+ |
PCSK2 | up-regulates activity
cleavage
|
IAPP |
0.478 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261791 |
Arg33 |
ESHQVEKrKCNTATC |
in vitro |
|
pmid |
sentence |
10931181 |
The processing of proinsulin to insulin occurs in the secretory granules at the C-terminal end of pairs of basic amino acids, Arg31-Arg32 and Lys64-Arg65 [9,10]. Following cleavage, by the prohormone convertases, PC3 (also known as PC1) and PC2, the pair of basic amino acids are removed rapidly by carboxypeptidase E (CPE) to produce the mature insulin molecule |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PCSK2 | down-regulates quantity
cleavage
|
OXT |
0.269 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270328 |
|
|
Homo sapiens |
Hypophysis |
pmid |
sentence |
11690596 |
Oxytocin-extended form is further cleaved by enzymatic activity to yield the nine-amino-acid active peptide, OT. The proteolysis may involve several pro-hormone convertases, convertase 2 (PC2) (20p11-1-11.2) and convertase 5 (PC5) (9q21.3) (Gabreels et al 1998). Both enzymes are found in OT neurosecretory vesicles and are a part of a family of subtilisen/kexinlike convertases (Seidah et al 1994). It is a product of the OT gene located at human gene locus 20p13 (Rao et al 1992). The processing cascade results in the production of neurophysin I and OT extended form (OT-X), which is OT with a C-terminal, three-amino-acid extension. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Oxytocin signaling |
+ |
PCSK2 | up-regulates quantity
cleavage
|
Oxytocin |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270335 |
|
|
Homo sapiens |
Hypophysis |
pmid |
sentence |
11690596 |
Oxytocin-extended form is further cleaved by enzymatic activity to yield the nine-amino-acid active peptide, OT. The proteolysis may involve several pro-hormone convertases, convertase 2 (PC2) (20p11-1-11.2) and convertase 5 (PC5) (9q21.3) (Gabreels et al 1998). Both enzymes are found in OT neurosecretory vesicles and are a part of a family of subtilisen/kexinlike convertases (Seidah et al 1994). It is a product of the OT gene located at human gene locus 20p13 (Rao et al 1992). The processing cascade results in the production of neurophysin I and OT extended form (OT-X), which is OT with a C-terminal, three-amino-acid extension. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Oxytocin signaling |
+ |
EGR1 | up-regulates quantity by expression
transcriptional regulation
|
PCSK2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253896 |
|
|
Homo sapiens |
|
pmid |
sentence |
9359835 |
we show that the transcription factor EGR-1 interacts with two distinct elements within the proximal human PC2 promoter region. Transfection experiments also demonstrate that EGR-1 is able to enhance PC2 promoter activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PCSK2 | up-regulates quantity
cleavage
|
Neurophysin 1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270337 |
|
|
Homo sapiens |
Hypophysis |
pmid |
sentence |
11690596 |
Oxytocin-extended form is further cleaved by enzymatic activity to yield the nine-amino-acid active peptide, OT. The proteolysis may involve several pro-hormone convertases, convertase 2 (PC2) (20p11-1-11.2) and convertase 5 (PC5) (9q21.3) (Gabreels et al 1998). Both enzymes are found in OT neurosecretory vesicles and are a part of a family of subtilisen/kexinlike convertases (Seidah et al 1994). It is a product of the OT gene located at human gene locus 20p13 (Rao et al 1992). The processing cascade results in the production of neurophysin I and OT extended form (OT-X), which is OT with a C-terminal, three-amino-acid extension. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Oxytocin signaling |
+ |
PCSK2 | up-regulates quantity
cleavage
|
Corticotropin |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268725 |
|
|
|
|
pmid |
sentence |
24631756 |
POMC is post-translationally cleaved by prohormone convertase enzymes 1 and 2 (PC1, PC2) into ACTH, an N-terminal glycopeptide |
|
Publications: |
1 |