| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| The human HS 1 gene ( HCLS 1 , hematopoietic cell specific Lyn substrate 1 ) expressed in human hematopoietic cells encodes a major substrate of protein tyrosine kinase , p75HS1 . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| In contrast , doubly autophosphorylated Lyn exhibits reduced activity toward protein substrates such as phospho p50 / HS1 ( hematopoietic lineage cell specific protein ) and p57 / PDI ( protein disulfide isomerase related protein ) , whose multiple sequential / processive phosphorylation relies on the accessibility of the SH 2 domain of the kinase . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| The HS 1 gene is expressed specifically in hematopoietic cells and encodes p75HS1 , which carries both helix turn helix and Src homology 3 motifs . p75HS1 showed rapid tyrosine phosphorylation and association with a Src like kinase , Lyn , after crosslinking of membrane bound IgM . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| We also show that the HS 1 peptide can be used for the specific monitoring of p72syk since neither the two Src related c Fgr and Lyn kinases ( needing a hydrophobic instead of acidic residue at position 1 ) nor CSK appreciably phosphorylate it . . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| The sequential phosphorylation of p50 / HS1 as well as its specific blockage by the HS 1 phosphopeptide is also observable if c Fgr is replaced by two other Src related kinases , namely , Lyn and Fyn , as secondary phosphorylating agents . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| A similar binding pattern was observed with Lyn and HS 1 , but not with Fyn and HS 1 , in which the Fyn SH 2 region associates with HS 1 upon TCR stimulation but the Fyn SH 3 region does not associate with HS 1 regardless of TCR stimulation . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| Here , we show that BCR associated tyrosine kinases Lyn and Syk synergistically phosphorylate HS 1 , and that Tyr 378 and Tyr 397 of HS 1 are the critical residues for its BCR induced phosphorylation . ^^^ Wild type HS 1 , but not the mutant , localized to the nucleus under the synergy of Lyn and Syk . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| In two of five such escapees , alterations in either Syk , HS 1 , and / or Lyn were observed . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| Because HS 1 associates with the p 56 ( lck ) and p 59 ( lyn ) tyrosine kinases in vitro and in vivo , and becomes tyrosine phosphorylated upon various receptor stimulations , our present data suggest that HS 1 mediates linkage between Lck or Lyn and Grb 2 in lymphoid lineage cells . . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| The binding of antigen to the B cell antigen receptor ( BCR ) results in the activation of protein tyrosine kinases ( PTKs ) such as Lyn and Syk , and the phosphorylation of several substrate proteins including HS 1 and SLP 65 . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| We have now identified tyrosine 222 as the HS 1 residue phosphorylated by the Src family protein kinases c Fgr and Lyn , and we show that a truncated form of HS 1 ( HS 1 208 401 ) lacking the N terminal putative DNA binding region and the C terminal Src homology 3 ( SH 3 ) domain is still able to undergo all the steps of sequential phosphorylation as efficiently as full length HS 1 . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| The biochemical characteristics of the proteins ( isoelectric point and relative molecular mass ) obtained and the subsequent use of antibodies that are specific for different cellular proteins confirmed the participation of HS 1 , Vav , Ig alpha , Lyn and Btk in antigen receptor mediated signal transduction . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| HS 1 interacts with Lyn and is critical for erythropoietin induced differentiation of erythroid cells . ^^^ Here we show that the hemopoietic specific protein HS 1 interacted directly with the SH 3 domain of Lyn , via its proline rich region . ^^^ A truncated HS 1 , bearing the Lyn binding domain , was introduced into J2E erythroleukemic cells to determine the impact upon responsiveness to erythropoietin . ^^^ The inability of cells containing the truncated HS 1 to differentiate may be a consequence of markedly reduced levels of Lyn and GATA 1 . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| With the aim of interfering with the signaling pathways mediated by the SH 2 domains of Src like tyrosine kinases , we synthesized a tyrosyl phospho decapeptide , corresponding to the sequence 392 401 of HS 1 protein , which inhibits the secondary phosphorylation of HS 1 protein catalyzed by the Src like kinases c Fgr or Lyn . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| OBJECTIVE : To investigate whether polymorphism ( s ) or mutation ( s ) in the hematopoietic cell specific Lyn substrate 1 ( HS 1 ) gene are involved in the pathogenesis of systemic lupus erythematosus ( SLE ) . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| In contrast , translocation of HS 1 into rafts was normal in a Lyn knock out B cell line , and an HS 1 mutant at the tyrosine residue Tyr 222 targeted by Lyn maintained the ability to partition into rafts upon BCR cross linking . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| Thrombin induced tyrosine phosphorylation of HS 1 in human platelets is sequentially catalyzed by Syk and Lyn tyrosine kinases and associated with the cellular migration of the protein . ^^^ By means of specific inhibitors ( PP 2 , SU 6656 , and piceatannol ) and phosphopeptide specific antibodies , as well as by coimmunoprecipitation and binding competition experiments , we show that Syk acts as the primary kinase that phosphorylates HS 1 at Tyr 397 and that Syk phosphorylation is required for HS 1 interaction with the Lyn SH 2 domain . ^^^ Upon docking to Syk phosphorylated HS 1 , Lyn catalyzes the secondary phosphorylation of the protein at Tyr 222 . ^^^ Once the secondary Tyr phosphorylation of HS 1 is accomplished the protein dissociates from Lyn and undergoes a dephosphorylation process . ^^^ HS 1 Tyr phosphorylation does not occur when thrombin induced actin assembly is inhibited by cytochalasin D even under conditions in which Syk and Lyn are still active . ^^^ |
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| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P14317 and P07948 |
Pubmed |
SVM Score :0.0 |
| NA |
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