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STX8_HUMAN
ID   STX8_HUMAN              Reviewed;         236 AA.
AC   Q9UNK0; O60712; Q53XT8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Syntaxin-8;
GN   Name=STX8;
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=9852078; DOI=10.1074/jbc.273.51.34171;
RA   Steegmaier M., Yang B., Yoo J.-S., Huang B., Shen M., Yu S., Luo Y.,
RA   Scheller R.H.;
RT   "Three novel proteins of the syntaxin/SNAP-25 family.";
RL   J. Biol. Chem. 273:34171-34179(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=10198254; DOI=10.1006/bbrc.1999.0503;
RA   Thoreau V., Berges T., Callebaut I., Guillier-Gencik Z., Gressin L.,
RA   Bernheim A., Karst F., Mornon J.-P., Kitzis A., Chomel J.-C.;
RT   "Molecular cloning, expression analysis, and chromosomal localization of
RT   human syntaxin 8 (STX8).";
RL   Biochem. Biophys. Res. Commun. 257:577-583(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Subramaniam V.N., Loh E., Hong W.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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   [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   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: Vesicle trafficking protein that functions in the early
CC       secretory pathway, possibly by mediating retrograde transport from cis-
CC       Golgi membranes to the ER.
CC   -!- SUBUNIT: Forms a SNARE complex with STX7, VTI1B and VAMP8 which
CC       functions in the homotypic fusion of late endosomes. Part of the SNARE
CC       core complex containing STX7, VAMP8 and VTI1B. Interacts with VAMP8 (By
CC       similarity). Interacts with HECTD3 (By similarity). Interacts with TPC1
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O88983}.
CC   -!- INTERACTION:
CC       Q9UNK0; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-727240, EBI-19125216;
CC       Q9UNK0; P07307-3: ASGR2; NbExp=3; IntAct=EBI-727240, EBI-12808270;
CC       Q9UNK0; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-727240, EBI-747430;
CC       Q9UNK0; Q13323: BIK; NbExp=3; IntAct=EBI-727240, EBI-700794;
CC       Q9UNK0; Q8WZ55: BSND; NbExp=3; IntAct=EBI-727240, EBI-7996695;
CC       Q9UNK0; Q496F6: CD300E; NbExp=3; IntAct=EBI-727240, EBI-18010148;
CC       Q9UNK0; P11912: CD79A; NbExp=3; IntAct=EBI-727240, EBI-7797864;
CC       Q9UNK0; Q9HA82: CERS4; NbExp=3; IntAct=EBI-727240, EBI-2622997;
CC       Q9UNK0; O95484: CLDN9; NbExp=3; IntAct=EBI-727240, EBI-18341636;
CC       Q9UNK0; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-727240, EBI-18013275;
CC       Q9UNK0; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-727240, EBI-6942903;
CC       Q9UNK0; Q9BPW9-4: DHRS9; NbExp=3; IntAct=EBI-727240, EBI-19157435;
CC       Q9UNK0; Q15125: EBP; NbExp=3; IntAct=EBI-727240, EBI-3915253;
CC       Q9UNK0; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-727240, EBI-781551;
CC       Q9UNK0; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-727240, EBI-18636064;
CC       Q9UNK0; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-727240, EBI-18304435;
CC       Q9UNK0; O15552: FFAR2; NbExp=3; IntAct=EBI-727240, EBI-2833872;
CC       Q9UNK0; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-727240, EBI-3918971;
CC       Q9UNK0; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-727240, EBI-12142257;
CC       Q9UNK0; P48165: GJA8; NbExp=3; IntAct=EBI-727240, EBI-17458373;
CC       Q9UNK0; P08034: GJB1; NbExp=3; IntAct=EBI-727240, EBI-17565645;
CC       Q9UNK0; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-727240, EBI-3917143;
CC       Q9UNK0; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-727240, EBI-11955647;
CC       Q9UNK0; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-727240, EBI-13345167;
CC       Q9UNK0; O15529: GPR42; NbExp=3; IntAct=EBI-727240, EBI-18076404;
CC       Q9UNK0; Q8TED1: GPX8; NbExp=3; IntAct=EBI-727240, EBI-11721746;
CC       Q9UNK0; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-727240, EBI-10266796;
CC       Q9UNK0; Q96MG2: JSRP1; NbExp=5; IntAct=EBI-727240, EBI-11305455;
CC       Q9UNK0; Q16558-2: KCNMB1; NbExp=3; IntAct=EBI-727240, EBI-17703887;
CC       Q9UNK0; Q96PE7: MCEE; NbExp=3; IntAct=EBI-727240, EBI-10292326;
CC       Q9UNK0; Q07820: MCL1; NbExp=3; IntAct=EBI-727240, EBI-1003422;
CC       Q9UNK0; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-727240, EBI-11956541;
CC       Q9UNK0; Q99735: MGST2; NbExp=3; IntAct=EBI-727240, EBI-11324706;
CC       Q9UNK0; O14880: MGST3; NbExp=3; IntAct=EBI-727240, EBI-724754;
CC       Q9UNK0; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-727240, EBI-6163737;
CC       Q9UNK0; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-727240, EBI-12806656;
CC       Q9UNK0; Q96E29: MTERF3; NbExp=3; IntAct=EBI-727240, EBI-7825321;
CC       Q9UNK0; Q68D85: NCR3LG1; NbExp=3; IntAct=EBI-727240, EBI-14061804;
CC       Q9UNK0; Q9Y375: NDUFAF1; NbExp=3; IntAct=EBI-727240, EBI-741874;
CC       Q9UNK0; Q8N183: NDUFAF2; NbExp=3; IntAct=EBI-727240, EBI-2682365;
CC       Q9UNK0; O00623: PEX12; NbExp=3; IntAct=EBI-727240, EBI-594836;
CC       Q9UNK0; Q86VR2: RETREG3; NbExp=5; IntAct=EBI-727240, EBI-10192441;
CC       Q9UNK0; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-727240, EBI-18397230;
CC       Q9UNK0; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-727240, EBI-3920694;
CC       Q9UNK0; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-727240, EBI-17247926;
CC       Q9UNK0; O95470: SGPL1; NbExp=3; IntAct=EBI-727240, EBI-1046170;
CC       Q9UNK0; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-727240, EBI-18159983;
CC       Q9UNK0; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-727240, EBI-17595455;
CC       Q9UNK0; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-727240, EBI-17280858;
CC       Q9UNK0; P49675: STAR; NbExp=3; IntAct=EBI-727240, EBI-722932;
CC       Q9UNK0; Q9H169-2: STMN4; NbExp=3; IntAct=EBI-727240, EBI-20117546;
CC       Q9UNK0; Q16623: STX1A; NbExp=3; IntAct=EBI-727240, EBI-712466;
CC       Q9UNK0; P32856-2: STX2; NbExp=3; IntAct=EBI-727240, EBI-11956649;
CC       Q9UNK0; Q12846: STX4; NbExp=6; IntAct=EBI-727240, EBI-744942;
CC       Q9UNK0; Q13190: STX5; NbExp=3; IntAct=EBI-727240, EBI-714206;
CC       Q9UNK0; Q6PL24: TMED8; NbExp=4; IntAct=EBI-727240, EBI-11603430;
CC       Q9UNK0; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-727240, EBI-8638294;
CC       Q9UNK0; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-727240, EBI-11724423;
CC       Q9UNK0; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-727240, EBI-6269551;
CC       Q9UNK0; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-727240, EBI-10982110;
CC       Q9UNK0; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-727240, EBI-2548832;
CC       Q9UNK0; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-727240, EBI-11724433;
CC       Q9UNK0; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-727240, EBI-12345267;
CC       Q9UNK0; O95859: TSPAN12; NbExp=3; IntAct=EBI-727240, EBI-2466403;
CC       Q9UNK0; O95183: VAMP5; NbExp=4; IntAct=EBI-727240, EBI-10191195;
CC       Q9UNK0; Q9UEU0: VTI1B; NbExp=7; IntAct=EBI-727240, EBI-723716;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type IV
CC       membrane protein {ECO:0000250}. Note=Preferentially associated with the
CC       early endosome. To a lesser extent, also present in late endosome, the
CC       plasma membrane and coated pits (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart. Also found in brain,
CC       kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas.
CC   -!- PTM: Ubiquitinated by HECTD3. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; AF115323; AAD20831.1; -; mRNA.
DR   EMBL; AF062077; AAC36466.1; -; mRNA.
DR   EMBL; AF036715; AAC95285.1; -; mRNA.
DR   EMBL; BT007319; AAP35983.1; -; mRNA.
DR   EMBL; CH471108; EAW90029.1; -; Genomic_DNA.
DR   EMBL; BC009713; AAH09713.1; -; mRNA.
DR   CCDS; CCDS32565.1; -.
DR   RefSeq; NP_004844.1; NM_004853.2.
DR   AlphaFoldDB; Q9UNK0; -.
DR   SMR; Q9UNK0; -.
DR   BioGRID; 114867; 217.
DR   DIP; DIP-47274N; -.
DR   IntAct; Q9UNK0; 136.
DR   MINT; Q9UNK0; -.
DR   STRING; 9606.ENSP00000305255; -.
DR   iPTMnet; Q9UNK0; -.
DR   PhosphoSitePlus; Q9UNK0; -.
DR   SwissPalm; Q9UNK0; -.
DR   BioMuta; STX8; -.
DR   DMDM; 9297054; -.
DR   EPD; Q9UNK0; -.
DR   jPOST; Q9UNK0; -.
DR   MassIVE; Q9UNK0; -.
DR   MaxQB; Q9UNK0; -.
DR   PaxDb; Q9UNK0; -.
DR   PeptideAtlas; Q9UNK0; -.
DR   PRIDE; Q9UNK0; -.
DR   ProteomicsDB; 85299; -.
DR   Antibodypedia; 726; 194 antibodies from 27 providers.
DR   DNASU; 9482; -.
DR   Ensembl; ENST00000306357.9; ENSP00000305255.2; ENSG00000170310.15.
DR   GeneID; 9482; -.
DR   KEGG; hsa:9482; -.
DR   MANE-Select; ENST00000306357.9; ENSP00000305255.2; NM_004853.3; NP_004844.1.
DR   UCSC; uc002glx.4; human.
DR   CTD; 9482; -.
DR   DisGeNET; 9482; -.
DR   GeneCards; STX8; -.
DR   HGNC; HGNC:11443; STX8.
DR   HPA; ENSG00000170310; Low tissue specificity.
DR   MIM; 604203; gene.
DR   neXtProt; NX_Q9UNK0; -.
DR   OpenTargets; ENSG00000170310; -.
DR   PharmGKB; PA36240; -.
DR   VEuPathDB; HostDB:ENSG00000170310; -.
DR   eggNOG; KOG3202; Eukaryota.
DR   GeneTree; ENSGT00390000007779; -.
DR   HOGENOM; CLU_099972_1_0_1; -.
DR   InParanoid; Q9UNK0; -.
DR   OMA; CGYWIVI; -.
DR   OrthoDB; 1455798at2759; -.
DR   PhylomeDB; Q9UNK0; -.
DR   TreeFam; TF323262; -.
DR   PathwayCommons; Q9UNK0; -.
DR   SignaLink; Q9UNK0; -.
DR   BioGRID-ORCS; 9482; 13 hits in 1081 CRISPR screens.
DR   ChiTaRS; STX8; human.
DR   GeneWiki; STX8; -.
DR   GenomeRNAi; 9482; -.
DR   Pharos; Q9UNK0; Tbio.
DR   PRO; PR:Q9UNK0; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9UNK0; protein.
DR   Bgee; ENSG00000170310; Expressed in sperm and 205 other tissues.
DR   ExpressionAtlas; Q9UNK0; baseline and differential.
DR   Genevisible; Q9UNK0; HS.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR   GO; GO:0055037; C:recycling endosome; 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:0031982; C:vesicle; IDA:UniProtKB.
DR   GO; GO:0019869; F:chloride channel inhibitor activity; 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:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR   GO; GO:0045022; P:early endosome to late endosome transport; IDA:UniProtKB.
DR   GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   CDD; cd15852; SNARE_Syntaxin8; 1.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR041875; Syntaxin-8_SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; PTHR19957; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..236
FT                   /note="Syntaxin-8"
FT                   /id="PRO_0000210217"
FT   TOPO_DOM        1..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..232
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..236
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          145..207
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   COILED          42..65
FT                   /evidence="ECO:0000255"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88983"
FT   CONFLICT        78
FT                   /note="R -> Q (in Ref. 1; AAD20831)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   236 AA;  26907 MW;  1E64A0DA77584CC4 CRC64;
     MAPDPWFSTY DSTCQIAQEI AEKIQQRNQY ERKGEKAPKL TVTIRALLQN LKEKIALLKD
     LLLRAVSTHQ ITQLEGDRRQ NLLDDLVTRE RLLLASFKNE GAEPDLIRSS LMSEEAKRGA
     PNPWLFEEPE ETRGLGFDEI RQQQQKIIQE QDAGLDALSS IISRQKQMGQ EIGNELDEQN
     EIIDDLANLV ENTDEKLRNE TRRVNMVDRK SASCGMIMVI LLLLVAIVVV AVWPTN
 
 
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