ID SC24B_HUMAN Reviewed; 1268 AA. AC O95487; B7ZKM8; B7ZKN4; Q0VG08; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 27-MAR-2024, entry version 197. DE RecName: Full=Protein transport protein Sec24B {ECO:0000305}; DE AltName: Full=SEC24-related protein B; GN Name=SEC24B {ECO:0000312|HGNC:HGNC:10704}; 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), SUBUNIT, SUBCELLULAR LOCATION, AND RP TOPOLOGY. RC TISSUE=B-cell; RX PubMed=10075675; DOI=10.1074/jbc.274.12.7833; RA Pagano A., Letourneur F., Garcia-Estefania D., Carpentier J.-L., Orci L., RA Paccaud J.-P.; RT "Sec24 proteins and sorting at the endoplasmic reticulum."; RL J. Biol. Chem. 274:7833-7840(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain, and Eye; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, 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 FUNCTION, SUBUNIT, INTERACTION WITH SEC22B, AND MUTAGENESIS OF ARG-715. RX PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017; RA Mancias J.D., Goldberg J.; RT "The transport signal on Sec22 for packaging into COPII-coated vesicles is RT a conformational epitope."; RL Mol. Cell 26:403-414(2007). RN [6] RP IDENTIFICATION BY 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 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=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP INTERACTION WITH RNF139. RX PubMed=19706601; DOI=10.1074/jbc.m109.041376; RA Irisawa M., Inoue J., Ozawa N., Mori K., Sato R.; RT "The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 RT hampers ER to Golgi transport of sterol regulatory element-binding protein- RT 2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 RT cleavage."; RL J. Biol. Chem. 284:28995-29004(2009). RN [9] 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 [10] RP FUNCTION, AND INTERACTION WITH TMED2 AND TMED10. RX PubMed=20427317; DOI=10.1242/jcs.062950; RA Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.; RT "Selective export of human GPI-anchored proteins from the endoplasmic RT reticulum."; RL J. Cell Sci. 123:1705-1715(2010). RN [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-329 AND SER-1224, AND RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-55 (ISOFORM 3), AND IDENTIFICATION BY MASS RP 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). RN [14] RP INTERACTION WITH CNIH4. RX PubMed=24405750; DOI=10.1111/tra.12148; RA Sauvageau E., Rochdi M.D., Oueslati M., Hamdan F.F., Percherancier Y., RA Simpson J.C., Pepperkok R., Bouvier M.; RT "CNIH4 interacts with newly synthesized GPCR and controls their export from RT the endoplasmic reticulum."; RL Traffic 15:383-400(2014). RN [15] {ECO:0007744|PDB:3EH1} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 518-1268 IN COMPLEX WITH ZINC, RP AND FUNCTION. RX PubMed=18843296; DOI=10.1038/emboj.2008.208; RA Mancias J.D., Goldberg J.; RT "Structural basis of cargo membrane protein discrimination by the human RT COPII coat machinery."; RL EMBO J. 27:2918-2928(2008). RN [16] RP INTERACTION WITH STING1. RX PubMed=32690950; DOI=10.1038/s41590-020-0730-5; RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L., RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F., RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T., RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T., RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O., RA Thomsen M.K., Paludan S.R.; RT "STEEP mediates STING ER exit and activation of signaling."; RL Nat. Immunol. 21:868-879(2020). RN [17] RP ERRATUM OF PUBMED:32690950. RX PubMed=32929276; DOI=10.1038/s41590-020-0803-5; RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L., RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F., RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T., RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T., RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O., RA Thomsen M.K., Paludan S.R.; RL Nat. Immunol. 21:1468-1469(2020). CC -!- FUNCTION: Component of the coat protein complex II (COPII) which CC promotes the formation of transport vesicles from the endoplasmic CC reticulum (ER). The coat has two main functions, the physical CC deformation of the endoplasmic reticulum membrane into vesicles and the CC selection of cargo molecules for their transport to the Golgi complex CC (PubMed:17499046, PubMed:20427317, PubMed:18843296). Plays a central CC role in cargo selection within the COPII complex and together with CC SEC24A may have a different specificity compared to SEC24C and SEC24D. CC May package preferentially cargos with cytoplasmic DxE or LxxLE motifs CC and may also recognize conformational epitopes (PubMed:17499046, CC PubMed:18843296). {ECO:0000269|PubMed:17499046, CC ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}. CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24 CC complex, the Sec13/31 complex and SAR1 (PubMed:10075675, CC PubMed:17499046). Interacts with STING1; promoting STING1 translocation CC to COPII vesicles in a STEEP1-dependent manner (PubMed:32690950). CC Interacts with RNF139 (PubMed:19706601). Interacts with TMED2 and CC TMED10 (PubMed:20427317). Interacts with CNIH4 (PubMed:24405750). CC {ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:17499046, CC ECO:0000269|PubMed:19706601, ECO:0000269|PubMed:20427317, CC ECO:0000269|PubMed:24405750, ECO:0000269|PubMed:32690950}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle CC membrane {ECO:0000269|PubMed:10075675}; Peripheral membrane protein CC {ECO:0000305|PubMed:10075675}; Cytoplasmic side CC {ECO:0000305|PubMed:10075675}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:10075675}; Peripheral membrane protein CC {ECO:0000269|PubMed:10075675}; Cytoplasmic side CC {ECO:0000269|PubMed:10075675}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:10075675}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O95487-1; Sequence=Displayed; CC Name=2; CC IsoId=O95487-2; Sequence=VSP_035987; CC Name=3; CC IsoId=O95487-3; Sequence=VSP_054432, VSP_054433; CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA10335.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ131245; CAA10335.1; ALT_FRAME; mRNA. DR EMBL; AC105314; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138782; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC040137; AAH40137.1; -; mRNA. DR EMBL; BC117135; AAI17136.1; -; mRNA. DR EMBL; BC143268; AAI43269.1; -; mRNA. DR EMBL; BC143276; AAI43277.1; -; mRNA. DR CCDS; CCDS43260.1; -. [O95487-2] DR CCDS; CCDS47124.1; -. [O95487-1] DR CCDS; CCDS75179.1; -. [O95487-3] DR RefSeq; NP_001036199.1; NM_001042734.3. [O95487-2] DR RefSeq; NP_001287742.1; NM_001300813.2. [O95487-3] DR RefSeq; NP_001305014.1; NM_001318085.1. DR RefSeq; NP_001305015.1; NM_001318086.1. DR RefSeq; NP_006314.2; NM_006323.4. [O95487-1] DR PDB; 3EH1; X-ray; 1.80 A; A=518-1268. DR PDBsum; 3EH1; -. DR AlphaFoldDB; O95487; -. DR SMR; O95487; -. DR BioGRID; 115696; 249. DR ComplexPortal; CPX-2360; COPII vesicle coat complex. DR CORUM; O95487; -. DR IntAct; O95487; 78. DR MINT; O95487; -. DR STRING; 9606.ENSP00000428564; -. DR GlyCosmos; O95487; 31 sites, 2 glycans. DR GlyGen; O95487; 42 sites, 3 O-linked glycans (42 sites). DR iPTMnet; O95487; -. DR PhosphoSitePlus; O95487; -. DR SwissPalm; O95487; -. DR BioMuta; SEC24B; -. DR EPD; O95487; -. DR jPOST; O95487; -. DR MassIVE; O95487; -. DR MaxQB; O95487; -. DR PaxDb; 9606-ENSP00000428564; -. DR PeptideAtlas; O95487; -. DR ProteomicsDB; 50915; -. [O95487-1] DR ProteomicsDB; 50916; -. [O95487-2] DR ProteomicsDB; 7184; -. DR Pumba; O95487; -. DR Antibodypedia; 48510; 56 antibodies from 13 providers. DR DNASU; 10427; -. DR Ensembl; ENST00000265175.5; ENSP00000265175.4; ENSG00000138802.11. [O95487-1] DR Ensembl; ENST00000399100.6; ENSP00000382051.2; ENSG00000138802.11. [O95487-2] DR Ensembl; ENST00000504968.6; ENSP00000428564.1; ENSG00000138802.11. [O95487-3] DR GeneID; 10427; -. DR KEGG; hsa:10427; -. DR MANE-Select; ENST00000265175.5; ENSP00000265175.4; NM_006323.5; NP_006314.2. DR UCSC; uc003hzk.4; human. [O95487-1] DR AGR; HGNC:10704; -. DR CTD; 10427; -. DR DisGeNET; 10427; -. DR GeneCards; SEC24B; -. DR HGNC; HGNC:10704; SEC24B. DR HPA; ENSG00000138802; Low tissue specificity. DR MIM; 607184; gene. DR neXtProt; NX_O95487; -. DR OpenTargets; ENSG00000138802; -. DR PharmGKB; PA35627; -. DR VEuPathDB; HostDB:ENSG00000138802; -. DR eggNOG; KOG1985; Eukaryota. DR GeneTree; ENSGT00950000182924; -. DR HOGENOM; CLU_004589_2_0_1; -. DR InParanoid; O95487; -. DR OMA; CAHYAMS; -. DR OrthoDB; 977017at2759; -. DR PhylomeDB; O95487; -. DR TreeFam; TF354244; -. DR PathwayCommons; O95487; -. DR Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF). DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-5694530; Cargo concentration in the ER. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; O95487; -. DR SIGNOR; O95487; -. DR BioGRID-ORCS; 10427; 20 hits in 1155 CRISPR screens. DR ChiTaRS; SEC24B; human. DR EvolutionaryTrace; O95487; -. DR GeneWiki; SEC24B; -. DR GenomeRNAi; 10427; -. DR Pharos; O95487; Tbio. DR PRO; PR:O95487; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O95487; Protein. DR Bgee; ENSG00000138802; Expressed in cartilage tissue and 217 other cell types or tissues. DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl. DR GO; GO:0021747; P:cochlear nucleus development; IEA:Ensembl. DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB. DR GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl. DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl. DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl. DR GO; GO:0061156; P:pulmonary artery morphogenesis; IEA:Ensembl. DR GO; GO:1901301; P:regulation of cargo loading into COPII-coated vesicle; IEA:Ensembl. DR GO; GO:0090178; P:regulation of establishment of planar polarity involved in neural tube closure; IEA:Ensembl. DR CDD; cd01479; Sec24-like; 1. DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1. DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1. DR Gene3D; 3.40.20.10; Severin; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR007123; Gelsolin-like_dom. DR InterPro; IPR036180; Gelsolin-like_dom_sf. DR InterPro; IPR006900; Sec23/24_helical_dom. DR InterPro; IPR036175; Sec23/24_helical_dom_sf. DR InterPro; IPR006896; Sec23/24_trunk_dom. DR InterPro; IPR012990; Sec23_24_beta_S. DR InterPro; IPR041742; Sec24-like_trunk_dom. DR InterPro; IPR036465; vWFA_dom_sf. DR InterPro; IPR006895; Znf_Sec23_Sec24. DR InterPro; IPR036174; Znf_Sec23_Sec24_sf. DR PANTHER; PTHR13803:SF42; PROTEIN TRANSPORT PROTEIN SEC24B; 1. DR PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1. DR Pfam; PF00626; Gelsolin; 1. DR Pfam; PF08033; Sec23_BS; 1. DR Pfam; PF04815; Sec23_helical; 1. DR Pfam; PF04811; Sec23_trunk; 1. DR Pfam; PF04810; zf-Sec23_Sec24; 1. DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1. DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1. DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1. DR Genevisible; O95487; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Membrane; KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome; KW Transport; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..1268 FT /note="Protein transport protein Sec24B" FT /id="PRO_0000205155" FT REPEAT 1141..1213 FT /note="Gelsolin-like" FT /evidence="ECO:0000255" FT REGION 1..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 216..263 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 303..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 362..451 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 605..629 FT /note="Zinc finger-like" FT COMPBIAS 42..57 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 216..236 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..263 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 375..390 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 426..451 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 605 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:3EH1" FT BINDING 608 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:3EH1" FT BINDING 626 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:3EH1" FT BINDING 629 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:3EH1" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 329 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1224 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 44 FT /note="N -> NETGFHHVAQASLELLDPSNLPASASQIAGST (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054432" FT VAR_SEQ 354..388 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_035987" FT VAR_SEQ 496 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054433" FT VARIANT 456 FT /note="A -> G (in dbSNP:rs35705351)" FT /id="VAR_047934" FT MUTAGEN 715 FT /note="R->A: Decreased ability to package the SNARESEC22B FT cargo into COPII vesicles. Has no effect on other cargos FT packaging." FT /evidence="ECO:0000269|PubMed:17499046" FT CONFLICT 23 FT /note="A -> S (in Ref. 1; CAA10335)" FT /evidence="ECO:0000305" FT HELIX 520..522 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 524..526 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 527..529 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 548..553 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 557..559 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 560..570 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 571..577 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 582..585 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 606..608 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 617..625 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 627..629 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 632..634 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 637..639 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 651..653 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 655..658 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 660..666 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 668..670 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 672..674 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 679..685 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 688..693 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 695..706 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 707..709 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 717..731 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 740..745 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 755..757 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 759..761 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 762..765 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 766..775 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 776..778 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 790..801 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 802..804 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 806..812 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 831..834 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 835..837 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 847..857 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 860..866 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 874..877 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 879..882 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 883..885 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 888..890 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 896..898 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 900..915 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 919..928 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 932..943 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 945..954 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 960..968 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 974..985 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 991..1003 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1006..1011 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1015..1032 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1035..1054 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1066..1068 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1069..1071 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1074..1082 FT /evidence="ECO:0007829|PDB:3EH1" FT TURN 1085..1087 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1095..1107 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1110..1117 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1120..1123 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1133..1135 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1138..1140 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1150..1152 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1157..1162 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1164..1171 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1177..1182 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1189..1191 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1194..1196 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1205..1219 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1221..1223 FT /evidence="ECO:0007829|PDB:3EH1" FT STRAND 1226..1236 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1237..1241 FT /evidence="ECO:0007829|PDB:3EH1" FT HELIX 1255..1267 FT /evidence="ECO:0007829|PDB:3EH1" FT MOD_RES O95487-3:55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" SQ SEQUENCE 1268 AA; 137418 MW; 0E08B982D0982F84 CRC64; MSAPAGSSHP AASARIPPKF GGAAVSGAAA PAGPGAGPAP HQQNGPAQNQ MQVPSGYGLH HQNYIAPSGH YSQGPGKMTS LPLDTQCGDY YSALYTVPTQ NVTPNTVNQQ PGAQQLYSRG PPAPHIVGST LGSFQGAASS ASHLHTSASQ PYSSFVNHYN SPAMYSASSS VASQGFPSTC GHYAMSTVSN AAYPSVSYPS LPAGDTYGQM FTSQNAPTVR PVKDNSFSGQ NTAISHPSPL PPLPSQQHHQ QQSLSGYSTL TWSSPGLPST QDNLIRNHTG SLAVANNNPT ITVADSLSCP VMQNVQPPKS SPVVSTVLSG SSGSSSTRTP PTANHPVEPV TSVTQPSELL QQKGVQYGEY VNNQASSAPT PLSSTSDDEE EEEEDEEAGV DSSSTTSSAS PMPNSYDALE GGSYPDMLSS SASSPAPDPA PEPDPASAPA PASAPAPVVP QPSKMAKPFG YGYPTLQPGY QNATAPLISG VQPSNPVYSG FQQYPQQYPG VNQLSSSIGG LSLQSSPQPE SLRPVNLTQE RNILPMTPVW APVPNLNADL KKLNCSPDSF RCTLTNIPQT QALLNKAKLP LGLLLHPFRD LTQLPVITSN TIVRCRSCRT YINPFVSFID QRRWKCNLCY RVNDVPEEFM YNPLTRSYGE PHKRPEVQNS TVEFIASSDY MLRPPQPAVY LFVLDVSHNA VEAGYLTILC QSLLENLDKL PGDSRTRIGF MTFDSTIHFY NLQEGLSQPQ MLIVSDIDDV FLPTPDSLLV NLYESKELIK DLLNALPNMF TNTRETHSAL GPALQAAFKL MSPTGGRVSV FQTQLPSLGA GLLQSREDPN QRSSTKVVQH LGPATDFYKK LALDCSGQQT AVDLFLLSSQ YSDLASLACM SKYSAGCIYY YPSFHYTHNP SQAEKLQKDL KRYLTRKIGF EAVMRIRCTK GLSMHTFHGN FFVRSTDLLS LANINPDAGF AVQLSIEESL TDTSLVCFQT ALLYTSSKGE RRIRVHTLCL PVVSSLADVY AGVDVQAAIC LLANMAVDRS VSSSLSDARD ALVNAVVDSL SAYGSTVSNL QHSALMAPSS LKLFPLYVLA LLKQKAFRTG TSTRLDDRVY AMCQIKSQPL VHLMKMIHPN LYRIDRLTDE GAVHVNDRIV PQPPLQKLSA EKLTREGAFL MDCGSVFYIW VGKGCDNNFI EDVLGYTNFA SIPQKMTHLP ELDTLSSERA RSFITWLRDS RPLSPILHIV KDESPAKAEF FQHLIEDRTE AAFSYYEFLL HVQQQICK //