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1.A.156.1.1
Sec61β (Sec61B) of 95 aas with one C-terminal TMS. Platelet hyperreactivity increases the risk of cardiovascular thrombosis in diabetes and failure of antiplatelet drug therapies. Elevated basal and agonist-induced calcium flux is a fundamental cause of platelet hyperreactivity in diabetes. Using a high-sensitivity, unbiased proteomic platform, Kong et al. 2025 consistently detected over 2,400 intracellular proteins and identified proteins that were differentially released by platelets in type 2 diabetes. They found that SEC61 translocon subunit β (SEC61B) was increased in platelets from humans and mice with hyperglycemia and in megakaryocytes from mice with hyperglycemia. SEC61 is known to act as an endoplasmic reticulum (ER) calcium leak channel in nucleated cells (Kong et al. 2025). Using HEK293 cells, SEC61B overexpression increased calcium flux into the cytosol and decreased protein synthesis. Concordantly, platelets in hyperglycemic mice mobilized more calcium and had decreased protein synthesis. Platelets in both humans and mice with hyperglycemia had increased ER stress. ER stress induced the expression of platelet SEC61B and increased cytosolic calcium. Inhibition of SEC61 with anisomycin decreased platelet calcium flux and inhibited platelet aggregation in vitro and in vivo (Kong et al. 2025).

Accession Number:P60468
Protein Name:SEC61 beta subunit
Length:96
Molecular Weight:9974.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Endoplasmic reticulum membrane1 / Single-pass membrane protein2
Substrate calcium(2+)

Cross database links:

RefSeq: NP_006799.1   
Entrez Gene ID: 10952   
Pfam: PF03911   
OMIM: 609214  gene
KEGG: hsa:10952   

Gene Ontology

GO:0031205 C:endoplasmic reticulum Sec complex
GO:0016021 C:integral to membrane
GO:0048408 F:epidermal growth factor binding
GO:0030433 P:ER-associated protein catabolic process
GO:0000060 P:protein import into nucleus, translocation
GO:0030970 P:retrograde protein transport, ER to cytosol
GO:0055085 P:transmembrane transport

References (11)

[1] “Evolutionary conservation of components of the protein translocation complex.”  Hartmann E.et.al.   8107851
[2] “DNA sequence and analysis of human chromosome 9.”  Humphray S.J.et.al.   15164053
[3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[4] “Mammalian Sec61 is associated with Sec62 and Sec63.”  Meyer H.-A.et.al.   10799540
[5] “Global phosphoproteome of HT-29 human colon adenocarcinoma cells.”  Kim J.-E.et.al.   16083285
[6] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[7] “Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.”  Yu L.-R.et.al.   17924679
[8] “Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.”  Molina H.et.al.   17287340
[9] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[10] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[11] “Large-scale proteomics analysis of the human kinome.”  Oppermann F.S.et.al.   19369195
Structure:
4cg5   6W6L     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA GTGGMWRFYT 
61:	EDSPGLKVGP VPVLVMSLLF IASVFMLHIW GKYTRS