Human Gene CPB2 (ENST00000181383.10_8) from GENCODE V47lift37
  Description: carboxypeptidase B2, transcript variant 1 (from RefSeq NM_001872.5)
Gencode Transcript: ENST00000181383.10_8
Gencode Gene: ENSG00000080618.17_11
Transcript (Including UTRs)
   Position: hg19 chr13:46,627,321-46,679,168 Size: 51,848 Total Exon Count: 11 Strand: -
Coding Region
   Position: hg19 chr13:46,627,749-46,679,144 Size: 51,396 Coding Exon Count: 11 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr13:46,627,321-46,679,168)mRNA (may differ from genome)Protein (423 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
AlphaFoldBioGPSEnsemblEntrez GeneExonPrimerGeneCards
HGNCMalacardsMGIOMIMPubMedReactome
UniProtKBWikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: CBPB2_HUMAN
DESCRIPTION: RecName: Full=Carboxypeptidase B2; EC=3.4.17.20; AltName: Full=Carboxypeptidase U; Short=CPU; AltName: Full=Plasma carboxypeptidase B; Short=pCPB; AltName: Full=Thrombin-activable fibrinolysis inhibitor; Short=TAFI; Flags: Precursor;
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.
CATALYTIC ACTIVITY: Release of C-terminal Arg and Lys from a polypeptide.
COFACTOR: Binds 1 zinc ion per subunit.
ENZYME REGULATION: TAFI/CPB2 is unique among carboxypeptidases in that it spontaneously inactivates with a short half-life, a property that is crucial for its role in controlling blood clot lysis. The zymogen is stabilized by interactions with the activation peptide. Release of the activation peptide increases a dynamic flap mobility and in time this leads to conformational changes that disrupt the catalytic site and expose a cryptic thrombin-cleavage site present at Arg-324.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Plasma; synthesized in the liver.
PTM: N-glycosylated. N-glycan at Asn-108: Hex5HexNAc4.
SIMILARITY: Belongs to the peptidase M14 family.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cpb2/";

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: CPB2
Diseases sorted by gene-association score: factor xiii deficiency (11), chronic thromboembolic pulmonary hypertension (8), byssinosis (7), meningococcal infection (5)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 237.75 RPKM in Liver
Total median expression: 241.61 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -1.7024-0.071 Picture PostScript Text
3' UTR -81.70428-0.191 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR000834 - Peptidase_M14
IPR003146 - Prot_inh_M14A
IPR009020 - Prot_inh_propept

Pfam Domains:
PF00246 - Zinc carboxypeptidase
PF02244 - Carboxypeptidase activation peptide

SCOP Domains:
53187 - Zn-dependent exopeptidases
54897 - Protease propeptides/inhibitors

Protein Data Bank (PDB) 3-D Structure
MuPIT help
3D66 - X-ray MuPIT 3D67 - X-ray MuPIT 3D68 - X-ray MuPIT 3LMS - X-ray


ModBase Predicted Comparative 3D Structure on Q96IY4
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologNo orthologNo ortholog
Gene DetailsGene Details    
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 RGDEnsembl   
      
      

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0004180 carboxypeptidase activity
GO:0004181 metallocarboxypeptidase activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding

Biological Process:
GO:0003331 positive regulation of extracellular matrix constituent secretion
GO:0006508 proteolysis
GO:0007596 blood coagulation
GO:0007599 hemostasis
GO:0009408 response to heat
GO:0010757 negative regulation of plasminogen activation
GO:0030449 regulation of complement activation
GO:0042493 response to drug
GO:0042730 fibrinolysis
GO:0051918 negative regulation of fibrinolysis
GO:0071333 cellular response to glucose stimulus
GO:0097421 liver regeneration
GO:2000346 negative regulation of hepatocyte proliferation

Cellular Component:
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005623 cell
GO:0070062 extracellular exosome


-  Descriptions from all associated GenBank mRNAs
  M75106 - Human prepro-plasma carboxypeptidase B mRNA, complete cds.
AB011969 - Homo sapiens mRNA for carboxypeptidase B-like protein, complete cds.
BC007057 - Homo sapiens carboxypeptidase B2 (plasma), mRNA (cDNA clone MGC:12495 IMAGE:3934520), complete cds.
AK290829 - Homo sapiens cDNA FLJ76035 complete cds, highly similar to Homo sapiens carboxypeptidase B2 (plasma, carboxypeptidase U) (CPB2), transcript variant 1, mRNA.
BT006936 - Homo sapiens carboxypeptidase B2 (plasma, carboxypeptidase U) mRNA, complete cds.
DQ890567 - Synthetic construct clone IMAGE:100003197; FLH164008.01X; RZPDo839B09162D carboxypeptidase B2 (plasma, carboxypeptidase U) (CPB2) gene, encodes complete protein.
KJ896633 - Synthetic construct Homo sapiens clone ccsbBroadEn_06027 CPB2 gene, encodes complete protein.
KR710156 - Synthetic construct Homo sapiens clone CCSBHm_00010147 CPB2 (CPB2) mRNA, encodes complete protein.
KR710157 - Synthetic construct Homo sapiens clone CCSBHm_00010148 CPB2 (CPB2) mRNA, encodes complete protein.
EU176478 - Synthetic construct Homo sapiens clone IMAGE:100011331; FLH164007.01L; RZPDo839A02253D carboxypeptidase B2 (plasma) (CPB2) gene, encodes complete protein.
AB590176 - Synthetic construct DNA, clone: pFN21AE1485, Homo sapiens CPB2 gene for carboxypeptidase B2, without stop codon, in Flexi system.
CU675521 - Synthetic construct Homo sapiens gateway clone IMAGE:100017238 5' read CPB2 mRNA.
JD086341 - Sequence 67365 from Patent EP1572962.
JD447998 - Sequence 429022 from Patent EP1572962.
JD467151 - Sequence 448175 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  BioCarta from NCI Cancer Genome Anatomy Project
h_fibrinolysisPathway - Fibrinolysis Pathway

Reactome (by CSHL, EBI, and GO)

Protein Q96IY4 (Reactome details) participates in the following event(s):

R-HSA-8852809 CPN, CPB2 cleave C3a, C5a
R-HSA-2028294 Mast Cell Carboxypeptidase hydrolyzes Angiotensin-(1-10) to Yield Angiotensin-(1-9)
R-HSA-977606 Regulation of Complement cascade
R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
R-HSA-166658 Complement cascade
R-HSA-2980736 Peptide hormone metabolism
R-HSA-168249 Innate Immune System
R-HSA-392499 Metabolism of proteins
R-HSA-168256 Immune System

-  Other Names for This Gene
  Alternate Gene Symbols: A8K464, CBPB2_HUMAN, ENST00000181383.1, ENST00000181383.2, ENST00000181383.3, ENST00000181383.4, ENST00000181383.5, ENST00000181383.6, ENST00000181383.7, ENST00000181383.8, ENST00000181383.9, NM_001872, Q15114, Q5T9K1, Q5T9K2, Q96IY4, Q9P2Y6, uc317cfc.1, uc317cfc.2
UCSC ID: ENST00000181383.10_8
RefSeq Accession: NM_001872.5
Protein: Q96IY4 (aka CBPB2_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.