ID   STXB5_HUMAN             Reviewed;        1151 AA.
AC   Q5T5C0; Q14DF3; Q5T5C1; Q5T5C2; Q8NBG8; Q96NG9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Syntaxin-binding protein 5;
DE   AltName: Full=Lethal(2) giant larvae protein homolog 3;
DE   AltName: Full=Tomosyn-1;
GN   Name=STXBP5; Synonyms=LLGL3;
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 [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Cerebellum;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 373-1151 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 670-1151 (ISOFORM 2).
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., 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-762, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692; SER-759 AND SER-1131,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759 AND THR-1039, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Plays a regulatory role in calcium-dependent exocytosis and
CC       neurotransmitter release. Inhibits membrane fusion between transport
CC       vesicles and the plasma membrane. May modulate the assembly of trans-
CC       SNARE complexes between transport vesicles and the plasma membrane.
CC       Inhibits translocation of GLUT4 from intracellular vesicles to the
CC       plasma membrane. Competes with STXBP1 for STX1 binding (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with STX1A and STX1B via its v-SNARE homology
CC       domain. Part of a complex that contains STX1, STXBP5, SNAP25 and SYT1.
CC       Part of a complex that contains STXBP5, STX4A and SNAP23 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic
CC       vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC       {ECO:0000250}. Synapse {ECO:0000250}. Note=Cytoplasmic, and associated
CC       with vesicular membranes and the plasma membrane. Detected at synapses
CC       and on synaptic vesicles (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5T5C0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5T5C0-2; Sequence=VSP_016205;
CC       Name=3;
CC         IsoId=Q5T5C0-3; Sequence=VSP_016204;
CC   -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC03475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL356415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL355365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC113382; AAI13383.1; -; mRNA.
DR   EMBL; AK055484; BAB70930.1; -; mRNA.
DR   EMBL; AK090549; BAC03475.1; ALT_INIT; mRNA.
DR   CCDS; CCDS47499.1; -. [Q5T5C0-1]
DR   CCDS; CCDS5211.1; -. [Q5T5C0-2]
DR   RefSeq; NP_001121187.1; NM_001127715.2. [Q5T5C0-1]
DR   RefSeq; NP_640337.3; NM_139244.4. [Q5T5C0-2]
DR   AlphaFoldDB; Q5T5C0; -.
DR   SMR; Q5T5C0; -.
DR   BioGRID; 126417; 35.
DR   IntAct; Q5T5C0; 10.
DR   STRING; 9606.ENSP00000321826; -.
DR   iPTMnet; Q5T5C0; -.
DR   PhosphoSitePlus; Q5T5C0; -.
DR   BioMuta; STXBP5; -.
DR   DMDM; 74762236; -.
DR   EPD; Q5T5C0; -.
DR   jPOST; Q5T5C0; -.
DR   MassIVE; Q5T5C0; -.
DR   MaxQB; Q5T5C0; -.
DR   PaxDb; 9606-ENSP00000321826; -.
DR   PeptideAtlas; Q5T5C0; -.
DR   ProteomicsDB; 64509; -. [Q5T5C0-1]
DR   ProteomicsDB; 64510; -. [Q5T5C0-2]
DR   ProteomicsDB; 64511; -. [Q5T5C0-3]
DR   Pumba; Q5T5C0; -.
DR   Antibodypedia; 33249; 72 antibodies from 15 providers.
DR   DNASU; 134957; -.
DR   Ensembl; ENST00000321680.11; ENSP00000321826.6; ENSG00000164506.16. [Q5T5C0-1]
DR   Ensembl; ENST00000367480.7; ENSP00000356450.3; ENSG00000164506.16. [Q5T5C0-3]
DR   Ensembl; ENST00000367481.7; ENSP00000356451.3; ENSG00000164506.16. [Q5T5C0-2]
DR   Ensembl; ENST00000706849.1; ENSP00000516590.1; ENSG00000164506.16. [Q5T5C0-2]
DR   Ensembl; ENST00000706850.1; ENSP00000516591.1; ENSG00000164506.16. [Q5T5C0-2]
DR   GeneID; 134957; -.
DR   KEGG; hsa:134957; -.
DR   MANE-Select; ENST00000321680.11; ENSP00000321826.6; NM_001127715.4; NP_001121187.1.
DR   UCSC; uc003qlz.4; human. [Q5T5C0-1]
DR   AGR; HGNC:19665; -.
DR   CTD; 134957; -.
DR   DisGeNET; 134957; -.
DR   GeneCards; STXBP5; -.
DR   HGNC; HGNC:19665; STXBP5.
DR   HPA; ENSG00000164506; Tissue enhanced (parathyroid).
DR   MIM; 604586; gene.
DR   neXtProt; NX_Q5T5C0; -.
DR   OpenTargets; ENSG00000164506; -.
DR   PharmGKB; PA134954258; -.
DR   VEuPathDB; HostDB:ENSG00000164506; -.
DR   eggNOG; KOG1983; Eukaryota.
DR   GeneTree; ENSGT00950000182906; -.
DR   HOGENOM; CLU_002808_0_0_1; -.
DR   InParanoid; Q5T5C0; -.
DR   OMA; IVWKFFD; -.
DR   OrthoDB; 415950at2759; -.
DR   PhylomeDB; Q5T5C0; -.
DR   TreeFam; TF314585; -.
DR   PathwayCommons; Q5T5C0; -.
DR   SignaLink; Q5T5C0; -.
DR   BioGRID-ORCS; 134957; 14 hits in 1153 CRISPR screens.
DR   ChiTaRS; STXBP5; human.
DR   GeneWiki; STXBP5; -.
DR   GenomeRNAi; 134957; -.
DR   Pharos; Q5T5C0; Tbio.
DR   PRO; PR:Q5T5C0; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q5T5C0; Protein.
DR   Bgee; ENSG00000164506; Expressed in adrenal tissue and 170 other cell types or tissues.
DR   ExpressionAtlas; Q5T5C0; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0098674; C:extrinsic component of neuronal dense core vesicle membrane; IEA:Ensembl.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0017075; F:syntaxin-1 binding; ISS:BHF-UCL.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045921; P:positive regulation of exocytosis; ISS:BHF-UCL.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR   GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR   GO; GO:0010807; P:regulation of synaptic vesicle priming; IEA:Ensembl.
DR   CDD; cd15893; R-SNARE_STXBP5; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR000664; Lethal2_giant.
DR   InterPro; IPR013905; Lgl_C_dom.
DR   InterPro; IPR013577; LLGL2.
DR   InterPro; IPR042855; V_SNARE_CC.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR10241; LETHAL 2 GIANT LARVAE PROTEIN; 1.
DR   PANTHER; PTHR10241:SF22; SYNTAXIN-BINDING PROTEIN 5; 1.
DR   Pfam; PF08596; Lgl_C; 1.
DR   Pfam; PF08366; LLGL; 1.
DR   Pfam; PF00400; WD40; 1.
DR   PRINTS; PR00962; LETHAL2GIANT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 2.
DR   PROSITE; PS50892; V_SNARE; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; Q5T5C0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Exocytosis; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Synapse; Transport;
KW   WD repeat.
FT   CHAIN           1..1151
FT                   /note="Syntaxin-binding protein 5"
FT                   /id="PRO_0000051244"
FT   REPEAT          61..94
FT                   /note="WD 1"
FT   REPEAT          101..140
FT                   /note="WD 2"
FT   REPEAT          145..181
FT                   /note="WD 3"
FT   REPEAT          200..234
FT                   /note="WD 4"
FT   REPEAT          240..272
FT                   /note="WD 5"
FT   REPEAT          294..336
FT                   /note="WD 6"
FT   REPEAT          344..378
FT                   /note="WD 7"
FT   REPEAT          400..477
FT                   /note="WD 8"
FT   REPEAT          505..619
FT                   /note="WD 9"
FT   REPEAT          633..695
FT                   /note="WD 10"
FT   REPEAT          794..851
FT                   /note="WD 11"
FT   REPEAT          860..934
FT                   /note="WD 12"
FT   REPEAT          939..983
FT                   /note="WD 13"
FT   REPEAT          997..1020
FT                   /note="WD 14"
FT   DOMAIN          1086..1146
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT   REGION          14..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..581
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..898
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         692
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         723
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WU70"
FT   MOD_RES         759
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18088087,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         762
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   MOD_RES         782
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K400"
FT   MOD_RES         784
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K400"
FT   MOD_RES         785
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         900
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K400"
FT   MOD_RES         902
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K400"
FT   MOD_RES         1039
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1058
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K400"
FT   MOD_RES         1131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         716..768
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_016204"
FT   VAR_SEQ         716..751
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016205"
FT   VARIANT         436
FT                   /note="N -> S (in dbSNP:rs1039084)"
FT                   /id="VAR_035235"
SQ   SEQUENCE   1151 AA;  127573 MW;  247083A17DEA4811 CRC64;
     MRKFNIRKVL DGLTAGSSSA SQQQQQQHPP GNREPEIQET LQSEHFQLCK TVRHGFPYQP
     SALAFDPVQK ILAVGTQTGA LRLFGRPGVE CYCQHDSGAA VIQLQFLINE GALVSALADD
     TLHLWNLRQK RPAILHSLKF CRERVTFCHL PFQSKWLYVG TERGNIHIVN VESFTLSGYV
     IMWNKAIELS SKSHPGPVVH ISDNPMDEGK LLIGFESGTV VLWDLKSKKA DYRYTYDEAI
     HSVAWHHEGK QFICSHSDGT LTIWNVRSPA KPVQTITPHG KQLKDGKKPE PCKPILKVEF
     KTTRSGEPFI ILSGGLSYDT VGRRPCLTVM HGKSTAVLEM DYSIVDFLTL CETPYPNDFQ
     EPYAVVVLLE KDLVLIDLAQ NGYPIFENPY PLSIHESPVT CCEYFADCPV DLIPALYSVG
     ARQKRQGYSK KEWPINGGNW GLGAQSYPEI IITGHADGSV KFWDASAITL QVLYKLKTSK
     VFEKSRNKDD RPNTDIVDED PYAIQIISWC PESRMLCIAG VSAHVIIYRF SKQEVITEVI
     PMLEVRLLYE INDVETPEGE QPPPLPTPVG GSNPQPIPPQ SHPSTSSSSS DGLRDNVPCL
     KVKNSPLKQS PGYQTELVIQ LVWVGGEPPQ QITSLAVNSS YGLVVFGNCN GIAMVDYLQK
     AVLLNLGTIE LYGSNDPYRR EPRSPRKSRQ PSGAGLCDIS EGTVVPEDRC KSPTSGSSSP
     HNSDDEQKMN NFIEKVKTKS RKFSKMVAND IAKMSRKLSL PTDLKPDLDV KDNSFSRSRS
     SSVTSIDKES REAISALHFC ETFTRKTDSS PSPCLWVGTT LGTVLVIALN LPPGGEQRLL
     QPVIVSPSGT ILRLKGAILR MAFLDTTGCL IPPAYEPWRE HNVPEEKDEK EKLKKRRPVS
     VSPSSSQEIS ENQYAVICSE KQAKVISLPT QNCAYKQNIT ETSFVLRGDI VALSNSICLA
     CFCANGHIMT FSLPSLRPLL DVYYLPLTNM RIARTFCFTN NGQALYLVSP TEIQRLTYSQ
     ETCENLQEML GELFTPVETP EAPNRGFFKG LFGGGAQSLD REELFGESSS GKASRSLAQH
     IPGPGGIEGV KGAASGVVGE LARARLALDE RGQKLGDLEE RTAAMLSSAE SFSKHAHEIM
     LKYKDKKWYQ F
//