| + |
CSNK2A2 | up-regulates activity 
phosphorylation
|
PTPRC |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251032 |
Ser1001 |
SKESEHDsDESSDDD |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 10066810 |
Mutational analysis of CK2 consensus sites showed that the target for CK2 was in an acidic insert of 19 amino acids in the D2 domain, and Ser to Ala mutations at amino acids 965, 968, 969, and 973 abrogated CK2 phosphorylation of CD45. CK2 phosphorylation increased CD45 activity 3-fold toward phosphorylated myelin basic protein, and this increase was reversible by PP2A treatment. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251029 |
Ser1004 |
SEHDSDEsSDDDSDS |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 10066810 |
Mutational analysis of CK2 consensus sites showed that the target for CK2 was in an acidic insert of 19 amino acids in the D2 domain, and Ser to Ala mutations at amino acids 965, 968, 969, and 973 abrogated CK2 phosphorylation of CD45. CK2 phosphorylation increased CD45 activity 3-fold toward phosphorylated myelin basic protein, and this increase was reversible by PP2A treatment. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251030 |
Ser1005 |
EHDSDESsDDDSDSE |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 10066810 |
Mutational analysis of CK2 consensus sites showed that the target for CK2 was in an acidic insert of 19 amino acids in the D2 domain, and Ser to Ala mutations at amino acids 965, 968, 969, and 973 abrogated CK2 phosphorylation of CD45. CK2 phosphorylation increased CD45 activity 3-fold toward phosphorylated myelin basic protein, and this increase was reversible by PP2A treatment. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251031 |
Ser1009 |
DESSDDDsDSEEPSK |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 10066810 |
Mutational analysis of CK2 consensus sites showed that the target for CK2 was in an acidic insert of 19 amino acids in the D2 domain, and Ser to Ala mutations at amino acids 965, 968, 969, and 973 abrogated CK2 phosphorylation of CD45. CK2 phosphorylation increased CD45 activity 3-fold toward phosphorylated myelin basic protein, and this increase was reversible by PP2A treatment. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | up-regulates
phosphorylation
|
PTPRC |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65281 |
Ser1001 |
SKESEHDsDESSDDD |
Homo sapiens |
|
| pmid |
sentence |
| 10066810 |
Mutational analysis of ck2 consensus sites showed that the target for ck2 was in an acidic insert of 19 amino acids in the d2 domain, and ser to ala mutations at amino acids 965, 968, 969, and 973 abrogated ck2 phosphorylation of cd45. Ck2 phosphorylation increased cd45 activity 3-fold toward phosphorylated myelin basic protein, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65269 |
Ser1004 |
SEHDSDEsSDDDSDS |
Homo sapiens |
|
| pmid |
sentence |
| 10066810 |
Mutational analysis of ck2 consensus sites showed that the target for ck2 was in an acidic insert of 19 amino acids in the d2 domain, and ser to ala mutations at amino acids 965, 968, 969, and 973 abrogated ck2 phosphorylation of cd45. Ck2 phosphorylation increased cd45 activity 3-fold toward phosphorylated myelin basic protein, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65273 |
Ser1005 |
EHDSDESsDDDSDSE |
Homo sapiens |
|
| pmid |
sentence |
| 10066810 |
Mutational analysis of ck2 consensus sites showed that the target for ck2 was in an acidic insert of 19 amino acids in the d2 domain, and ser to ala mutations at amino acids 965, 968, 969, and 973 abrogated ck2 phosphorylation of cd45. Ck2 phosphorylation increased cd45 activity 3-fold toward phosphorylated myelin basic protein, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65277 |
Ser1009 |
DESSDDDsDSEEPSK |
Homo sapiens |
|
| pmid |
sentence |
| 10066810 |
Mutational analysis of ck2 consensus sites showed that the target for ck2 was in an acidic insert of 19 amino acids in the d2 domain, and ser to ala mutations at amino acids 965, 968, 969, and 973 abrogated ck2 phosphorylation of cd45. Ck2 phosphorylation increased cd45 activity 3-fold toward phosphorylated myelin basic protein, |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PTPRC | down-regulates activity 
dephosphorylation
|
JAK2 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248348 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248349 |
Tyr1008 |
LPQDKEYyKVKEPGE |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248347 |
|
|
Mus musculus |
BMMC Cell |
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255679 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24252238 |
Src homology-2 (SH2) containing tyrosine phosphatase and CD45 tyrosine phosphatase play a major role in modulating JAK-STAT pathway. SH2 containing tyrosine phosphatases include SHP1 and SHP2 (shatterproof 1 & 2). Their SH2 domains allow attachment to the phospho-tyrosine residues present on activated receptors, JAKs or STAT proteins, leading to dephosphorylation of the substrates. |
|
| Publications: |
4 |
Organism: |
Mus Musculus, Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML |
| + |
PTPRC | down-regulates activity
dephosphorylation
|
JAK1 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248355 |
Tyr1034 |
AIETDKEyYTVKDDR |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248356 |
Tyr1035 |
IETDKEYyTVKDDRD |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
PTPRC | down-regulates activity
dephosphorylation
|
TYK2 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248357 |
Tyr1054 |
AVPEGHEyYRVREDG |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248358 |
Tyr1055 |
VPEGHEYyRVREDGD |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
CSK | up-regulates
phosphorylation
|
PTPRC |
0.482 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-26785 |
Tyr1218 |
MVSTFEQyQFLYDVI |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 7507203 |
Tyrosine phosphorylation of cd45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
PTPRC | up-regulates activity
dephosphorylation
|
SKAP1 |
0.367 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248360 |
Tyr232 |
EEEKEETyDDIDGFD |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 11909961 |
Mutational analysis demonstrated the pivotal role of Tyr-232 in SKAP55 in the association with CD45. In Jurkat cells, anti-CD3 antibody stimulation promoted SKAP55 tyrosine phosphorylation and translocation from the cytoplasm to the membrane. Overexpression of SKAP55 in these cells induced transcriptional activation of the IL-2 promoter, while mutant SKAP55-Y232F totally suppressed the promoter activity. Furthermore, overexpression of SKAP55-Y232F also caused the tyrosine hyperphosphorylation of Fyn with a decreased kinase activity. Thus, SKAP55 is an essential adapter to couple CD45 with the Src family kinases for dephosphorylation and, thus, positively regulates TCR signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRC | down-regulates activity
dephosphorylation
|
LCK |
0.79 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248351 |
Tyr394 |
RLIEDNEyTAREGAK |
Homo sapiens |
|
| pmid |
sentence |
| 11259588 |
Importantly, and in disagreement with the model that CD45 only activates Lck in vivo, the kinase activity of Lck from cells lacking CD45 was substantially increased. These results support a model in which CD45 dephosphorylates both Tyr505 and Tyr394, the net effect in normal thymocytes being a decrease in enzymatic activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
PTPRC | down-regulates activity
dephosphorylation
|
LYN |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248353 |
Tyr397 |
RVIEDNEyTAREGAK |
Mus musculus |
B-lymphocyte |
| pmid |
sentence |
| 10415030 |
CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells.| Phosphoamino acid analysis confirmed that Lyn is tyrosine phosphorylated with little serine or threonine phosphorylation. In CD45-negative cells, two bands at 8.2 and 4.1 kDa were phosphorylated in the absence of B cell Ag receptor (BCR) ligation. The 8.2-kDa band corresponded to a fragment containing the positive regulatory site (Tyr397), as assessed by its size and its phosphorylation in an in vitro kinase assay. The 4.1-kDa band was phosphorylated by COOH-terminal Src kinase, suggesting that it contains the COOH-terminal negative regulatory site (Tyr508) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248354 |
Tyr508 |
YTATEGQyQQQP |
Mus musculus |
B-lymphocyte |
| pmid |
sentence |
| 10415030 |
CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells.| Phosphoamino acid analysis confirmed that Lyn is tyrosine phosphorylated with little serine or threonine phosphorylation. In CD45-negative cells, two bands at 8.2 and 4.1 kDa were phosphorylated in the absence of B cell Ag receptor (BCR) ligation. The 8.2-kDa band corresponded to a fragment containing the positive regulatory site (Tyr397), as assessed by its size and its phosphorylation in an in vitro kinase assay. The 4.1-kDa band was phosphorylated by COOH-terminal Src kinase, suggesting that it contains the COOH-terminal negative regulatory site (Tyr508) |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
PTPRC | up-regulates activity
dephosphorylation
|
LCK |
0.79 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248350 |
Tyr505 |
FTATEGQyQPQP |
Homo sapiens |
|
| pmid |
sentence |
| 11259588 |
Importantly, and in disagreement with the model that CD45 only activates Lck in vivo, the kinase activity of Lck from cells lacking CD45 was substantially increased. These results support a model in which CD45 dephosphorylates both Tyr505 and Tyr394, the net effect in normal thymocytes being a decrease in enzymatic activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259933 |
Tyr505 |
FTATEGQyQPQP |
Mus musculus |
T-lymphocyte |
| pmid |
sentence |
| 17719247 |
CD45 differentially regulates the negatively acting pTyr-505 and positively acting pTyr-394 p56(lck) tyrosine kinase phosphorylation sites. We propose that high wild-type CD45 expression is necessary to dephosphorylate p56(lck) pTyr-394, suppressing CD4 T+ cell lineage commitment and hyperactivity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | T cell activation |
| + |
PTPRC | up-regulates activity
dephosphorylation
|
FYN |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248352 |
Tyr531 |
FTATEPQyQPGENL |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11909961 |
On the membrane SKAP55, via its phosphorylated Tyr-271, further binds the SH2 domain of Fyn to replace the low-affinity bound inhibitory site of the kinase. Consequently, CD45 may have transiently disassociated with the Tyr-232 residue of SKAP55 through dephosphorylation and simultaneously interacted with the released the phosphorylated inhibitory tyrosine residue of Fyn for dephosphorylation, resulting in activation of the Src family kinase Fyn and initiation of TCR-engaged signal transduction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
PTPRC | up-regulates
dephosphorylation
|
JAK1 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87154 |
|
|
Homo sapiens |
B-lymphocyte, RAMOS Cell |
| pmid |
sentence |
| 11994288 |
These negative regulatory effects on ig class switching were concomitant with the ability of cd45 to dephosphorylate the induced phosphorylation of jak1, jak3, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRC | up-regulates
dephosphorylation
|
JAK3 |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87157 |
|
|
Homo sapiens |
B-lymphocyte, RAMOS Cell |
| pmid |
sentence |
| 11994288 |
These negative regulatory effects on ig class switching were concomitant with the ability of cd45 to dephosphorylate the induced phosphorylation of jak1, jak3, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRC | down-regulates activity
dephosphorylation
|
JAK3 |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248359 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AML1-ETO | down-regulates quantity by repression 
transcriptional regulation
|
PTPRC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255686 |
|
|
Mus musculus |
Leukemia Cell |
| pmid |
sentence |
| 22740448 |
Chromosome translocation 8q22;21q22 [t(8;21)] is commonly associated with acute myeloid leukemia (AML), and the resulting AML1-ETO fusion proteins are involved in the pathogenesis of AML. To identify novel molecular and therapeutic targets, we performed combined gene expression microarray and promoter occupancy (ChIP-chip) profiling using Lin(-)/Sca1(-)/cKit(+) cells, the major leukemia cell population, from an AML mouse model induced by AML1-ETO9a (AE9a).CD45, a protein tyrosine phosphatase and a negative regulator of cytokine/growth factor receptor and JAK/STAT signaling, is among those targets. Its expression is substantially down-regulated in leukemia cells. Consequently, JAK/STAT signaling is enhanced. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML |
| + |
PTPRC | down-regulates activity
dephosphorylation
|
PRKCD |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277028 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11124968 |
Taken together, these data indicate that CD45 inhibits PMA dependent PKCdelta activation by impeding PMA dependent PKCdelta tyrosine phosphorylation.|reduction in CD45 expression caused the duration of peak PMA-induced MEK and extracellular signal-regulated kinase (ERK) 1/2 activity to increase from 5 min to 30 min while leading to a 4-fold increase in PMA-dependent PKCdelta activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTPRC
- 
- 