+ |
TTK | up-regulates
phosphorylation
|
HSPA9 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156181 |
Ser65 |
IDLGTTNsCVAVMEG |
Homo sapiens |
|
pmid |
sentence |
17573779 |
Mortalin binds to mps1, and is phosphorylated by mps1 on thr62 and ser65. The phosphorylated mortalin then super-activates mps1 in a feedback manner. Mps1-associated acceleration of centrosome duplication depends on the presence of mortalin and super-activation by the thr62/ser65 phosphorylated mortalin |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156185 |
Thr62 |
VVGIDLGtTNSCVAV |
Homo sapiens |
|
pmid |
sentence |
17573779 |
Mortalin binds to mps1, and is phosphorylated by mps1 on thr62 and ser65. The phosphorylated mortalin then super-activates mps1 in a feedback manner. Mps1-associated acceleration of centrosome duplication depends on the presence of mortalin and super-activation by the thr62/ser65 phosphorylated mortalin |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
HSPA9 | down-regulates activity
binding
|
MVD |
0.349 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265890 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
12646231 |
Mortalin binds to mevalonate pyrophosphate decarboxyl ase in mammalian cell. Mot-2 inactivates MPD resulting in decreased amounts of the steady state Ras protein. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
HSPA9 | form complex
binding
|
TIM23 complex |
0.678 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267693 |
|
|
|
|
pmid |
sentence |
32074073 |
The human TIM23 complex is formed by the core components TIM50 (50), TIM23 (23) and TIM17A/B (17A/B). The sorting elements are TIM21 (21) and ROMO1, and the motor elements include TIM44 (44), PAM18 (18; DNAJC15 and DNAJC19), PAM16 (16; MAGMAS), mtHSP70 (Mortalin) and GrpE. |
|
Publications: |
1 |
+ |
HSPA9 | up-regulates activity
relocalization
|
iron-sulfur cluster |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262131 |
|
|
|
|
pmid |
sentence |
27714045 |
Cluster transfer from ISCU to recipient apoproteins is assisted by a dedicated chaperone/cochaperone (HSPA9/HSC20) system that facilitates cluster release from the primary scaffold ISCU and transfer to recipient apoproteins or to intermediate carriers |
|
Publications: |
1 |