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P07204 (TRBM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 184. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thrombomodulin

Short name=TM
Alternative name(s):
Fetomodulin
CD_antigen=CD141
Gene names
Name:THBD
Synonyms:THRM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Endothelial cells are unique in synthesizing thrombomodulin.

Post-translational modification

N-glycosylated. Ref.8

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

Involvement in disease

Thrombophilia due to thrombomodulin defect (THPH12) [MIM:614486]: A hemostatic disorder characterized by a tendency to thrombosis.
Note: 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. Ref.15 Ref.16 Ref.20

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype. Ref.21 Ref.22

Sequence similarities

Contains 1 C-type lectin domain.

Contains 6 EGF-like domains.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Hemolytic uremic syndrome
Thrombophilia
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

embryo development

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement. Source: Reactome

negative regulation of blood coagulation

Traceable author statement PubMed 17379830. Source: BHF-UCL

negative regulation of fibrinolysis

Traceable author statement PubMed 17379830. Source: BHF-UCL

negative regulation of platelet activation

Traceable author statement PubMed 17379830. Source: BHF-UCL

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay PubMed 17379830. Source: BHF-UCL

extracellular space

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Traceable author statement PubMed 10336638. Source: ProtInc

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

receptor activity

Traceable author statement Ref.2. Source: ProtInc

transmembrane signaling receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

F2P007344EBI-941422,EBI-297094

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1
Chain19 – 575557Thrombomodulin
PRO_0000007771

Regions

Topological domain19 – 515497Extracellular Potential
Transmembrane516 – 53924Helical; Potential
Topological domain540 – 57536Cytoplasmic Potential
Domain31 – 169139C-type lectin
Domain241 – 28141EGF-like 1
Domain284 – 32441EGF-like 2
Domain325 – 36339EGF-like 3; calcium-binding Potential
Domain365 – 40541EGF-like 4
Domain404 – 44037EGF-like 5
Domain441 – 48141EGF-like 6; calcium-binding Potential

Amino acid modifications

Modified residue3421(3R)-3-hydroxyasparagine Ref.9
Glycosylation471N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4901O-linked (Xyl...) (chondroitin sulfate)
Glycosylation4921O-linked (Xyl...) (chondroitin sulfate) Ref.8
Disulfide bond137 ↔ 158 By similarity
Disulfide bond245 ↔ 256 By similarity
Disulfide bond252 ↔ 265 By similarity
Disulfide bond267 ↔ 280 By similarity
Disulfide bond288 ↔ 296 By similarity
Disulfide bond292 ↔ 308 By similarity
Disulfide bond310 ↔ 323 By similarity
Disulfide bond329 ↔ 340 By similarity
Disulfide bond336 ↔ 349 By similarity
Disulfide bond351 ↔ 362 By similarity
Disulfide bond369 ↔ 378 By similarity
Disulfide bond374 ↔ 388 By similarity
Disulfide bond390 ↔ 404
Disulfide bond408 ↔ 413
Disulfide bond417 ↔ 425
Disulfide bond427 ↔ 439
Disulfide bond445 ↔ 455 By similarity
Disulfide bond451 ↔ 464 By similarity
Disulfide bond466 ↔ 480 By similarity

Natural variations

Natural variant341D → E in AHUS6. Ref.22
VAR_063673
Natural variant431A → T in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. Ref.16 Ref.18 Ref.21
Corresponds to variant rs1800576 [ dbSNP | Ensembl ].
VAR_011368
Natural variant531D → G in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. Ref.21
VAR_063223
Natural variant791G → A. Ref.16
Corresponds to variant rs1800577 [ dbSNP | Ensembl ].
VAR_011369
Natural variant811V → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. Ref.21
VAR_063224
Natural variant1621A → P.
Corresponds to variant rs36110902 [ dbSNP | Ensembl ].
VAR_049011
Natural variant2361A → G in AHUS6. Ref.22
VAR_063674
Natural variant4731A → V. Ref.5 Ref.7 Ref.17 Ref.19 Ref.20 Ref.21
Corresponds to variant rs1042579 [ dbSNP | Ensembl ].
VAR_011370
Natural variant4861D → 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. Ref.15 Ref.16 Ref.20 Ref.21
Corresponds to variant rs41348347 [ dbSNP | Ensembl ].
VAR_011371
Natural variant4951P → S in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. Ref.16 Ref.21
Corresponds to variant rs1800578 [ dbSNP | Ensembl ].
VAR_011372
Natural variant5011P → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. Ref.16 Ref.21
Corresponds to variant rs1800579 [ dbSNP | Ensembl ].
VAR_011373

Secondary structure

................................... 575
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07204 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 9AF03CD151227D52

FASTA57560,329
        10         20         30         40         50         60 
MLGVLVLGAL ALAGLGFPAP AEPQPGGSQC VEHDCFALYP GPATFLNASQ ICDGLRGHLM 

        70         80         90        100        110        120 
TVRSSVAADV ISLLLNGDGG VGRRRLWIGL QLPPGCGDPK RLGPLRGFQW VTGDNNTSYS 

       130        140        150        160        170        180 
RWARLDLNGA PLCGPLCVAV SAAEATVPSE PIWEEQQCEV KADGFLCEFH FPATCRPLAV 

       190        200        210        220        230        240 
EPGAAAAAVS ITYGTPFAAR GADFQALPVG SSAAVAPLGL QLMCTAPPGA VQGHWAREAP 

       250        260        270        280        290        300 
GAWDCSVENG GCEHACNAIP GAPRCQCPAG AALQADGRSC TASATQSCND LCEHFCVPNP 

       310        320        330        340        350        360 
DQPGSYSCMC ETGYRLAADQ HRCEDVDDCI LEPSPCPQRC VNTQGGFECH CYPNYDLVDG 

       370        380        390        400        410        420 
ECVEPVDPCF RANCEYQCQP LNQTSYLCVC AEGFAPIPHE PHRCQMFCNQ TACPADCDPN 

       430        440        450        460        470        480 
TQASCECPEG YILDDGFICT DIDECENGGF CSGVCHNLPG TFECICGPDS ALARHIGTDC 

       490        500        510        520        530        540 
DSGKVDGGDS GSGEPPPSPT PGSTLTPPAV GLVHSGLLIG ISIASLCLVV ALLALLCHLR 

       550        560        570 
KKQGAARAKM EYKCAAPSKE VVLQHVRTER TPQRL 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation."
Suzuki K., Kusumoto H., Deyashiki Y., Nishioka J., Maruyama I., Zushi M., Kawahara S., Honda G., Yamamoto S., Horiguchi S.
EMBO J. 6:1891-1897(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-43.
[2]"Human thrombomodulin: complete cDNA sequence and chromosome localization of the gene."
Wen D., Dittman W.A., Ye R.D., Deaven L.L., Majerus P.W., Sadler J.E.
Biochemistry 26:4350-4357(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]"Human thrombomodulin gene is intron depleted: nucleic acid sequences of the cDNA and gene predict protein structure and suggest sites of regulatory control."
Jackman R.W., Beeler D.L., Fritze L., Soff G., Rosenberg R.D.
Proc. Natl. Acad. Sci. U.S.A. 84:6425-6429(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Gene structure of human thrombomodulin, a cofactor for thrombin-catalyzed activation of protein C."
Shirai T., Shiojiri S., Ito H., Yamamoto S., Kusumoto H., Deyashiki Y., Maruyama I., Suzuki K.
J. Biochem. 103:281-285(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]SeattleSNPs variation discovery resource
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-473.
[6]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-473.
Tissue: Brain and Lung.
[8]"Identification of the predominant glycosaminoglycan-attachment site in soluble recombinant human thrombomodulin: potential regulation of functionality 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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-492, MUTAGENESIS.
[9]"Urinary thrombomodulin, its isolation and characterization."
Yamamoto S., Mizoguchi T., Tamaki T., Ohkuchi M., Kimura S., Aoki N.
J. Biochem. 113:433-440(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT ASN-342.
[10]"The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin."
Adler M., Seto M.H., Nitecki D.E., Lin J.H., Light D.R., Morser J.
J. Biol. Chem. 270:23366-23372(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 389-407.
[11]"Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin."
Meininger D.P., Hunter M.J., Komives E.A.
Protein Sci. 4:1683-1695(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 364-407.
[12]"Thrombin-bound structure of an EGF subdomain from human thrombomodulin determined by transferred nuclear Overhauser effects."
Srinivasan J., Hu S., Hrabal R., Zhu Y., Komives E.A., Ni F.
Biochemistry 33:13553-13560(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 427-444.
[13]"Structural resiliency of an EGF-like subdomain bound to its target protein, thrombin."
Hrabal R., Komives E.A., Ni F.
Protein Sci. 5:195-203(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 427-444.
[14]"Structure of the fifth EGF-like domain of thrombomodulin: an EGF-like domain with a novel disulfide-bonding pattern."
Sampoli Benitez B.A., Hunter M.J., Meininger D.P., Komives E.A.
J. Mol. Biol. 273:913-926(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 405-444.
[15]"The first mutation identified in the thrombomodulin gene in a 45-year-old man presenting with thromboembolic disease."
Oehlin A.-K., Marlar R.A.
Blood 85:330-336(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THPH12 TYR-486.
[16]"Thrombomodulin gene variations and thromboembolic disease."
Oehlin A.-K., Norlund L., Marlar R.A.
Thromb. Haemost. 78:396-400(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THPH12 TYR-486, VARIANTS THR-43; ALA-79; SER-495 AND LEU-501.
[17]"A common thrombomodulin amino acid dimorphism is associated with myocardial infarction."
Norlund L., Holm J., Zoller B., Oehlin A.-K.
Thromb. Haemost. 77:248-251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-473.
[18]"A mutation in the thrombomodulin gene, 127G to A coding for Ala25Thr, and the risk of myocardial infarction in men."
Doggen C.J.M., Kunz G., Rosendaal F.R., Lane D.A., Vos H.L., Stubbs P.J., Manger Cats V., Ireland H.
Thromb. Haemost. 80:743-748(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-43.
[19]"Thrombomodulin Ala455Val polymorphism and risk of coronary heart disease."
Wu K.K., Aleksic N., Ahn C., Boerwinkle E., Folsom A.R., Juneja H.
Circulation 103:1386-1389(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-473.
[20]"Mutations in the thrombomodulin gene are rare in patients with severe thrombophilia."
Faioni E.M., Franchi F., Castaman G., Biguzzi E., Rodeghiero F.
Br. J. Haematol. 118:595-599(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THPH12 TYR-486, VARIANT VAL-473.
[21]"Thrombomodulin mutations in atypical hemolytic-uremic syndrome."
Delvaeye M., Noris M., De Vriese A., Esmon C.T., Esmon N.L., Ferrell G., Del-Favero J., Plaisance S., Claes B., Lambrechts D., Zoja C., Remuzzi G., Conway E.M.
N. Engl. J. Med. 361:345-357(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AHUS6 THR-43; GLY-53; LEU-81; TYR-486; SER-495 AND LEU-501, CHARACTERIZATION OF VARIANTS AHUS6 THR-43; GLY-53; LEU-81; TYR-486; SER-495 AND LEU-501, VARIANT VAL-473.
[22]"Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome."
Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.
Hum. Mutat. 31:E1445-E1460(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AHUS6 GLU-34 AND GLY-236.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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. Translation: CAB51954.1.
BC035602 mRNA. Translation: AAH35602.2.
BC053357 mRNA. Translation: AAH53357.1.
PIRTHHUB. A41442.
RefSeqNP_000352.1. NM_000361.2.
UniGeneHs.2030.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ADXNMR-A405-444[»]
1DQBNMR-A362-444[»]
1DX5X-ray2.30I/J/K/L363-480[»]
1EGTNMR-A427-444[»]
1FGDNMR-A427-444[»]
1FGENMR-A425-444[»]
1HLTX-ray3.00R426-444[»]
1TMRNMR-A389-407[»]
1ZAQNMR-A364-407[»]
2ADXNMR-A405-444[»]
3GISX-ray2.40X/Y/Z363-483[»]
ProteinModelPortalP07204.
SMRP07204. Positions 23-170, 211-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112914. 3 interactions.
IntActP07204. 4 interactions.
STRING9606.ENSP00000366307.

Chemistry

DrugBankDB00055. Drotrecogin alfa.

PTM databases

PhosphoSiteP07204.
UniCarbKBP07204.

Polymorphism databases

DMDM136170.

Proteomic databases

PaxDbP07204.
PRIDEP07204.

Protocols and materials databases

DNASU7056.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377103; ENSP00000366307; ENSG00000178726.
GeneID7056.
KEGGhsa:7056.
UCSCuc002wss.3. human.

Organism-specific databases

CTD7056.
GeneCardsGC20M023026.
H-InvDBHIX0174703.
HGNCHGNC:11784. THBD.
HPACAB002425.
HPA002982.
MIM188040. gene.
612926. phenotype.
614486. phenotype.
neXtProtNX_P07204.
Orphanet217023. Atypical hemolytic uremic syndrome with thrombomodulin anomaly.
3324. Familial thrombomodulin anomalies.
PharmGKBPA36496.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147686.
HOGENOMHOG000114624.
HOVERGENHBG000291.
InParanoidP07204.
KOK03907.
OMALCGPLCV.
OrthoDBEOG70ZZMW.
PhylomeDBP07204.
TreeFamTF330714.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

BgeeP07204.
CleanExHS_THBD.
GenevestigatorP07204.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR016316. CD93/CD141.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001491. Thrombomodulin.
IPR015149. Tme5_EGF-like.
[Graphical view]
PfamPF07645. EGF_CA. 2 hits.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]
PIRSFPIRSF001775. CD93/CD141. 1 hit.
PRINTSPR00907. THRMBOMODULN.
SMARTSM00034. CLECT. 1 hit.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS00010. 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.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTHBD. human.
EvolutionaryTraceP07204.
GeneWikiThrombomodulin.
GenomeRNAi7056.
NextBio27593.
PROP07204.
SOURCESearch...

Entry information

Entry nameTRBM_HUMAN
AccessionPrimary (citable) accession number: P07204
Secondary accession number(s): Q8IV29, Q9UC32
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 184 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries