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Syntaxin-10 (Syn10)

 STX10_HUMAN             Reviewed;         249 AA.
O60499; A6NC41; Q6IAP4; Q96AE8;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
27-SEP-2017, entry version 148.
RecName: Full=Syntaxin-10;
Short=Syn10;
Name=STX10; Synonyms=SYN10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9446797; DOI=10.1006/bbrc.1997.7966;
Tang B.L., Low D.Y.H., Tan A.E.H., Hong W.;
"Syntaxin 10: a member of the syntaxin family localized to the trans-
Golgi network.";
Biochem. Biophys. Res. Commun. 242:345-350(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH VSP52.
PubMed=15878329; DOI=10.1016/j.yexcr.2005.01.022;
Liewen H., Meinhold-Heerlein I., Oliveira V., Schwarzenbacher R.,
Luo G., Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.;
"Characterization of the human GARP (Golgi associated retrograde
protein) complex.";
Exp. Cell Res. 306:24-34(2005).
[6]
FUNCTION.
PubMed=18195106; DOI=10.1083/jcb.200707136;
Ganley I.G., Espinosa E., Pfeffer S.R.;
"A syntaxin 10-SNARE complex distinguishes two distinct transport
routes from endosomes to the trans-Golgi in human cells.";
J. Cell Biol. 180:159-172(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-143, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-140 AND
SER-143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND THR-110, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-134; SER-140
AND SER-143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: SNARE involved in vesicular transport from the late
endosomes to the trans-Golgi network.
{ECO:0000269|PubMed:18195106}.
-!- SUBUNIT: Interacts with VPS52. {ECO:0000269|PubMed:15878329}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
Single-pass type IV membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O60499-1; Sequence=Displayed;
Name=2;
IsoId=O60499-2; Sequence=VSP_006347;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at high levels in heart, skeletal
muscle and pancreas.
-!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF035531; AAC05087.1; -; mRNA.
EMBL; CR457110; CAG33391.1; -; mRNA.
EMBL; AC011446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017237; AAH17237.1; -; mRNA.
CCDS; CCDS32922.1; -. [O60499-1]
CCDS; CCDS62571.1; -. [O60499-2]
PIR; JC5922; JC5922.
RefSeq; NP_001258540.1; NM_001271611.1. [O60499-2]
RefSeq; NP_003756.1; NM_003765.2. [O60499-1]
UniGene; Hs.43812; -.
PDB; 4DND; X-ray; 1.40 A; A=1-108.
PDBsum; 4DND; -.
ProteinModelPortal; O60499; -.
SMR; O60499; -.
BioGrid; 114225; 25.
DIP; DIP-60563N; -.
IntAct; O60499; 6.
STRING; 9606.ENSP00000466298; -.
iPTMnet; O60499; -.
PhosphoSitePlus; O60499; -.
SwissPalm; O60499; -.
EPD; O60499; -.
MaxQB; O60499; -.
PaxDb; O60499; -.
PeptideAtlas; O60499; -.
PRIDE; O60499; -.
TopDownProteomics; O60499-1; -. [O60499-1]
Ensembl; ENST00000343587; ENSP00000339350; ENSG00000104915. [O60499-2]
Ensembl; ENST00000587230; ENSP00000466298; ENSG00000104915. [O60499-1]
GeneID; 8677; -.
KEGG; hsa:8677; -.
UCSC; uc021upq.3; human. [O60499-1]
CTD; 8677; -.
EuPathDB; HostDB:ENSG00000104915.14; -.
GeneCards; STX10; -.
HGNC; HGNC:11428; STX10.
HPA; HPA035303; -.
HPA; HPA056439; -.
MIM; 603765; gene.
neXtProt; NX_O60499; -.
OpenTargets; ENSG00000104915; -.
PharmGKB; PA36228; -.
eggNOG; KOG3202; Eukaryota.
eggNOG; ENOG410ZZA3; LUCA.
GeneTree; ENSGT00390000008991; -.
HOGENOM; HOG000237350; -.
HOVERGEN; HBG007194; -.
InParanoid; O60499; -.
KO; K08498; -.
OMA; RWCELLQ; -.
OrthoDB; EOG091G0KE5; -.
PhylomeDB; O60499; -.
Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
SIGNOR; O60499; -.
GeneWiki; STX10; -.
GenomeRNAi; 8677; -.
PMAP-CutDB; O60499; -.
PRO; PR:O60499; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104915; -.
CleanEx; HS_STX10; -.
ExpressionAtlas; O60499; baseline and differential.
Genevisible; O60499; HS.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
InterPro; IPR010989; SNARE.
InterPro; IPR015260; Syntaxin-6_N.
InterPro; IPR006012; Syntaxin/epimorphin_CS.
InterPro; IPR000727; T_SNARE_dom.
Pfam; PF05739; SNARE; 1.
Pfam; PF09177; Syntaxin-6_N; 1.
SMART; SM00397; t_SNARE; 1.
SUPFAM; SSF47661; SSF47661; 1.
PROSITE; PS00914; SYNTAXIN; 1.
PROSITE; PS50192; T_SNARE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Golgi apparatus; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 249 Syntaxin-10.
/FTId=PRO_0000210220.
TOPO_DOM 2 228 Cytoplasmic. {ECO:0000255}.
TRANSMEM 229 249 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
DOMAIN 157 219 t-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
COILED 41 69 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 110 110 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 76 124 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006347.
HELIX 7 30 {ECO:0000244|PDB:4DND}.
HELIX 42 73 {ECO:0000244|PDB:4DND}.
HELIX 75 78 {ECO:0000244|PDB:4DND}.
HELIX 82 106 {ECO:0000244|PDB:4DND}.
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


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