TRBM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRBM_HUMAN
• UniProt AC: P07204
• Protein Name: Thrombomodulin
• Gene Name: THBD
• Organism: Homo sapiens (Human).
• Sequence Length: 575
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated..
• Protein Sequence: MLGVLVLGALALAGLGFPAPAEPQPGGSQCVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGDGGVGRRRLWIGLQLPPGCGDPKRLGPLRGFQWVTGDNNTSYSRWARLDLNGAPLCGPLCVAVSAAEATVPSEPIWEEQQCEVKADGFLCEFHFPATCRPLAVEPGAAAAAVSITYGTPFAARGADFQALPVGSSAAVAPLGLQLMCTAPPGAVQGHWAREAPGAWDCSVENGGCEHACNAIPGAPRCQCPAGAALQADGRSCTASATQSCNDLCEHFCVPNPDQPGSYSCMCETGYRLAADQHRCEDVDDCILEPSPCPQRCVNTQGGFECHCYPNYDLVDGECVEPVDPCFRANCEYQCQPLNQTSYLCVCAEGFAPIPHEPHRCQMFCNQTACPADCDPNTQASCECPEGYILDDGFICTDIDECENGGFCSGVCHNLPGTFECICGPDSALARHIGTDCDSGKVDGGDSGSGEPPPSPTPGSTLTPPAVGLVHSGLLIGISIASLCLVVALLALLCHLRKKQGAARAKMEYKCAAPSKEVVLQHVRTERTPQRL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	N-linked_Glycosylation	PGPATFLNASQICDG CCCCCCCCHHHHCCC	33.10	UniProtKB CARBOHYD
115	N-linked_Glycosylation	FQWVTGDNNTSYSRW EEEECCCCCCCEEEE	55.83	UniProtKB CARBOHYD
116	N-linked_Glycosylation	QWVTGDNNTSYSRWA EEECCCCCCCEEEEE	34.83	UniProtKB CARBOHYD
212	Phosphorylation	QALPVGSSAAVAPLG EEECCCCCEECCCCC	17.83	24719451
291	Sulfoxidation	ATQSCNDLCEHFCVP HHHCHHHHHHHCCCC	1.99	1334978
342	Hydroxylation	PCPQRCVNTQGGFEC CCCCCCEECCCCEEE	30.25	8390446
382	N-linked_Glycosylation	EYQCQPLNQTSYLCV EEECCCCCCCEEEEE	50.17	UniProtKB CARBOHYD
388	Sulfoxidation	LNQTSYLCVCAEGFA CCCCEEEEEEECCCC	1.47	1334978
409	N-linked_Glycosylation	HRCQMFCNQTACPAD CCCCEEECCCCCCCC	30.85	UniProtKB CARBOHYD
490	O-linked_Glycosylation	GKVDGGDSGSGEPPP CCCCCCCCCCCCCCC	37.83	-
492	O-linked_Glycosylation	VDGGDSGSGEPPPSP CCCCCCCCCCCCCCC	43.89	8216207
553	Ubiquitination	ARAKMEYKCAAPSKE HHHHCEEEECCCCHH	12.23	29901268
559	Ubiquitination	YKCAAPSKEVVLQHV EEECCCCHHHHHHHH	54.17	29967540
571	Phosphorylation	QHVRTERTPQRL--- HHHHCCCCCCCC---	19.96	27794612

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TRBM_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRBM_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TRBM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THRB_HUMAN	F2	physical	2544585

Drug and Disease Associations

• Kegg Disease
• H00080: Systemic lupus erythematosus
• H00223: Inherited thrombophilia
• OMIM Disease
• 614486: Thrombophilia due to thrombomodulin defect (THPH12)
• 612926: Hemolytic uremic syndrome atypical 6 (AHUS6)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Hydroxylation

"Urinary thrombomodulin, its isolation and characterization.";
Yamamoto S., Mizoguchi T., Tamaki T., Ohkuchi M., Kimura S., Aoki N.;
J. Biochem. 113:433-440(1993).
Cited for: HYDROXYLATION AT ASN-342.
PubMed: 8390446

O-linked Glycosylation

"Identification of the predominant glycosaminoglycan-attachment sitein soluble recombinant human thrombomodulin: potential regulation offunctionality by glycosyltransferase competition for serine 474.";
Gerlitz B., Hassell T., Vlahos C.J., Parkinson J.F., Bang N.U.,Grinnell B.W.;
Biochem. J. 295:131-140(1993).
Cited for: GLYCOSYLATION AT SER-492, AND MUTAGENESIS.
PubMed: 8216207