| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Physical and functional interactions between Cas and c Src induce tamoxifen resistance of breast cancer cells through pathways involving epidermal growth factor receptor and signal transducer and activator of transcription 5b . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| In vivo binding experiments in COS cells showed that binding of Stat 5 to the EpoR was mediated through the Stat 5 Src homology 2 ( SH 2 ) domain . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Our results show that STAT 1 , STAT 3 , and STAT 5 exist in a constitutively phosphorylated state in 5 src transformed 32Dcl3 cells , while such constitutive phosphorylation is not seen in 5 fgr transformed cell lines . ^^^ However , STAT 1 and STAT 5 , which also exist in a constitutively phosphorylated state in 5 src transformed 32Dcl3 cells , do not coimmunoprecipitate with 5 Src , suggesting that these proteins either interact weakly with 5 Src or are phosphorylated by a mechanism distinctive from that of STAT3 . . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Activated Jak 2 then phosphorylates these receptors and thereby recruits various signaling molecules containing the Src homology ( SH ) 2 domain , including Stat 5 , to the tyrosine phosphorylated receptors . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Transcription from STAT 5 responsive gene promoter regions of the beta casein , oncostatin M , and the cytokine inducible Src homology 2 domain containing protein genes was observed . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| We show here that BCR / ABL induces phosphorylation and activation of STAT 5 by a mechanism that requires the BCR / ABL Src homology ( SH ) 2 domain and the proline rich binding site of the SH 3 domain . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| These results suggest that STAT 5 activation by src may occur by a mechanism distinct from that employed in cytokine activation of the JAK / STAT pathway , resulting in the selective nuclear translocation of STAT5B . . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Co expression experiments in insect and mammalian cells demonstrated that both PDGF beta receptor ( PDGF beta R ) and Jak 1 , but not c Src , induced the activation of Stat 5 . ^^^ The role of the cytoplasmic tyrosine kinases in the PDGF induced activation of Stat 5 was further investigated by overexpressing kinase negative ( KN ) and wild type Jak and c Src kinases . ^^^ Jak 1 KN or Jak 2 KN had no effect but both Src KN and wild type c Src similarly decreased the PDGF beta R induced activation of Stat 5 . ^^^ Taken together , these results indicate that Stat 5 is a direct substrate for PDGF beta R and that the activation does not require Jak 1 , Jak 2 , c Src or Fyn tyrosine kinases . . ^^^ The activation of both Src and Stat 5 is dependent on the same tyrosine residues Tyr ( 579 ) and Tyr ( 581 ) in PDGF beta R ; thus the observed inhibition by Src might result from competition for binding of Stat 5 to the receptor . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Among them , cytokine induced Src homology 2 ( SH 2 ) protein ( CIS ) was found to inhibit the interleukin 3 and erythropietin mediated STAT 5 signaling pathway . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Our results show that Src can tyrosine phosphorylate Stat 1 and Stat 3 but not Stat 5 in this system . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Src directly tyrosine phosphorylates STAT 5 on its activation site and is involved in erythropoietin induced signaling pathway . ^^^ Reduction of Src diminished tyrosine phosphorylation of STAT 5 in K 562 cells regardless of EPO treatment . ^^^ The tyrosine phosphorylation level of STAT 5 induced by EPO in F 36P cells was reduced in the presence of PP 1 or PP 2 selective Src inhibitor . ^^^ In addition , the expression of dominant negative Src in F 36P cells reduced the tyrosine phosphorylation of STAT 5 . ^^^ When Src and STAT 5 were co expressed in COS 7 cells , tyrosine phosphorylation of STAT 5 was observed , and tyrosine residue 694 ( Tyr 694 ) of STAT5A was identified as the major phosphorylation site by Src . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| The cytokine inducible src homology 2 ( SH 2 ) proteins , CIS ( cytokine inducible SH 2 domain protein ) and SOCS 3 ( suppressor of cytokine signaling 3 ) , are implicated in the negative regulation of prolactin ( PRL ) receptor mediated activation of signal transducer and activator of transcription 5 ( STAT 5 ) . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Studies on the potential signaling mechanisms demonstrated that in cells expressing inhibitor resistant Bcr Abl mutants , PP 1 and CGP 76030 inhibited the activity of Src family tyrosine kinases and Akt but not signal transducer and activator of transcription 5 ( STAT 5 ) and JUN kinase ( Jnk ) . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| STAT 5 activation induced by diabetic LDL depends on LDL glycation and occurs via src kinase activity . ^^^ Pretreatment with the src kinase inhibitor PP 1 abrogated both STAT 5 activation and the expression of p 21 ( waf ) induced by gly LDL . ^^^ Consistently , gly LDL failed to activate STAT 5 in src ( / ) fibroblasts . ^^^ Collectively , our results provide evidence for the role of glycation in dm LDL mediated effects and for a specific role of src kinase in STAT 5 dependent p 21 ( waf ) expression . . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| The Src family kinase Hck couples BCR / ABL to STAT 5 activation in myeloid leukemia cells . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Bcr Abl constitutively activates several signaling proteins important for the proliferation and survival of myeloid progenitors , including the Src family kinases Hck and Lyn , the Stat 5 transcription factor and upstream components of the Ras / Erk pathway . ^^^ These data implicate the Src kinase family in Stat 5 and Erk activation downstream of Bcr Abl , and identify myeloid specific Src kinases as potential drug targets in CML . . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Further analysis of factor independent mutants with low or undetectable Src activity revealed a constitutive phosphorylation of the common beta chain of the GM CSF receptor and STAT 5 . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| These two STATs are more similar to those of Drosophila , Anopheles , and mammalian STAT 5 in the DNA binding and Src homology 2 domains . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Expression of src homology domain 2 ( SH 2 ) containing tyrosine phosphatase 1 ( SHP 1 ) , phosphorylated Janus kinase 2 ( p JAK 2 ) , and phosphorylated signal transducer and activator of transcription 5 ( p STAT 5 ) was assessed with Western blot analysis . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Studies of signaling pathways downstream of Bcr Abl demonstrated that the addition of MPA to imatinib reduced the phosphorylation of both Stat 5 and Lyn , a Src kinase family member . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Stat 5 is activated by a broad spectrum of cytokines , as well as non receptor tyrosine kinases , such as Src . ^^^ In this study , the DNA binding properties of the two closely related Stat 5 proteins , Stat5a and Stat5b , induced either by prolactin ( Prl ) or by Src were analyzed by electrophoretic mobility shift assays using several different Stat 5 binding sites . ^^^ Src induced Stat5b DNA binding complexes consistently displayed a slightly faster mobility than those induced by Prl , as well as differences in their ability to be supershifted by anti Stat 5 antibodies . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| TGF beta did not impair proximal signaling by Shc or STAT 5 , and induction of some downstream genes , including cytokine inducible Src homology 2 containing protein ( CIS ) , bcl 10 ( L ) , and bcl 2 , was spared . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Co immunoprecipitation analysis demonstrated interaction between c Src and STATs 3 or 5 and EGFR in SCCHN cells , but no heterodimerization was detected between STAT 3 and STAT 5 . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Two Tyr ( P ) null ( but Jak 2 coupled ) EpoR forms each retained < or=25 % of the wild type activity , whereas the add back of single Tyr ( P ) sites in the EpoR forms EE T Y 343 ( Stat 5 binding site ) , EE Y 479 ( p85 / phosphatidylinositol 3 kinase binding site ) , or EE Y 464 ( Src kinase binding site ) significantly enhanced activities ( to 100 , 95 , and 50 % of EE WT ( wild type ) levels , respectively ) . ^^^ Despite specific connection of EE T Y 343 to Stat 5 , the contributions of Kit to EpoR dependent proliferation did not involve Kit effects on Stat 5 activation ( but was limited by the mutation of Kit Tyr ( P ) 567 and Tyr ( P ) 569 Src kinase recruitment sites ) . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| B cell receptor engagement in SLP 65 deficient B cell lymphoma cells also resulted in tyrosine phosphorylation of the proliferation and survival related MAPK 1 and STAT 5 molecules , which was sensitive to silencing of the SRC kinase LYN . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Stem cell factor synergistically enhances thrombopoietin induced STAT 5 signaling in megakaryocyte progenitors through JAK 2 and Src kinase . ^^^ Signal transduction pathways that might synergize in TPO mediated STAT 5 transactivation were analyzed using specific pharmacological inhibitors and indicated an essential role for Janus activated kinase 2 ( JAK 2 ) and a partial role for Src family kinases . ^^^ In addition , the Src kinase inhibitor SU 6656 partially downregulated the additional effect of SCF costimulation on STAT 5 tyrosine phosphorylation . ^^^ SCF induced enhancement of JAK 2 phosphorylation was not affected by inhibition of Src kinase , suggesting that both JAK 2 and Src kinase mediate STAT 5 tyrosine phosphorylation . ^^^ Synergistic activation of JAK 2 and Src kinase may thus contribute to the enhanced STAT 5 signaling in the presence of TPO and SCF . . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| In contrast , the Src kinase inhibitor PP 1 significantly abolishes STAT 5 dependent transcription in Trk A expressing 293T cells and in BDNF treated primary cortical neurons . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| GM CSF induced phosphorylation of Jak 2 , Stat 5 , Hck ( the myeloid restricted Src kinase ) , Akt , Stat 3 , and Erk MAPKs in microglia . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Gab 2 is persistently tyrosine phosphorylated in Ba / F3 cells expressing caSTAT 5 ( constitutively activated STAT 5 ) , independent of JAK 2 ( Janus kinase 2 ) activation where it interacts with STAT 5 , p 85 and Grb 2 , but not with Shp 2 [ SH 2 ( Src homology 2 ) domain containing tyrosine phosphatase ] proteins . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Overexpression of c Src did not prevent suppression of STAT 5 activity by E 2 and ERalpha . ^^^ However , ERalpha did prevent basal increases in STAT 5 activity with overexpressed c Src . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| It has been shown that Src homology 2 ( SH 2 ) containing tyrosine phosphatase 1 attenuates the intensity of G CSF induced Stat 5 activation through interacting with the carboxy terminus of the G CSF R . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Treatment with the selective Src family inhibitor pyrazolopyrimidine PP 2 prevented STAT 5 phosphorylation at Tyr 694 , nuclear translocation of STAT 5 and the STAT 5 DNA complex formation . ^^^ Our results demonstrate , for the first time , that stimulation with Col 4 induces STAT 5 phosphorylation of endogenous STAT 5 at Tyr 694 , nuclear translocation of STAT 5 and increases in STAT 5 DNA binding activity via a Src dependent pathway in MCF 7 cells . . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| STAT 5 phosphorylation in malignant melanoma is important for survival and is mediated through SRC and JAK 1 kinases . ^^^ The investigation of the underlying mechanism revealed specific STAT 5 activation by recombinant human epidermal growth factor ( rEGF ) . rEGF induced activation of STAT 5 occurred in vitro through the non receptor tyrosine kinases transforming gene ( src ) of Rous Sarcoma virus and Janus kinase 1 . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| STAT 5 activation appeared to be regulated by Janus kinases ( JAKs ) and SRC family kinases ( SFKs ) , since inhibitors of these kinases inhibited the localization of STAT 5 proteins to the nucleus . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| In addition , reduced expression of tyrosine phosphatase , Src homology region 2 domain containing phosphatase 1 , and decreased total phosphatase activity in EryPs partly explain the persistent activation of STAT 5 . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| SH 2 Bbeta ( R555E ) with a defective Src homology 2 domain was unable to stimulate JAK 2 and JAK 2 mediated tyrosyl phosphorylation of Stat5B and Stat 3 . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| STAT5b inhibition was not reversed by overexpression of the heterodimerization partner of PPAR ( retinoid 10 receptor ) or the nuclear receptor coactivators P 300 and SRC 1 , suggesting that STAT5b does not inhibit PPARalpha by competing for these limiting cellular cofactors . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| Previously , we reported that whereas both signal transducers and activators of transcription ( STAT ) 5A and STAT5B can be activated with respect to tyrosine phosphorylation and DNA binding potential by Src kinase , only STAT5B was translocated to the nucleus , where it presumably activates unique downstream responses . ^^^ To help elucidate the functional consequences of STAT5B activation by 5 src , the properties of stably transfected NIH 3T3 cells containing both an intact and a dominant negative , COOH terminal truncated isoform of STAT5B were investigated . ^^^ STAT5B enhanced the transforming potential of 5 Src as reflected by both an increase in focus formation and growth in soft agar . ^^^ STAT5B also enhanced 5 Src induced cell cycle progression and cell motility in NIH 3T3 cells . ^^^ Furthermore , the dominant negative , COOH terminal truncated isoform of STAT5B was able to partially suppress 5 Src mediated cell transformation . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| STAT5b , a Mediator of Synergism between c Src and the Epidermal Growth Factor Receptor . ^^^ Here , we investigate the contribution of the signal transducers and activators of transcription ( STAT5b ) in the signaling pathways regulated by EGFR and c Src overexpression in human breast tumor cell lines as well as in a mouse fibroblast model ( C3H10T1 / 2 ) . ^^^ We demonstrate that 1 ) activation of STAT5b by EGF requires overexpression of the EGFR , 2 ) co overexpression of c Src alone does not result in EGF induced activation of STAT5b but enhances that seen in EGFR overexpressing cells , and 3 ) EGF induced tyrosine phosphorylation of STAT5b requires Tyr ( 845 ) of the EGFR . ^^^ Furthermore , the stable overexpression of a kinase defective c Src in the context of EGFR overexpression results in a decrease in the tyrosine phosphorylation of STAT5b in response to EGF and a more dramatic decrease in EGF induced transcriptional activation of STAT5b , suggesting an integral role for c Src in the physiological actions of STAT5b . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| EGF receptor mediated , c Src dependent , activation of Stat5b is downregulated in mitogenically responsive hepatocytes . ^^^ The Src tyrosine kinase inhibitor CGP 77675 blocked the EGF induced activation of Stat5b , but did not affect the Stat5b activation by growth hormone ( GH ) or prolactin ( PRL ) . ^^^ The results show that EGF induces tyrosine phosphorylation and DNA binding activity of Stat5b in a manner different from GH and PRL , apparently by a Src dependent mechanism . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| However , the Src family of nonreceptor kinases [ constitutively active 5 src and epithelial growth factor induced c src ] tyrosine phosphorylated STAT5b ( A630P ) . ^^^ The 5 src induced phospho STAT5b ( A630P ) translocated to the nucleus but , unlike wild type Stat5b , was unable to bind DNA . ^^^ CONCLUSIONS : The A630P mutation disrupts the src homology 2 architecture such that : 1 ) mutant STAT5b most likely can not dock to phospho tyrosines on ligand activated receptors ; and 2 ) stable interactions with DNA are prevented . ^^^ |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P51692 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|