+ |
NME1 | up-regulates
phosphorylation
|
NME1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198667 |
His118 |
QVGRNIIhGSDSVES |
Homo sapiens |
|
pmid |
sentence |
22869372 |
Ndpk catalytic function requires autophosphorylation at the catalytic his-118 residue. the simplest interpretation of these data is that ampk does not directly phosphorylate ndpk-a at ser-120 or ser-122 (or at any other site) but rather enhances ndpk-a autophosphorylation at his-118. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Lung |
+ |
CDK1 | up-regulates
phosphorylation
|
NME1 |
0.269 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160493 |
Ser120 |
GRNIIHGsDSVESAE |
Homo sapiens |
|
pmid |
sentence |
18234856 |
Application of this approach to the discovery of cdk1-cyclin b substrates yielded identification of >70 substrates and phosphorylation sites. Many of these sites are known to be phosphorylated in vivo, but most of the proteins have not been characterized as cdk1-cyclin b substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 |
phosphorylation
|
NME1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250300 |
Ser120 |
GRNIIHGsDSVESAE |
in vitro |
|
pmid |
sentence |
8810265 |
For autophosphorylated rNm23-H1, phosphorylation was observed at serine 44 and on a fragment containing serines 120, 122, and 125.The biochemical function of Nm23 serine phosphorylation is unknown. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250301 |
Ser122 |
NIIHGSDsVESAEKE |
in vitro |
|
pmid |
sentence |
8810265 |
For autophosphorylated rNm23-H1, phosphorylation was observed at serine 44 and on a fragment containing serines 120, 122, and 125.The biochemical function of Nm23 serine phosphorylation is unknown. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250198 |
Ser125 |
HGSDSVEsAEKEIGL |
in vitro |
|
pmid |
sentence |
8810265 |
For autophosphorylated rNm23-H1, phosphorylation was observed at serine 44 and on a fragment containing serines 120, 122, and 125.The biochemical function of Nm23 serine phosphorylation is unknown. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
CyclinB/CDK1 | up-regulates
phosphorylation
|
NME1 |
0.275 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-216825 |
Ser120 |
GRNIIHGsDSVESAE |
Homo sapiens |
|
pmid |
sentence |
18234856 |
Application of this approach to the discovery of cdk1-cyclin b substrates yielded identification of >70 substrates and phosphorylation sites. Many of these sites are known to be phosphorylated in vivo, but most of the proteins have not been characterized as cdk1-cyclin b substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 |
phosphorylation
|
KSR1 |
0.56 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250299 |
Ser406 |
TRLRRTEsVPSDINN |
in vitro |
|
pmid |
sentence |
12105213 |
Mutation of Ser392 to alanine consistently reduced Nm23-H1 phosphorylation, confirming it as a site of Nm23-H1 kinase activity The unique phosphorylation pattern of KSR by Nm23-H1 will be the subject of further investigation to determine its effects on KSR protein binding, subcellular localization, response to various signals, etc. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
NME1 | down-regulates
phosphorylation
|
KSR1 |
0.56 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-90390 |
Ser406 |
TRLRRTEsVPSDINN |
Homo sapiens |
|
pmid |
sentence |
12105213 |
Autophosphorylated recombinant nm23-h1 phosphorylated ksr in vitro. Using site-directed mutagenesis, we found that nm23-h1 phosphorylated ksr serine 392, a 14-3-3-binding site, consistent with the recent identification of c-tak1 as a kinase for this site. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | up-regulates activity
phosphorylation
|
NME1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250303 |
Ser44 |
GLKFMQAsEDLLKEH |
Homo sapiens |
MCF-7 Cell |
pmid |
sentence |
8245015 |
An acid-stable (nonhistidine) phosphorylation was identified on autophosphorylated purified recombinant Nm23 proteins and [32P]orthophosphate-labeled human breast carcinoma and murine melanoma Nm23. Phosphoamino acid analysis identified serine as the acid-stable phosphorylation and serine 44 as the major site of phosphorylation. The biological relevance of the novel phosphorylation identified herein is suggested by the direct correlation of in vivo Nm23 acid-stable phosphorylation levels, but not Nm23 NDPK activity, with suppression of tumor metastatic potential among control and nm23-1 transfected murine melanoma cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
MET |
0.336 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255164 |
|
|
Homo sapiens |
MDA-MB-435 Cell |
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
LPAR1 |
0.416 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255163 |
|
|
Homo sapiens |
MDA-MB-435 Cell |
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
NETO2 |
0.26 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255166 |
|
|
Homo sapiens |
|
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SET | down-regulates
binding
|
NME1 |
0.717 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-99205 |
|
|
Homo sapiens |
|
pmid |
sentence |
12628186 |
Tumor suppressor nm23-h1 is a granzyme a-activated dnase during ctl-mediated apoptosis, and the nucleosome assembly protein set is its inhibitor. / nm23-h1 binds to set and is released from inhibition by gzma cleavage of set. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
SMO |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255168 |
|
|
Homo sapiens |
MDA-MB-435 Cell |
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
L1CAM |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255161 |
|
|
Homo sapiens |
|
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
MMP2 |
0.337 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255165 |
|
|
Homo sapiens |
MDA-MB-435 Cell |
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
PTN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255167 |
|
|
Homo sapiens |
MDA-MB-435 Cell |
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
FZD1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255162 |
|
|
Homo sapiens |
MDA-MB-435 Cell |
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
CCN2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255160 |
|
|
Homo sapiens |
|
pmid |
sentence |
17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |