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Identification
HMDB Protein ID HMDBP10016
Secondary Accession Numbers
  • 15954
Name Carboxypeptidase B2
Synonyms
  1. CPU
  2. Carboxypeptidase U
  3. Plasma carboxypeptidase B
  4. TAFI
  5. Thrombin-activable fibrinolysis inhibitor
  6. pCPB
Gene Name CPB2
Protein Type Enzyme
Biological Properties
General Function Involved in metallocarboxypeptidase activity
Specific Function Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities
Pathways Not Available
Reactions Not Available
GO Classification
Function
exopeptidase activity
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
transition metal ion binding
zinc ion binding
metallocarboxypeptidase activity
carboxypeptidase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Chromosome:1
Locus 13q14.11
SNPs CPB2
Gene Sequence
>1272 bp
ATGAAGCTTTGCAGCCTTGCAGTCCTTGTACCCATTGTTCTCTTCTGTGAGCAGCATGTC
TTCGCGTTTCAGAGTGGCCAAGTTCTAGCTGCTCTTCCTAGAACCTCTAGGCAAGTTCAA
GTTCTACAGAATCTTACTACAACATATGAGATTGTTCTCTGGCAGCCGGTAACAGCTGAC
CTTATTGTGAAGAAAAAACAAGTCCATTTTTTTGTAAATGCATCTGATGTCGACAATGTG
AAAGCCCATTTAAATGTGAGCGGAATTCCATGCAGTGTCTTGCTGGCAGATGTGGAAGAT
CTTATTCAACAGCAGATTTCCAACGACACAGTCAGCCCCCGAGCCTCCGCATCGTACTAT
GAACAGTATCACTCACTAAATGAAATCTATTCTTGGATAGAATTTATAACTGAGAGGCAT
CCTGATATGCTTACAAAAATCCACATTGGATCCTCATTTGAGAAGTACCCACTCTATGTT
TTAAAGGTTTCTGGAAAAGAACAAGCAGCCAAAAATGCCATATGGATTGACTGTGGAATC
CATGCCAGAGAATGGATCTCTCCTGCTTTCTGCTTGTGGTTCATAGGCCATATAACTCAA
TTCTATGGGATAATAGGGCAATATACCAATCTCCTGAGGCTTGTGGATTTCTATGTTATG
CCAGTGGTTAATGTGGATGGTTATGACTACTCATGGAAAAAGAATCGAATGTGGAGAAAG
AACCGTTCTTTCTATGCGAACAATCATTGCATCGGAACAGACCTGAATAGGAACTTTGCT
TCCAAACACTGGTGTGAGGAAGGTGCATCCAGTTCCTCATGCTCGGAAACCTACTGTGGA
CTTTATCCTGAGTCAGAACCAGAAGTGAAGGCAGTGGCTAGTTTCTTGAGAAGAAATATC
AACCAGATTAAAGCATACATCAGCATGCATTCATACTCCCAGCATATAGTGTTTCCATAT
TCCTATACACGAAGTAAAAGCAAAGACCATGAGGAACTGTCTCTAGTAGCCAGTGAAGCA
GTTCGTGCTATTGAGAAAACTAGTAAAAATACCAGGTATACACATGGCCATGGCTCAGAA
ACCTTATACCTAGCTCCTGGAGGTGGGGACGATTGGATCTATGATTTGGGCATCAAATAT
TCGTTTACAATTGAACTTCGAGATACGGGCACATACGGATTCTTGCTGCCGGAGCGTTAC
ATCAAACCCACCTGTAGAGAAGCTTTTGCCGCTGTCTCTAAAATAGCTTGGCATGTCATT
AGGAATGTTTAA
Protein Properties
Number of Residues 423
Molecular Weight 48411.8
Theoretical pI 7.77
Pfam Domain Function
Signals
  • 1-22
Transmembrane Regions
  • None
Protein Sequence
>Carboxypeptidase B2
MKLCSLAVLVPIVLFCEQHVFAFQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTAD
LIVKKKQVHFFVNASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYY
EQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQAAKNAIWIDCGI
HAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPVVNVDGYDYSWKKNRMWRK
NRSFYANNHCIGTDLNRNFASKHWCEEGASSSSCSETYCGLYPESEPEVKAVASFLRRNI
NQIKAYISMHSYSQHIVFPYSYTRSKSKDHEELSLVASEAVRAIEKTSKNTRYTHGHGSE
TLYLAPGGGDDWIYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVI
RNV
GenBank ID Protein 126273569
UniProtKB/Swiss-Prot ID Q96IY4
UniProtKB/Swiss-Prot Entry Name CBPB2_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001872.3
GeneCard ID CPB2
GenAtlas ID CPB2
HGNC ID HGNC:2300
References
General References
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  4. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952 ]
  5. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed:15057823 ]
  6. Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D: Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J Biol Chem. 1991 Nov 15;266(32):21833-8. [PubMed:1939207 ]
  7. Valnickova Z, Christensen T, Skottrup P, Thogersen IB, Hojrup P, Enghild JJ: Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation. Biochemistry. 2006 Feb 7;45(5):1525-35. [PubMed:16445295 ]