STX10_HUMAN
ID STX10_HUMAN Reviewed; 249 AA.
AC O60499; A6NC41; Q6IAP4; Q96AE8;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Syntaxin-10;
DE Short=Syn10;
GN Name=STX10; Synonyms=SYN10;
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).
RX PubMed=9446797; DOI=10.1006/bbrc.1997.7966;
RA Tang B.L., Low D.Y.H., Tan A.E.H., Hong W.;
RT "Syntaxin 10: a member of the syntaxin family localized to the trans-Golgi
RT network.";
RL Biochem. Biophys. Res. Commun. 242:345-350(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 INTERACTION WITH VSP52.
RX PubMed=15878329; DOI=10.1016/j.yexcr.2005.01.022;
RA Liewen H., Meinhold-Heerlein I., Oliveira V., Schwarzenbacher R., Luo G.,
RA Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.;
RT "Characterization of the human GARP (Golgi associated retrograde protein)
RT complex.";
RL Exp. Cell Res. 306:24-34(2005).
RN [6]
RP FUNCTION.
RX PubMed=18195106; DOI=10.1083/jcb.200707136;
RA Ganley I.G., Espinosa E., Pfeffer S.R.;
RT "A syntaxin 10-SNARE complex distinguishes two distinct transport routes
RT from endosomes to the trans-Golgi in human cells.";
RL J. Cell Biol. 180:159-172(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-143, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-140 AND SER-143, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND THR-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-134; SER-140 AND
RP SER-143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [14]
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).
RN [15]
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: SNARE involved in vesicular transport from the late endosomes
CC to the trans-Golgi network. {ECO:0000269|PubMed:18195106}.
CC -!- SUBUNIT: Interacts with VPS52. {ECO:0000269|PubMed:15878329}.
CC -!- INTERACTION:
CC O60499-1; Q9UID3-1: VPS51; NbExp=5; IntAct=EBI-16067850, EBI-16067837;
CC O60499-2; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-12094584, EBI-745535;
CC O60499-2; Q5JRM2: CXorf66; NbExp=3; IntAct=EBI-12094584, EBI-12823659;
CC O60499-2; Q16623: STX1A; NbExp=3; IntAct=EBI-12094584, EBI-712466;
CC O60499-2; Q12846: STX4; NbExp=3; IntAct=EBI-12094584, EBI-744942;
CC O60499-2; Q96IK0: TMEM101; NbExp=3; IntAct=EBI-12094584, EBI-3922699;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type IV membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60499-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60499-2; Sequence=VSP_006347;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart, skeletal muscle
CC and pancreas.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AF035531; AAC05087.1; -; mRNA.
DR EMBL; CR457110; CAG33391.1; -; mRNA.
DR EMBL; AC011446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017237; AAH17237.1; -; mRNA.
DR CCDS; CCDS32922.1; -. [O60499-1]
DR CCDS; CCDS62571.1; -. [O60499-2]
DR PIR; JC5922; JC5922.
DR RefSeq; NP_001258540.1; NM_001271611.1. [O60499-2]
DR RefSeq; NP_003756.1; NM_003765.2. [O60499-1]
DR PDB; 4DND; X-ray; 1.40 A; A=1-108.
DR PDBsum; 4DND; -.
DR AlphaFoldDB; O60499; -.
DR SMR; O60499; -.
DR BioGRID; 114225; 143.
DR DIP; DIP-60563N; -.
DR IntAct; O60499; 34.
DR MINT; O60499; -.
DR STRING; 9606.ENSP00000466298; -.
DR iPTMnet; O60499; -.
DR MetOSite; O60499; -.
DR PhosphoSitePlus; O60499; -.
DR SwissPalm; O60499; -.
DR BioMuta; STX10; -.
DR EPD; O60499; -.
DR jPOST; O60499; -.
DR MassIVE; O60499; -.
DR MaxQB; O60499; -.
DR PaxDb; O60499; -.
DR PeptideAtlas; O60499; -.
DR PRIDE; O60499; -.
DR ProteomicsDB; 49434; -. [O60499-1]
DR ProteomicsDB; 49435; -. [O60499-2]
DR TopDownProteomics; O60499-1; -. [O60499-1]
DR Antibodypedia; 43275; 164 antibodies from 20 providers.
DR DNASU; 8677; -.
DR Ensembl; ENST00000343587.9; ENSP00000339350.4; ENSG00000104915.15. [O60499-2]
DR Ensembl; ENST00000587230.6; ENSP00000466298.1; ENSG00000104915.15. [O60499-1]
DR GeneID; 8677; -.
DR KEGG; hsa:8677; -.
DR MANE-Select; ENST00000587230.6; ENSP00000466298.1; NM_003765.3; NP_003756.1.
DR UCSC; uc021upq.3; human. [O60499-1]
DR CTD; 8677; -.
DR DisGeNET; 8677; -.
DR GeneCards; STX10; -.
DR HGNC; HGNC:11428; STX10.
DR HPA; ENSG00000104915; Low tissue specificity.
DR MIM; 603765; gene.
DR neXtProt; NX_O60499; -.
DR OpenTargets; ENSG00000104915; -.
DR PharmGKB; PA36228; -.
DR VEuPathDB; HostDB:ENSG00000104915; -.
DR eggNOG; KOG3202; Eukaryota.
DR GeneTree; ENSGT00940000163101; -.
DR HOGENOM; CLU_061883_1_0_1; -.
DR InParanoid; O60499; -.
DR OMA; DMKDHMV; -.
DR OrthoDB; 1563292at2759; -.
DR PhylomeDB; O60499; -.
DR PathwayCommons; O60499; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; O60499; -.
DR SIGNOR; O60499; -.
DR BioGRID-ORCS; 8677; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; STX10; human.
DR GeneWiki; STX10; -.
DR GenomeRNAi; 8677; -.
DR Pharos; O60499; Tbio.
DR PRO; PR:O60499; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O60499; protein.
DR Bgee; ENSG00000104915; Expressed in monocyte and 196 other tissues.
DR ExpressionAtlas; O60499; baseline and differential.
DR Genevisible; O60499; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR015260; Syntaxin-6_N.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF09177; Syntaxin-6_N; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..249
FT /note="Syntaxin-10"
FT /id="PRO_0000210220"
FT TOPO_DOM 2..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 157..219
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 41..69
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 76..124
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006347"
FT HELIX 7..30
FT /evidence="ECO:0007829|PDB:4DND"
FT HELIX 42..73
FT /evidence="ECO:0007829|PDB:4DND"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:4DND"
FT HELIX 82..106
FT /evidence="ECO:0007829|PDB:4DND"
SQ SEQUENCE 249 AA; 28114 MW; 795AB3055F25AD5F CRC64;
MSLEDPFFVV RGEVQKAVNT ARGLYQRWCE LLQESAAVGR EELDWTTNEL RNGLRSIEWD
LEDLEETIGI VEANPGKFKL PAGDLQERKV FVERMREAVQ EMKDHMVSPT AVAFLERNNR
EILAGKPAAQ KSPSDLLDAS AVSATSRYIE EQQATQQLIM DEQDQQLEMV SGSIQVLKHM
SGRVGEELDE QGIMLDAFAQ EMDHTQSRMD GVLRKLAKVS HMTSDRRQWC AIAVLVGVLL
LVLILLFSL
