Full text data of STX6
STX6
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Syntaxin-6
Syntaxin-6
UniProt
O43752
ID STX6_HUMAN Reviewed; 255 AA.
AC O43752; B2R652; Q5VY08; Q6FH83;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Syntaxin-6;
GN Name=STX6;
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=10080545;
RA Martin-Martin B., Nabokina S.M., Lazo P.A., Mollinedo F.;
RT "Co-expression of several human syntaxin genes in neutrophils and
RT differentiating HL-60 cells: variant isoforms and detection of
RT syntaxin 1.";
RL J. Leukoc. Biol. 65:397-406(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GOPC.
RX PubMed=11384996; DOI=10.1074/jbc.M104137200;
RA Charest A., Lane K., McMahon K., Housman D.E.;
RT "Association of a novel PDZ domain-containing peripheral Golgi protein
RT with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein
RT (NSF) attachment protein receptor) protein syntaxin 6.";
RL J. Biol. Chem. 276:29456-29465(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 47-117 IN COMPLEX WITH
RP STX12; VTI1A AND VAMP4, AND SUBUNIT.
RX PubMed=17159904; DOI=10.1038/sj.emboj.7601467;
RA Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J.,
RA Wahl M.C., Jahn R.;
RT "Early endosomal SNAREs form a structurally conserved SNARE complex
RT and fuse liposomes with multiple topologies.";
RL EMBO J. 26:9-18(2007).
CC -!- FUNCTION: Involved in intracellular vesicle trafficking.
CC -!- SUBUNIT: Binds EEA1. Interacts with VPS45A. Interacts with MARCH2
CC and MARCH3 (By similarity). Interacts with GOPC. Identified in a
CC complex containing STX6, STX12, VAMP4 and VTI1A.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC IV membrane protein (Potential).
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR EMBL; AJ002078; CAA05177.1; -; mRNA.
DR EMBL; CR541856; CAG46654.1; -; mRNA.
DR EMBL; CR541873; CAG46671.1; -; mRNA.
DR EMBL; AK312440; BAG35349.1; -; mRNA.
DR EMBL; AL356267; CAH72301.1; -; Genomic_DNA.
DR EMBL; AL162431; CAH72301.1; JOINED; Genomic_DNA.
DR EMBL; AL162431; CAH74088.1; -; Genomic_DNA.
DR EMBL; AL356267; CAH74088.1; JOINED; Genomic_DNA.
DR EMBL; CH471067; EAW91091.1; -; Genomic_DNA.
DR EMBL; BC009944; AAH09944.1; -; mRNA.
DR RefSeq; NP_005810.1; NM_005819.5.
DR UniGene; Hs.518417; -.
DR UniGene; Hs.737037; -.
DR PDB; 2NPS; X-ray; 2.50 A; D=169-234.
DR PDBsum; 2NPS; -.
DR ProteinModelPortal; O43752; -.
DR SMR; O43752; 4-109, 170-232.
DR IntAct; O43752; 9.
DR MINT; MINT-5002256; -.
DR STRING; 9606.ENSP00000258301; -.
DR PhosphoSite; O43752; -.
DR PaxDb; O43752; -.
DR PeptideAtlas; O43752; -.
DR PRIDE; O43752; -.
DR DNASU; 10228; -.
DR Ensembl; ENST00000258301; ENSP00000258301; ENSG00000135823.
DR GeneID; 10228; -.
DR KEGG; hsa:10228; -.
DR UCSC; uc010pnr.2; human.
DR CTD; 10228; -.
DR GeneCards; GC01M180941; -.
DR HGNC; HGNC:11441; STX6.
DR HPA; HPA038558; -.
DR MIM; 603944; gene.
DR neXtProt; NX_O43752; -.
DR PharmGKB; PA36238; -.
DR eggNOG; NOG46901; -.
DR HOGENOM; HOG000237350; -.
DR HOVERGEN; HBG007194; -.
DR InParanoid; O43752; -.
DR KO; K08498; -.
DR OMA; QVVREMK; -.
DR OrthoDB; EOG7JHM7F; -.
DR PhylomeDB; O43752; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; STX6; human.
DR EvolutionaryTrace; O43752; -.
DR GeneWiki; STX6; -.
DR GenomeRNAi; 10228; -.
DR NextBio; 38729; -.
DR PRO; PR:O43752; -.
DR ArrayExpress; O43752; -.
DR Bgee; O43752; -.
DR CleanEx; HS_STX6; -.
DR Genevestigator; O43752; -.
DR GO; GO:0030136; C:clathrin-coated vesicle; TAS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IBA:RefGenome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:BHF-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:RefGenome.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:RefGenome.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; IPI:UniProtKB.
DR InterPro; IPR015260; Syntaxin-6_N.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR010989; t-SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
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; Coiled coil; Complete proteome;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 255 Syntaxin-6.
FT /FTId=PRO_0000210208.
FT TOPO_DOM 2 234 Cytoplasmic (Potential).
FT TRANSMEM 235 255 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT DOMAIN 163 225 t-SNARE coiled-coil homology.
FT COILED 41 74 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 152 152 Phosphoserine.
FT CONFLICT 77 77 K -> R (in Ref. 2; CAG46654).
FT HELIX 173 229
SQ SEQUENCE 255 AA; 29176 MW; CC05C025DE1FE89E CRC64;
MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQDPSTATR EEIDWTTNEL RNNLRSIEWD
LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQVVR DMKDQMSTSS VQALAERKNR
QALLGDSGSQ NWSTGTTDKY GRLDRELQRA NSHFIEEQQA QQQLIVEQQD EQLELVSGSI
GVLKNMSQRI GGELEEQAVM LEDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI
LFAVLLVVLI LFLVL
//
ID STX6_HUMAN Reviewed; 255 AA.
AC O43752; B2R652; Q5VY08; Q6FH83;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Syntaxin-6;
GN Name=STX6;
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=10080545;
RA Martin-Martin B., Nabokina S.M., Lazo P.A., Mollinedo F.;
RT "Co-expression of several human syntaxin genes in neutrophils and
RT differentiating HL-60 cells: variant isoforms and detection of
RT syntaxin 1.";
RL J. Leukoc. Biol. 65:397-406(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GOPC.
RX PubMed=11384996; DOI=10.1074/jbc.M104137200;
RA Charest A., Lane K., McMahon K., Housman D.E.;
RT "Association of a novel PDZ domain-containing peripheral Golgi protein
RT with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein
RT (NSF) attachment protein receptor) protein syntaxin 6.";
RL J. Biol. Chem. 276:29456-29465(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 47-117 IN COMPLEX WITH
RP STX12; VTI1A AND VAMP4, AND SUBUNIT.
RX PubMed=17159904; DOI=10.1038/sj.emboj.7601467;
RA Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J.,
RA Wahl M.C., Jahn R.;
RT "Early endosomal SNAREs form a structurally conserved SNARE complex
RT and fuse liposomes with multiple topologies.";
RL EMBO J. 26:9-18(2007).
CC -!- FUNCTION: Involved in intracellular vesicle trafficking.
CC -!- SUBUNIT: Binds EEA1. Interacts with VPS45A. Interacts with MARCH2
CC and MARCH3 (By similarity). Interacts with GOPC. Identified in a
CC complex containing STX6, STX12, VAMP4 and VTI1A.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC IV membrane protein (Potential).
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR EMBL; AJ002078; CAA05177.1; -; mRNA.
DR EMBL; CR541856; CAG46654.1; -; mRNA.
DR EMBL; CR541873; CAG46671.1; -; mRNA.
DR EMBL; AK312440; BAG35349.1; -; mRNA.
DR EMBL; AL356267; CAH72301.1; -; Genomic_DNA.
DR EMBL; AL162431; CAH72301.1; JOINED; Genomic_DNA.
DR EMBL; AL162431; CAH74088.1; -; Genomic_DNA.
DR EMBL; AL356267; CAH74088.1; JOINED; Genomic_DNA.
DR EMBL; CH471067; EAW91091.1; -; Genomic_DNA.
DR EMBL; BC009944; AAH09944.1; -; mRNA.
DR RefSeq; NP_005810.1; NM_005819.5.
DR UniGene; Hs.518417; -.
DR UniGene; Hs.737037; -.
DR PDB; 2NPS; X-ray; 2.50 A; D=169-234.
DR PDBsum; 2NPS; -.
DR ProteinModelPortal; O43752; -.
DR SMR; O43752; 4-109, 170-232.
DR IntAct; O43752; 9.
DR MINT; MINT-5002256; -.
DR STRING; 9606.ENSP00000258301; -.
DR PhosphoSite; O43752; -.
DR PaxDb; O43752; -.
DR PeptideAtlas; O43752; -.
DR PRIDE; O43752; -.
DR DNASU; 10228; -.
DR Ensembl; ENST00000258301; ENSP00000258301; ENSG00000135823.
DR GeneID; 10228; -.
DR KEGG; hsa:10228; -.
DR UCSC; uc010pnr.2; human.
DR CTD; 10228; -.
DR GeneCards; GC01M180941; -.
DR HGNC; HGNC:11441; STX6.
DR HPA; HPA038558; -.
DR MIM; 603944; gene.
DR neXtProt; NX_O43752; -.
DR PharmGKB; PA36238; -.
DR eggNOG; NOG46901; -.
DR HOGENOM; HOG000237350; -.
DR HOVERGEN; HBG007194; -.
DR InParanoid; O43752; -.
DR KO; K08498; -.
DR OMA; QVVREMK; -.
DR OrthoDB; EOG7JHM7F; -.
DR PhylomeDB; O43752; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; STX6; human.
DR EvolutionaryTrace; O43752; -.
DR GeneWiki; STX6; -.
DR GenomeRNAi; 10228; -.
DR NextBio; 38729; -.
DR PRO; PR:O43752; -.
DR ArrayExpress; O43752; -.
DR Bgee; O43752; -.
DR CleanEx; HS_STX6; -.
DR Genevestigator; O43752; -.
DR GO; GO:0030136; C:clathrin-coated vesicle; TAS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IBA:RefGenome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:BHF-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:RefGenome.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:RefGenome.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; IPI:UniProtKB.
DR InterPro; IPR015260; Syntaxin-6_N.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR010989; t-SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
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; Coiled coil; Complete proteome;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 255 Syntaxin-6.
FT /FTId=PRO_0000210208.
FT TOPO_DOM 2 234 Cytoplasmic (Potential).
FT TRANSMEM 235 255 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT DOMAIN 163 225 t-SNARE coiled-coil homology.
FT COILED 41 74 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 152 152 Phosphoserine.
FT CONFLICT 77 77 K -> R (in Ref. 2; CAG46654).
FT HELIX 173 229
SQ SEQUENCE 255 AA; 29176 MW; CC05C025DE1FE89E CRC64;
MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQDPSTATR EEIDWTTNEL RNNLRSIEWD
LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQVVR DMKDQMSTSS VQALAERKNR
QALLGDSGSQ NWSTGTTDKY GRLDRELQRA NSHFIEEQQA QQQLIVEQQD EQLELVSGSI
GVLKNMSQRI GGELEEQAVM LEDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI
LFAVLLVVLI LFLVL
//
MIM
603944
*RECORD*
*FIELD* NO
603944
*FIELD* TI
*603944 SYNTAXIN 6; STX6
*FIELD* TX
DESCRIPTION
STX6 belongs to the Qbc subfamily of SNARE proteins (see 600322) and
read morelocalizes to the trans-Golgi network (TGN) and endosomes. It has a role
in sorting proteins from endosomes toward either the TGN or lysosomes
(summary by Cheng et al., 2010).
CLONING
By RT-PCR with primers based on the sequence of rat syntaxin-6,
Martin-Martin et al. (1999) isolated a human syntaxin-6 cDNA.
GENE FUNCTION
Exocytosis of various types of cytoplasmic granules present in human
neutrophils plays a critical role in neutrophil biology and appears to
regulate a number of neutrophil functions in both inflammation and
infection. To elucidate the mechanisms that regulate neutrophil
exocytosis, Martin-Martin et al. (1999) studied the expression of
syntaxins, cellular receptors for transport vesicles (see 603765), in
neutrophils. By RT-PCR, they found that neutrophils and peripheral blood
lymphocytes express numerous syntaxins, including syntaxin-1A (186590),
-3 (600876), and -6. The expression of several syntaxin genes increased
during dimethyl sulfoxide-induced differentiation of a human
promyelocytic leukemia cell line toward the neutrophil lineage.
By immunolocalization analysis, Advani et al. (1998) found that STX6
partially colocalizes with VAMP4 (606909) in a punctate juxtanuclear
staining pattern. By immunoprecipitation of rat brain detergent
extracts, Steegmaier et al. (1999) found that STX6 exists in a complex
with VAMP4.
Western blot analysis and immunofluorescence microscopy by Charest et
al. (2001) showed that FIG (GOPC; 606845) interacted through its
C-terminal coiled-coil domain with syntaxin-6 in the Golgi apparatus.
They proposed that FIG may be involved in membrane vesicle trafficking.
Cheng et al. (2010) showed that both STX6 and CAL (GOPC) were involved
in downregulation of CFTR (602421) via lysosome-mediated degradation.
STX6 bound the N terminus of CFTR, and CAL independently bound the C
terminus of CFTR. Overexpression of STX6 reduced cell surface expression
of CFTR and caused its instability, but not in the absence of CAL.
STX6-dependent CFTR instability was sensitive to lysosome inhibition.
Overexpression of a dominant-negative STX6 mutant or knockdown of STX6
resulted in CFTR stability. STX6 and CAL had no effect on the stability
of CFTR with the cystic fibrosis (219700)-associated delta-F508 mutation
(602421.0001), which is retained in the endoplasmic reticulum (ER) and
undergoes ER-associated degradation. Cheng et al. (2010) concluded that
STX6 and CAL function in the TGN and direct trafficking of CFTR to the
lysosome.
BIOCHEMICAL FEATURES
Misura et al. (2002) provided a description of the 3-dimensional
structure of the amino-terminal domain of syntaxin-6. Secondary
structure prediction of SNARE proteins showed that the N-terminal
domains of many syntaxin and SNAP25 (600322) family members are likely
to be similar to one another, but are distinct from those of the VAMP
family members (see VAMP1, 185880), indicating that syntaxin and SNAP25
SNAREs may have shared a common ancestor.
*FIELD* RF
1. Advani, R. J.; Bae, H.-R.; Bock, J. B.; Chao, D. S.; Doung, Y.-C.;
Prekeris, R.; Yoo, J.-S.; Scheller, R. H.: Seven novel mammalian
SNARE proteins localize to distinct membrane compartments. J. Biol.
Chem. 273: 10317-10324, 1998.
2. Charest, A.; Lane, K.; McMahon, K.; Housman, D. E.: Association
of a novel PDZ domain-containing peripheral Golgi protein with the
Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF)
attachment protein receptor) protein syntaxin 6. J. Biol. Chem. 276:
29456-29465, 2001.
3. Cheng, J.; Cebotaru, V.; Cebotaru, L.; Guggino, W. B.: Syntaxin
6 and CAL mediate the degradation of the cystic fibrosis transmembrane
conductance regulator. Molec. Biol. Cell 21: 1178-1187, 2010.
4. Martin-Martin, B.; Nabokina, S. M.; Lazo, P. A.; Mollinedo, F.
: Co-expression of several human syntaxin genes in neutrophils and
differentiating HL-60 cells: various isoforms and detection of syntaxin
1. J. Leuko. Biol. 65: 397-406, 1999.
5. Misura, K. M. S.; Bock, J. B.; Gonzalez, L. C., Jr.; Scheller,
R. H.; Weis, W. I.: Three-dimensional structure of the amino-terminal
domain of syntaxin 6, a SNAP-25 C homolog. Proc. Nat. Acad. Sci. 99:
9184-9189, 2002.
6. Steegmaier, M.; Klumperman, J.; Foletti, D. L.; Yoo, J.-S.; Scheller,
R. H.: Vesicle-associated membrane protein 4 is implicated in trans-Golgi
network vesicle trafficking. Molec. Biol. Cell 10: 1957-1972, 1999.
*FIELD* CN
Patricia A. Hartz - updated: 12/16/2011
Victor A. McKusick - updated: 9/27/2002
Patricia A. Hartz - updated: 5/7/2002
*FIELD* CD
Rebekah S. Rasooly: 6/29/1999
*FIELD* ED
mgross: 03/06/2012
terry: 12/16/2011
alopez: 9/27/2002
carol: 5/7/2002
mgross: 6/29/1999
*RECORD*
*FIELD* NO
603944
*FIELD* TI
*603944 SYNTAXIN 6; STX6
*FIELD* TX
DESCRIPTION
STX6 belongs to the Qbc subfamily of SNARE proteins (see 600322) and
read morelocalizes to the trans-Golgi network (TGN) and endosomes. It has a role
in sorting proteins from endosomes toward either the TGN or lysosomes
(summary by Cheng et al., 2010).
CLONING
By RT-PCR with primers based on the sequence of rat syntaxin-6,
Martin-Martin et al. (1999) isolated a human syntaxin-6 cDNA.
GENE FUNCTION
Exocytosis of various types of cytoplasmic granules present in human
neutrophils plays a critical role in neutrophil biology and appears to
regulate a number of neutrophil functions in both inflammation and
infection. To elucidate the mechanisms that regulate neutrophil
exocytosis, Martin-Martin et al. (1999) studied the expression of
syntaxins, cellular receptors for transport vesicles (see 603765), in
neutrophils. By RT-PCR, they found that neutrophils and peripheral blood
lymphocytes express numerous syntaxins, including syntaxin-1A (186590),
-3 (600876), and -6. The expression of several syntaxin genes increased
during dimethyl sulfoxide-induced differentiation of a human
promyelocytic leukemia cell line toward the neutrophil lineage.
By immunolocalization analysis, Advani et al. (1998) found that STX6
partially colocalizes with VAMP4 (606909) in a punctate juxtanuclear
staining pattern. By immunoprecipitation of rat brain detergent
extracts, Steegmaier et al. (1999) found that STX6 exists in a complex
with VAMP4.
Western blot analysis and immunofluorescence microscopy by Charest et
al. (2001) showed that FIG (GOPC; 606845) interacted through its
C-terminal coiled-coil domain with syntaxin-6 in the Golgi apparatus.
They proposed that FIG may be involved in membrane vesicle trafficking.
Cheng et al. (2010) showed that both STX6 and CAL (GOPC) were involved
in downregulation of CFTR (602421) via lysosome-mediated degradation.
STX6 bound the N terminus of CFTR, and CAL independently bound the C
terminus of CFTR. Overexpression of STX6 reduced cell surface expression
of CFTR and caused its instability, but not in the absence of CAL.
STX6-dependent CFTR instability was sensitive to lysosome inhibition.
Overexpression of a dominant-negative STX6 mutant or knockdown of STX6
resulted in CFTR stability. STX6 and CAL had no effect on the stability
of CFTR with the cystic fibrosis (219700)-associated delta-F508 mutation
(602421.0001), which is retained in the endoplasmic reticulum (ER) and
undergoes ER-associated degradation. Cheng et al. (2010) concluded that
STX6 and CAL function in the TGN and direct trafficking of CFTR to the
lysosome.
BIOCHEMICAL FEATURES
Misura et al. (2002) provided a description of the 3-dimensional
structure of the amino-terminal domain of syntaxin-6. Secondary
structure prediction of SNARE proteins showed that the N-terminal
domains of many syntaxin and SNAP25 (600322) family members are likely
to be similar to one another, but are distinct from those of the VAMP
family members (see VAMP1, 185880), indicating that syntaxin and SNAP25
SNAREs may have shared a common ancestor.
*FIELD* RF
1. Advani, R. J.; Bae, H.-R.; Bock, J. B.; Chao, D. S.; Doung, Y.-C.;
Prekeris, R.; Yoo, J.-S.; Scheller, R. H.: Seven novel mammalian
SNARE proteins localize to distinct membrane compartments. J. Biol.
Chem. 273: 10317-10324, 1998.
2. Charest, A.; Lane, K.; McMahon, K.; Housman, D. E.: Association
of a novel PDZ domain-containing peripheral Golgi protein with the
Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF)
attachment protein receptor) protein syntaxin 6. J. Biol. Chem. 276:
29456-29465, 2001.
3. Cheng, J.; Cebotaru, V.; Cebotaru, L.; Guggino, W. B.: Syntaxin
6 and CAL mediate the degradation of the cystic fibrosis transmembrane
conductance regulator. Molec. Biol. Cell 21: 1178-1187, 2010.
4. Martin-Martin, B.; Nabokina, S. M.; Lazo, P. A.; Mollinedo, F.
: Co-expression of several human syntaxin genes in neutrophils and
differentiating HL-60 cells: various isoforms and detection of syntaxin
1. J. Leuko. Biol. 65: 397-406, 1999.
5. Misura, K. M. S.; Bock, J. B.; Gonzalez, L. C., Jr.; Scheller,
R. H.; Weis, W. I.: Three-dimensional structure of the amino-terminal
domain of syntaxin 6, a SNAP-25 C homolog. Proc. Nat. Acad. Sci. 99:
9184-9189, 2002.
6. Steegmaier, M.; Klumperman, J.; Foletti, D. L.; Yoo, J.-S.; Scheller,
R. H.: Vesicle-associated membrane protein 4 is implicated in trans-Golgi
network vesicle trafficking. Molec. Biol. Cell 10: 1957-1972, 1999.
*FIELD* CN
Patricia A. Hartz - updated: 12/16/2011
Victor A. McKusick - updated: 9/27/2002
Patricia A. Hartz - updated: 5/7/2002
*FIELD* CD
Rebekah S. Rasooly: 6/29/1999
*FIELD* ED
mgross: 03/06/2012
terry: 12/16/2011
alopez: 9/27/2002
carol: 5/7/2002
mgross: 6/29/1999