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SC24B_HUMAN
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   03-AUG-2022, entry version 188.
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};
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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; 189.
DR   CORUM; O95487; -.
DR   IntAct; O95487; 45.
DR   MINT; O95487; -.
DR   STRING; 9606.ENSP00000428564; -.
DR   GlyGen; O95487; 31 sites, 2 O-linked glycans (31 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; O95487; -.
DR   PeptideAtlas; O95487; -.
DR   PRIDE; O95487; -.
DR   ProteomicsDB; 50915; -. [O95487-1]
DR   ProteomicsDB; 50916; -. [O95487-2]
DR   ProteomicsDB; 7184; -.
DR   Antibodypedia; 48510; 38 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   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; CDSNFIE; -.
DR   OrthoDB; 330236at2759; -.
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; 18 hits in 1076 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 215 other tissues.
DR   Genevisible; O95487; HS.
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; 3.40.20.10; -; 1.
DR   Gene3D; 3.40.50.410; -; 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   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; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF81811; SSF81811; 1.
DR   SUPFAM; SSF82754; SSF82754; 1.
DR   SUPFAM; SSF82919; SSF82919; 1.
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 SNARE SEC22B
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
 
 
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