dyve et al. (2009) determined that
SNX8 regulates endosome-to-Golgi transport of Shiga toxin and the plant
toxin ricin, possibly via 2 different mechanisms. Knockdown of SNX8
increased Shiga toxin transport to the Golgi, but it moderately reduced
ricin transport. Knockdown of SNX8 had no effect on endocytosis of Shiga
toxin or ricin. Overexpression of fluorescence-tagged SNX8 resulted in a
change in morphology of SNX8-positive structures from small puncta to
enlarged vesicles or compartments. Inhibition of PI3 kinase (see 601232)
resulted in loss of punctate SNX8 localization. Dyve et al. (2009)
concluded that SNX8 is likely a negative regulator of endosome-to-Golgi
trafficking.
MAPPING
Hartz (2012) mapped the SNX8 gene to chromosome 7p22.3 based on an
alignment of the SNX8 sequence (GenBank GENBANK AF121858) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Dyve, A. B.; Bergan, J.; Utskarpen, A.; Sandvig, K.: Sorting nexin
8 regulates endosome-to-Golgi transport. Biochem. Biophys. Res. Commun. 390:
109-114, 2009.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/24/2012.
3. Teasdale, R. D.; Loci, D.; Houghton, F.; Karlsson, L.; Gleeson,
P. A.: A large family of endosome-localized proteins related to sorting
nexin 1. Biochem. J. 358: 7-16, 2001.
*FIELD* CD
Patricia A. Hartz: 11/1/2012
*FIELD* ED
mgross: 11/01/2012
*RECORD*
*FIELD* NO
614905
*FIELD* TI
*614905 SORTING NEXIN 8; SNX8
*FIELD* TX
DESCRIPTION
SNX8 belongs to a large family of proteins characterized by the presence
read moreof an SNX-type phox (see 608512) homology (PX) domain with conserved
arg-arg-tyr-X-asp/glu and pro-pro-X-pro-X-lys motifs. SNX family members
are predicted to be involved in the sorting of endosomes (Teasdale et
al., 2001).
CLONING
By searching databases for sequences similar to yeast Snx1 (601272),
Teasdale et al. (2001) identified human SNX8. The deduced protein has a
171-amino acid SNX-PH domain in its N-terminal half and a coiled-coil
domain in its C-terminal half.
Using confocal microscopy, Dyve et al. (2009) found that
fluorescence-tagged SNX8 partly colocalized with the endosome marker
EEA1 (605070) in punctate vesicular structures in transfected HeLa
cells. It also partly colocalized with the retromer components SNX1,
VPS35 (601501), SNX2 (605929), and VPS26 (VPS26A; 605506).
GENE FUNCTION
By knockdown of SNX8 in HeLa cells, Dyve et al. (2009) determined that
SNX8 regulates endosome-to-Golgi transport of Shiga toxin and the plant
toxin ricin, possibly via 2 different mechanisms. Knockdown of SNX8
increased Shiga toxin transport to the Golgi, but it moderately reduced
ricin transport. Knockdown of SNX8 had no effect on endocytosis of Shiga
toxin or ricin. Overexpression of fluorescence-tagged SNX8 resulted in a
change in morphology of SNX8-positive structures from small puncta to
enlarged vesicles or compartments. Inhibition of PI3 kinase (see 601232)
resulted in loss of punctate SNX8 localization. Dyve et al. (2009)
concluded that SNX8 is likely a negative regulator of endosome-to-Golgi
trafficking.
MAPPING
Hartz (2012) mapped the SNX8 gene to chromosome 7p22.3 based on an
alignment of the SNX8 sequence (GenBank GENBANK AF121858) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Dyve, A. B.; Bergan, J.; Utskarpen, A.; Sandvig, K.: Sorting nexin
8 regulates endosome-to-Golgi transport. Biochem. Biophys. Res. Commun. 390:
109-114, 2009.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/24/2012.
3. Teasdale, R. D.; Loci, D.; Houghton, F.; Karlsson, L.; Gleeson,
P. A.: A large family of endosome-localized proteins related to sorting
nexin 1. Biochem. J. 358: 7-16, 2001.
*FIELD* CD
Patricia A. Hartz: 11/1/2012
*FIELD* ED
mgross: 11/01/2012