THBD
entrez
7056
canonical
uniprot
P07204
canonical
ensembl
ENSG00000178726
resolver
ensp
ENSP00000366307
resolver
enst
ENST00000377103
resolver
genesymbol
THBD
resolver
genesymbol_syn
THRM
resolver
hgnc
HGNC:11784
resolver
uniprot
Q8IV29
resolver
uniprot
Q9UC32
resolver
uniprot_entry
TRBM_HUMAN
resolver
uniprot_sec
Q8IV29
resolver
uniprot_sec
Q9UC32
resolver
amino_acid_sequence
MLGVLVLGALALAGLGFPAPAEPQPGGSQCVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGDGGVGRRRLWIGLQLPPGCGDPKRLGPLRGFQWVTGDNNTSYSRWARLDLNGAPLCGPLCVAVSAAEATVPSEPIWEEQQCEVKADGFLCEFHFPATCRPLAVEPGAAAAAVSITYGTPFAARGADFQALPVGSSAAVAPLGLQLMCTAPPGAVQGHWAREAPGAWDCSVENGGCEHACNAIPGAPRCQCPAGAALQADGRSCTASATQSCNDLCEHFCVPNPDQPGSYSCMCETGYRLAADQHRCEDVDDCILEPSPCPQRCVNTQGGFECHCYPNYDLVDGECVEPVDPCFRANCEYQCQPLNQTSYLCVCAEGFAPIPHEPHRCQMFCNQTACPADCDPNTQASCECPEGYILDDGFICTDIDECENGGFCSGVCHNLPGTFECICGPDSALARHIGTDCDSGKVDGGDSGSGEPPPSPTPGSTLTPPAVGLVHSGLLIGISIASLCLVVALLALLCHLRKKQGAARAKMEYKCAAPSKEVVLQHVRTERTPQRL
uniprot
proteins
disease_involvement
DISEASE: Thrombophilia due to thrombomodulin defect (THPH12) [MIM:614486]: A hemostatic disorder characterized by a tendency to thrombosis. {ECO:0000269|PubMed:12139752, ECO:0000269|PubMed:7811989, ECO:0000269|PubMed:9198186}. Note=The disease may be caused by variants affecting the gene represented in this entry. The role of thrombomodulin in thrombosis is controversial. It is likely that genetic or environmental risk factors in addition to THBD variation are involved in the pathogenesis of venous thrombosis.; DISEASE: Hemolytic uremic syndrome, atypical, 6 (AHUS6) [MIM:612926]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. {ECO:0000269|PubMed:19625716, ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
uniprot
proteins
function
FUNCTION: Endothelial cell receptor that plays a critical role in regulating several physiological processes including hemostasis, coagulation, fibrinolysis, inflammation, and angiogenesis (PubMed:10761923). Acts as a cofactor for thrombin activation of protein C/PROC on the surface of vascular endothelial cells leading to initiation of the activated protein C anticoagulant pathway (PubMed:29323190, PubMed:33836597, PubMed:9395524). Also accelerates the activation of the plasma carboxypeptidase B2/CPB2, which catalyzes removal of C-terminal basic amino acids from its substrates including kinins or anaphylatoxins leading to fibrinolysis inhibition (PubMed:26663133). Plays critical protective roles in changing the cleavage specificity of protease-activated receptor 1/PAR1, inhibiting endothelial cell permeability and inflammation (By similarity). Suppresses inflammation distinctly from its anticoagulant cofactor activity by sequestering HMGB1 thereby preventing it from engaging cellular receptors such as RAGE and contributing to the inflammatory response (PubMed:15841214). {ECO:0000250|UniProtKB:P15306, ECO:0000269|PubMed:10761923, ECO:0000269|PubMed:15841214, ECO:0000269|PubMed:26663133, ECO:0000269|PubMed:29323190, ECO:0000269|PubMed:33836597, ECO:0000269|PubMed:9395524}.
uniprot
proteins
mass_dalton
60329
uniprot
proteins
mutagenesis
MUTAGEN 490; /note="S->E: Improved overall glycosaminoglycan attachment, likely due to improved xylosyltransferase acceptor consensus sequence around Ser-492."; /evidence="ECO:0000269|PubMed:8216207"; MUTAGEN 492; /note="S->G: Reduced glycosaminoglycan attachment."; /evidence="ECO:0000269|PubMed:8216207
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:8216207}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:8390446}.
uniprot
proteins
pubmed
10761923
uniprot
proteins
pubmed
11245641
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12139752
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15841214
uniprot
proteins
pubmed
19625716
uniprot
proteins
pubmed
20513133
uniprot
proteins
pubmed
26663133
uniprot
proteins
pubmed
27055590
uniprot
proteins
pubmed
2819876
uniprot
proteins
pubmed
2820710
uniprot
proteins
pubmed
2822087
uniprot
proteins
pubmed
2836377
uniprot
proteins
pubmed
29323190
uniprot
proteins
pubmed
33836597
uniprot
proteins
pubmed
7559494
uniprot
proteins
pubmed
7811989
uniprot
proteins
pubmed
7947766
uniprot
proteins
pubmed
8216207
uniprot
proteins
pubmed
8390446
uniprot
proteins
pubmed
8528067
uniprot
proteins
pubmed
8745396
uniprot
proteins
pubmed
9157575
uniprot
proteins
pubmed
9198186
uniprot
proteins
pubmed
9367781
uniprot
proteins
pubmed
9395524
uniprot
proteins
pubmed
9843165
uniprot
proteins
sequence_length
575
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 516..539; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins