+ |
C1RL | up-regulates activity
cleavage
|
HP |
0.383 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256358 |
Arg161 |
NPANPVQrILGGHLD |
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
15385675 |
We demonstrate that coexpression of the proform of Hp (proHp) and C1r-LP in COS-1 cells effected cleavage of proHp in the endoplasmic reticulum. This cleavage depended on proteolytic activity of C1r-LP because mutation of the putative active-site Ser residue abolished the reaction. Furthermore, incubation of affinity-purified C1r-LP and proHp led to the cleavage of the latter protein. ProHp appeared to be cleaved at the expected site because substitution of Gly for Arg-161 blocked the reaction. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
HP | down-regulates quantity
binding
|
HBB |
0.764 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251815 |
|
|
Homo sapiens |
|
pmid |
sentence |
9315856 |
Haptoglobin forms a complex of extremely high affinity with Hb via a well-characterized globin site. Our results show that upon Hb-haptoglobin binding, the globin radical, loses its ability to be terminated by forming globin dimers. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HP | form complex
binding
|
hb:hp |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255283 |
|
|
Homo sapiens |
|
pmid |
sentence |
11854029 |
CD163 was identified as the endocytic receptor binding hemoglobin (Hb) in complex with the plasma protein haptoglobin (Hp). This specific receptor-ligand interaction leading to removal from plasma of the Hp-Hb complex-but not free Hp or Hb-now explains the depletion of circulating Hp in individuals with increased intravascular hemolysis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HP | up-regulates quantity by stabilization
binding
|
APOA1 |
0.723 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252106 |
|
|
Homo sapiens |
|
pmid |
sentence |
17824618 |
Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase. haptoglobin, when circulating at enhanced levels with free Hb during the acute phase of inflammation, might protect ApoA-I structure and function against hydroxyl radicals. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HP | down-regulates quantity
binding
|
HBA1 |
0.734 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251816 |
|
|
Homo sapiens |
|
pmid |
sentence |
9315856 |
Haptoglobin forms a complex of extremely high affinity with Hb via a well-characterized globin site. Our results show that upon Hb-haptoglobin binding, the globin radical, loses its ability to be terminated by forming globin dimers. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |