ID   STXB2_HUMAN             Reviewed;         593 AA.
AC   Q15833; B4E175; E7EQD5; Q9BU65;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Syntaxin-binding protein 2;
DE   AltName: Full=Protein unc-18 homolog 2;
DE            Short=Unc18-2;
DE   AltName: Full=Protein unc-18 homolog B;
DE            Short=Unc-18B;
GN   Name=STXBP2; Synonyms=UNC18B;
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), AND VARIANT VAL-526.
RX   PubMed=8921365; DOI=10.1006/geno.1996.0515;
RA   Ziegler S.F., Mortrud M.T., Swartz A.R., Baker E., Sutherland G.R.,
RA   Burmeister M., Mulligan J.T.;
RT   "Molecular characterization of a nonneuronal human UNC18 homolog.";
RL   Genomics 37:19-23(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT VAL-526.
RC   TISSUE=Kidney;
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 GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, INTERACTION WITH STX11, VARIANTS FHL5 PRO-209; ILE-232 DEL;
RP   HIS-292; TRP-405; GLN-405 AND LEU-477, AND CHARACTERIZATION OF VARIANTS
RP   FHL5 ILE-232 DEL; HIS-292; TRP-405; GLN-405 AND LEU-477.
RX   PubMed=19804848; DOI=10.1016/j.ajhg.2009.09.005;
RA   zur Stadt U., Rohr J., Seifert W., Koch F., Grieve S., Pagel J.,
RA   Strauss J., Kasper B., Nuernberg G., Becker C., Maul-Pavicic A., Beutel K.,
RA   Janka G., Griffiths G., Ehl S., Hennies H.C.;
RT   "Familial hemophagocytic lymphohistiocytosis type 5 (FHL-5) is caused by
RT   mutations in Munc18-2 and impaired binding to syntaxin 11.";
RL   Am. J. Hum. Genet. 85:482-492(2009).
RN   [8]
RP   FUNCTION, INTERACTION WITH STX11, AND VARIANT FHL5 LEU-477.
RX   PubMed=19884660; DOI=10.1172/jci40732;
RA   Cote M., Menager M.M., Burgess A., Mahlaoui N., Picard C., Schaffner C.,
RA   Al-Manjomi F., Al-Harbi M., Alangari A., Le Deist F., Gennery A.R.,
RA   Prince N., Cariou A., Nitschke P., Blank U., El-Ghazali G., Menasche G.,
RA   Latour S., Fischer A., de Saint Basile G.;
RT   "Munc18-2 deficiency causes familial hemophagocytic lymphohistiocytosis
RT   type 5 and impairs cytotoxic granule exocytosis in patient NK cells.";
RL   J. Clin. Invest. 119:3765-3773(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Involved in intracellular vesicle trafficking and vesicle
CC       fusion with membranes. Contributes to the granule exocytosis machinery
CC       through interaction with soluble N-ethylmaleimide-sensitive factor
CC       attachment protein receptor (SNARE) proteins that regulate membrane
CC       fusion. Regulates cytotoxic granule exocytosis in natural killer (NK)
CC       cells. {ECO:0000269|PubMed:19804848, ECO:0000269|PubMed:19884660}.
CC   -!- SUBUNIT: Interacts with STX1A, STX2 and STX3 (By similarity). Interacts
CC       with STX11. {ECO:0000250, ECO:0000269|PubMed:19804848,
CC       ECO:0000269|PubMed:19884660}.
CC   -!- INTERACTION:
CC       Q15833; O75558: STX11; NbExp=4; IntAct=EBI-4401015, EBI-714135;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q15833-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15833-2; Sequence=VSP_040121;
CC       Name=3;
CC         IsoId=Q15833-3; Sequence=VSP_055157;
CC   -!- TISSUE SPECIFICITY: Placenta, lung, liver, kidney and pancreas, as well
CC       as in peripheral blood lymphocytes.
CC   -!- DISEASE: Hemophagocytic lymphohistiocytosis, familial, 5, with or
CC       without microvillus inclusion disease (FHL5) [MIM:613101]: A rare,
CC       autosomal recessive disorder characterized by immune dysregulation with
CC       hypercytokinemia, defective function of natural killer cell, and
CC       massive infiltration of several organs by activated lymphocytes and
CC       macrophages. The clinical features of the disease include fever,
CC       hepatosplenomegaly, cytopenia, and less frequently neurological
CC       abnormalities ranging from irritability and hypotonia to seizures,
CC       cranial nerve deficits and ataxia. Some patients may present in early
CC       infancy with severe diarrhea, prior to the onset of typical FHL
CC       features, whereas others present later in childhood and have a more
CC       protracted course without diarrhea. The early-onset diarrhea is due to
CC       enteropathy reminiscent of microvillus inclusion disease.
CC       {ECO:0000269|PubMed:19804848, ECO:0000269|PubMed:19884660}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR   EMBL; U63533; AAC50762.1; -; mRNA.
DR   EMBL; BT006915; AAP35561.1; -; mRNA.
DR   EMBL; AK303701; BAG64687.1; -; mRNA.
DR   EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471139; EAW69018.1; -; Genomic_DNA.
DR   EMBL; BC002869; AAH02869.1; -; mRNA.
DR   CCDS; CCDS12181.1; -. [Q15833-1]
DR   CCDS; CCDS45948.1; -. [Q15833-2]
DR   CCDS; CCDS62522.1; -. [Q15833-3]
DR   RefSeq; NP_001120868.1; NM_001127396.2. [Q15833-2]
DR   RefSeq; NP_001258963.1; NM_001272034.1. [Q15833-3]
DR   RefSeq; NP_008880.2; NM_006949.3. [Q15833-1]
DR   PDB; 4CCA; X-ray; 2.60 A; A=1-593.
DR   PDBsum; 4CCA; -.
DR   AlphaFoldDB; Q15833; -.
DR   SMR; Q15833; -.
DR   BioGRID; 112682; 96.
DR   IntAct; Q15833; 17.
DR   STRING; 9606.ENSP00000413606; -.
DR   GlyGen; Q15833; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q15833; -.
DR   MetOSite; Q15833; -.
DR   PhosphoSitePlus; Q15833; -.
DR   SwissPalm; Q15833; -.
DR   BioMuta; STXBP2; -.
DR   DMDM; 313104015; -.
DR   OGP; Q15833; -.
DR   EPD; Q15833; -.
DR   jPOST; Q15833; -.
DR   MassIVE; Q15833; -.
DR   MaxQB; Q15833; -.
DR   PaxDb; 9606-ENSP00000413606; -.
DR   PeptideAtlas; Q15833; -.
DR   ProteomicsDB; 17549; -.
DR   ProteomicsDB; 60782; -. [Q15833-1]
DR   ProteomicsDB; 60783; -. [Q15833-2]
DR   Pumba; Q15833; -.
DR   Antibodypedia; 2787; 244 antibodies from 29 providers.
DR   DNASU; 6813; -.
DR   Ensembl; ENST00000221283.10; ENSP00000221283.4; ENSG00000076944.18. [Q15833-1]
DR   Ensembl; ENST00000414284.6; ENSP00000409471.1; ENSG00000076944.18. [Q15833-2]
DR   Ensembl; ENST00000441779.6; ENSP00000413606.2; ENSG00000076944.18. [Q15833-3]
DR   GeneID; 6813; -.
DR   KEGG; hsa:6813; -.
DR   MANE-Select; ENST00000221283.10; ENSP00000221283.4; NM_006949.4; NP_008880.2.
DR   UCSC; uc002mha.6; human. [Q15833-1]
DR   AGR; HGNC:11445; -.
DR   CTD; 6813; -.
DR   DisGeNET; 6813; -.
DR   GeneCards; STXBP2; -.
DR   GeneReviews; STXBP2; -.
DR   HGNC; HGNC:11445; STXBP2.
DR   HPA; ENSG00000076944; Tissue enhanced (lymphoid).
DR   MalaCards; STXBP2; -.
DR   MIM; 601717; gene.
DR   MIM; 613101; phenotype.
DR   neXtProt; NX_Q15833; -.
DR   OpenTargets; ENSG00000076944; -.
DR   Orphanet; 540; Familial hemophagocytic lymphohistiocytosis.
DR   PharmGKB; PA36242; -.
DR   VEuPathDB; HostDB:ENSG00000076944; -.
DR   eggNOG; KOG1300; Eukaryota.
DR   GeneTree; ENSGT00940000160045; -.
DR   InParanoid; Q15833; -.
DR   OMA; KQWPFVS; -.
DR   OrthoDB; 4609640at2759; -.
DR   PhylomeDB; Q15833; -.
DR   TreeFam; TF313242; -.
DR   PathwayCommons; Q15833; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-449836; Other interleukin signaling.
DR   SignaLink; Q15833; -.
DR   SIGNOR; Q15833; -.
DR   BioGRID-ORCS; 6813; 11 hits in 1151 CRISPR screens.
DR   ChiTaRS; STXBP2; human.
DR   GeneWiki; Syntaxin_binding_protein_2; -.
DR   GenomeRNAi; 6813; -.
DR   Pharos; Q15833; Tbio.
DR   PRO; PR:Q15833; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q15833; Protein.
DR   Bgee; ENSG00000076944; Expressed in granulocyte and 146 other cell types or tissues.
DR   ExpressionAtlas; Q15833; baseline and differential.
DR   GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR   GO; GO:0044194; C:cytolytic granule; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR   GO; GO:0070820; C:tertiary granule; IDA:UniProtKB.
DR   GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR   GO; GO:0030348; F:syntaxin-3 binding; IPI:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0001909; P:leukocyte mediated cytotoxicity; IMP:UniProtKB.
DR   GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR   GO; GO:0043312; P:neutrophil degranulation; IEP:UniProtKB.
DR   GO; GO:0043304; P:regulation of mast cell degranulation; ISS:UniProtKB.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.25.40.60; -; 1.
DR   Gene3D; 3.40.50.1910; -; 1.
DR   Gene3D; 3.40.50.2060; -; 1.
DR   InterPro; IPR043154; Sec-1-like_dom1.
DR   InterPro; IPR043127; Sec-1-like_dom3a.
DR   InterPro; IPR001619; Sec1-like.
DR   InterPro; IPR027482; Sec1-like_dom2.
DR   InterPro; IPR036045; Sec1-like_sf.
DR   PANTHER; PTHR11679:SF27; SYNTAXIN-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR11679; VESICLE PROTEIN SORTING-ASSOCIATED; 1.
DR   Pfam; PF00995; Sec1; 1.
DR   PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR   SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 1.
DR   Genevisible; Q15833; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disease variant; Exocytosis;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..593
FT                   /note="Syntaxin-binding protein 2"
FT                   /id="PRO_0000206281"
FT   REGION          444..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         82
FT                   /note="K -> KAQAQRVIHLPQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055157"
FT   VAR_SEQ         83..85
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_040121"
FT   VARIANT         209
FT                   /note="L -> P (in FHL5; dbSNP:rs121918541)"
FT                   /evidence="ECO:0000269|PubMed:19804848"
FT                   /id="VAR_063814"
FT   VARIANT         232
FT                   /note="Missing (in FHL5; leads to a complete loss of the
FT                   ability to interact with STX11)"
FT                   /evidence="ECO:0000269|PubMed:19804848"
FT                   /id="VAR_063815"
FT   VARIANT         292
FT                   /note="R -> H (in FHL5; leads to a complete loss of the
FT                   ability to interact with STX11; dbSNP:rs746897867)"
FT                   /evidence="ECO:0000269|PubMed:19804848"
FT                   /id="VAR_063816"
FT   VARIANT         405
FT                   /note="R -> Q (in FHL5; leads to a complete loss of the
FT                   ability to interact with STX11; dbSNP:rs773360200)"
FT                   /evidence="ECO:0000269|PubMed:19804848"
FT                   /id="VAR_063817"
FT   VARIANT         405
FT                   /note="R -> W (in FHL5; leads to a complete loss of the
FT                   ability to interact with STX11; dbSNP:rs769717341)"
FT                   /evidence="ECO:0000269|PubMed:19804848"
FT                   /id="VAR_063818"
FT   VARIANT         477
FT                   /note="P -> L (in FHL5; leads to a complete loss of the
FT                   ability to interact with STX11; dbSNP:rs121918540)"
FT                   /evidence="ECO:0000269|PubMed:19804848,
FT                   ECO:0000269|PubMed:19884660"
FT                   /id="VAR_063819"
FT   VARIANT         526
FT                   /note="I -> V (in dbSNP:rs6791)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:8921365"
FT                   /id="VAR_014934"
FT   CONFLICT        348
FT                   /note="H -> R (in Ref. 3; BAG64687)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..15
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   TURN            16..22
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           35..42
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           47..51
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   TURN            52..54
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          71..77
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          102..108
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           112..119
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           123..126
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          127..132
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          141..146
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           152..157
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           159..164
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           165..182
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           196..215
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   TURN            217..220
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           225..227
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          229..233
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           241..243
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           249..256
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          263..267
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           286..291
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   TURN            296..298
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           299..314
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           327..331
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           333..357
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           360..373
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           385..393
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           400..414
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           419..428
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           432..434
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           435..439
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           440..443
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           478..487
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   TURN            493..495
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          498..500
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          533..538
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           544..556
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   TURN            557..559
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   STRAND          562..570
FT                   /evidence="ECO:0007829|PDB:4CCA"
FT   HELIX           573..582
FT                   /evidence="ECO:0007829|PDB:4CCA"
SQ   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
//