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Protein

Thrombomodulin

Gene

THBD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • calcium ion binding Source: ProtInc
  • signaling receptor activity Source: ProtInc
  • transmembrane signaling receptor activity Source: InterPro

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionReceptor
Biological processBlood coagulation, Hemostasis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-202733 Cell surface interactions at the vascular wall

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P07204

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Thrombomodulin
Short name:
TM
Alternative name(s):
Fetomodulin
CD_antigen: CD141
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:THBD
Synonyms:THRM
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000178726.6

Human Gene Nomenclature Database

More...
HGNCi
HGNC:11784 THBD

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
188040 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P07204

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini19 – 515ExtracellularSequence analysisAdd BLAST497
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei516 – 539HelicalSequence analysisAdd BLAST24
Topological domaini540 – 575CytoplasmicSequence analysisAdd BLAST36

Keywords - Cellular componenti

Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Thrombophilia due to thrombomodulin defect (THPH12)3 Publications
The disease may be caused by mutations 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 descriptionA hemostatic disorder characterized by a tendency to thrombosis.
See also OMIM:614486
Hemolytic uremic syndrome atypical 6 (AHUS6)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
Disease descriptionAn 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.
See also OMIM:612926
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06367334D → E in AHUS6. 1 Publication1
Natural variantiVAR_01136843A → T in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 3 PublicationsCorresponds to variant dbSNP:rs1800576EnsemblClinVar.1
Natural variantiVAR_06322353D → G in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 PublicationCorresponds to variant dbSNP:rs121918667EnsemblClinVar.1
Natural variantiVAR_06322481V → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 Publication1
Natural variantiVAR_063674236A → G in AHUS6. 1 PublicationCorresponds to variant dbSNP:rs758686992Ensembl.1
Natural variantiVAR_011372495P → S in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 PublicationsCorresponds to variant dbSNP:rs1800578EnsemblClinVar.1
Natural variantiVAR_011373501P → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 PublicationsCorresponds to variant dbSNP:rs1800579EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Hemolytic uremic syndrome, Thrombophilia

Organism-specific databases

DisGeNET

More...
DisGeNETi
7056

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
THBD

MalaCards human disease database

More...
MalaCardsi
THBD
MIMi612926 phenotype
614486 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000178726

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
217023 Atypical hemolytic-uremic syndrome with thrombomodulin anomaly
436169 Thrombomodulin-related bleeding disorder

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36496

Chemistry databases

Drug and drug target database

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DrugBanki
DB00055 Drotrecogin alfa
DB01050 Ibuprofen

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
THBD

Domain mapping of disease mutations (DMDM)

More...
DMDMi
136170

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 181 PublicationAdd BLAST18
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000777119 – 575ThrombomodulinAdd BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi47N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi115N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi116N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi137 ↔ 158By similarity
Disulfide bondi245 ↔ 256By similarity
Disulfide bondi252 ↔ 265By similarity
Disulfide bondi267 ↔ 280By similarity
Disulfide bondi288 ↔ 296By similarity
Disulfide bondi292 ↔ 308By similarity
Disulfide bondi310 ↔ 323By similarity
Disulfide bondi329 ↔ 340By similarity
Disulfide bondi336 ↔ 349By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei342(3R)-3-hydroxyasparagine1 Publication1
Disulfide bondi351 ↔ 362By similarity
Disulfide bondi369 ↔ 378Combined sources
Disulfide bondi374 ↔ 388Combined sources
Glycosylationi382N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi390 ↔ 404Combined sources
Disulfide bondi408 ↔ 413Combined sources
Glycosylationi409N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi417 ↔ 425Combined sources
Disulfide bondi427 ↔ 439Combined sources
Disulfide bondi445 ↔ 455Combined sources
Disulfide bondi451 ↔ 464Combined sources
Disulfide bondi466 ↔ 480Combined sources
Glycosylationi490O-linked (Xyl...) (chondroitin sulfate) serine1
Glycosylationi492O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.1 Publication
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Proteoglycan

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P07204

MaxQB - The MaxQuant DataBase

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MaxQBi
P07204

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P07204

PeptideAtlas

More...
PeptideAtlasi
P07204

PRoteomics IDEntifications database

More...
PRIDEi
P07204

ProteomicsDB human proteome resource

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ProteomicsDBi
51973

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
591

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07204

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P07204

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P07204

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P07204

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Endothelial cells are unique in synthesizing thrombomodulin.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000178726 Expressed in 203 organ(s), highest expression level in left coronary artery

CleanEx database of gene expression profiles

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CleanExi
HS_THBD

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P07204 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB002425
HPA002982

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ITGAL, ITGAM and ITGB2.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
F2P007344EBI-941422,EBI-297094

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112914, 5 interactors

Protein interaction database and analysis system

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IntActi
P07204, 25 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000366307

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P07204

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P07204

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07204

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini31 – 169C-type lectinPROSITE-ProRule annotationAdd BLAST139
Domaini241 – 281EGF-like 1PROSITE-ProRule annotationAdd BLAST41
Domaini284 – 324EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini325 – 363EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini365 – 405EGF-like 4PROSITE-ProRule annotationAdd BLAST41
Domaini404 – 440EGF-like 5PROSITE-ProRule annotationAdd BLAST37
Domaini441 – 481EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni481 – 515Involved in alpha-L/beta-2 and alpha-M/beta-2 integrin binding1 PublicationAdd BLAST35

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Extracellular region (481-515) contains a binding side for alpha-L/beta-2 and alpha-M/beta-2 integrin.1 Publication

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IF0T Eukaryota
ENOG410Y5JS LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000163276

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000114624

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000291

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07204

KEGG Orthology (KO)

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KOi
K03907

Identification of Orthologs from Complete Genome Data

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OMAi
LCGPLCV

Database of Orthologous Groups

More...
OrthoDBi
EOG091G06M1

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07204

TreeFam database of animal gene trees

More...
TreeFami
TF330714

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR016316 CD141
IPR026823 cEGF
IPR016187 CTDL_fold
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR009030 Growth_fac_rcpt_cys_sf
IPR015149 Tme5_EGF-like

The PANTHER Classification System

More...
PANTHERi
PTHR24036:SF5 PTHR24036:SF5, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12662 cEGF, 1 hit
PF07645 EGF_CA, 1 hit
PF00059 Lectin_C, 1 hit
PF09064 Tme5_EGF_like, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00034 CLECT, 1 hit
SM00181 EGF, 6 hits
SM00179 EGF_CA, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56436 SSF56436, 1 hit
SSF57184 SSF57184, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00010 ASX_HYDROXYL, 2 hits
PS50041 C_TYPE_LECTIN_2, 1 hit
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 4 hits
PS01187 EGF_CA, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P07204-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLGVLVLGAL ALAGLGFPAP AEPQPGGSQC VEHDCFALYP GPATFLNASQ
60 70 80 90 100
ICDGLRGHLM TVRSSVAADV ISLLLNGDGG VGRRRLWIGL QLPPGCGDPK
110 120 130 140 150
RLGPLRGFQW VTGDNNTSYS RWARLDLNGA PLCGPLCVAV SAAEATVPSE
160 170 180 190 200
PIWEEQQCEV KADGFLCEFH FPATCRPLAV EPGAAAAAVS ITYGTPFAAR
210 220 230 240 250
GADFQALPVG SSAAVAPLGL QLMCTAPPGA VQGHWAREAP GAWDCSVENG
260 270 280 290 300
GCEHACNAIP GAPRCQCPAG AALQADGRSC TASATQSCND LCEHFCVPNP
310 320 330 340 350
DQPGSYSCMC ETGYRLAADQ HRCEDVDDCI LEPSPCPQRC VNTQGGFECH
360 370 380 390 400
CYPNYDLVDG ECVEPVDPCF RANCEYQCQP LNQTSYLCVC AEGFAPIPHE
410 420 430 440 450
PHRCQMFCNQ TACPADCDPN TQASCECPEG YILDDGFICT DIDECENGGF
460 470 480 490 500
CSGVCHNLPG TFECICGPDS ALARHIGTDC DSGKVDGGDS GSGEPPPSPT
510 520 530 540 550
PGSTLTPPAV GLVHSGLLIG ISIASLCLVV ALLALLCHLR KKQGAARAKM
560 570
EYKCAAPSKE VVLQHVRTER TPQRL
Length:575
Mass (Da):60,329
Last modified:February 1, 1991 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9AF03CD151227D52
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06367334D → E in AHUS6. 1 Publication1
Natural variantiVAR_01136843A → T in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 3 PublicationsCorresponds to variant dbSNP:rs1800576EnsemblClinVar.1
Natural variantiVAR_06322353D → G in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 PublicationCorresponds to variant dbSNP:rs121918667EnsemblClinVar.1
Natural variantiVAR_01136979G → A1 PublicationCorresponds to variant dbSNP:rs1800577Ensembl.1
Natural variantiVAR_06322481V → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 Publication1
Natural variantiVAR_049011162A → P. Corresponds to variant dbSNP:rs36110902Ensembl.1
Natural variantiVAR_063674236A → G in AHUS6. 1 PublicationCorresponds to variant dbSNP:rs758686992Ensembl.1
Natural variantiVAR_011370473A → V6 PublicationsCorresponds to variant dbSNP:rs1042579EnsemblClinVar.1
Natural variantiVAR_011371486D → Y in THPH12 and AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 4 PublicationsCorresponds to variant dbSNP:rs41348347EnsemblClinVar.1
Natural variantiVAR_011372495P → S in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 PublicationsCorresponds to variant dbSNP:rs1800578EnsemblClinVar.1
Natural variantiVAR_011373501P → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 PublicationsCorresponds to variant dbSNP:rs1800579EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X05495 mRNA Translation: CAA29045.1
M16552 mRNA Translation: AAB59508.1
J02973 Genomic DNA Translation: AAA61175.1
D00210 Genomic DNA Translation: BAA00149.1
AF495471 Genomic DNA Translation: AAM03232.1
AL049651 Genomic DNA No translation available.
BC035602 mRNA Translation: AAH35602.2
BC053357 mRNA Translation: AAH53357.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS13148.1

Protein sequence database of the Protein Information Resource

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PIRi
A41442 THHUB

NCBI Reference Sequences

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RefSeqi
NP_000352.1, NM_000361.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.2030

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000377103; ENSP00000366307; ENSG00000178726

Database of genes from NCBI RefSeq genomes

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GeneIDi
7056

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:7056

UCSC genome browser

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UCSCi
uc002wss.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Thrombomodulin entry

SeattleSNPs
Functional Glycomics Gateway - Glycan Binding

Thrombomodulin

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05495 mRNA Translation: CAA29045.1
M16552 mRNA Translation: AAB59508.1
J02973 Genomic DNA Translation: AAA61175.1
D00210 Genomic DNA Translation: BAA00149.1
AF495471 Genomic DNA Translation: AAM03232.1
AL049651 Genomic DNA No translation available.
BC035602 mRNA Translation: AAH35602.2
BC053357 mRNA Translation: AAH53357.1
CCDSiCCDS13148.1
PIRiA41442 THHUB
RefSeqiNP_000352.1, NM_000361.2
UniGeneiHs.2030

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ADXNMR-A405-444[»]
1DQBNMR-A364-444[»]
1DX5X-ray2.30I/J/K/L363-480[»]
1EGTNMR-A427-444[»]
1FGDNMR-A427-444[»]
1FGENMR-A425-444[»]
1HLTX-ray3.00R426-444[»]
1TMRNMR-A389-405[»]
1ZAQNMR-A364-407[»]
2ADXNMR-A405-444[»]
3GISX-ray2.40X/Y/Z363-483[»]
5TO3X-ray2.34B363-483[»]
ProteinModelPortaliP07204
SMRiP07204
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112914, 5 interactors
IntActiP07204, 25 interactors
STRINGi9606.ENSP00000366307

Chemistry databases

DrugBankiDB00055 Drotrecogin alfa
DB01050 Ibuprofen

PTM databases

GlyConnecti591
iPTMnetiP07204
PhosphoSitePlusiP07204
SwissPalmiP07204
UniCarbKBiP07204

Polymorphism and mutation databases

BioMutaiTHBD
DMDMi136170

Proteomic databases

EPDiP07204
MaxQBiP07204
PaxDbiP07204
PeptideAtlasiP07204
PRIDEiP07204
ProteomicsDBi51973

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
7056
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377103; ENSP00000366307; ENSG00000178726
GeneIDi7056
KEGGihsa:7056
UCSCiuc002wss.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7056
DisGeNETi7056
EuPathDBiHostDB:ENSG00000178726.6

GeneCards: human genes, protein and diseases

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GeneCardsi
THBD
GeneReviewsiTHBD

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0174703
HGNCiHGNC:11784 THBD
HPAiCAB002425
HPA002982
MalaCardsiTHBD
MIMi188040 gene
612926 phenotype
614486 phenotype
neXtProtiNX_P07204
OpenTargetsiENSG00000178726
Orphaneti217023 Atypical hemolytic-uremic syndrome with thrombomodulin anomaly
436169 Thrombomodulin-related bleeding disorder
PharmGKBiPA36496

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IF0T Eukaryota
ENOG410Y5JS LUCA
GeneTreeiENSGT00940000163276
HOGENOMiHOG000114624
HOVERGENiHBG000291
InParanoidiP07204
KOiK03907
OMAiLCGPLCV
OrthoDBiEOG091G06M1
PhylomeDBiP07204
TreeFamiTF330714

Enzyme and pathway databases

ReactomeiR-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-202733 Cell surface interactions at the vascular wall
SIGNORiP07204

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
THBD human
EvolutionaryTraceiP07204

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Thrombomodulin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
7056

Protein Ontology

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PROi
PR:P07204

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000178726 Expressed in 203 organ(s), highest expression level in left coronary artery
CleanExiHS_THBD
GenevisibleiP07204 HS

Family and domain databases

Gene3Di3.10.100.10, 1 hit
InterProiView protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR016316 CD141
IPR026823 cEGF
IPR016187 CTDL_fold
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR009030 Growth_fac_rcpt_cys_sf
IPR015149 Tme5_EGF-like
PANTHERiPTHR24036:SF5 PTHR24036:SF5, 1 hit
PfamiView protein in Pfam
PF12662 cEGF, 1 hit
PF07645 EGF_CA, 1 hit
PF00059 Lectin_C, 1 hit
PF09064 Tme5_EGF_like, 1 hit
SMARTiView protein in SMART
SM00034 CLECT, 1 hit
SM00181 EGF, 6 hits
SM00179 EGF_CA, 4 hits
SUPFAMiSSF56436 SSF56436, 1 hit
SSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 2 hits
PS50041 C_TYPE_LECTIN_2, 1 hit
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 4 hits
PS01187 EGF_CA, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTRBM_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07204
Secondary accession number(s): Q8IV29, Q9UC32
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1991
Last modified: December 5, 2018
This is version 226 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  3. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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