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Protein transport protein Sec24B (SEC24-related protein B)

 SC24B_HUMAN             Reviewed;        1268 AA.
O95487; B7ZKM8; B7ZKN4; Q0VG08;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
07-APR-2021, entry version 183.
RecName: Full=Protein transport protein Sec24B {ECO:0000305};
AltName: Full=SEC24-related protein B;
Name=SEC24B {ECO:0000312|HGNC:HGNC:10704};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION, AND
TOPOLOGY.
TISSUE=B-cell;
PubMed=10075675; DOI=10.1074/jbc.274.12.7833;
Pagano A., Letourneur F., Garcia-Estefania D., Carpentier J.-L., Orci L.,
Paccaud J.-P.;
"Sec24 proteins and sorting at the endoplasmic reticulum.";
J. Biol. Chem. 274:7833-7840(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[5]
FUNCTION, SUBUNIT, INTERACTION WITH SEC22B, AND MUTAGENESIS OF ARG-715.
PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
Mancias J.D., Goldberg J.;
"The transport signal on Sec22 for packaging into COPII-coated vesicles is
a conformational epitope.";
Mol. Cell 26:403-414(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
INTERACTION WITH RNF139.
PubMed=19706601; DOI=10.1074/jbc.m109.041376;
Irisawa M., Inoue J., Ozawa N., Mori K., Sato R.;
"The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8
hampers ER to Golgi transport of sterol regulatory element-binding protein-
2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2
cleavage.";
J. Biol. Chem. 284:28995-29004(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
FUNCTION, AND INTERACTION WITH TMED2 AND TMED10.
PubMed=20427317; DOI=10.1242/jcs.062950;
Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
"Selective export of human GPI-anchored proteins from the endoplasmic
reticulum.";
J. Cell Sci. 123:1705-1715(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-329 AND SER-1224, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-55 (ISOFORM 3), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
INTERACTION WITH CNIH4.
PubMed=24405750; DOI=10.1111/tra.12148;
Sauvageau E., Rochdi M.D., Oueslati M., Hamdan F.F., Percherancier Y.,
Simpson J.C., Pepperkok R., Bouvier M.;
"CNIH4 interacts with newly synthesized GPCR and controls their export from
the endoplasmic reticulum.";
Traffic 15:383-400(2014).
[15] {ECO:0007744|PDB:3EH1}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 518-1268 IN COMPLEX WITH ZINC,
AND FUNCTION.
PubMed=18843296; DOI=10.1038/emboj.2008.208;
Mancias J.D., Goldberg J.;
"Structural basis of cargo membrane protein discrimination by the human
COPII coat machinery.";
EMBO J. 27:2918-2928(2008).
[16]
INTERACTION WITH STING1.
PubMed=32690950; DOI=10.1038/s41590-020-0730-5;
Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
Thomsen M.K., Paludan S.R.;
"STEEP mediates STING ER exit and activation of signaling.";
Nat. Immunol. 21:868-879(2020).
[17]
ERRATUM OF PUBMED:32690950.
PubMed=32929276; DOI=10.1038/s41590-020-0803-5;
Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
Thomsen M.K., Paludan S.R.;
Nat. Immunol. 21:1468-1469(2020).
-!- FUNCTION: Component of the coat protein complex II (COPII) which
promotes the formation of transport vesicles from the endoplasmic
reticulum (ER). The coat has two main functions, the physical
deformation of the endoplasmic reticulum membrane into vesicles and the
selection of cargo molecules for their transport to the Golgi complex
(PubMed:17499046, PubMed:20427317, PubMed:18843296). Plays a central
role in cargo selection within the COPII complex and together with
SEC24A may have a different specificity compared to SEC24C and SEC24D.
May package preferentially cargos with cytoplasmic DxE or LxxLE motifs
and may also recognize conformational epitopes (PubMed:17499046,
PubMed:18843296). {ECO:0000269|PubMed:17499046,
ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
-!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
complex, the Sec13/31 complex and SAR1 (PubMed:10075675,
PubMed:17499046). Interacts with STING1; promoting STING1 translocation
to COPII vesicles in a STEEP1-dependent manner (PubMed:32690950).
Interacts with RNF139 (PubMed:19706601). Interacts with TMED2 and
TMED10 (PubMed:20427317). Interacts with CNIH4 (PubMed:24405750).
{ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:17499046,
ECO:0000269|PubMed:19706601, ECO:0000269|PubMed:20427317,
ECO:0000269|PubMed:24405750, ECO:0000269|PubMed:32690950}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
membrane {ECO:0000269|PubMed:10075675}; Peripheral membrane protein
{ECO:0000305|PubMed:10075675}; Cytoplasmic side
{ECO:0000305|PubMed:10075675}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10075675}; Peripheral membrane protein
{ECO:0000269|PubMed:10075675}; Cytoplasmic side
{ECO:0000269|PubMed:10075675}. Cytoplasm, cytosol
{ECO:0000269|PubMed:10075675}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O95487-1; Sequence=Displayed;
Name=2;
IsoId=O95487-2; Sequence=VSP_035987;
Name=3;
IsoId=O95487-3; Sequence=VSP_054432, VSP_054433;
-!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA10335.1; Type=Frameshift; Evidence={ECO:0000305};
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EMBL; AJ131245; CAA10335.1; ALT_FRAME; mRNA.
EMBL; AC105314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC040137; AAH40137.1; -; mRNA.
EMBL; BC117135; AAI17136.1; -; mRNA.
EMBL; BC143268; AAI43269.1; -; mRNA.
EMBL; BC143276; AAI43277.1; -; mRNA.
CCDS; CCDS43260.1; -. [O95487-2]
CCDS; CCDS47124.1; -. [O95487-1]
CCDS; CCDS75179.1; -. [O95487-3]
RefSeq; NP_001036199.1; NM_001042734.3. [O95487-2]
RefSeq; NP_001287742.1; NM_001300813.2. [O95487-3]
RefSeq; NP_001305014.1; NM_001318085.1.
RefSeq; NP_001305015.1; NM_001318086.1.
RefSeq; NP_006314.2; NM_006323.4. [O95487-1]
PDB; 3EH1; X-ray; 1.80 A; A=518-1268.
PDBsum; 3EH1; -.
SMR; O95487; -.
BioGRID; 115696; 135.
CORUM; O95487; -.
IntAct; O95487; 40.
MINT; O95487; -.
STRING; 9606.ENSP00000428564; -.
GlyGen; O95487; 5 sites, 1 O-linked glycan (5 sites).
iPTMnet; O95487; -.
PhosphoSitePlus; O95487; -.
SwissPalm; O95487; -.
BioMuta; SEC24B; -.
EPD; O95487; -.
jPOST; O95487; -.
MassIVE; O95487; -.
MaxQB; O95487; -.
PaxDb; O95487; -.
PeptideAtlas; O95487; -.
PRIDE; O95487; -.
ProteomicsDB; 50915; -. [O95487-1]
ProteomicsDB; 50916; -. [O95487-2]
ProteomicsDB; 7184; -.
Antibodypedia; 48510; 30 antibodies.
Ensembl; ENST00000265175; ENSP00000265175; ENSG00000138802. [O95487-1]
Ensembl; ENST00000399100; ENSP00000382051; ENSG00000138802. [O95487-2]
Ensembl; ENST00000504968; ENSP00000428564; ENSG00000138802. [O95487-3]
GeneID; 10427; -.
KEGG; hsa:10427; -.
UCSC; uc003hzk.4; human. [O95487-1]
CTD; 10427; -.
DisGeNET; 10427; -.
GeneCards; SEC24B; -.
HGNC; HGNC:10704; SEC24B.
HPA; ENSG00000138802; Low tissue specificity.
MIM; 607184; gene.
neXtProt; NX_O95487; -.
OpenTargets; ENSG00000138802; -.
PharmGKB; PA35627; -.
VEuPathDB; HostDB:ENSG00000138802.11; -.
eggNOG; KOG1985; Eukaryota.
GeneTree; ENSGT00950000182924; -.
HOGENOM; CLU_004589_2_0_1; -.
InParanoid; O95487; -.
OMA; CAHYAMS; -.
OrthoDB; 330236at2759; -.
PhylomeDB; O95487; -.
TreeFam; TF354244; -.
PathwayCommons; O95487; -.
Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
BioGRID-ORCS; 10427; 11 hits in 993 CRISPR screens.
ChiTaRS; SEC24B; human.
EvolutionaryTrace; O95487; -.
GeneWiki; SEC24B; -.
GenomeRNAi; 10427; -.
Pharos; O95487; Tbio.
PRO; PR:O95487; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; O95487; protein.
Bgee; ENSG00000138802; Expressed in sigmoid colon and 249 other tissues.
Genevisible; O95487; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
GO; GO:0021747; P:cochlear nucleus development; IEA:Ensembl.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl.
GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0061156; P:pulmonary artery morphogenesis; IEA:Ensembl.
GO; GO:1901301; P:regulation of cargo loading into COPII-coated vesicle; IEA:Ensembl.
GO; GO:0090178; P:regulation of establishment of planar polarity involved in neural tube closure; IEA:Ensembl.
CDD; cd01479; Sec24-like; 1.
Gene3D; 3.40.20.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
InterPro; IPR007123; Gelsolin-like_dom.
InterPro; IPR036180; Gelsolin-like_dom_sf.
InterPro; IPR006900; Sec23/24_helical_dom.
InterPro; IPR036175; Sec23/24_helical_dom_sf.
InterPro; IPR006896; Sec23/24_trunk_dom.
InterPro; IPR012990; Sec23_24_beta_S.
InterPro; IPR041742; Sec24-like_trunk_dom.
InterPro; IPR036465; vWFA_dom_sf.
InterPro; IPR006895; Znf_Sec23_Sec24.
InterPro; IPR036174; Znf_Sec23_Sec24_sf.
Pfam; PF00626; Gelsolin; 1.
Pfam; PF08033; Sec23_BS; 1.
Pfam; PF04815; Sec23_helical; 1.
Pfam; PF04811; Sec23_trunk; 1.
Pfam; PF04810; zf-Sec23_Sec24; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF81811; SSF81811; 1.
SUPFAM; SSF82754; SSF82754; 1.
SUPFAM; SSF82919; SSF82919; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cytoplasm;
Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Membrane;
Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
Transport; Zinc.
INIT_MET 1
/note="Removed"
/evidence="ECO:0007744|PubMed:19413330"
CHAIN 2..1268
/note="Protein transport protein Sec24B"
/id="PRO_0000205155"
REPEAT 1141..1213
/note="Gelsolin-like"
/evidence="ECO:0000255"
REGION 605..629
/note="Zinc finger-like"
COMPBIAS 379..387
/note="Poly-Glu"
METAL 605
/note="Zinc"
/evidence="ECO:0007744|PDB:3EH1"
METAL 608
/note="Zinc"
/evidence="ECO:0007744|PDB:3EH1"
METAL 626
/note="Zinc"
/evidence="ECO:0007744|PDB:3EH1"
METAL 629
/note="Zinc"
/evidence="ECO:0007744|PDB:3EH1"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0007744|PubMed:19413330"
MOD_RES 329
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 1224
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
VAR_SEQ 44
/note="N -> NETGFHHVAQASLELLDPSNLPASASQIAGST (in isoform
3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_054432"
VAR_SEQ 354..388
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_035987"
VAR_SEQ 496
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_054433"
VARIANT 456
/note="A -> G (in dbSNP:rs35705351)"
/id="VAR_047934"
MUTAGEN 715
/note="R->A: Decreased ability to package the SNARE SEC22B
cargo into COPII vesicles. Has no effect on other cargos
packaging."
/evidence="ECO:0000269|PubMed:17499046"
CONFLICT 23
/note="A -> S (in Ref. 1; CAA10335)"
/evidence="ECO:0000305"
HELIX 520..522
/evidence="ECO:0007744|PDB:3EH1"
STRAND 524..526
/evidence="ECO:0007744|PDB:3EH1"
TURN 527..529
/evidence="ECO:0007744|PDB:3EH1"
HELIX 548..553
/evidence="ECO:0007744|PDB:3EH1"
TURN 557..559
/evidence="ECO:0007744|PDB:3EH1"
STRAND 560..570
/evidence="ECO:0007744|PDB:3EH1"
HELIX 571..577
/evidence="ECO:0007744|PDB:3EH1"
STRAND 582..585
/evidence="ECO:0007744|PDB:3EH1"
TURN 606..608
/evidence="ECO:0007744|PDB:3EH1"
STRAND 617..625
/evidence="ECO:0007744|PDB:3EH1"
TURN 627..629
/evidence="ECO:0007744|PDB:3EH1"
STRAND 632..634
/evidence="ECO:0007744|PDB:3EH1"
HELIX 637..639
/evidence="ECO:0007744|PDB:3EH1"
HELIX 651..653
/evidence="ECO:0007744|PDB:3EH1"
HELIX 655..658
/evidence="ECO:0007744|PDB:3EH1"
STRAND 660..666
/evidence="ECO:0007744|PDB:3EH1"
HELIX 668..670
/evidence="ECO:0007744|PDB:3EH1"
STRAND 672..674
/evidence="ECO:0007744|PDB:3EH1"
STRAND 679..685
/evidence="ECO:0007744|PDB:3EH1"
HELIX 688..693
/evidence="ECO:0007744|PDB:3EH1"
HELIX 695..706
/evidence="ECO:0007744|PDB:3EH1"
TURN 707..709
/evidence="ECO:0007744|PDB:3EH1"
STRAND 717..731
/evidence="ECO:0007744|PDB:3EH1"
STRAND 740..745
/evidence="ECO:0007744|PDB:3EH1"
HELIX 755..757
/evidence="ECO:0007744|PDB:3EH1"
STRAND 759..761
/evidence="ECO:0007744|PDB:3EH1"
TURN 762..765
/evidence="ECO:0007744|PDB:3EH1"
HELIX 766..775
/evidence="ECO:0007744|PDB:3EH1"
HELIX 776..778
/evidence="ECO:0007744|PDB:3EH1"
HELIX 790..801
/evidence="ECO:0007744|PDB:3EH1"
TURN 802..804
/evidence="ECO:0007744|PDB:3EH1"
STRAND 806..812
/evidence="ECO:0007744|PDB:3EH1"
HELIX 831..834
/evidence="ECO:0007744|PDB:3EH1"
STRAND 835..837
/evidence="ECO:0007744|PDB:3EH1"
HELIX 847..857
/evidence="ECO:0007744|PDB:3EH1"
STRAND 860..866
/evidence="ECO:0007744|PDB:3EH1"
HELIX 874..877
/evidence="ECO:0007744|PDB:3EH1"
HELIX 879..882
/evidence="ECO:0007744|PDB:3EH1"
TURN 883..885
/evidence="ECO:0007744|PDB:3EH1"
STRAND 888..890
/evidence="ECO:0007744|PDB:3EH1"
TURN 896..898
/evidence="ECO:0007744|PDB:3EH1"
HELIX 900..915
/evidence="ECO:0007744|PDB:3EH1"
STRAND 919..928
/evidence="ECO:0007744|PDB:3EH1"
STRAND 932..943
/evidence="ECO:0007744|PDB:3EH1"
STRAND 945..954
/evidence="ECO:0007744|PDB:3EH1"
STRAND 960..968
/evidence="ECO:0007744|PDB:3EH1"
STRAND 974..985
/evidence="ECO:0007744|PDB:3EH1"
STRAND 991..1003
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1006..1011
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1015..1032
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1035..1054
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1066..1068
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1069..1071
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1074..1082
/evidence="ECO:0007744|PDB:3EH1"
TURN 1085..1087
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1095..1107
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1110..1117
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1120..1123
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1133..1135
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1138..1140
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1150..1152
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1157..1162
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1164..1171
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1177..1182
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1189..1191
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1194..1196
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1205..1219
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1221..1223
/evidence="ECO:0007744|PDB:3EH1"
STRAND 1226..1236
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1237..1241
/evidence="ECO:0007744|PDB:3EH1"
HELIX 1255..1267
/evidence="ECO:0007744|PDB:3EH1"
MOD_RES O95487-3:55
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
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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WP2272: Pathogenic Escherichia coli infection
WP1616: ABC transporters
WP1689: Porphyrin and chlorophyll metabolism
WP1713: Two-component system
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WP731: Sterol regulatory element binding protein related
WP1909: Signal regulatory protein (SIRP) family interactions
WP1685: Peptidoglycan biosynthesis
WP1624: Bacterial secretion system
WP1692: Protein export
WP2324: AGE/RAGE pathway
WP1650: Fluorobenzoate degradation
WP1939: Unfolded Protein Response
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WP1700: Selenoamino acid metabolism
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Related Genes :
[SEC24B] Protein transport protein Sec24B (SEC24-related protein B)
[SEC24A] Protein transport protein Sec24A (SEC24-related protein A)
[Sec24a] Protein transport protein Sec24A (SEC24-related protein A)
[SEC24 ANU1 YIL109C] Protein transport protein SEC24 (Abnormal nuclear morphology 1)
[SEC24A] Protein transport protein Sec24A (SEC24-related protein A)
[RNF139 TRC8] E3 ubiquitin-protein ligase RNF139 (EC 2.3.2.27) (RING finger protein 139) (RING-type E3 ubiquitin transferase RNF139) (Translocation in renal carcinoma on chromosome 8 protein)
[YIPF5 FINGER5 YIP1A PP12723 SB140 UNQ3123/PRO10275] Protein YIPF5 (Five-pass transmembrane protein localizing in the Golgi apparatus and the endoplasmic reticulum 5) (Smooth muscle cell-associated protein 5) (SMAP-5) (YIP1 family member 5) (YPT-interacting protein 1 A)
[SEC23B] Protein transport protein Sec23B (hSec23B) (SEC23-related protein B)
[sec24b creb5] Cyclic AMP-responsive element-binding protein 5
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Integral membrane protein p23) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[TMED2 RNP24] Transmembrane emp24 domain-containing protein 2 (Membrane protein p24A) (p24) (p24 family protein beta-1) (p24beta1)
[Scap] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (S31I125) (S31III125) (Tmp-21-I) (Transmembrane protein Tmp21) (p23) (p24 family protein delta-1) (p24delta1) (p24delta)
[Tmed10 Tmp21] Transmembrane emp24 domain-containing protein 10 (Protein Tmed10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[Tmed10 Tmp21] Transmembrane emp24 domain-containing protein 10 (Protein Tmed10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Integral membrane protein p23) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[Tmed2 Rnp24] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (RNP21.4) (p24 family protein beta-1) (p24beta1)
[SCAP] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[Tmed2 Rnp24 Sid394] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (Sid 394) (p24 family protein beta-1) (p24beta1)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[STING1 ERIS MITA TMEM173] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[SCAP KIAA0199 PSEC0227] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[Scap Kiaa0199] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
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[Sting1 Tmem173] Stimulator of interferon genes protein (rSTING) (Transmembrane protein 173)
[STING1 TMEM173] Stimulator of interferon genes protein (STING) (Transmembrane protein 173)
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Bibliography :
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