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Protein transport protein Sec24D (SEC24-related protein D)

 SC24D_HUMAN             Reviewed;        1032 AA.
O94855; Q8IYI7;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
07-APR-2021, entry version 178.
RecName: Full=Protein transport protein Sec24D {ECO:0000305};
AltName: Full=SEC24-related protein D;
Name=SEC24D {ECO:0000312|HGNC:HGNC:10706};
Synonyms=KIAA0755 {ECO:0000312|EMBL:BAA34475.2};
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), SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Pancreas;
PubMed=10329445; DOI=10.1006/bbrc.1999.0574;
Tang B.L., Kausalya J., Low D.Y.H., Lock M.L., Hong W.;
"A family of mammalian proteins homologous to yeast Sec24p.";
Biochem. Biophys. Res. Commun. 258:679-684(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI. The
complete sequences of 100 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 5:277-286(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph;
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).
[5]
FUNCTION, AND SUBUNIT.
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]
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).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[9]
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).
[10]
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).
[11]
INVOLVEMENT IN CLCRP2, AND VARIANTS CLCRP2 PRO-978 AND PHE-1015.
PubMed=25683121; DOI=10.1016/j.ajhg.2015.01.002;
Garbes L., Kim K., Riess A., Hoyer-Kuhn H., Beleggia F., Bevot A.,
Kim M.J., Huh Y.H., Kweon H.S., Savarirayan R., Amor D., Kakadia P.M.,
Lindig T., Kagan K.O., Becker J., Boyadjiev S.A., Wollnik B., Semler O.,
Bohlander S.K., Kim J., Netzer C.;
"Mutations in SEC24D, encoding a component of the COPII machinery, cause a
syndromic form of osteogenesis imperfecta.";
Am. J. Hum. Genet. 96:432-439(2015).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13] {ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 266-1032 IN COMPLEX WITH CARGO
PEPTIDES; SEC23A AND ZINC, FUNCTION, AND INTERACTION WITH GOSR2 AND STX5.
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).
[14] {ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYW, ECO:0007744|PDB:5KYX, ECO:0007744|PDB:5KYY}
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 266-1032 IN COMPLEX WITH SEC23A
AND ZINC, AND INTERACTION WITH SEC23A.
PubMed=27551091; DOI=10.1073/pnas.1605916113;
Ma W., Goldberg J.;
"TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large
COPII coats.";
Proc. Natl. Acad. Sci. U.S.A. 113:10061-10066(2016).
-!- 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
SEC24C may have a different specificity compared to SEC24A and SEC24B
(PubMed:17499046, PubMed:20427317, PubMed:18843296). May more
specifically package GPI-anchored proteins through the cargo receptor
TMED10 (PubMed:20427317). May also be specific for IxM motif-containing
cargos like the SNAREs GOSR2 and STX5 (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:17499046,
PubMed:27551091). Interacts with TMED2 and TMED10 (PubMed:20427317).
Interacts with CNIH4 (PubMed:24405750). Interacts with GOSR2 (via IxM
motif) and STX5 (via IxM motif); recruits GOSR2 and STX5 into COPII-
coated vesicles (PubMed:18843296). {ECO:0000269|PubMed:17499046,
ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317,
ECO:0000269|PubMed:24405750, ECO:0000269|PubMed:27551091}.
-!- INTERACTION:
O94855; Q01844: EWSR1; NbExp=3; IntAct=EBI-748817, EBI-739737;
O94855; Q15437: SEC23B; NbExp=6; IntAct=EBI-748817, EBI-742673;
O94855; Q15427: SF3B4; NbExp=3; IntAct=EBI-748817, EBI-348469;
O94855-2; Q15436: SEC23A; NbExp=3; IntAct=EBI-12081096, EBI-81088;
O94855-2; Q15437: SEC23B; NbExp=3; IntAct=EBI-12081096, EBI-742673;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
membrane {ECO:0000269|PubMed:10329445}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P53992}; Cytoplasmic side
{ECO:0000250|UniProtKB:P53992}. Endoplasmic reticulum membrane
{ECO:0000305|PubMed:10329445}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P53992}; Cytoplasmic side
{ECO:0000250|UniProtKB:P53992}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P53992}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O94855-1; Sequence=Displayed;
Name=2;
IsoId=O94855-2; Sequence=VSP_035761;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with higher amounts in
placenta, pancreas, heart and liver. {ECO:0000269|PubMed:10329445}.
-!- DISEASE: Cole-Carpenter syndrome 2 (CLCRP2) [MIM:616294]: A form of
Cole-Carpenter syndrome, a disorder characterized by features of
osteogenesis imperfecta such as bone deformities and severe bone
fragility with frequent fractures, in association with
craniosynostosis, ocular proptosis, hydrocephalus, growth failure and
distinctive facial features. Craniofacial findings include marked
frontal bossing, midface hypoplasia, and micrognathia. Despite the
craniosynostosis and hydrocephalus, intellectual development is normal.
CLCRP2 inheritance is autosomal recessive.
{ECO:0000269|PubMed:25683121}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA34475.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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EMBL; AF130464; AAD28756.2; -; mRNA.
EMBL; AB018298; BAA34475.2; ALT_INIT; mRNA.
EMBL; CH471229; EAW73656.1; -; Genomic_DNA.
EMBL; BC035761; AAH35761.1; -; mRNA.
CCDS; CCDS3710.1; -. [O94855-1]
RefSeq; NP_001304995.1; NM_001318066.1. [O94855-2]
RefSeq; NP_055637.2; NM_014822.3. [O94855-1]
RefSeq; XP_005263436.1; XM_005263379.2. [O94855-2]
PDB; 3EFO; X-ray; 2.70 A; B=266-1032.
PDB; 3EG9; X-ray; 3.00 A; B=266-1032.
PDB; 5KYU; X-ray; 3.51 A; B=266-1032.
PDB; 5KYW; X-ray; 3.20 A; B=266-1032.
PDB; 5KYX; X-ray; 3.52 A; B=266-1032.
PDB; 5KYY; X-ray; 3.40 A; B=266-1032.
PDBsum; 3EFO; -.
PDBsum; 3EG9; -.
PDBsum; 5KYU; -.
PDBsum; 5KYW; -.
PDBsum; 5KYX; -.
PDBsum; 5KYY; -.
SMR; O94855; -.
BioGRID; 115204; 40.
IntAct; O94855; 19.
MINT; O94855; -.
STRING; 9606.ENSP00000280551; -.
iPTMnet; O94855; -.
MetOSite; O94855; -.
PhosphoSitePlus; O94855; -.
SwissPalm; O94855; -.
BioMuta; SEC24D; -.
EPD; O94855; -.
jPOST; O94855; -.
MassIVE; O94855; -.
MaxQB; O94855; -.
PaxDb; O94855; -.
PeptideAtlas; O94855; -.
PRIDE; O94855; -.
ProteomicsDB; 50488; -. [O94855-1]
ProteomicsDB; 50489; -. [O94855-2]
Antibodypedia; 26618; 97 antibodies.
DNASU; 9871; -.
Ensembl; ENST00000280551; ENSP00000280551; ENSG00000150961. [O94855-1]
GeneID; 9871; -.
KEGG; hsa:9871; -.
UCSC; uc003ici.5; human. [O94855-1]
CTD; 9871; -.
DisGeNET; 9871; -.
GeneCards; SEC24D; -.
HGNC; HGNC:10706; SEC24D.
HPA; ENSG00000150961; Low tissue specificity.
MalaCards; SEC24D; -.
MIM; 607186; gene.
MIM; 616294; phenotype.
neXtProt; NX_O94855; -.
OpenTargets; ENSG00000150961; -.
Orphanet; 2050; Cole-Carpenter syndrome.
PharmGKB; PA35629; -.
VEuPathDB; HostDB:ENSG00000150961.14; -.
eggNOG; KOG1984; Eukaryota.
GeneTree; ENSGT00950000182924; -.
HOGENOM; CLU_004589_1_1_1; -.
InParanoid; O94855; -.
OMA; QNGAHAS; -.
OrthoDB; 330236at2759; -.
PhylomeDB; O94855; -.
TreeFam; TF300464; -.
PathwayCommons; O94855; -.
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; 9871; 3 hits in 989 CRISPR screens.
ChiTaRS; SEC24D; human.
EvolutionaryTrace; O94855; -.
GeneWiki; SEC24D; -.
GenomeRNAi; 9871; -.
Pharos; O94855; Tbio.
PRO; PR:O94855; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; O94855; protein.
Bgee; ENSG00000150961; Expressed in stromal cell of endometrium and 215 other tissues.
ExpressionAtlas; O94855; baseline and differential.
Genevisible; O94855; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0000149; F:SNARE binding; IPI:UniProtKB.
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:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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.
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.
1: Evidence at protein level;
3D-structure; Alternative splicing; Craniosynostosis; Cytoplasm;
Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum;
ER-Golgi transport; Membrane; Metal-binding; Osteogenesis imperfecta;
Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc.
CHAIN 1..1032
/note="Protein transport protein Sec24D"
/id="PRO_0000205157"
REPEAT 901..974
/note="Gelsolin-like"
/evidence="ECO:0000255"
REGION 363..388
/note="Zinc finger-like"
COMPBIAS 10..293
/note="Pro-rich"
METAL 363
/note="Zinc"
/evidence="ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9,
ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX"
METAL 366
/note="Zinc"
/evidence="ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9,
ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX"
METAL 385
/note="Zinc"
/evidence="ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9,
ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX"
METAL 388
/note="Zinc"
/evidence="ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9,
ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX"
MOD_RES 266
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
VAR_SEQ 224
/note="Q -> QA (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_035761"
VARIANT 42
/note="M -> T (in dbSNP:rs10029206)"
/id="VAR_047472"
VARIANT 193
/note="P -> L (in dbSNP:rs6844109)"
/id="VAR_047473"
VARIANT 496
/note="F -> I (in dbSNP:rs11723368)"
/id="VAR_047474"
VARIANT 978
/note="Q -> P (in CLCRP2; dbSNP:rs786204846)"
/evidence="ECO:0000269|PubMed:25683121"
/id="VAR_073658"
VARIANT 1015
/note="S -> F (in CLCRP2; dbSNP:rs760670617)"
/evidence="ECO:0000269|PubMed:25683121"
/id="VAR_073659"
CONFLICT 559
/note="P -> S (in Ref. 1; AAD28756 and 2; BAA34475)"
/evidence="ECO:0000305"
HELIX 267..278
/evidence="ECO:0007744|PDB:3EFO"
STRAND 281..284
/evidence="ECO:0007744|PDB:3EFO"
STRAND 287..289
/evidence="ECO:0007744|PDB:3EFO"
STRAND 300..302
/evidence="ECO:0007744|PDB:3EFO"
STRAND 304..306
/evidence="ECO:0007744|PDB:3EFO"
TURN 309..311
/evidence="ECO:0007744|PDB:3EFO"
STRAND 312..322
/evidence="ECO:0007744|PDB:3EFO"
HELIX 323..329
/evidence="ECO:0007744|PDB:3EFO"
STRAND 334..337
/evidence="ECO:0007744|PDB:3EFO"
TURN 356..358
/evidence="ECO:0007744|PDB:3EFO"
TURN 364..366
/evidence="ECO:0007744|PDB:3EFO"
STRAND 375..377
/evidence="ECO:0007744|PDB:3EFO"
HELIX 378..380
/evidence="ECO:0007744|PDB:3EFO"
STRAND 382..384
/evidence="ECO:0007744|PDB:3EFO"
TURN 386..388
/evidence="ECO:0007744|PDB:3EFO"
STRAND 391..393
/evidence="ECO:0007744|PDB:3EFO"
HELIX 396..398
/evidence="ECO:0007744|PDB:3EFO"
STRAND 404..406
/evidence="ECO:0007744|PDB:3EFO"
TURN 408..410
/evidence="ECO:0007744|PDB:3EFO"
HELIX 411..413
/evidence="ECO:0007744|PDB:3EFO"
HELIX 415..418
/evidence="ECO:0007744|PDB:3EFO"
STRAND 420..425
/evidence="ECO:0007744|PDB:3EFO"
HELIX 428..430
/evidence="ECO:0007744|PDB:3EFO"
HELIX 432..434
/evidence="ECO:0007744|PDB:3EFO"
STRAND 441..447
/evidence="ECO:0007744|PDB:3EFO"
HELIX 450..454
/evidence="ECO:0007744|PDB:3EFO"
HELIX 457..468
/evidence="ECO:0007744|PDB:3EFO"
HELIX 469..471
/evidence="ECO:0007744|PDB:3EFO"
STRAND 478..480
/evidence="ECO:0007744|PDB:3EFO"
STRAND 484..498
/evidence="ECO:0007744|PDB:3EFO"
STRAND 507..511
/evidence="ECO:0007744|PDB:3EFO"
STRAND 522..527
/evidence="ECO:0007744|PDB:3EFO"
TURN 529..532
/evidence="ECO:0007744|PDB:3EFO"
HELIX 533..548
/evidence="ECO:0007744|PDB:3EFO"
HELIX 558..571
/evidence="ECO:0007744|PDB:3EFO"
STRAND 575..581
/evidence="ECO:0007744|PDB:3EFO"
STRAND 587..589
/evidence="ECO:0007744|PDB:3EFO"
HELIX 607..611
/evidence="ECO:0007744|PDB:3EFO"
STRAND 614..616
/evidence="ECO:0007744|PDB:3EFO"
HELIX 617..627
/evidence="ECO:0007744|PDB:3EFO"
STRAND 630..636
/evidence="ECO:0007744|PDB:3EFO"
HELIX 644..647
/evidence="ECO:0007744|PDB:3EFO"
HELIX 649..653
/evidence="ECO:0007744|PDB:3EFO"
STRAND 658..660
/evidence="ECO:0007744|PDB:3EFO"
HELIX 666..682
/evidence="ECO:0007744|PDB:3EFO"
STRAND 685..695
/evidence="ECO:0007744|PDB:3EFO"
STRAND 699..707
/evidence="ECO:0007744|PDB:3EFO"
STRAND 711..714
/evidence="ECO:0007744|PDB:3EFO"
STRAND 716..724
/evidence="ECO:0007744|PDB:3EFO"
STRAND 727..735
/evidence="ECO:0007744|PDB:3EFO"
TURN 739..741
/evidence="ECO:0007744|PDB:3EFO"
STRAND 742..752
/evidence="ECO:0007744|PDB:3EFO"
STRAND 758..771
/evidence="ECO:0007744|PDB:3EFO"
HELIX 773..778
/evidence="ECO:0007744|PDB:3EFO"
HELIX 782..796
/evidence="ECO:0007744|PDB:3EFO"
TURN 797..799
/evidence="ECO:0007744|PDB:3EFO"
HELIX 802..823
/evidence="ECO:0007744|PDB:3EFO"
STRAND 832..835
/evidence="ECO:0007744|PDB:3EFO"
HELIX 837..839
/evidence="ECO:0007744|PDB:3EFO"
HELIX 842..851
/evidence="ECO:0007744|PDB:3EFO"
HELIX 853..855
/evidence="ECO:0007744|PDB:3EFO"
STRAND 858..861
/evidence="ECO:0007744|PDB:3EFO"
HELIX 863..875
/evidence="ECO:0007744|PDB:3EFO"
HELIX 878..885
/evidence="ECO:0007744|PDB:3EFO"
STRAND 888..891
/evidence="ECO:0007744|PDB:3EFO"
STRAND 897..899
/evidence="ECO:0007744|PDB:3EFO"
HELIX 910..912
/evidence="ECO:0007744|PDB:3EFO"
STRAND 918..922
/evidence="ECO:0007744|PDB:3EFO"
STRAND 924..931
/evidence="ECO:0007744|PDB:3EFO"
HELIX 937..944
/evidence="ECO:0007744|PDB:3EFO"
STRAND 945..948
/evidence="ECO:0007744|PDB:3EFO"
HELIX 949..951
/evidence="ECO:0007744|PDB:3EFO"
HELIX 966..978
/evidence="ECO:0007744|PDB:3EFO"
STRAND 986..992
/evidence="ECO:0007744|PDB:3EFO"
HELIX 998..1001
/evidence="ECO:0007744|PDB:3EFO"
HELIX 1016..1029
/evidence="ECO:0007744|PDB:3EFO"
SEQUENCE 1032 AA; 113010 MW; B46E566F096F37F0 CRC64;
MSQQGYVATP PYSQPQPGIG LSPPHYGHYG DPSHTASPTG MMKPAGPLGA TATRGMLPPG
PPPPGPHQFG QNGAHATGHP PQRFPGPPPV NNVASSHAPY QPSAQSSYPG PISTSSVTQL
GSQLSAMQIN SYGSGMAPPS QGPPGPLSAT SLQTPPRPPQ PSILQPGSQV LPPPPTTLNG
PGASPLPLPM YRPDGLSGPP PPNAQYQPPP LPGQTLGAGY PPQQANSGPQ MAGAQLSYPG
GFPGGPAQMA GPPQPQKKLD PDSIPSPIQV IENDRASRGG QVYATNTRGQ IPPLVTTDCM
IQDQGNASPR FIRCTTYCFP CTSDMAKQAQ IPLAAVIKPF ATIPSNESPL YLVNHGESGP
VRCNRCKAYM CPFMQFIEGG RRYQCGFCNC VNDVPPFYFQ HLDHIGRRLD HYEKPELSLG
SYEYVATLDY CRKSKPPNPP AFIFMIDVSY SNIKNGLVKL ICEELKTMLE KIPKEEQEET
SAIRVGFITY NKVLHFFNVK SNLAQPQMMV VTDVGEVFVP LLDGFLVNYQ ESQSVIHNLL
DQIPDMFADS NENETVFAPV IQAGMEALKA ADCPGKLFIF HSSLPTAEAP GKLKNRDDKK
LVNTDKEKIL FQPQTNVYDS LAKDCVAHGC SVTLFLFPSQ YVDVASLGLV PQLTGGTLYK
YNNFQMHLDR QQFLNDLRND IEKKIGFDAI MRVRTSTGFR ATDFFGGILM NNTTDVEMAA
IDCDKAVTVE FKHDDKLSED SGALIQCAVL YTTISGQRRL RIHNLGLNCS SQLADLYKSC
ETDALINFFA KSAFKAVLHQ PLKVIREILV NQTAHMLACY RKNCASPSAA SQLILPDSMK
VLPVYMNCLL KNCVLLSRPE ISTDERAYQR QLVMTMGVAD SQLFFYPQLL PIHTLDVKST
MLPAAVRCSE SRLSEEGIFL LANGLHMFLW LGVSSPPELI QGIFNVPSFA HINTDMTLLP
EVGNPYSQQL RMIMGIIQQK RPYSMKLTIV KQREQPEMVF RQFLVEDKGL YGGSSYVDFL
CCVHKEICQL LN


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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1616: ABC transporters
WP1689: Porphyrin and chlorophyll metabolism
WP1713: Two-component system
WP1502: Mitochondrial biogenesis
WP2199: Seed Development
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
WP1371: G Protein Signaling Pathways
WP1700: Selenoamino acid metabolism
WP346: Protein Modifications
WP1659: Glycine, serine and threonine metabolism
WP1665: Limonene and pinene degradation
WP2032: TSH signaling pathway
WP73: G Protein Signaling Pathways
WP1675: Nitrogen metabolism
WP211: BMP signaling pathway
WP2218: sGC
WP813: G Protein Signaling Pathways

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)
[SEC23B] Protein transport protein Sec23B (hSec23B) (SEC23-related protein B)
[SEC24A] Protein transport protein Sec24A (SEC24-related protein A)
[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)
[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)
[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)
[SF3B4 SAP49] Splicing factor 3B subunit 4 (Pre-mRNA-splicing factor SF3b 49 kDa subunit) (Spliceosome-associated protein 49) (SAP 49)
[EWSR1 EWS] RNA-binding protein EWS (EWS oncogene) (Ewing sarcoma breakpoint region 1 protein)
[Stx5 Stx5a] Syntaxin-5
[sec24 NCU02391] Protein transport protein sec24
[TMED2 RNP24] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (p24 family protein beta-1) (p24beta1) (Fragment)
[MIA3 KIAA0268 TANGO UNQ6077/PRO20088] Transport and Golgi organization protein 1 homolog (TANGO1) (C219-reactive peptide) (D320) (Melanoma inhibitory activity protein 3)
[SEC13 ANU3 YLR208W L8167.4] Protein transport protein SEC13
[SAR1 YPL218W] Small COPII coat GTPase SAR1 (EC 3.6.5.-) (GTP-binding protein SAR1) (Secretion-associated RAS-related protein 1)
[SEC22 SLY2 TSL26 YLR268W L8479.3] Protein transport protein SEC22 (Suppressor of loss of YPT1 protein 2)
[sec24 DDB_G0281255] Protein transport protein SEC24
[BET1 SLY12 YIL004C YIA4C] Protein transport protein BET1 (Suppressor of loss of YPT1 protein 12) (Protein SLY12)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

Bibliography :
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