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Protein transport protein Sec24C (SEC24-related protein C)

 SC24C_HUMAN             Reviewed;        1094 AA.
P53992; B4DZT4; Q8WV25;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 3.
07-APR-2021, entry version 200.
RecName: Full=Protein transport protein Sec24C {ECO:0000305};
AltName: Full=SEC24-related protein C;
Name=SEC24C {ECO:0000312|HGNC:HGNC:10705};
Synonyms=KIAA0079 {ECO:0000312|EMBL:BAA07558.2};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7584044; DOI=10.1093/dnares/1.5.223;
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
Kawarabayasi Y., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. II. The
coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
cDNA clones from human cell line KG-1.";
DNA Res. 1:223-229(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-109.
TISSUE=Muscle;
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=10214955; DOI=10.1016/s0014-5793(99)00303-8;
Tani K., Oyama Y., Hatsuzawa K., Tagaya M.;
"Hypothetical protein KIAA0079 is a mammalian homologue of yeast Sec24p.";
FEBS Lett. 447:247-250(1999).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[7]
SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
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).
[8]
INTERACTION WITH DDHD1.
PubMed=17428803; DOI=10.1074/jbc.m611237200;
Iinuma T., Shiga A., Nakamoto K., O'Brien M.B., Aridor M., Arimitsu N.,
Tagaya M., Tani K.;
"Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic
reticulum.";
J. Biol. Chem. 282:17632-17639(2007).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, AND 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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
INTERACTION WITH STING1.
PubMed=30842662; DOI=10.1038/s41586-019-1006-9;
Gui X., Yang H., Li T., Tan X., Shi P., Li M., Du F., Chen Z.J.;
"Autophagy induction via STING1 trafficking is a primordial function of the
cGAS pathway.";
Nature 567:262-266(2019).
[17] {ECO:0007744|PDB:3EH2}
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 329-1094 IN COMPLEX WITH ZINC,
FUNCTION, INTERACTION WITH GOSR2 AND STX5, AND MUTAGENESIS OF
895-LEU--LEU-897.
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).
-!- 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:10214955, PubMed:17499046, PubMed:18843296, PubMed:20427317).
Plays a central role in cargo selection within the COPII complex and
together with SEC24D 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:10214955, 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:10214955,
PubMed:10075675, PubMed:17499046). Interacts with TMED2 and TMED10
(PubMed:20427317). Interacts with GOSR2 (via IxM motif) and STX5 (via
IxM motif); recruits GOSR2 and STX5 into COPII-coated vesicles
(PubMed:18843296). Interacts with DDHD1 (PubMed:17428803). Interacts
with STING1; promoting STING1 translocation to the COPII vesicles
(PubMed:30842662). {ECO:0000269|PubMed:10075675,
ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:17428803,
ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296,
ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:30842662}.
-!- INTERACTION:
P53992; P00540: MOS; NbExp=4; IntAct=EBI-81134, EBI-1757866;
P53992; Q15436: SEC23A; NbExp=5; IntAct=EBI-81134, EBI-81088;
P53992; O43516: WIPF1; NbExp=3; IntAct=EBI-81134, EBI-346356;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
membrane {ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:10329445};
Peripheral membrane protein {ECO:0000269|PubMed:10075675}; Cytoplasmic
side {ECO:0000269|PubMed:10075675}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:10329445}; 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=2;
Name=1;
IsoId=P53992-1; Sequence=Displayed;
Name=2;
IsoId=P53992-2; Sequence=VSP_056516;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10329445}.
-!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA07558.2; Type=Frameshift; Evidence={ECO:0000305};
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EMBL; D38555; BAA07558.2; ALT_SEQ; mRNA.
EMBL; AK303085; BAG64196.1; -; mRNA.
EMBL; AC022400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC018928; AAH18928.1; -; mRNA.
CCDS; CCDS7332.1; -. [P53992-1]
RefSeq; NP_004913.2; NM_004922.3. [P53992-1]
RefSeq; NP_940999.1; NM_198597.2. [P53992-1]
PDB; 3EH2; X-ray; 2.35 A; A/B/C=329-1094.
PDB; 6PU1; X-ray; 2.28 A; B=228-242.
PDBsum; 3EH2; -.
PDBsum; 6PU1; -.
SMR; P53992; -.
BioGRID; 114991; 156.
DIP; DIP-30981N; -.
IntAct; P53992; 42.
MINT; P53992; -.
STRING; 9606.ENSP00000343405; -.
iPTMnet; P53992; -.
MetOSite; P53992; -.
PhosphoSitePlus; P53992; -.
SwissPalm; P53992; -.
BioMuta; SEC24C; -.
DMDM; 257051070; -.
EPD; P53992; -.
jPOST; P53992; -.
MassIVE; P53992; -.
MaxQB; P53992; -.
PaxDb; P53992; -.
PeptideAtlas; P53992; -.
PRIDE; P53992; -.
ProteomicsDB; 5623; -.
ProteomicsDB; 56640; -. [P53992-1]
Antibodypedia; 45407; 155 antibodies.
DNASU; 9632; -.
Ensembl; ENST00000339365; ENSP00000343405; ENSG00000176986. [P53992-1]
Ensembl; ENST00000345254; ENSP00000321845; ENSG00000176986. [P53992-1]
GeneID; 9632; -.
KEGG; hsa:9632; -.
UCSC; uc001juw.4; human. [P53992-1]
CTD; 9632; -.
DisGeNET; 9632; -.
GeneCards; SEC24C; -.
HGNC; HGNC:10705; SEC24C.
HPA; ENSG00000176986; Low tissue specificity.
MalaCards; SEC24C; -.
MIM; 607185; gene.
neXtProt; NX_P53992; -.
OpenTargets; ENSG00000176986; -.
Orphanet; 567; 22q11.2 deletion syndrome.
PharmGKB; PA35628; -.
VEuPathDB; HostDB:ENSG00000176986.15; -.
eggNOG; KOG1984; Eukaryota.
GeneTree; ENSGT01020000231018; -.
HOGENOM; CLU_004589_1_1_1; -.
InParanoid; P53992; -.
OMA; DTPPEYF; -.
OrthoDB; 118368at2759; -.
PhylomeDB; P53992; -.
TreeFam; TF300464; -.
PathwayCommons; P53992; -.
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; 9632; 13 hits in 999 CRISPR screens.
ChiTaRS; SEC24C; human.
EvolutionaryTrace; P53992; -.
GeneWiki; SEC24C; -.
GenomeRNAi; 9632; -.
Pharos; P53992; Tbio.
PRO; PR:P53992; -.
Proteomes; UP000005640; Chromosome 10.
RNAct; P53992; protein.
Bgee; ENSG00000176986; Expressed in lower esophagus mucosa and 244 other tissues.
ExpressionAtlas; P53992; baseline and differential.
Genevisible; P53992; 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; 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: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.
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; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
Endoplasmic reticulum; ER-Golgi transport; Membrane; Metal-binding;
Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc.
CHAIN 1..1094
/note="Protein transport protein Sec24C"
/id="PRO_0000205156"
REPEAT 962..1034
/note="Gelsolin-like"
/evidence="ECO:0000255"
REGION 425..450
/note="Zinc finger-like"
METAL 425
/note="Zinc"
/evidence="ECO:0007744|PDB:3EH2"
METAL 428
/note="Zinc"
/evidence="ECO:0007744|PDB:3EH2"
METAL 447
/note="Zinc"
/evidence="ECO:0007744|PDB:3EH2"
METAL 450
/note="Zinc"
/evidence="ECO:0007744|PDB:3EH2"
MOD_RES 214
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18669648"
VAR_SEQ 1..752
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_056516"
VARIANT 109
/note="P -> S (in dbSNP:rs17851695)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_058690"
VARIANT 934
/note="L -> P (in dbSNP:rs16930872)"
/id="VAR_057174"
MUTAGEN 895..897
/note="LIL->AAA: Loss of packaging into COPII-coated
vesicles of the IxM motif-containing cargos GOSR2 and
STX5."
/evidence="ECO:0000269|PubMed:18843296"
HELIX 331..340
/evidence="ECO:0007744|PDB:3EH2"
STRAND 343..346
/evidence="ECO:0007744|PDB:3EH2"
STRAND 362..364
/evidence="ECO:0007744|PDB:3EH2"
STRAND 366..368
/evidence="ECO:0007744|PDB:3EH2"
TURN 371..373
/evidence="ECO:0007744|PDB:3EH2"
STRAND 374..384
/evidence="ECO:0007744|PDB:3EH2"
HELIX 385..391
/evidence="ECO:0007744|PDB:3EH2"
STRAND 395..399
/evidence="ECO:0007744|PDB:3EH2"
STRAND 413..415
/evidence="ECO:0007744|PDB:3EH2"
HELIX 418..420
/evidence="ECO:0007744|PDB:3EH2"
TURN 426..428
/evidence="ECO:0007744|PDB:3EH2"
STRAND 437..439
/evidence="ECO:0007744|PDB:3EH2"
HELIX 440..442
/evidence="ECO:0007744|PDB:3EH2"
STRAND 444..446
/evidence="ECO:0007744|PDB:3EH2"
TURN 448..450
/evidence="ECO:0007744|PDB:3EH2"
STRAND 453..455
/evidence="ECO:0007744|PDB:3EH2"
TURN 458..461
/evidence="ECO:0007744|PDB:3EH2"
HELIX 462..466
/evidence="ECO:0007744|PDB:3EH2"
STRAND 467..469
/evidence="ECO:0007744|PDB:3EH2"
HELIX 477..480
/evidence="ECO:0007744|PDB:3EH2"
STRAND 482..487
/evidence="ECO:0007744|PDB:3EH2"
HELIX 490..492
/evidence="ECO:0007744|PDB:3EH2"
HELIX 494..496
/evidence="ECO:0007744|PDB:3EH2"
STRAND 503..509
/evidence="ECO:0007744|PDB:3EH2"
HELIX 512..516
/evidence="ECO:0007744|PDB:3EH2"
HELIX 519..530
/evidence="ECO:0007744|PDB:3EH2"
HELIX 531..533
/evidence="ECO:0007744|PDB:3EH2"
STRAND 546..560
/evidence="ECO:0007744|PDB:3EH2"
STRAND 569..573
/evidence="ECO:0007744|PDB:3EH2"
TURN 576..578
/evidence="ECO:0007744|PDB:3EH2"
STRAND 587..589
/evidence="ECO:0007744|PDB:3EH2"
TURN 591..594
/evidence="ECO:0007744|PDB:3EH2"
HELIX 595..609
/evidence="ECO:0007744|PDB:3EH2"
HELIX 620..632
/evidence="ECO:0007744|PDB:3EH2"
STRAND 637..643
/evidence="ECO:0007744|PDB:3EH2"
STRAND 649..651
/evidence="ECO:0007744|PDB:3EH2"
HELIX 661..663
/evidence="ECO:0007744|PDB:3EH2"
HELIX 669..672
/evidence="ECO:0007744|PDB:3EH2"
HELIX 679..689
/evidence="ECO:0007744|PDB:3EH2"
STRAND 692..698
/evidence="ECO:0007744|PDB:3EH2"
HELIX 706..709
/evidence="ECO:0007744|PDB:3EH2"
HELIX 711..715
/evidence="ECO:0007744|PDB:3EH2"
STRAND 720..722
/evidence="ECO:0007744|PDB:3EH2"
HELIX 728..744
/evidence="ECO:0007744|PDB:3EH2"
STRAND 747..757
/evidence="ECO:0007744|PDB:3EH2"
STRAND 761..769
/evidence="ECO:0007744|PDB:3EH2"
STRAND 773..776
/evidence="ECO:0007744|PDB:3EH2"
STRAND 778..784
/evidence="ECO:0007744|PDB:3EH2"
STRAND 789..797
/evidence="ECO:0007744|PDB:3EH2"
TURN 801..803
/evidence="ECO:0007744|PDB:3EH2"
STRAND 805..814
/evidence="ECO:0007744|PDB:3EH2"
STRAND 820..834
/evidence="ECO:0007744|PDB:3EH2"
HELIX 835..840
/evidence="ECO:0007744|PDB:3EH2"
HELIX 844..858
/evidence="ECO:0007744|PDB:3EH2"
TURN 859..861
/evidence="ECO:0007744|PDB:3EH2"
HELIX 864..885
/evidence="ECO:0007744|PDB:3EH2"
HELIX 899..901
/evidence="ECO:0007744|PDB:3EH2"
HELIX 904..912
/evidence="ECO:0007744|PDB:3EH2"
TURN 915..917
/evidence="ECO:0007744|PDB:3EH2"
HELIX 925..937
/evidence="ECO:0007744|PDB:3EH2"
HELIX 940..947
/evidence="ECO:0007744|PDB:3EH2"
STRAND 950..953
/evidence="ECO:0007744|PDB:3EH2"
HELIX 972..974
/evidence="ECO:0007744|PDB:3EH2"
STRAND 980..984
/evidence="ECO:0007744|PDB:3EH2"
STRAND 986..993
/evidence="ECO:0007744|PDB:3EH2"
HELIX 999..1006
/evidence="ECO:0007744|PDB:3EH2"
HELIX 1011..1013
/evidence="ECO:0007744|PDB:3EH2"
HELIX 1027..1040
/evidence="ECO:0007744|PDB:3EH2"
STRAND 1043..1045
/evidence="ECO:0007744|PDB:3EH2"
STRAND 1048..1056
/evidence="ECO:0007744|PDB:3EH2"
HELIX 1059..1063
/evidence="ECO:0007744|PDB:3EH2"
TURN 1072..1074
/evidence="ECO:0007744|PDB:3EH2"
HELIX 1078..1092
/evidence="ECO:0007744|PDB:3EH2"
SEQUENCE 1094 AA; 118325 MW; 5E308E4B8E596ECE CRC64;
MNVNQSVPPV PPFGQPQPIY PGYHQSSYGG QSGSTAPAIP YGAYNGPVPG YQQTPPQGMS
RAPPSSGAPP ASTAQAPCGQ AAYGQFGQGD VQNGPSSTVQ MQRLPGSQPF GSPLAPVGNQ
PPVLQPYGPP PTSAQVATQL SGMQISGAVA PAPPSSGLGF GPPTSLASAS GSFPNSGLYG
SYPQGQAPPL SQAQGHPGIQ TPQRSAPSQA SSFTPPASGG PRLPSMTGPL LPGQSFGGPS
VSQPNHVSSP PQALPPGTQM TGPLGPLPPM HSPQQPGYQP QQNGSFGPAR GPQSNYGGPY
PAAPTFGSQP GPPQPLPPKR LDPDAIPSPI QVIEDDRNNR GTEPFVTGVR GQVPPLVTTN
FLVKDQGNAS PRYIRCTSYN IPCTSDMAKQ AQVPLAAVIK PLARLPPEEA SPYVVDHGES
GPLRCNRCKA YMCPFMQFIE GGRRFQCCFC SCINDVPPQY FQHLDHTGKR VDAYDRPELS
LGSYEFLATV DYCKNNKFPS PPAFIFMIDV SYNAIRTGLV RLLCEELKSL LDFLPREGGA
EESAIRVGFV TYNKVLHFYN VKSSLAQPQM MVVSDVADMF VPLLDGFLVN VNESRAVITS
LLDQIPEMFA DTRETETVFV PVIQAGMEAL KAAECAGKLF LFHTSLPIAE APGKLKNRDD
RKLINTDKEK TLFQPQTGAY QTLAKECVAQ GCCVDLFLFP NQYVDVATLS VVPQLTGGSV
YKYASFQVEN DQERFLSDLR RDVQKVVGFD AVMRVRTSTG IRAVDFFGAF YMSNTTDVEL
AGLDGDKTVT VEFKHDDRLN EESGALLQCA LLYTSCAGQR RLRIHNLALN CCTQLADLYR
NCETDTLINY MAKFAYRGVL NSPVKAVRDT LITQCAQILA CYRKNCASPS SAGQLILPEC
MKLLPVYLNC VLKSDVLQPG AEVTTDDRAY VRQLVTSMDV TETNVFFYPR LLPLTKSPVE
STTEPPAVRA SEERLSNGDI YLLENGLNLF LWVGASVQQG VVQSLFSVSS FSQITSGLSV
LPVLDNPLSK KVRGLIDSLR AQRSRYMKLT VVKQEDKMEM LFKHFLVEDK SLSGGASYVD
FLCHMHKEIR QLLS


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EIAAB46508 Membrane transport protein XK,Rat,Rattus norvegicus,Xk,XK homolog,Xkh,Xkr1,XK-related protein 1,Xrg1
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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
WP731: Sterol regulatory element binding protein related
WP2199: Seed Development
WP1624: Bacterial secretion system
WP1909: Signal regulatory protein (SIRP) family interactions
WP1685: Peptidoglycan biosynthesis
WP1692: Protein export
WP2324: AGE/RAGE pathway
WP1650: Fluorobenzoate degradation
WP346: Protein Modifications
WP1659: Glycine, serine and threonine metabolism
WP1939: Unfolded Protein Response
WP1371: G Protein Signaling Pathways
WP1700: Selenoamino acid metabolism
WP1665: Limonene and pinene degradation
WP2032: TSH signaling pathway
WP1675: Nitrogen metabolism
WP211: BMP signaling pathway
WP73: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP2218: sGC

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)
[MIA3 KIAA0268 TANGO UNQ6077/PRO20088] Transport and Golgi organization protein 1 homolog (TANGO1) (C219-reactive peptide) (D320) (Melanoma inhibitory activity protein 3)
[Mia3 Kiaa0268 Tango] Transport and Golgi organization protein 1 homolog (TANGO1) (Melanoma inhibitory activity protein 3)
[SEC24A] Protein transport protein Sec24A (SEC24-related protein A)
[Tmed10 Tmp21] Transmembrane emp24 domain-containing protein 10 (Protein Tmed10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[Slc6a4 Htt Sert] Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)
[MIA2 CTAGE5 MEA11 MEA6 MGEA11 MGEA6] Melanoma inhibitory activity protein 2 (MIA protein 2) (CTAGE family member 5 ER export factor) (Cutaneous T-cell lymphoma-associated antigen 5) (Meningioma-expressed antigen 6/11)
[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) (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)
[Sting1 Eris Mita Mpys Tmem173] Stimulator of interferon genes protein (mSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (MMITA) (Transmembrane protein 173)
[STING1 ERIS MITA TMEM173] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[SLC6A4 HTT SERT] Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)
[SEC23B] Protein transport protein Sec23B (hSec23B) (SEC23-related protein B)
[DDHD1 KIAA1705] Phospholipase DDHD1 (EC 3.1.1.-) (DDHD domain-containing protein 1) (Phosphatidic acid-preferring phospholipase A1 homolog) (PA-PLA1)
[Stx5 Stx5a] Syntaxin-5
[BET1 SLY12 YIL004C YIA4C] Protein transport protein BET1 (Suppressor of loss of YPT1 protein 12) (Protein SLY12)
[Sting1 Tmem173] Stimulator of interferon genes protein (rSTING) (Transmembrane protein 173)
[STING1 TMEM173] Stimulator of interferon genes protein (STING) (Transmembrane protein 173)
[STING1 TMEM173] Stimulator of interferon genes protein (poSTING) (Transmembrane protein 173)
[WIPF1 WASPIP WIP] WAS/WASL-interacting protein family member 1 (Protein PRPL-2) (Wiskott-Aldrich syndrome protein-interacting protein) (WASP-interacting protein)

Bibliography :
No related Items