Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Prothrombin  

UniProtKB / Swiss-Prot ID :  THRB_BOVIN

Gene Name (Synonyms) : 
F2  

Species :  Bos taurus (Bovine). 

Subcellular Localization :  Secreted, extracellular space. 

Protein Function :  Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). 

Protein Sequence MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREE...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHCCCCCCEECCCHHHHHHEEECCCCCCCCCHHCCCCCEEEEECCCCCCHHH...
Protein Variant
LocationDescription
600D -> N.
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
504-carboxyglutamate.KGFLEEVRK
CCCCHHCCC
52.78UniProtKB
Link-
514-carboxyglutamate.GFLEEVRKG
CCCHHCCCC
50.17UniProtKB
Link-
584-carboxyglutamate.KGNLERECL
CCCEEEEEC
50.89UniProtKB
Link-
604-carboxyglutamate.NLERECLEE
CEEEEECCC
33.79UniProtKB
Link-
634-carboxyglutamate.RECLEEPCS
EEECCCCCC
72.11UniProtKB
Link-
644-carboxyglutamate.ECLEEPCSR
EECCCCCCH
38.36UniProtKB
Link-
694-carboxyglutamate.PCSREEAFE
CCCHHHCCC
37.07UniProtKB
Link-
704-carboxyglutamate.CSREEAFEA
CCHHHCCCC
58.51UniProtKB
Link-
734-carboxyglutamate.EEAFEALES
HHCCCCCCC
60.43UniProtKB
Link-
764-carboxyglutamate.FEALESLSA
CCCCCCCCC
57.59UniProtKB
Link-
120N-linked (GlcNAc...).NYRGNVSVT
CCEEECCCC
17.56UniProtKB
Link-
144N-linked (GlcNAc...).KPEINSTTH
CCCCCCCCC
31.48UniProtKB
Link-
419N-linked (GlcNAc...).PWDKNFTVD
CCCCCCCCC
35.04UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1.";
Soriano-Garcia M., Padmanabhan K., de Vos A.M., Tulinsky A.;
Biochemistry 31:2554-2566(1992).
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF ACTIVATION PEPTIDE 1 INCOMPLEX WITH CALCIUM IONS, DISULFIDE BONDS, AND GLYCOSYLATION ATASN-120 AND ASN-144.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures