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Syntaxin-binding protein 2 (Protein unc-18 homolog 2) (Unc18-2) (Protein unc-18 homolog B) (Unc-18B)

 STXB2_HUMAN             Reviewed;         593 AA.
Q15833; B4E175; E7EQD5; Q9BU65;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
22-NOV-2017, entry version 150.
RecName: Full=Syntaxin-binding protein 2;
AltName: Full=Protein unc-18 homolog 2;
Short=Unc18-2;
AltName: Full=Protein unc-18 homolog B;
Short=Unc-18B;
Name=STXBP2; Synonyms=UNC18B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-526.
PubMed=8921365; DOI=10.1006/geno.1996.0515;
Ziegler S.F., Mortrud M.T., Swartz A.R., Baker E., Sutherland G.R.,
Burmeister M., Mulligan J.T.;
"Molecular characterization of a nonneuronal human UNC18 homolog.";
Genomics 37:19-23(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
VAL-526.
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, INTERACTION WITH STX11, VARIANTS FHL5 PRO-209; ILE-232 DEL;
HIS-292; TRP-405; GLN-405 AND LEU-477, AND CHARACTERIZATION OF
VARIANTS FHL5 ILE-232 DEL; HIS-292; TRP-405; GLN-405 AND LEU-477.
PubMed=19804848; DOI=10.1016/j.ajhg.2009.09.005;
zur Stadt U., Rohr J., Seifert W., Koch F., Grieve S., Pagel J.,
Strauss J., Kasper B., Nuernberg G., Becker C., Maul-Pavicic A.,
Beutel K., Janka G., Griffiths G., Ehl S., Hennies H.C.;
"Familial hemophagocytic lymphohistiocytosis type 5 (FHL-5) is caused
by mutations in Munc18-2 and impaired binding to syntaxin 11.";
Am. J. Hum. Genet. 85:482-492(2009).
[8]
FUNCTION, INTERACTION WITH STX11, AND VARIANT FHL5 LEU-477.
PubMed=19884660; DOI=10.1172/JCI40732;
Cote M., Menager M.M., Burgess A., Mahlaoui N., Picard C.,
Schaffner C., Al-Manjomi F., Al-Harbi M., Alangari A., Le Deist F.,
Gennery A.R., Prince N., Cariou A., Nitschke P., Blank U.,
El-Ghazali G., Menasche G., Latour S., Fischer A., de Saint Basile G.;
"Munc18-2 deficiency causes familial hemophagocytic
lymphohistiocytosis type 5 and impairs cytotoxic granule exocytosis in
patient NK cells.";
J. Clin. Invest. 119:3765-3773(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Involved in intracellular vesicle trafficking and
vesicle fusion with membranes. Contributes to the granule
exocytosis machinery through interaction with soluble N-
ethylmaleimide-sensitive factor attachment protein receptor
(SNARE) proteins that regulate membrane fusion. Regulates
cytotoxic granule exocytosis in natural killer (NK) cells.
{ECO:0000269|PubMed:19804848, ECO:0000269|PubMed:19884660}.
-!- SUBUNIT: Interacts with STX1A, STX2 and STX3 (By similarity).
Interacts with STX11. {ECO:0000250, ECO:0000269|PubMed:19804848,
ECO:0000269|PubMed:19884660}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q15833-1; Sequence=Displayed;
Name=2;
IsoId=Q15833-2; Sequence=VSP_040121;
Name=3;
IsoId=Q15833-3; Sequence=VSP_055157;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Placenta, lung, liver, kidney and pancreas, as
well as in peripheral blood lymphocytes.
-!- DISEASE: Familial hemophagocytic lymphohistiocytosis 5 (FHL5)
[MIM:613101]: A rare disorder characterized by immune
dysregulation with hypercytokinemia, defective function of natural
killer cell, and massive infiltration of several organs by
activated lymphocytes and macrophages. The clinical features of
the disease include fever, hepatosplenomegaly, cytopenia, and less
frequently neurological abnormalities ranging from irritability
and hypotonia to seizures, cranial nerve deficits and ataxia.
{ECO:0000269|PubMed:19804848, ECO:0000269|PubMed:19884660}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
{ECO:0000305}.
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EMBL; U63533; AAC50762.1; -; mRNA.
EMBL; BT006915; AAP35561.1; -; mRNA.
EMBL; AK303701; BAG64687.1; -; mRNA.
EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471139; EAW69018.1; -; Genomic_DNA.
EMBL; BC002869; AAH02869.1; -; mRNA.
CCDS; CCDS12181.1; -. [Q15833-1]
CCDS; CCDS45948.1; -. [Q15833-2]
CCDS; CCDS62522.1; -. [Q15833-3]
RefSeq; NP_001120868.1; NM_001127396.2. [Q15833-2]
RefSeq; NP_001258963.1; NM_001272034.1. [Q15833-3]
RefSeq; NP_008880.2; NM_006949.3. [Q15833-1]
UniGene; Hs.515104; -.
PDB; 4CCA; X-ray; 2.60 A; A=1-593.
PDBsum; 4CCA; -.
ProteinModelPortal; Q15833; -.
SMR; Q15833; -.
BioGrid; 112682; 24.
IntAct; Q15833; 6.
MINT; MINT-4718353; -.
STRING; 9606.ENSP00000221283; -.
iPTMnet; Q15833; -.
PhosphoSitePlus; Q15833; -.
DMDM; 313104015; -.
OGP; Q15833; -.
EPD; Q15833; -.
MaxQB; Q15833; -.
PaxDb; Q15833; -.
PeptideAtlas; Q15833; -.
PRIDE; Q15833; -.
DNASU; 6813; -.
Ensembl; ENST00000221283; ENSP00000221283; ENSG00000076944. [Q15833-1]
Ensembl; ENST00000414284; ENSP00000409471; ENSG00000076944. [Q15833-2]
Ensembl; ENST00000441779; ENSP00000413606; ENSG00000076944. [Q15833-3]
GeneID; 6813; -.
KEGG; hsa:6813; -.
UCSC; uc002mha.6; human. [Q15833-1]
CTD; 6813; -.
DisGeNET; 6813; -.
EuPathDB; HostDB:ENSG00000076944.14; -.
GeneCards; STXBP2; -.
GeneReviews; STXBP2; -.
H-InvDB; HIX0021726; -.
HGNC; HGNC:11445; STXBP2.
HPA; HPA015564; -.
HPA; HPA063868; -.
MalaCards; STXBP2; -.
MIM; 601717; gene.
MIM; 613101; phenotype.
neXtProt; NX_Q15833; -.
OpenTargets; ENSG00000076944; -.
Orphanet; 540; Familial hemophagocytic lymphohistiocytosis.
PharmGKB; PA36242; -.
eggNOG; KOG1300; Eukaryota.
eggNOG; COG5158; LUCA.
GeneTree; ENSGT00390000005206; -.
HOGENOM; HOG000232146; -.
HOVERGEN; HBG052710; -.
InParanoid; Q15833; -.
KO; K15300; -.
OMA; NLYCPFR; -.
OrthoDB; EOG091G0WUI; -.
PhylomeDB; Q15833; -.
TreeFam; TF313242; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-449836; Other interleukin signaling.
SIGNOR; Q15833; -.
ChiTaRS; STXBP2; human.
GeneWiki; Syntaxin_binding_protein_2; -.
GenomeRNAi; 6813; -.
PRO; PR:Q15833; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000076944; -.
CleanEx; HS_STXBP2; -.
ExpressionAtlas; Q15833; baseline and differential.
Genevisible; Q15833; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
GO; GO:0044194; C:cytolytic granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042581; C:specific granule; IDA:UniProtKB.
GO; GO:0070820; C:tertiary granule; IDA:UniProtKB.
GO; GO:0042589; C:zymogen granule membrane; IEA:Ensembl.
GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
GO; GO:0030348; F:syntaxin-3 binding; IPI:UniProtKB.
GO; GO:0001909; P:leukocyte mediated cytotoxicity; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; IEP:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0043304; P:regulation of mast cell degranulation; ISS:UniProtKB.
GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
InterPro; IPR001619; Sec1-like.
InterPro; IPR036045; Sec1-like_sf.
PANTHER; PTHR11679; PTHR11679; 1.
Pfam; PF00995; Sec1; 1.
PIRSF; PIRSF005715; VPS45_Sec1; 1.
SUPFAM; SSF56815; SSF56815; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Exocytosis; Polymorphism; Protein transport;
Reference proteome; Transport.
CHAIN 1 593 Syntaxin-binding protein 2.
/FTId=PRO_0000206281.
VAR_SEQ 82 82 K -> KAQAQRVIHLPQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055157.
VAR_SEQ 83 85 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_040121.
VARIANT 209 209 L -> P (in FHL5; dbSNP:rs121918541).
{ECO:0000269|PubMed:19804848}.
/FTId=VAR_063814.
VARIANT 232 232 Missing (in FHL5; leads to a complete
loss of the ability to interact with
STX11). {ECO:0000269|PubMed:19804848}.
/FTId=VAR_063815.
VARIANT 292 292 R -> H (in FHL5; leads to a complete loss
of the ability to interact with STX11;
dbSNP:rs746897867).
{ECO:0000269|PubMed:19804848}.
/FTId=VAR_063816.
VARIANT 405 405 R -> Q (in FHL5; leads to a complete loss
of the ability to interact with STX11;
dbSNP:rs773360200).
{ECO:0000269|PubMed:19804848}.
/FTId=VAR_063817.
VARIANT 405 405 R -> W (in FHL5; leads to a complete loss
of the ability to interact with STX11;
dbSNP:rs769717341).
{ECO:0000269|PubMed:19804848}.
/FTId=VAR_063818.
VARIANT 477 477 P -> L (in FHL5; leads to a complete loss
of the ability to interact with STX11;
dbSNP:rs121918540).
{ECO:0000269|PubMed:19804848,
ECO:0000269|PubMed:19884660}.
/FTId=VAR_063819.
VARIANT 526 526 I -> V (in dbSNP:rs6791).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:8921365}.
/FTId=VAR_014934.
CONFLICT 348 348 H -> R (in Ref. 3; BAG64687).
{ECO:0000305}.
HELIX 6 15 {ECO:0000244|PDB:4CCA}.
TURN 16 22 {ECO:0000244|PDB:4CCA}.
STRAND 29 33 {ECO:0000244|PDB:4CCA}.
HELIX 35 42 {ECO:0000244|PDB:4CCA}.
HELIX 47 51 {ECO:0000244|PDB:4CCA}.
TURN 52 54 {ECO:0000244|PDB:4CCA}.
STRAND 55 58 {ECO:0000244|PDB:4CCA}.
STRAND 71 77 {ECO:0000244|PDB:4CCA}.
HELIX 81 89 {ECO:0000244|PDB:4CCA}.
STRAND 102 108 {ECO:0000244|PDB:4CCA}.
HELIX 112 119 {ECO:0000244|PDB:4CCA}.
HELIX 123 126 {ECO:0000244|PDB:4CCA}.
STRAND 127 132 {ECO:0000244|PDB:4CCA}.
STRAND 141 146 {ECO:0000244|PDB:4CCA}.
HELIX 152 157 {ECO:0000244|PDB:4CCA}.
HELIX 159 164 {ECO:0000244|PDB:4CCA}.
HELIX 165 182 {ECO:0000244|PDB:4CCA}.
STRAND 188 191 {ECO:0000244|PDB:4CCA}.
STRAND 193 195 {ECO:0000244|PDB:4CCA}.
HELIX 196 215 {ECO:0000244|PDB:4CCA}.
TURN 217 220 {ECO:0000244|PDB:4CCA}.
HELIX 225 227 {ECO:0000244|PDB:4CCA}.
STRAND 229 233 {ECO:0000244|PDB:4CCA}.
HELIX 235 237 {ECO:0000244|PDB:4CCA}.
HELIX 241 243 {ECO:0000244|PDB:4CCA}.
HELIX 249 256 {ECO:0000244|PDB:4CCA}.
STRAND 263 267 {ECO:0000244|PDB:4CCA}.
STRAND 276 280 {ECO:0000244|PDB:4CCA}.
STRAND 282 284 {ECO:0000244|PDB:4CCA}.
HELIX 286 291 {ECO:0000244|PDB:4CCA}.
TURN 296 298 {ECO:0000244|PDB:4CCA}.
HELIX 299 314 {ECO:0000244|PDB:4CCA}.
HELIX 327 331 {ECO:0000244|PDB:4CCA}.
HELIX 333 357 {ECO:0000244|PDB:4CCA}.
HELIX 360 373 {ECO:0000244|PDB:4CCA}.
HELIX 385 393 {ECO:0000244|PDB:4CCA}.
HELIX 400 414 {ECO:0000244|PDB:4CCA}.
HELIX 419 428 {ECO:0000244|PDB:4CCA}.
HELIX 432 434 {ECO:0000244|PDB:4CCA}.
HELIX 435 439 {ECO:0000244|PDB:4CCA}.
HELIX 440 443 {ECO:0000244|PDB:4CCA}.
HELIX 478 487 {ECO:0000244|PDB:4CCA}.
TURN 493 495 {ECO:0000244|PDB:4CCA}.
STRAND 498 500 {ECO:0000244|PDB:4CCA}.
STRAND 533 538 {ECO:0000244|PDB:4CCA}.
HELIX 544 556 {ECO:0000244|PDB:4CCA}.
TURN 557 559 {ECO:0000244|PDB:4CCA}.
STRAND 562 570 {ECO:0000244|PDB:4CCA}.
HELIX 573 582 {ECO:0000244|PDB:4CCA}.
SEQUENCE 593 AA; 66453 MW; 98E27B55309168A9 CRC64;
MAPSGLKAVV GEKILSGVIR SVKKDGEWKV LIMDHPSMRI LSSCCKMSDI LAEGITIVED
INKRREPIPS LEAIYLLSPT EKSVQALIKD FQGTPTFTYK AAHIFFTDTC PEPLFSELGR
SRLAKVVKTL KEIHLAFLPY EAQVFSLDAP HSTYNLYCPF RAEERTRQLE VLAQQIATLC
ATLQEYPAIR YRKGPEDTAQ LAHAVLAKLN AFKADTPSLG EGPEKTRSQL LIMDRAADPV
SPLLHELTFQ AMAYDLLDIE QDTYRYETTG LSEAREKAVL LDEDDDLWVE LRHMHIADVS
KKVTELLRTF CESKRLTTDK ANIKDLSQIL KKMPQYQKEL NKYSTHLHLA DDCMKHFKGS
VEKLCSVEQD LAMGSDAEGE KIKDSMKLIV PVLLDAAVPA YDKIRVLLLY ILLRNGVSEE
NLAKLIQHAN VQAHSSLIRN LEQLGGTVTN PGGSGTSSRL EPRERMEPTY QLSRWTPVIK
DVMEDAVEDR LDRNLWPFVS DPAPTASSQA AVSARFGHWH KNKAGIEARA GPRLIVYVMG
GVAMSEMRAA YEVTRATEGK WEVLIGSSHI LTPTRFLDDL KALDKKLEDI ALP


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EIAAB40490 Homo sapiens,Human,N-Sec1,p67,Protein unc-18 homolog 1,Protein unc-18 homolog A,STXBP1,Syntaxin-binding protein 1,Unc18-1,UNC18A,Unc-18A
EIAAB40497 Mouse,Munc18-2,Mus musculus,MUSEC1,Protein unc-18 homolog 2,Protein unc-18 homolog B,Stxbp2,Syntaxin-binding protein 2,Unc18-2,Unc18b,Unc-18B
EIAAB40493 Homo sapiens,Human,Protein unc-18 homolog 2,Protein unc-18 homolog B,STXBP2,Syntaxin-binding protein 2,Unc18-2,UNC18B,Unc-18B
EIAAB40491 Bos taurus,Bovine,N-Sec1,p67,Protein unc-18 homolog 1,Protein unc-18 homolog A,STXBP1,Syntaxin-binding protein 1,Unc18-1,UNC18A,Unc-18A
EIAAB40494 Munc18-2,Protein unc-18 homolog 2,Protein unc-18 homolog B,Rat,Rattus norvegicus,Stxbp2,Syntaxin-binding protein 2,Unc18-2,Unc18b,Unc-18B
EIAAB40496 Munc18-2,Pig,Protein unc-18 homolog 2,Protein unc-18 homolog B,STXBP2,Sus scrofa,Syntaxin-binding protein 2,Unc18-2,UNC18B,Unc-18B
EIAAB40492 Mouse,Mus musculus,Protein unc-18 homolog 1,Protein unc-18 homolog A,Stxbp1,Syntaxin-binding protein 1,Unc18-1,Unc-18A
EIAAB40488 Chicken,Gallus gallus,N-Sec1,Protein unc-18 homolog 1,Protein unc-18 homolog A,STXBP1,Syntaxin-binding protein 1,Unc18-1,UNC18A,Unc-18A
EIAAB40495 Canis familiaris,Canis lupus familiaris,Dog,Protein unc-18 homolog 2,Protein unc-18 homolog B,STXBP2,Syntaxin-binding protein 2,Unc18-2,Unc-18B
EIAAB34392 Fox-1 homolog B,Fox-1 homolog Fxh,Fox2,Fxh,Hexaribonucleotide-binding protein 2,Hrnbp2,Mouse,Mus musculus,Rbfox2,Rbm9,RNA binding protein fox-1 homolog 2,RNA-binding motif protein 9,RNA-binding protei
EIAAB34386 A2BP,A2BP1,Ataxin-2-binding protein 1,FOX1,Fox-1 homolog A,Hexaribonucleotide-binding protein 1,Homo sapiens,HRNBP1,Human,RBFOX1,RNA binding protein fox-1 homolog 1
EIAAB27925 Influenza virus NS1A-binding protein homolog,Ivns1abp,Kelch family protein Nd1-L,Kiaa0850,Mouse,Mus musculus,Nd1,Nd1L,ND1-L2,Nd1S,Nd1-S,Ns1,NS1-binding protein homolog,Ns1bp,NS1-BP
EIAAB34390 Bos taurus,Bovine,Fox-1 homolog B,FOX2,RBFOX2,RBM9,RNA binding protein fox-1 homolog 2,RNA-binding motif protein 9,RNA-binding protein 9
EIAAB34389 Fox-1 homolog B,Fox2,Rat,Rattus norvegicus,Rbfox2,Rbm9,RNA binding protein fox-1 homolog 2,RNA-binding motif protein 9,RNA-binding protein 9
EIAAB40502 Lethal(2) giant larvae protein homolog 3,Llgl3,Rat,Rattus norvegicus,Stxbp5,Syntaxin-binding protein 5,Tomosyn-1
EIAAB40249 Lethal(2) giant larvae protein homolog 4,Llgl4,Mouse,Mus musculus,Stxbp5l,Syntaxin-binding protein 5-like,Tomosyn-2
EIAAB40504 Kiaa4253,Lethal(2) giant larvae protein homolog 3,Llgl3,Mouse,Mus musculus,Stxbp5,Syntaxin-binding protein 5,Tomosyn-1
EIAAB40503 Homo sapiens,Human,Lethal(2) giant larvae protein homolog 3,LLGL3,STXBP5,Syntaxin-binding protein 5,Tomosyn-1
EIAAB40250 Homo sapiens,Human,KIAA1006,Lethal(2) giant larvae protein homolog 4,LLGL4,STXBP5L,Syntaxin-binding protein 5-like,Tomosyn-2
EIAAB34391 Fox-1 homolog B,FOX2,Hexaribonucleotide-binding protein 2,Homo sapiens,HRNBP2,Human,RBFOX2,RBM9,Repressor of tamoxifen transcriptional activity,RNA binding protein fox-1 homolog 2,RNA-binding motif pr
EIAAB34387 A2bp,A2bp1,Ataxin-2-binding protein 1,Fox1,Fox-1 homolog A,MNCb-3035,Mouse,Mus musculus,Rbfox1,RNA binding protein fox-1 homolog 1
EIAAB37532 C14orf163,FKSG23,Homo sapiens,Human,KIAA0917,SCFD1,Sec1 family domain-containing protein 1,SLY1 homolog,Sly1p,STXBP1L2,Syntaxin-binding protein 1-like 2


 

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