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Protein

Thrombomodulin

Gene

THBD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

GO - Molecular functioni

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

GO - Biological processi

  • blood coagulation Source: Reactome
  • female pregnancy Source: Ensembl
  • leukocyte migration Source: Reactome
  • negative regulation of blood coagulation Source: BHF-UCL
  • negative regulation of fibrinolysis Source: BHF-UCL
  • negative regulation of platelet activation Source: BHF-UCL
  • response to cAMP Source: Ensembl
  • response to lipopolysaccharide Source: Ensembl
  • response to X-ray Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_1439. Common Pathway of Fibrin Clot Formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Thrombomodulin
Short name:
TM
Alternative name(s):
Fetomodulin
CD_antigen: CD141
Gene namesi
Name:THBD
Synonyms:THRM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11784. THBD.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 515497ExtracellularSequence AnalysisAdd
BLAST
Transmembranei516 – 53924HelicalSequence AnalysisAdd
BLAST
Topological domaini540 – 57536CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • extracellular space Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

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
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti486 – 4861D → 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 Publications
Corresponds to variant rs41348347 [ dbSNP | Ensembl ].
VAR_011371
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341D → E in AHUS6. 1 Publication
VAR_063673
Natural varianti43 – 431A → T in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 3 Publications
Corresponds to variant rs1800576 [ dbSNP | Ensembl ].
VAR_011368
Natural varianti53 – 531D → G in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 Publication
VAR_063223
Natural varianti81 – 811V → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 Publication
VAR_063224
Natural varianti236 – 2361A → G in AHUS6. 1 Publication
VAR_063674
Natural varianti486 – 4861D → 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 Publications
Corresponds to variant rs41348347 [ dbSNP | Ensembl ].
VAR_011371
Natural varianti495 – 4951P → S in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 Publications
Corresponds to variant rs1800578 [ dbSNP | Ensembl ].
VAR_011372
Natural varianti501 – 5011P → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 Publications
Corresponds to variant rs1800579 [ dbSNP | Ensembl ].
VAR_011373

Keywords - Diseasei

Disease mutation, Hemolytic uremic syndrome, Thrombophilia

Organism-specific databases

MIMi612926. phenotype.
614486. phenotype.
Orphaneti217023. Atypical hemolytic-uremic syndrome with thrombomodulin anomaly.
PharmGKBiPA36496.

Chemistry

DrugBankiDB00055. Drotrecogin alfa.
DB01050. Ibuprofen.

Polymorphism and mutation databases

BioMutaiTHBD.
DMDMi136170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 575557ThrombomodulinPRO_0000007771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
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
Modified residuei342 – 3421(3R)-3-hydroxyasparagine1 Publication
Disulfide bondi351 ↔ 362By similarity
Disulfide bondi369 ↔ 378By similarity
Disulfide bondi374 ↔ 388By similarity
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi390 ↔ 404
Disulfide bondi408 ↔ 413
Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi417 ↔ 425
Disulfide bondi427 ↔ 439
Disulfide bondi445 ↔ 455By similarity
Disulfide bondi451 ↔ 464By similarity
Disulfide bondi466 ↔ 480By similarity
Glycosylationi490 – 4901O-linked (Xyl...) (chondroitin sulfate)
Glycosylationi492 – 4921O-linked (Xyl...) (chondroitin sulfate)1 Publication

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

Proteomic databases

MaxQBiP07204.
PaxDbiP07204.
PRIDEiP07204.

PTM databases

PhosphoSiteiP07204.
UniCarbKBiP07204.

Expressioni

Tissue specificityi

Endothelial cells are unique in synthesizing thrombomodulin.

Gene expression databases

BgeeiP07204.
CleanExiHS_THBD.
GenevisibleiP07204. HS.

Organism-specific databases

HPAiCAB002425.
HPA002982.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112914. 3 interactions.
IntActiP07204. 4 interactions.
STRINGi9606.ENSP00000366307.

Structurei

Secondary structure

1
575
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi368 – 3714Combined sources
Beta strandi375 – 3806Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi386 – 3894Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi400 – 4067Combined sources
Beta strandi410 – 4145Combined sources
Beta strandi419 – 4213Combined sources
Beta strandi424 – 4263Combined sources
Turni428 – 4303Combined sources
Beta strandi431 – 4344Combined sources
Turni435 – 4373Combined sources
Beta strandi438 – 4414Combined sources
Helixi444 – 4474Combined sources
Beta strandi452 – 4576Combined sources
Beta strandi459 – 4668Combined sources
Beta strandi468 – 4714Combined sources
Beta strandi473 – 4775Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP07204.
SMRiP07204. Positions 244-480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07204.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 169139C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini241 – 28141EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini284 – 32441EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini325 – 36339EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini365 – 40541EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini404 – 44037EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini441 – 48141EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 6 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG147686.
GeneTreeiENSGT00770000120465.
HOGENOMiHOG000114624.
HOVERGENiHBG000291.
InParanoidiP07204.
KOiK03907.
OMAiLCGPLCV.
OrthoDBiEOG70ZZMW.
PhylomeDBiP07204.
TreeFamiTF330714.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR016316. 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.
IPR015149. Tme5_EGF-like.
[Graphical view]
PfamiPF07645. EGF_CA. 2 hits.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]
PIRSFiPIRSF001775. CD93/CD141. 1 hit.
SMARTiSM00034. CLECT. 1 hit.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

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
Checksum:i9AF03CD151227D52
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341D → E in AHUS6. 1 Publication
VAR_063673
Natural varianti43 – 431A → T in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 3 Publications
Corresponds to variant rs1800576 [ dbSNP | Ensembl ].
VAR_011368
Natural varianti53 – 531D → G in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 Publication
VAR_063223
Natural varianti79 – 791G → A.1 Publication
Corresponds to variant rs1800577 [ dbSNP | Ensembl ].
VAR_011369
Natural varianti81 – 811V → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 Publication
VAR_063224
Natural varianti162 – 1621A → P.
Corresponds to variant rs36110902 [ dbSNP | Ensembl ].
VAR_049011
Natural varianti236 – 2361A → G in AHUS6. 1 Publication
VAR_063674
Natural varianti473 – 4731A → V.6 Publications
Corresponds to variant rs1042579 [ dbSNP | Ensembl ].
VAR_011370
Natural varianti486 – 4861D → 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 Publications
Corresponds to variant rs41348347 [ dbSNP | Ensembl ].
VAR_011371
Natural varianti495 – 4951P → S in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 Publications
Corresponds to variant rs1800578 [ dbSNP | Ensembl ].
VAR_011372
Natural varianti501 – 5011P → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 Publications
Corresponds to variant rs1800579 [ dbSNP | Ensembl ].
VAR_011373

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. Translation: CAB51954.1.
BC035602 mRNA. Translation: AAH35602.2.
BC053357 mRNA. Translation: AAH53357.1.
CCDSiCCDS13148.1.
PIRiA41442. THHUB.
RefSeqiNP_000352.1. NM_000361.2.
UniGeneiHs.2030.

Genome annotation databases

EnsembliENST00000377103; ENSP00000366307; ENSG00000178726.
GeneIDi7056.
KEGGihsa:7056.
UCSCiuc002wss.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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. Translation: CAB51954.1.
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:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP07204.
SMRiP07204. Positions 244-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112914. 3 interactions.
IntActiP07204. 4 interactions.
STRINGi9606.ENSP00000366307.

Chemistry

DrugBankiDB00055. Drotrecogin alfa.
DB01050. Ibuprofen.

PTM databases

PhosphoSiteiP07204.
UniCarbKBiP07204.

Polymorphism and mutation databases

BioMutaiTHBD.
DMDMi136170.

Proteomic databases

MaxQBiP07204.
PaxDbiP07204.
PRIDEiP07204.

Protocols and materials databases

DNASUi7056.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377103; ENSP00000366307; ENSG00000178726.
GeneIDi7056.
KEGGihsa:7056.
UCSCiuc002wss.3. human.

Organism-specific databases

CTDi7056.
GeneCardsiGC20M023026.
GeneReviewsiTHBD.
H-InvDBHIX0174703.
HGNCiHGNC:11784. THBD.
HPAiCAB002425.
HPA002982.
MIMi188040. gene.
612926. phenotype.
614486. phenotype.
neXtProtiNX_P07204.
Orphaneti217023. Atypical hemolytic-uremic syndrome with thrombomodulin anomaly.
PharmGKBiPA36496.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG147686.
GeneTreeiENSGT00770000120465.
HOGENOMiHOG000114624.
HOVERGENiHBG000291.
InParanoidiP07204.
KOiK03907.
OMAiLCGPLCV.
OrthoDBiEOG70ZZMW.
PhylomeDBiP07204.
TreeFamiTF330714.

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_1439. Common Pathway of Fibrin Clot Formation.

Miscellaneous databases

ChiTaRSiTHBD. human.
EvolutionaryTraceiP07204.
GeneWikiiThrombomodulin.
GenomeRNAii7056.
NextBioi27593.
PROiP07204.
SOURCEiSearch...

Gene expression databases

BgeeiP07204.
CleanExiHS_THBD.
GenevisibleiP07204. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR016316. 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.
IPR015149. Tme5_EGF-like.
[Graphical view]
PfamiPF07645. EGF_CA. 2 hits.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]
PIRSFiPIRSF001775. CD93/CD141. 1 hit.
SMARTiSM00034. CLECT. 1 hit.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00010. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiTRBM_HUMAN
AccessioniPrimary (citable) accession number: P07204
Secondary accession number(s): Q8IV29, Q9UC32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1991
Last modified: June 24, 2015
This is version 197 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.