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P07204

- TRBM_HUMAN

UniProt

P07204 - TRBM_HUMAN

Protein

Thrombomodulin

Gene

THBD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 189 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    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

    1. calcium ion binding Source: ProtInc
    2. carbohydrate binding Source: InterPro
    3. protein binding Source: IntAct
    4. receptor activity Source: ProtInc
    5. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. embryo development Source: Ensembl
    3. female pregnancy Source: Ensembl
    4. leukocyte migration Source: Reactome
    5. negative regulation of blood coagulation Source: BHF-UCL
    6. negative regulation of fibrinolysis Source: BHF-UCL
    7. negative regulation of platelet activation Source: BHF-UCL
    8. response to cAMP Source: Ensembl
    9. response to lipopolysaccharide Source: Ensembl
    10. response to X-ray Source: Ensembl

    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.

    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: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11784. THBD.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. extracellular space Source: Ensembl
    3. integral component of plasma membrane Source: ProtInc
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Thrombophilia due to thrombomodulin defect (THPH12) [MIM:614486]: A hemostatic disorder characterized by a tendency to thrombosis.3 Publications
    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.
    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) [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.2 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
    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.
    3324. Familial thrombomodulin anomalies.
    PharmGKBiPA36496.

    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.
    GenevestigatoriP07204.

    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 – 3714
    Beta strandi375 – 3806
    Beta strandi382 – 3843
    Beta strandi386 – 3894
    Beta strandi391 – 3933
    Beta strandi394 – 3974
    Beta strandi400 – 4067
    Beta strandi410 – 4145
    Beta strandi419 – 4213
    Beta strandi424 – 4263
    Turni428 – 4303
    Beta strandi431 – 4344
    Turni435 – 4373
    Beta strandi438 – 4414
    Helixi444 – 4474
    Beta strandi452 – 4576
    Beta strandi459 – 4668
    Beta strandi468 – 4714
    Beta strandi473 – 4775

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 22-170, 244-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07204.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei516 – 53924HelicalSequence AnalysisAdd
    BLAST

    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.
    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. 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]
    PfamiPF07645. EGF_CA. 2 hits.
    PF09064. Tme5_EGF_like. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001775. CD93/CD141. 1 hit.
    PRINTSiPR00907. THRMBOMODULN.
    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

    MLGVLVLGAL ALAGLGFPAP AEPQPGGSQC VEHDCFALYP GPATFLNASQ    50
    ICDGLRGHLM TVRSSVAADV ISLLLNGDGG VGRRRLWIGL QLPPGCGDPK 100
    RLGPLRGFQW VTGDNNTSYS RWARLDLNGA PLCGPLCVAV SAAEATVPSE 150
    PIWEEQQCEV KADGFLCEFH FPATCRPLAV EPGAAAAAVS ITYGTPFAAR 200
    GADFQALPVG SSAAVAPLGL QLMCTAPPGA VQGHWAREAP GAWDCSVENG 250
    GCEHACNAIP GAPRCQCPAG AALQADGRSC TASATQSCND LCEHFCVPNP 300
    DQPGSYSCMC ETGYRLAADQ HRCEDVDDCI LEPSPCPQRC VNTQGGFECH 350
    CYPNYDLVDG ECVEPVDPCF RANCEYQCQP LNQTSYLCVC AEGFAPIPHE 400
    PHRCQMFCNQ TACPADCDPN TQASCECPEG YILDDGFICT DIDECENGGF 450
    CSGVCHNLPG TFECICGPDS ALARHIGTDC DSGKVDGGDS GSGEPPPSPT 500
    PGSTLTPPAV GLVHSGLLIG ISIASLCLVV ALLALLCHLR KKQGAARAKM 550
    EYKCAAPSKE VVLQHVRTER TPQRL 575
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi136170.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13148.1.
    PIRi A41442. THHUB.
    RefSeqi NP_000352.1. NM_000361.2.
    UniGenei Hs.2030.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 427-444 [» ]
    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 [» ]
    ProteinModelPortali P07204.
    SMRi P07204. Positions 22-170, 244-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112914. 3 interactions.
    IntActi P07204. 4 interactions.
    STRINGi 9606.ENSP00000366307.

    Chemistry

    DrugBanki DB00055. Drotrecogin alfa.

    PTM databases

    PhosphoSitei P07204.
    UniCarbKBi P07204.

    Polymorphism databases

    DMDMi 136170.

    Proteomic databases

    MaxQBi P07204.
    PaxDbi P07204.
    PRIDEi P07204.

    Protocols and materials databases

    DNASUi 7056.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377103 ; ENSP00000366307 ; ENSG00000178726 .
    GeneIDi 7056.
    KEGGi hsa:7056.
    UCSCi uc002wss.3. human.

    Organism-specific databases

    CTDi 7056.
    GeneCardsi GC20M023026.
    GeneReviewsi THBD.
    H-InvDB HIX0174703.
    HGNCi HGNC:11784. THBD.
    HPAi CAB002425.
    HPA002982.
    MIMi 188040. gene.
    612926. phenotype.
    614486. phenotype.
    neXtProti NX_P07204.
    Orphaneti 217023. Atypical hemolytic uremic syndrome with thrombomodulin anomaly.
    3324. Familial thrombomodulin anomalies.
    PharmGKBi PA36496.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147686.
    HOGENOMi HOG000114624.
    HOVERGENi HBG000291.
    InParanoidi P07204.
    KOi K03907.
    OMAi LCGPLCV.
    OrthoDBi EOG70ZZMW.
    PhylomeDBi P07204.
    TreeFami TF330714.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1439. Common Pathway.

    Miscellaneous databases

    ChiTaRSi THBD. human.
    EvolutionaryTracei P07204.
    GeneWikii Thrombomodulin.
    GenomeRNAii 7056.
    NextBioi 27593.
    PROi P07204.
    SOURCEi Search...

    Gene expression databases

    Bgeei P07204.
    CleanExi HS_THBD.
    Genevestigatori P07204.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi 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_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 ]
    Pfami PF07645. EGF_CA. 2 hits.
    PF09064. Tme5_EGF_like. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001775. CD93/CD141. 1 hit.
    PRINTSi PR00907. THRMBOMODULN.
    SMARTi SM00034. CLECT. 1 hit.
    SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 189 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