Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Carboxypeptidase B2  

UniProtKB / Swiss-Prot ID :  CBPB2_BOVIN

Gene Name (Synonyms) : 
CPB2  

Species :  Bos taurus (Bovine). 

Subcellular Localization :  Secreted (By similarity). 

Protein Function :  Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down- regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. 

Protein Sequence MKLYSLGVLVATVLFCGEHAFAFQRGQVLSALPRTSRQVQILQNVTTTYKIVLWQPVAAEYIVKGYEVHF...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHHHHCEECCCCEEEEEECCHHHHHHHHHHHHHHHHEEECCCCCCCCCCCCEEEE...
Protein Variant -
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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
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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
44N-linked (GlcNAc...).QILQNVTTT
HHHHHHHHH
29.65UniProtKB
Link-
73N-linked (GlcNAc...).HFFVNASDV
EEEECCCCC
28.68UniProtKB
Link-
85N-linked (GlcNAc...).KAHLNASRI
HHHHHHCCC
26.46UniProtKB
Link-
108N-linked (GlcNAc...).QQTSNDTIS
HHHHHHCCC
54.56UniProtKB
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 crystal structure of thrombin-activable fibrinolysis inhibitor(TAFI) provides the structural basis for its intrinsic activity andthe short half-life of TAFIa.";
Anand K., Pallares I., Valnickova Z., Christensen T., Vendrell J.,Wendt K.U., Schreuder H.A., Enghild J.J., Aviles F.X.;
J. Biol. Chem. 283:29416-29423(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-423, GLYCOSYLATION ATASN-44; ASN-73; ASN-85 AND ASN-108, ACTIVE SITE, ZINC-BINDING SITES,AND DISULFID BONDS.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures