Full text data of STXBP3
STXBP3
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Syntaxin-binding protein 3 (Platelet Sec1 protein; PSP; Protein unc-18 homolog 3; Unc18-3; Protein unc-18 homolog C; Unc-18C)
Syntaxin-binding protein 3 (Platelet Sec1 protein; PSP; Protein unc-18 homolog 3; Unc18-3; Protein unc-18 homolog C; Unc-18C)
UniProt
O00186
ID STXB3_HUMAN Reviewed; 592 AA.
AC O00186; A8K269; A8K5K7; Q53FW1; Q86YJ3; Q9UPD7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Syntaxin-binding protein 3;
DE AltName: Full=Platelet Sec1 protein;
DE Short=PSP;
DE AltName: Full=Protein unc-18 homolog 3;
DE Short=Unc18-3;
DE AltName: Full=Protein unc-18 homolog C;
DE Short=Unc-18C;
GN Name=STXBP3;
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], AND VARIANTS GLY-433 AND GLY-546.
RC TISSUE=Brain;
RX PubMed=8824310;
RA Gengyo-Ando K., Kitayama H., Mukaida M., Ikawa Y.;
RT "A murine neural-specific homolog corrects cholinergic defects in
RT Caenorhabditis elegans unc-18 mutants.";
RL J. Neurosci. 16:6695-6702(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STX4, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RC TISSUE=Leukemic T-cell;
RX PubMed=10194441;
RA Reed G.L., Houng A.K., Fitzgerald M.L.;
RT "Human platelets contain SNARE proteins and a Sec1p homologue that
RT interacts with syntaxin 4 and is phosphorylated after thrombin
RT activation: implications for platelet secretion.";
RL Blood 93:2617-2626(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus, and Tongue;
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 MRNA].
RC TISSUE=Lung;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [8]
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).
CC -!- FUNCTION: Together with STX4 and VAMP2, may play a role in
CC insulin-dependent movement of GLUT4 and in docking/fusion of
CC intracellular GLUT4-containing vesicles with the cell surface in
CC adipocytes (By similarity).
CC -!- SUBUNIT: Interacts with DOC2B; the interaction is direct, occurs
CC at the cell membrane, excludes interaction with STX4 and regulates
CC glucose-stimulated insulin secretion (By similarity). Interacts
CC with STX4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=In
CC platelets, predominantly cytosolic. Low amounts membrane-
CC associated.
CC -!- TISSUE SPECIFICITY: Megakaryocytes and platelets.
CC -!- PTM: Phosphorylated by PKC in platelets in response to thrombin
CC stimulation; phosphorylation inhibits binding to STX4.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
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DR EMBL; D63506; BAA19482.1; -; mRNA.
DR EMBL; AF032922; AAC69606.1; -; mRNA.
DR EMBL; AK290134; BAF82823.1; -; mRNA.
DR EMBL; AK291322; BAF84011.1; -; mRNA.
DR EMBL; AK312910; BAG35756.1; -; mRNA.
DR EMBL; AK223170; BAD96890.1; -; mRNA.
DR EMBL; AL591719; CAH72066.1; -; Genomic_DNA.
DR EMBL; AL449266; CAH72066.1; JOINED; Genomic_DNA.
DR EMBL; AL449266; CAI14350.1; -; Genomic_DNA.
DR EMBL; AL591719; CAI14350.1; JOINED; Genomic_DNA.
DR EMBL; CH471122; EAW56330.1; -; Genomic_DNA.
DR EMBL; BC038099; AAH38099.1; -; mRNA.
DR EMBL; BC047764; AAH47764.1; -; mRNA.
DR RefSeq; NP_009200.2; NM_007269.2.
DR UniGene; Hs.530436; -.
DR ProteinModelPortal; O00186; -.
DR SMR; O00186; 7-584.
DR IntAct; O00186; 3.
DR MINT; MINT-4525992; -.
DR STRING; 9606.ENSP00000359025; -.
DR PhosphoSite; O00186; -.
DR PaxDb; O00186; -.
DR PRIDE; O00186; -.
DR Ensembl; ENST00000370008; ENSP00000359025; ENSG00000116266.
DR GeneID; 6814; -.
DR KEGG; hsa:6814; -.
DR UCSC; uc001dvy.3; human.
DR CTD; 6814; -.
DR GeneCards; GC01P109289; -.
DR HGNC; HGNC:11446; STXBP3.
DR HPA; HPA027225; -.
DR MIM; 608339; gene.
DR neXtProt; NX_O00186; -.
DR PharmGKB; PA36243; -.
DR eggNOG; COG5158; -.
DR HOGENOM; HOG000232146; -.
DR HOVERGEN; HBG052710; -.
DR InParanoid; O00186; -.
DR KO; K15301; -.
DR OMA; CKKEDEW; -.
DR OrthoDB; EOG78PV8M; -.
DR PhylomeDB; O00186; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; STXBP3; human.
DR GeneWiki; Syntaxin_binding_protein_3; -.
DR GenomeRNAi; 6814; -.
DR NextBio; 26593; -.
DR PRO; PR:O00186; -.
DR Bgee; O00186; -.
DR CleanEx; HS_STXBP3; -.
DR Genevestigator; O00186; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0070820; C:tertiary granule; IDA:UniProtKB.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
DR GO; GO:0043312; P:neutrophil degranulation; IEP:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR Gene3D; 3.40.50.1910; -; 2.
DR InterPro; IPR027482; Sec-1-like_dom2.
DR InterPro; IPR001619; Sec1-like.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Cytoplasm; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT CHAIN 1 592 Syntaxin-binding protein 3.
FT /FTId=PRO_0000206285.
FT REGION 1 255 Mediates interaction with DOC2B (By
FT similarity).
FT VARIANT 295 295 R -> Q (in dbSNP:rs2275344).
FT /FTId=VAR_052470.
FT VARIANT 433 433 E -> G (in dbSNP:rs1044136).
FT /FTId=VAR_017570.
FT VARIANT 546 546 C -> G (in dbSNP:rs1044137).
FT /FTId=VAR_017571.
FT CONFLICT 104 104 K -> R (in Ref. 7; AAH38099).
FT CONFLICT 150 150 L -> R (in Ref. 7; AAH38099).
FT CONFLICT 242 242 F -> I (in Ref. 4; BAD96890).
FT CONFLICT 277 277 E -> G (in Ref. 1; BAA19482).
FT CONFLICT 285 285 E -> D (in Ref. 3; BAF84011).
SQ SEQUENCE 592 AA; 67764 MW; AAFA268E2D328EC7 CRC64;
MAPPVAERGL KSVVWQKIKA TVFDDCKKEG EWKIMLLDEF TTKLLASCCK MTDLLEEGIT
VVENIYKNRE PVRQMKALYF ITPTSKSVDC FLHDFASKSE NKYKAAYIYF TDFCPDNLFN
KIKASCSKSI RRCKEINISF IPHESQVYTL DVPDAFYYCY SPDPGNAKGK DAIMETMADQ
IVTVCATLDE NPGVRYKSKP LDNASKLAQL VEKKLEDYYK IDEKSLIKGK THSQLLIIDR
GFDPVSTVLH ELTFQAMAYD LLPIENDTYK YKTDGKEKEA ILEEEDDLWV RIRHRHIAVV
LEEIPKLMKE ISSTKKATEG KTSLSALTQL MKKMPHFRKQ ITKQVVHLNL AEDCMNKFKL
NIEKLCKTEQ DLALGTDAEG QKVKDSMRVL LPVLLNKNHD NCDKIRAILL YIFSINGTTE
ENLDRLIQNV KIENESDMIR NWSYLGVPIV PQSQQGKPLR KDRSAEETFQ LSRWTPFIKD
IMEDAIDNRL DSKEWPYCSQ CPAVWNGSGA VSARQKPRAN YLEDRKNGSK LIVFVIGGIT
YSEVRCAYEV SQAHKSCEVI IGSTHVLTPK KLLDDIKMLN KPKDKVSLIK DE
//
ID STXB3_HUMAN Reviewed; 592 AA.
AC O00186; A8K269; A8K5K7; Q53FW1; Q86YJ3; Q9UPD7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Syntaxin-binding protein 3;
DE AltName: Full=Platelet Sec1 protein;
DE Short=PSP;
DE AltName: Full=Protein unc-18 homolog 3;
DE Short=Unc18-3;
DE AltName: Full=Protein unc-18 homolog C;
DE Short=Unc-18C;
GN Name=STXBP3;
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], AND VARIANTS GLY-433 AND GLY-546.
RC TISSUE=Brain;
RX PubMed=8824310;
RA Gengyo-Ando K., Kitayama H., Mukaida M., Ikawa Y.;
RT "A murine neural-specific homolog corrects cholinergic defects in
RT Caenorhabditis elegans unc-18 mutants.";
RL J. Neurosci. 16:6695-6702(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STX4, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RC TISSUE=Leukemic T-cell;
RX PubMed=10194441;
RA Reed G.L., Houng A.K., Fitzgerald M.L.;
RT "Human platelets contain SNARE proteins and a Sec1p homologue that
RT interacts with syntaxin 4 and is phosphorylated after thrombin
RT activation: implications for platelet secretion.";
RL Blood 93:2617-2626(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus, and Tongue;
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 MRNA].
RC TISSUE=Lung;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [8]
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).
CC -!- FUNCTION: Together with STX4 and VAMP2, may play a role in
CC insulin-dependent movement of GLUT4 and in docking/fusion of
CC intracellular GLUT4-containing vesicles with the cell surface in
CC adipocytes (By similarity).
CC -!- SUBUNIT: Interacts with DOC2B; the interaction is direct, occurs
CC at the cell membrane, excludes interaction with STX4 and regulates
CC glucose-stimulated insulin secretion (By similarity). Interacts
CC with STX4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=In
CC platelets, predominantly cytosolic. Low amounts membrane-
CC associated.
CC -!- TISSUE SPECIFICITY: Megakaryocytes and platelets.
CC -!- PTM: Phosphorylated by PKC in platelets in response to thrombin
CC stimulation; phosphorylation inhibits binding to STX4.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
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DR EMBL; D63506; BAA19482.1; -; mRNA.
DR EMBL; AF032922; AAC69606.1; -; mRNA.
DR EMBL; AK290134; BAF82823.1; -; mRNA.
DR EMBL; AK291322; BAF84011.1; -; mRNA.
DR EMBL; AK312910; BAG35756.1; -; mRNA.
DR EMBL; AK223170; BAD96890.1; -; mRNA.
DR EMBL; AL591719; CAH72066.1; -; Genomic_DNA.
DR EMBL; AL449266; CAH72066.1; JOINED; Genomic_DNA.
DR EMBL; AL449266; CAI14350.1; -; Genomic_DNA.
DR EMBL; AL591719; CAI14350.1; JOINED; Genomic_DNA.
DR EMBL; CH471122; EAW56330.1; -; Genomic_DNA.
DR EMBL; BC038099; AAH38099.1; -; mRNA.
DR EMBL; BC047764; AAH47764.1; -; mRNA.
DR RefSeq; NP_009200.2; NM_007269.2.
DR UniGene; Hs.530436; -.
DR ProteinModelPortal; O00186; -.
DR SMR; O00186; 7-584.
DR IntAct; O00186; 3.
DR MINT; MINT-4525992; -.
DR STRING; 9606.ENSP00000359025; -.
DR PhosphoSite; O00186; -.
DR PaxDb; O00186; -.
DR PRIDE; O00186; -.
DR Ensembl; ENST00000370008; ENSP00000359025; ENSG00000116266.
DR GeneID; 6814; -.
DR KEGG; hsa:6814; -.
DR UCSC; uc001dvy.3; human.
DR CTD; 6814; -.
DR GeneCards; GC01P109289; -.
DR HGNC; HGNC:11446; STXBP3.
DR HPA; HPA027225; -.
DR MIM; 608339; gene.
DR neXtProt; NX_O00186; -.
DR PharmGKB; PA36243; -.
DR eggNOG; COG5158; -.
DR HOGENOM; HOG000232146; -.
DR HOVERGEN; HBG052710; -.
DR InParanoid; O00186; -.
DR KO; K15301; -.
DR OMA; CKKEDEW; -.
DR OrthoDB; EOG78PV8M; -.
DR PhylomeDB; O00186; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; STXBP3; human.
DR GeneWiki; Syntaxin_binding_protein_3; -.
DR GenomeRNAi; 6814; -.
DR NextBio; 26593; -.
DR PRO; PR:O00186; -.
DR Bgee; O00186; -.
DR CleanEx; HS_STXBP3; -.
DR Genevestigator; O00186; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0070820; C:tertiary granule; IDA:UniProtKB.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
DR GO; GO:0043312; P:neutrophil degranulation; IEP:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR Gene3D; 3.40.50.1910; -; 2.
DR InterPro; IPR027482; Sec-1-like_dom2.
DR InterPro; IPR001619; Sec1-like.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Cytoplasm; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT CHAIN 1 592 Syntaxin-binding protein 3.
FT /FTId=PRO_0000206285.
FT REGION 1 255 Mediates interaction with DOC2B (By
FT similarity).
FT VARIANT 295 295 R -> Q (in dbSNP:rs2275344).
FT /FTId=VAR_052470.
FT VARIANT 433 433 E -> G (in dbSNP:rs1044136).
FT /FTId=VAR_017570.
FT VARIANT 546 546 C -> G (in dbSNP:rs1044137).
FT /FTId=VAR_017571.
FT CONFLICT 104 104 K -> R (in Ref. 7; AAH38099).
FT CONFLICT 150 150 L -> R (in Ref. 7; AAH38099).
FT CONFLICT 242 242 F -> I (in Ref. 4; BAD96890).
FT CONFLICT 277 277 E -> G (in Ref. 1; BAA19482).
FT CONFLICT 285 285 E -> D (in Ref. 3; BAF84011).
SQ SEQUENCE 592 AA; 67764 MW; AAFA268E2D328EC7 CRC64;
MAPPVAERGL KSVVWQKIKA TVFDDCKKEG EWKIMLLDEF TTKLLASCCK MTDLLEEGIT
VVENIYKNRE PVRQMKALYF ITPTSKSVDC FLHDFASKSE NKYKAAYIYF TDFCPDNLFN
KIKASCSKSI RRCKEINISF IPHESQVYTL DVPDAFYYCY SPDPGNAKGK DAIMETMADQ
IVTVCATLDE NPGVRYKSKP LDNASKLAQL VEKKLEDYYK IDEKSLIKGK THSQLLIIDR
GFDPVSTVLH ELTFQAMAYD LLPIENDTYK YKTDGKEKEA ILEEEDDLWV RIRHRHIAVV
LEEIPKLMKE ISSTKKATEG KTSLSALTQL MKKMPHFRKQ ITKQVVHLNL AEDCMNKFKL
NIEKLCKTEQ DLALGTDAEG QKVKDSMRVL LPVLLNKNHD NCDKIRAILL YIFSINGTTE
ENLDRLIQNV KIENESDMIR NWSYLGVPIV PQSQQGKPLR KDRSAEETFQ LSRWTPFIKD
IMEDAIDNRL DSKEWPYCSQ CPAVWNGSGA VSARQKPRAN YLEDRKNGSK LIVFVIGGIT
YSEVRCAYEV SQAHKSCEVI IGSTHVLTPK KLLDDIKMLN KPKDKVSLIK DE
//
MIM
608339
*RECORD*
*FIELD* NO
608339
*FIELD* TI
*608339 SYNTAXIN-BINDING PROTEIN 3; STXBP3
;;UNC18, C. ELEGANS, HOMOLOG OF, 3;;
MUNC18-3;;
read moreMUNC18C;;
PLATELET SEC1 PROTEIN; PSP
*FIELD* TX
CLONING
Gengyo-Ando et al. (1996) cloned mouse Stxbp3, which they called
Munc18-3. The deduced protein contains 592 amino acids. By screening a
human fetal brain cDNA library using the mouse cDNA as probe,
Gengyo-Ando et al. (1996) cloned STXBP3. The deduced 592-amino acid
protein lacks hydrophobic sequences, suggesting that it is an
intracellular cytosolic protein. Human and mouse STXBP3 share 91% amino
acid identity. Northern blot analysis of mouse tissues detected a 2.8-kb
transcript in all tissues examined.
Using an antiplatelet antibody to screen an expression library developed
from a leukemia cell line that expressed platelet proteins, followed by
screening a megakaryocytic cell line cDNA library, Reed et al. (1999)
cloned STXBP3, which they called PSP. The deduced 592-amino acid protein
has a calculated molecular mass of 68 kD and contains sequence motifs
for protein kinase C (PKC; see 176982) and casein kinase II (see 115441)
phosphorylation. STXBP3 was predicted to be a hydrophilic protein.
Northern blot analysis detected a STXBP3 transcript of about 2.7 kb in 3
megakaryocytic cell lines. Western blot analysis detected a 68-kD
protein in platelet detergent extracts. STXBP3 partitioned with the
cytosolic platelet fraction, with small amounts in the particulate or
membrane fraction.
GENE FUNCTION
Reed et al. (1999) found that STXBP3 was phosphorylated in vivo in
permeabilized platelets activated by thrombin (176930). Phosphorylation
occurred within 1 minute and increased after 10 minutes of stimulation.
No phosphorylation was detected in nonactivated cells. Phosphorylation
was blocked by a PKC inhibitor.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the STXBP3
gene to chromosome 1 (TMAP SHGC-75260).
ANIMAL MODEL
To clarify the physiologic function of STXBP3 in insulin-stimulated
GLUT4 (SLC2A4; 138190) exocytosis, Kanda et al. (2005) generated mouse
embryos deficient in the syntaxin-4 (see 186591)-binding protein Stxbp3
and developed Stxbp3 -/- adipocytes from their mesenchymal fibroblasts.
The insulin-induced appearance of Glut4 at the cell surface was enhanced
in Stxbp3 -/- adipocytes compared to +/+ cells. Wortmannin, an inhibitor
of PI3K, inhibited insulin-stimulated Glut4 externalization in +/+ but
not -/- adipocytes. Kanda et al. (2005) suggested that disruption of the
interaction between syntaxin-4 and STXBP3 in adipocytes might result in
enhancement of insulin-stimulated GLUT4 externalization.
*FIELD* RF
1. Gengyo-Ando, K.; Kitayama, H.; Mukaida, M.; Ikawa, Y.: A murine
neural-specific homolog corrects cholinergic defects in Caenorhabditis
elegans unc-18 mutants. J. Neurosci. 16: 6695-6702, 1996.
2. Kanda, H.; Tamori, Y.; Shinoda, H.; Yoshikawa, M.; Sakaue, M.;
Udagawa, J.; Otani, H.; Tashiro, F.; Miyazaki, J.; Kasuga, M.: Adipocytes
from Munc18c-null mice show increased sensitivity to insulin-stimulated
GLUT4 externalization. J. Clin. Invest. 115: 291-301, 2005.
3. Reed, G. L.; Houng, A. K.; Fitzgerald, M. L.: Human platelets
contain SNARE proteins and a Sec1p homologue that interacts with syntaxin
4 and is phosphorylated after thrombin activation: implications for
platelet secretion. Blood 93: 2617-2626, 1999.
*FIELD* CN
Marla J. F. O'Neill - updated: 04/12/2005
*FIELD* CD
Patricia A. Hartz: 12/11/2003
*FIELD* ED
tkritzer: 04/12/2005
mgross: 12/11/2003
*RECORD*
*FIELD* NO
608339
*FIELD* TI
*608339 SYNTAXIN-BINDING PROTEIN 3; STXBP3
;;UNC18, C. ELEGANS, HOMOLOG OF, 3;;
MUNC18-3;;
read moreMUNC18C;;
PLATELET SEC1 PROTEIN; PSP
*FIELD* TX
CLONING
Gengyo-Ando et al. (1996) cloned mouse Stxbp3, which they called
Munc18-3. The deduced protein contains 592 amino acids. By screening a
human fetal brain cDNA library using the mouse cDNA as probe,
Gengyo-Ando et al. (1996) cloned STXBP3. The deduced 592-amino acid
protein lacks hydrophobic sequences, suggesting that it is an
intracellular cytosolic protein. Human and mouse STXBP3 share 91% amino
acid identity. Northern blot analysis of mouse tissues detected a 2.8-kb
transcript in all tissues examined.
Using an antiplatelet antibody to screen an expression library developed
from a leukemia cell line that expressed platelet proteins, followed by
screening a megakaryocytic cell line cDNA library, Reed et al. (1999)
cloned STXBP3, which they called PSP. The deduced 592-amino acid protein
has a calculated molecular mass of 68 kD and contains sequence motifs
for protein kinase C (PKC; see 176982) and casein kinase II (see 115441)
phosphorylation. STXBP3 was predicted to be a hydrophilic protein.
Northern blot analysis detected a STXBP3 transcript of about 2.7 kb in 3
megakaryocytic cell lines. Western blot analysis detected a 68-kD
protein in platelet detergent extracts. STXBP3 partitioned with the
cytosolic platelet fraction, with small amounts in the particulate or
membrane fraction.
GENE FUNCTION
Reed et al. (1999) found that STXBP3 was phosphorylated in vivo in
permeabilized platelets activated by thrombin (176930). Phosphorylation
occurred within 1 minute and increased after 10 minutes of stimulation.
No phosphorylation was detected in nonactivated cells. Phosphorylation
was blocked by a PKC inhibitor.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the STXBP3
gene to chromosome 1 (TMAP SHGC-75260).
ANIMAL MODEL
To clarify the physiologic function of STXBP3 in insulin-stimulated
GLUT4 (SLC2A4; 138190) exocytosis, Kanda et al. (2005) generated mouse
embryos deficient in the syntaxin-4 (see 186591)-binding protein Stxbp3
and developed Stxbp3 -/- adipocytes from their mesenchymal fibroblasts.
The insulin-induced appearance of Glut4 at the cell surface was enhanced
in Stxbp3 -/- adipocytes compared to +/+ cells. Wortmannin, an inhibitor
of PI3K, inhibited insulin-stimulated Glut4 externalization in +/+ but
not -/- adipocytes. Kanda et al. (2005) suggested that disruption of the
interaction between syntaxin-4 and STXBP3 in adipocytes might result in
enhancement of insulin-stimulated GLUT4 externalization.
*FIELD* RF
1. Gengyo-Ando, K.; Kitayama, H.; Mukaida, M.; Ikawa, Y.: A murine
neural-specific homolog corrects cholinergic defects in Caenorhabditis
elegans unc-18 mutants. J. Neurosci. 16: 6695-6702, 1996.
2. Kanda, H.; Tamori, Y.; Shinoda, H.; Yoshikawa, M.; Sakaue, M.;
Udagawa, J.; Otani, H.; Tashiro, F.; Miyazaki, J.; Kasuga, M.: Adipocytes
from Munc18c-null mice show increased sensitivity to insulin-stimulated
GLUT4 externalization. J. Clin. Invest. 115: 291-301, 2005.
3. Reed, G. L.; Houng, A. K.; Fitzgerald, M. L.: Human platelets
contain SNARE proteins and a Sec1p homologue that interacts with syntaxin
4 and is phosphorylated after thrombin activation: implications for
platelet secretion. Blood 93: 2617-2626, 1999.
*FIELD* CN
Marla J. F. O'Neill - updated: 04/12/2005
*FIELD* CD
Patricia A. Hartz: 12/11/2003
*FIELD* ED
tkritzer: 04/12/2005
mgross: 12/11/2003