P07204 (TRBM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thrombomodulin
Short name=TM

Alternative name(s):
Fetomodulin
CD_antigen=CD141

Gene names

Name:	THBD
Synonyms:	THRM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Blood coagulation Hemostasis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hemolytic uremic syndrome Thrombophilia
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome embryo development Inferred from electronic annotation. Source: Compara female pregnancy Inferred from electronic annotation. Source: Compara leukocyte migration Traceable author statement. Source: Reactome 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
Cellular_component	cell surface Inferred from direct assay PubMed 17379830. Source: BHF-UCL integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Molecular_function	calcium 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
F2	P00734	4	EBI-941422,EBI-297094

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.1

Chain

19 – 575

557

Thrombomodulin

PRO_0000007771

Regions

Topological domain

19 – 515

497

Extracellular Potential

Transmembrane

516 – 539

24

Helical; Potential

Topological domain

540 – 575

36

Cytoplasmic Potential

Domain

31 – 169

139

C-type lectin

Domain

241 – 281

41

EGF-like 1

Domain

284 – 324

41

EGF-like 2

Domain

325 – 363

39

EGF-like 3; calcium-binding Potential

Domain

365 – 405

41

EGF-like 4

Domain

404 – 440

37

EGF-like 5

Domain

441 – 481

41

EGF-like 6; calcium-binding Potential

Amino acid modifications

Modified residue

342

1

(3R)-3-hydroxyasparagine Ref.9

Glycosylation

47

1

N-linked (GlcNAc...) Potential

Glycosylation

115

1

N-linked (GlcNAc...) Potential

Glycosylation

116

1

N-linked (GlcNAc...) Potential

Glycosylation

382

1

N-linked (GlcNAc...) Potential

Glycosylation

409

1

N-linked (GlcNAc...) Potential

Glycosylation

490

1

O-linked (Xyl...) (chondroitin sulfate)

Glycosylation

492

1

O-linked (Xyl...) (chondroitin sulfate) Ref.8

Disulfide bond

137 ↔ 158

By similarity

Disulfide bond

245 ↔ 256

By similarity

Disulfide bond

252 ↔ 265

By similarity

Disulfide bond

267 ↔ 280

By similarity

Disulfide bond

288 ↔ 296

By similarity

Disulfide bond

292 ↔ 308

By similarity

Disulfide bond

310 ↔ 323

By similarity

Disulfide bond

329 ↔ 340

By similarity

Disulfide bond

336 ↔ 349

By similarity

Disulfide bond

351 ↔ 362

By similarity

Disulfide bond

369 ↔ 378

By similarity

Disulfide bond

374 ↔ 388

By similarity

Disulfide bond

390 ↔ 404

Disulfide bond

408 ↔ 413

Disulfide bond

417 ↔ 425

Disulfide bond

427 ↔ 439

Disulfide bond

445 ↔ 455

By similarity

Disulfide bond

451 ↔ 464

By similarity

Disulfide bond

466 ↔ 480

By similarity

Natural variations

Natural variant

34

1

D → E in AHUS6. Ref.22

VAR_063673

Natural variant

43

1

A → 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 variant

53

1

D → 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 variant

79

1

G → A. Ref.16
Corresponds to variant rs1800577 [ dbSNP | Ensembl ].

VAR_011369

Natural variant

81

1

V → 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 variant

162

1

A → P.
Corresponds to variant rs36110902 [ dbSNP | Ensembl ].

VAR_049011

Natural variant

236

1

A → G in AHUS6. Ref.22

VAR_063674

Natural variant

473

1

A → V. Ref.5 Ref.7 Ref.17 Ref.19 Ref.20 Ref.21
Corresponds to variant rs1042579 [ dbSNP | Ensembl ].

VAR_011370

Natural variant

486

1

D → 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 variant

495

1

P → 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 variant

501

1

P → 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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

575

Helix Strand Turn

Details...

Helix

368 – 371

4

Beta strand

375 – 380

6

Beta strand

382 – 384

3

Beta strand

386 – 389

4

Beta strand

391 – 393

3

Beta strand

394 – 397

4

Beta strand

400 – 406

7

Beta strand

410 – 414

5

Beta strand

419 – 421

3

Beta strand

424 – 426

3

Turn

428 – 430

3

Beta strand

431 – 434

4

Turn

435 – 437

3

Beta strand

438 – 441

4

Helix

444 – 447

4

Beta strand

452 – 457

6

Beta strand

459 – 466

8

Beta strand

468 – 471

4

Beta strand

473 – 477

5

Sequences

	Sequence		Length	Mass (Da)
	P07204 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 9AF03CD151227D52	FASTA	575	60,329
	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

References

	« Hide 'large scale' referencesShow '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. , 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

Wikipedia

Thrombomodulin entry

SeattleSNPs

Functional Glycomics Gateway - Glycan Binding

Thrombomodulin

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.

IPI

IPI00010737.

PIR

THHUB. A41442.

RefSeq

NP_000352.1. NM_000361.2.

UniGene

Hs.2030.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ADX	NMR	-	A	405-444	[»]
1DQB	NMR	-	A	364-444	[»]
1DX5	X-ray	2.30	I/J/K/L	363-480	[»]
1EGT	NMR	-	A	427-437	[»]
1FGD	NMR	-	A	427-444	[»]
1FGE	NMR	-	A	425-444	[»]
1HLT	X-ray	3.00	R	426-444	[»]
1TMR	NMR	-	A	389-405	[»]
1ZAQ	NMR	-	A	364-407	[»]
2ADX	NMR	-	A	405-444	[»]
3GIS	X-ray	2.40	X/Y/Z	363-483	[»]

ProteinModelPortal

P07204.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07204. 4 interactions.

STRING

9606.ENSP00000366307.

PTM databases

GlycoSuiteDB

P07204.

PhosphoSite

P07204.

Polymorphism databases

DMDM

136170.

Proteomic databases

PaxDb

P07204.

PRIDE

P07204.

Protocols and materials databases

DNASU

7056.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000377103; ENSP00000366307; ENSG00000178726.

GeneID

7056.

KEGG

hsa:7056.

UCSC

uc002wss.3. human.

Organism-specific databases

CTD

7056.

GeneCards

GC20M023026.

H-InvDB

HIX0174703.

HGNC

HGNC:11784. THBD.

HPA

CAB002425.
HPA002982.

MIM

188040. gene.
612926. phenotype.
614486. phenotype.

neXtProt

NX_P07204.

Orphanet

217023. Atypical hemolytic uremic syndrome with thrombomodulin anomaly.
3324. Familial thrombomodulin anomalies.

PharmGKB

PA36496.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG147686.

HOGENOM

HOG000114624.

HOVERGEN

HBG000291.

InParanoid

P07204.

KO

K03907.

OMA

FRGPATF.

OrthoDB

EOG41G350.

PhylomeDB

P07204.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

Bgee

P07204.

CleanEx

HS_THBD.

Genevestigator

P07204.

GermOnline

ENSG00000178726. Homo sapiens.

Family and domain databases

Gene3D

3.10.100.10. 1 hit.

InterPro

IPR001304. 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.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR001491. Thrombomodulin.
IPR015149. Tme5_EGF-like.
[Graphical view]

Pfam

PF07645. EGF_CA. 2 hits.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]

PIRSF

PIRSF001775. CD93/CD141. 1 hit.

PRINTS

PR00907. THRMBOMODULN.

SMART

SM00034. CLECT. 1 hit.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00010. ASX_HYDROXYL. 2 hits.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

THBD. human.

DrugBank

DB00055. Drotrecogin alfa.

EvolutionaryTrace

P07204.

GenomeRNAi

7056.

NextBio

27593.

SOURCE

Search...

Entry information

Entry name

TRBM_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 175 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.