STXB5_HUMAN
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 03-AUG-2022, entry version 162.
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; 30.
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; Q5T5C0; -.
DR PeptideAtlas; Q5T5C0; -.
DR PRIDE; Q5T5C0; -.
DR ProteomicsDB; 64509; -. [Q5T5C0-1]
DR ProteomicsDB; 64510; -. [Q5T5C0-2]
DR ProteomicsDB; 64511; -. [Q5T5C0-3]
DR Antibodypedia; 33249; 52 antibodies from 14 providers.
DR DNASU; 134957; -.
DR Ensembl; ENST00000321680.11; ENSP00000321826.6; ENSG00000164506.15. [Q5T5C0-1]
DR Ensembl; ENST00000367480.7; ENSP00000356450.3; ENSG00000164506.15. [Q5T5C0-3]
DR Ensembl; ENST00000367481.7; ENSP00000356451.3; ENSG00000164506.15. [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 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; VSSFHFC; -.
DR OrthoDB; 84844at2759; -.
DR PhylomeDB; Q5T5C0; -.
DR TreeFam; TF314585; -.
DR PathwayCommons; Q5T5C0; -.
DR SignaLink; Q5T5C0; -.
DR BioGRID-ORCS; 134957; 13 hits in 1077 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 169 other tissues.
DR ExpressionAtlas; Q5T5C0; baseline and differential.
DR Genevisible; Q5T5C0; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:BHF-UCL.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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 Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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; SSF50978; SSF50978; 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.
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
