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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

BioCyciZFISH:ENSG00000178726-MONOMER.
ReactomeiR-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-202733. Cell surface interactions at the vascular wall.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11784. THBD.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 515ExtracellularSequence analysisAdd BLAST497
Transmembranei516 – 539HelicalSequence analysisAdd BLAST24
Topological domaini540 – 575CytoplasmicSequence analysisAdd BLAST36

GO - Cellular componenti

  • apicolateral plasma membrane Source: Ensembl
  • cell surface Source: BHF-UCL
  • extracellular space Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
  • vacuolar membrane Source: Ensembl
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_011371486D → Y in THPH12 and AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 4 PublicationsCorresponds to variant rs41348347dbSNPEnsembl.1
Hemolytic uremic syndrome atypical 6 (AHUS6)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
Disease descriptionAn atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease.
See also OMIM:612926
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06367334D → E in AHUS6. 1 Publication1
Natural variantiVAR_01136843A → T in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 3 PublicationsCorresponds to variant rs1800576dbSNPEnsembl.1
Natural variantiVAR_06322353D → G in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 PublicationCorresponds to variant rs121918667dbSNPEnsembl.1
Natural variantiVAR_06322481V → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 Publication1
Natural variantiVAR_063674236A → G in AHUS6. 1 PublicationCorresponds to variant rs758686992dbSNPEnsembl.1
Natural variantiVAR_011371486D → Y in THPH12 and AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 4 PublicationsCorresponds to variant rs41348347dbSNPEnsembl.1
Natural variantiVAR_011372495P → S in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 PublicationsCorresponds to variant rs1800578dbSNPEnsembl.1
Natural variantiVAR_011373501P → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 PublicationsCorresponds to variant rs1800579dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Hemolytic uremic syndrome, Thrombophilia

Organism-specific databases

DisGeNETi7056.
MalaCardsiTHBD.
MIMi612926. phenotype.
614486. phenotype.
OpenTargetsiENSG00000178726.
Orphaneti217023. Atypical hemolytic-uremic syndrome with thrombomodulin anomaly.
PharmGKBiPA36496.

Chemistry databases

DrugBankiDB00055. Drotrecogin alfa.
DB01050. Ibuprofen.

Polymorphism and mutation databases

BioMutaiTHBD.
DMDMi136170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
ChainiPRO_000000777119 – 575ThrombomodulinAdd BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi47N-linked (GlcNAc...)Sequence analysis1
Glycosylationi115N-linked (GlcNAc...)Sequence analysis1
Glycosylationi116N-linked (GlcNAc...)Sequence analysis1
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(3R)-3-hydroxyasparagine1 Publication1
Disulfide bondi351 ↔ 362By similarity
Disulfide bondi369 ↔ 378By similarity
Disulfide bondi374 ↔ 388By similarity
Glycosylationi382N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi390 ↔ 404
Disulfide bondi408 ↔ 413
Glycosylationi409N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi417 ↔ 425
Disulfide bondi427 ↔ 439
Disulfide bondi445 ↔ 455By similarity
Disulfide bondi451 ↔ 464By similarity
Disulfide bondi466 ↔ 480By similarity
Glycosylationi490O-linked (Xyl...) (chondroitin sulfate)1
Glycosylationi492O-linked (Xyl...) (chondroitin sulfate)1 Publication1

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.
PeptideAtlasiP07204.
PRIDEiP07204.

PTM databases

PhosphoSitePlusiP07204.
SwissPalmiP07204.
UniCarbKBiP07204.

Expressioni

Tissue specificityi

Endothelial cells are unique in synthesizing thrombomodulin.

Gene expression databases

BgeeiENSG00000178726.
CleanExiHS_THBD.
GenevisibleiP07204. HS.

Organism-specific databases

HPAiCAB002425.
HPA002982.

Interactioni

Subunit structurei

Interacts with ITGAL, ITGAM and ITGB2.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112914. 4 interactors.
IntActiP07204. 4 interactors.
STRINGi9606.ENSP00000366307.

Structurei

Secondary structure

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi368 – 371Combined sources4
Beta strandi375 – 380Combined sources6
Beta strandi382 – 384Combined sources3
Beta strandi386 – 389Combined sources4
Beta strandi391 – 393Combined sources3
Beta strandi394 – 397Combined sources4
Beta strandi400 – 406Combined sources7
Beta strandi410 – 414Combined sources5
Beta strandi419 – 421Combined sources3
Beta strandi424 – 426Combined sources3
Turni428 – 430Combined sources3
Beta strandi431 – 434Combined sources4
Turni435 – 437Combined sources3
Beta strandi438 – 441Combined sources4
Helixi444 – 447Combined sources4
Beta strandi452 – 457Combined sources6
Beta strandi459 – 466Combined sources8
Beta strandi468 – 471Combined sources4
Beta strandi473 – 477Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP07204.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 169C-type lectinPROSITE-ProRule annotationAdd BLAST139
Domaini241 – 281EGF-like 1PROSITE-ProRule annotationAdd BLAST41
Domaini284 – 324EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini325 – 363EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini365 – 405EGF-like 4PROSITE-ProRule annotationAdd BLAST41
Domaini404 – 440EGF-like 5PROSITE-ProRule annotationAdd BLAST37
Domaini441 – 481EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni481 – 515Involved in alpha-L/beta-2 and alpha-M/beta-2 integrin binding1 PublicationAdd BLAST35

Domaini

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

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

eggNOGiENOG410IF0T. Eukaryota.
ENOG410Y5JS. LUCA.
GeneTreeiENSGT00810000125382.
HOGENOMiHOG000114624.
HOVERGENiHBG000291.
InParanoidiP07204.
KOiK03907.
OMAiLCGPLCV.
OrthoDBiEOG091G06M1.
PhylomeDBiP07204.
TreeFamiTF330714.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016316. CD141.
IPR026823. cEGF.
IPR016187. CTDL_fold.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR015149. Tme5_EGF-like.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00059. Lectin_C. 1 hit.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]
PIRSFiPIRSF001775. CD93/CD141. 1 hit.
SMARTiSM00034. CLECT. 1 hit.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 4 hits.
[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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06367334D → E in AHUS6. 1 Publication1
Natural variantiVAR_01136843A → T in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 3 PublicationsCorresponds to variant rs1800576dbSNPEnsembl.1
Natural variantiVAR_06322353D → G in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 PublicationCorresponds to variant rs121918667dbSNPEnsembl.1
Natural variantiVAR_01136979G → A.1 PublicationCorresponds to variant rs1800577dbSNPEnsembl.1
Natural variantiVAR_06322481V → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 1 Publication1
Natural variantiVAR_049011162A → P.Corresponds to variant rs36110902dbSNPEnsembl.1
Natural variantiVAR_063674236A → G in AHUS6. 1 PublicationCorresponds to variant rs758686992dbSNPEnsembl.1
Natural variantiVAR_011370473A → V.6 PublicationsCorresponds to variant rs1042579dbSNPEnsembl.1
Natural variantiVAR_011371486D → Y in THPH12 and AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 4 PublicationsCorresponds to variant rs41348347dbSNPEnsembl.1
Natural variantiVAR_011372495P → S in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 PublicationsCorresponds to variant rs1800578dbSNPEnsembl.1
Natural variantiVAR_011373501P → L in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation. 2 PublicationsCorresponds to variant rs1800579dbSNPEnsembl.1

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.4. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ADXNMR-A405-444[»]
1DQBNMR-A364-444[»]
1DX5X-ray2.30I/J/K/L363-480[»]
1EGTNMR-A427-444[»]
1FGDNMR-A427-444[»]
1FGENMR-A425-444[»]
1HLTX-ray3.00R426-444[»]
1TMRNMR-A389-405[»]
1ZAQNMR-A364-407[»]
2ADXNMR-A405-444[»]
3GISX-ray2.40X/Y/Z363-483[»]
ProteinModelPortaliP07204.
SMRiP07204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112914. 4 interactors.
IntActiP07204. 4 interactors.
STRINGi9606.ENSP00000366307.

Chemistry databases

DrugBankiDB00055. Drotrecogin alfa.
DB01050. Ibuprofen.

PTM databases

PhosphoSitePlusiP07204.
SwissPalmiP07204.
UniCarbKBiP07204.

Polymorphism and mutation databases

BioMutaiTHBD.
DMDMi136170.

Proteomic databases

MaxQBiP07204.
PaxDbiP07204.
PeptideAtlasiP07204.
PRIDEiP07204.

Protocols and materials databases

DNASUi7056.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7056.
DisGeNETi7056.
GeneCardsiTHBD.
GeneReviewsiTHBD.
H-InvDBHIX0174703.
HGNCiHGNC:11784. THBD.
HPAiCAB002425.
HPA002982.
MalaCardsiTHBD.
MIMi188040. gene.
612926. phenotype.
614486. phenotype.
neXtProtiNX_P07204.
OpenTargetsiENSG00000178726.
Orphaneti217023. Atypical hemolytic-uremic syndrome with thrombomodulin anomaly.
PharmGKBiPA36496.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF0T. Eukaryota.
ENOG410Y5JS. LUCA.
GeneTreeiENSGT00810000125382.
HOGENOMiHOG000114624.
HOVERGENiHBG000291.
InParanoidiP07204.
KOiK03907.
OMAiLCGPLCV.
OrthoDBiEOG091G06M1.
PhylomeDBiP07204.
TreeFamiTF330714.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000178726-MONOMER.
ReactomeiR-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-202733. Cell surface interactions at the vascular wall.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000178726.
CleanExiHS_THBD.
GenevisibleiP07204. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016316. CD141.
IPR026823. cEGF.
IPR016187. CTDL_fold.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR015149. Tme5_EGF-like.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00059. Lectin_C. 1 hit.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]
PIRSFiPIRSF001775. CD93/CD141. 1 hit.
SMARTiSM00034. CLECT. 1 hit.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 4 hits.
[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...

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: November 30, 2016
This is version 211 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

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 one 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.