STXB6_HUMAN
ID STXB6_HUMAN Reviewed; 210 AA.
AC Q8NFX7; D3DS78; Q8N3H1; Q8N8D5; Q96GF3; Q9P008;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Syntaxin-binding protein 6;
DE AltName: Full=Amisyn;
GN Name=STXBP6; ORFNames=HSPC156;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION
RP WITH STX1A; STX4A AND SNAP25, AND SUBCELLULAR LOCATION.
RX PubMed=12145319; DOI=10.1074/jbc.m204929200;
RA Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H.;
RT "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex
RT assembly.";
RL J. Biol. Chem. 277:28271-28279(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and Spinal ganglion;
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Forms non-fusogenic complexes with SNAP25 and STX1A and may
CC thereby modulate the formation of functional SNARE complexes and
CC exocytosis.
CC -!- SUBUNIT: Part of a ternary complex containing SNAP25 and STX1A that can
CC be dissociated by NAPA and NSF. Interacts with STX4A.
CC {ECO:0000269|PubMed:12145319}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12145319}. Membrane
CC {ECO:0000269|PubMed:12145319}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12145319}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NFX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFX7-2; Sequence=VSP_008073;
CC Name=3;
CC IsoId=Q8NFX7-3; Sequence=VSP_008071, VSP_008072;
CC -!- TISSUE SPECIFICITY: Detected at low levels in brain, and at very low
CC levels in heart, adrenal gland, testis, liver and kidney.
CC {ECO:0000269|PubMed:12145319}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM46624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF391153; AAM46624.1; ALT_INIT; mRNA.
DR EMBL; AF161505; AAF29120.1; -; mRNA.
DR EMBL; AK096957; BAC04911.1; -; mRNA.
DR EMBL; AL834346; CAD39012.2; -; mRNA.
DR EMBL; AL137164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65996.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65999.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66000.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66001.1; -; Genomic_DNA.
DR EMBL; BC009499; AAH09499.1; -; mRNA.
DR EMBL; BC067278; AAH67278.1; -; mRNA.
DR CCDS; CCDS9634.1; -. [Q8NFX7-1]
DR RefSeq; NP_001291405.1; NM_001304476.1. [Q8NFX7-1]
DR RefSeq; NP_001291406.1; NM_001304477.1. [Q8NFX7-1]
DR RefSeq; NP_054897.4; NM_014178.7. [Q8NFX7-1]
DR RefSeq; XP_016876720.1; XM_017021231.1. [Q8NFX7-1]
DR RefSeq; XP_016876721.1; XM_017021232.1.
DR RefSeq; XP_016876722.1; XM_017021233.1.
DR RefSeq; XP_016876723.1; XM_017021234.1.
DR RefSeq; XP_016876724.1; XM_017021235.1. [Q8NFX7-1]
DR RefSeq; XP_016876725.1; XM_017021236.1.
DR RefSeq; XP_016876726.1; XM_017021237.1.
DR RefSeq; XP_016876727.1; XM_017021238.1. [Q8NFX7-1]
DR RefSeq; XP_016876728.1; XM_017021239.1. [Q8NFX7-1]
DR RefSeq; XP_016876729.1; XM_017021240.1. [Q8NFX7-1]
DR RefSeq; XP_016876730.1; XM_017021241.1. [Q8NFX7-1]
DR RefSeq; XP_016876731.1; XM_017021242.1.
DR AlphaFoldDB; Q8NFX7; -.
DR SMR; Q8NFX7; -.
DR BioGRID; 118860; 21.
DR IntAct; Q8NFX7; 17.
DR MINT; Q8NFX7; -.
DR STRING; 9606.ENSP00000324302; -.
DR GlyGen; Q8NFX7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NFX7; -.
DR PhosphoSitePlus; Q8NFX7; -.
DR BioMuta; STXBP6; -.
DR DMDM; 34222907; -.
DR EPD; Q8NFX7; -.
DR jPOST; Q8NFX7; -.
DR MassIVE; Q8NFX7; -.
DR MaxQB; Q8NFX7; -.
DR PaxDb; Q8NFX7; -.
DR PeptideAtlas; Q8NFX7; -.
DR PRIDE; Q8NFX7; -.
DR ProteomicsDB; 73382; -. [Q8NFX7-1]
DR ProteomicsDB; 73383; -. [Q8NFX7-2]
DR ProteomicsDB; 73384; -. [Q8NFX7-3]
DR Antibodypedia; 22939; 223 antibodies from 30 providers.
DR DNASU; 29091; -.
DR Ensembl; ENST00000323944.10; ENSP00000324302.5; ENSG00000168952.16. [Q8NFX7-1]
DR Ensembl; ENST00000396700.5; ENSP00000379928.1; ENSG00000168952.16. [Q8NFX7-1]
DR Ensembl; ENST00000419632.6; ENSP00000397212.2; ENSG00000168952.16. [Q8NFX7-1]
DR Ensembl; ENST00000546511.5; ENSP00000449536.1; ENSG00000168952.16. [Q8NFX7-1]
DR Ensembl; ENST00000548369.1; ENSP00000447655.1; ENSG00000168952.16. [Q8NFX7-3]
DR Ensembl; ENST00000550887.5; ENSP00000449379.1; ENSG00000168952.16. [Q8NFX7-1]
DR GeneID; 29091; -.
DR KEGG; hsa:29091; -.
DR MANE-Select; ENST00000323944.10; ENSP00000324302.5; NM_001394410.1; NP_001381339.1.
DR UCSC; uc001wpt.5; human. [Q8NFX7-1]
DR CTD; 29091; -.
DR DisGeNET; 29091; -.
DR GeneCards; STXBP6; -.
DR HGNC; HGNC:19666; STXBP6.
DR HPA; ENSG00000168952; Low tissue specificity.
DR MIM; 607958; gene.
DR neXtProt; NX_Q8NFX7; -.
DR OpenTargets; ENSG00000168952; -.
DR PharmGKB; PA134985567; -.
DR VEuPathDB; HostDB:ENSG00000168952; -.
DR eggNOG; KOG1983; Eukaryota.
DR GeneTree; ENSGT00940000156499; -.
DR HOGENOM; CLU_101413_0_0_1; -.
DR InParanoid; Q8NFX7; -.
DR OMA; HTCQRYC; -.
DR OrthoDB; 201698at2759; -.
DR PhylomeDB; Q8NFX7; -.
DR PathwayCommons; Q8NFX7; -.
DR SignaLink; Q8NFX7; -.
DR BioGRID-ORCS; 29091; 6 hits in 1075 CRISPR screens.
DR ChiTaRS; STXBP6; human.
DR GenomeRNAi; 29091; -.
DR Pharos; Q8NFX7; Tbio.
DR PRO; PR:Q8NFX7; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8NFX7; protein.
DR Bgee; ENSG00000168952; Expressed in lateral nuclear group of thalamus and 170 other tissues.
DR ExpressionAtlas; Q8NFX7; baseline and differential.
DR Genevisible; Q8NFX7; HS.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0045920; P:negative regulation of exocytosis; TAS:ParkinsonsUK-UCL.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; IEA:InterPro.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:ParkinsonsUK-UCL.
DR CDD; cd14681; PH-STXBP6; 1.
DR CDD; cd15892; R-SNARE_STXBP6; 1.
DR InterPro; IPR028258; Sec3-PIP2_bind.
DR InterPro; IPR037821; STXBP6_PH.
DR InterPro; IPR037822; STXBP6_SNARE.
DR InterPro; IPR042855; V_SNARE_CC.
DR Pfam; PF15277; Sec3-PIP2_bind; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR SMART; SM01313; Sec3-PIP2_bind; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Membrane;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..210
FT /note="Syntaxin-binding protein 6"
FT /id="PRO_0000206782"
FT DOMAIN 151..210
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_008071"
FT VAR_SEQ 103..150
FT /note="LFENAFDQWVASTASEKCTFFQILHHTCQRYLTDRKPEFINCQSKIMG ->
FT MSACFLDTRRAAFLQCDLPSSYRILTLPESGHCGSAEPVSDAPALLLS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_008072"
FT VAR_SEQ 204..210
FT /note="LAMKHKC -> VTFRGRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008073"
FT CONFLICT 117
FT /note="S -> P (in Ref. 3; BAC04911)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="I -> T (in Ref. 3; BAC04911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 23554 MW; 7C046A90D4C4B2D8 CRC64;
MSAKSAISKE IFAPLDERML GAVQVKRRTK KKIPFLATGG QGEYLTYICL SVTNKKPTQA
SITKVKQFEG STSFVRRSQW MLEQLRQVNG IDPNGDSAEF DLLFENAFDQ WVASTASEKC
TFFQILHHTC QRYLTDRKPE FINCQSKIMG GNSILHSAAD SVTSAVQKAS QALNERGERL
GRAEEKTEDL KNSAQQFAET AHKLAMKHKC
