Relation Results

Summary

Name SIAH2
Full Name E3 ubiquitin-protein ligase SIAH2
Synonyms Seven in absentia homolog 2, Siah-2, hSiah2
Primary ID O43255
Links - -
Type protein
Relations 11
Function E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:9334332, PubMed:11483518, P ...
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Type: Score: Layout: SPV 
0.4130.20.3650.6160.4360.20.512DYRK2SIAH2MAPK14HIF1ASNCAIPPSMD4Ub:E2AKAP1

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ DYRK2up-regulates img/direct-activation.png phosphorylation SIAH2 0.413
Identifier Residue Sequence Organism Cell Line
SIGNOR-198721 Ser16 PSANKPCsKQPPPQP Homo sapiens
pmid sentence
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis.
Identifier Residue Sequence Organism Cell Line
SIGNOR-198725 Ser28 PQPQHTPsPAAPPAA Homo sapiens
pmid sentence
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis.
Identifier Residue Sequence Organism Cell Line
SIGNOR-198729 Ser68 GGGAGPVsPQHHELT Homo sapiens
pmid sentence
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis.
Identifier Residue Sequence Organism Cell Line
SIGNOR-198733 Thr119 PTCRGALtPSIRNLA Homo sapiens
pmid sentence
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis.
Identifier Residue Sequence Organism Cell Line
SIGNOR-198737 Thr26 PPPQPQHtPSPAAPP Homo sapiens
pmid sentence
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis.
Publications: 5 Organism: Homo Sapiens
+ MAPK14up-regulates img/direct-activation.png phosphorylation SIAH2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-149890 Homo sapiens
pmid sentence
We show that siah2 is subject to phosphorylation by p38 mapk, which increases siah2-mediated degradation of phd3.
Publications: 1 Organism: Homo Sapiens
+ SIAH2up-regulates img/indirect-activation.png HIF1A 0.365
Identifier Residue Sequence Organism Cell Line
SIGNOR-149893 Homo sapiens
pmid sentence
The ring finger ubiquitin ligase siah2 controls the stability of various substrates involved in stress and hypoxia responses, including the phd3, which controls the stability of hif-1alpha
Publications: 1 Organism: Homo Sapiens
+ SIAH2down-regulates img/direct_inhibition.png ubiquitination SNCAIP 0.616
Identifier Residue Sequence Organism Cell Line
SIGNOR-140651 Homo sapiens
pmid sentence
Siah proteins ubiquitylate synphilin-1 and promote its degradation through the ubiquitin proteasome system
Publications: 1 Organism: Homo Sapiens
+ SIAH2down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination PSMD4 0.436
Identifier Residue Sequence Organism Cell Line
SIGNOR-272748 in vitro
pmid sentence
S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes.The short half-life of S5a presumably is because of the presence of the UIM domain and reflects the ubiquitination of free S5a by many E3s.
Publications: 1 Organism: In Vitro
+ Ub:E2up-regulates activity img/direct-activation.png ubiquitination SIAH2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271121 Homo sapiens
pmid sentence
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t
Publications: 1 Organism: Homo Sapiens
+ SIAH2down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination AKAP1 0.512
Identifier Residue Sequence Organism Cell Line
SIGNOR-272641 Homo sapiens HEK-293 Cell
pmid sentence
Seven In-Absentia Homolog 2 (Siah2), an E3-ubiquitin ligase whose expression is induced in hypoxic conditions, formed a complex and degraded AKAP121.
Publications: 1 Organism: Homo Sapiens
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