CPB2
entrez
1361
canonical
uniprot
Q96IY4
canonical
ensembl
ENSG00000080618
resolver
ensp
ENSP00000181383
resolver
ensp
ENSP00000400714
resolver
enst
ENST00000439329
resolver
genesymbol
CPB2
resolver
hgnc
HGNC:2300
resolver
uniprot
A0A087WSY5
resolver
uniprot
A8K464
resolver
uniprot
Q15114
resolver
uniprot
Q5T9K1
resolver
uniprot
Q5T9K2
resolver
uniprot
Q9P2Y6
resolver
uniprot_entry
A0A087WSY5_HUMAN
resolver
uniprot_entry
CBPB2_HUMAN
resolver
uniprot_sec
A8K464
resolver
uniprot_sec
Q15114
resolver
uniprot_sec
Q5T9K1
resolver
uniprot_sec
Q5T9K2
resolver
uniprot_sec
Q9P2Y6
resolver
activity_regulation
ACTIVITY 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. {ECO:0000269|PubMed:18559974}.
uniprot
proteins
amino_acid_sequence
MKLCSLAVLVPIVLFCEQHVFAFQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTADLIVKKKQVHFFVNASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYYEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQAAKNAIWIDCGIHAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPVVNVDGYDYSWKKNRMWRKNRSFYANNHCIGTDLNRNFASKHWCEEGASSSSCSETYCGLYPESEPEVKAVASFLRRNINQIKAYISMHSYSQHIVFPYSYTRSKSKDHEELSLVASEAVRAIEKISKNTRYTHGHGSETLYLAPGGGDDWIYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRNV
uniprot
proteins
ec_number
3.4.17.20
uniprot
proteins
function
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. {ECO:0000269|PubMed:10574983}.
uniprot
proteins
mass_dalton
48424
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. N-glycan at Asn-108: Hex5HexNAc4. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16445295, ECO:0000269|PubMed:18559974, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}.
uniprot
proteins
protein_family
Peptidase M14 family
uniprot
proteins
pubmed
10574983
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16445295
uniprot
proteins
pubmed
18559974
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
1939207
uniprot
proteins
pubmed
20088943
uniprot
proteins
pubmed
22171320
uniprot
proteins
sequence_length
423
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted.
uniprot
proteins