Phosphotyrosine binding domain
WebPhosphotyrosine-binding domains in signal transduction. Protein phosphorylation provides molecular control of complex physiological events within cells. In many cases, … WebDec 19, 2014 · SH2D5 is a mammalian-specific, uncharacterized adaptor-like protein that contains an N-terminal phosphotyrosine-binding domain and a C-terminal Src homology 2 (SH2) domain. We show that SH2D5 is highly enriched in adult mouse brain, particularly in Purkinjie cells in the cerebellum and the cornu amm …
Phosphotyrosine binding domain
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WebNumb is a membrane-associated, phosphotyrosine binding (PTB) domain-containing protein that functions as an intrinsic determinant of cell fate during Drosophila development. We … WebAll three SHC1 proteins share the same domain arrangement consisting of an N-terminal phosphotyrosine-binding(PTB) domain and a C-terminal Src-homology2(SH2) domain. Both of the domains for the three proteins can bind to tyrosine-phosphorylated proteins but they are different in their phosphopeptide-binding specificities.
WebFeb 3, 2005 · The C2 domain of PKCdelta is a phosphotyrosine binding domain. In this issue of Cell, report that the C2 domain of the serine/threonine protein kinase Cdelta is a … WebMar 5, 2024 · Conserved Domains (3) summary cd07631 Location: 20 → 234 BAR_APPL1; The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing 1 cd13158 Location: 490 → 625
WebAug 7, 1998 · EGFR binding of Shc proteins results in their tyrosine phosphorylation and subsequent activation of the Ras and Erk pathways. Shc interaction with activated … WebSeveral other PI domains have been identified that may also have binding specificity for the NPXY motif. The terminology used at present to define these domains is unclear. The …
WebNov 17, 1995 · This leads to the incorporation of MA molecules into virus cores, and subsequently into uncoated viral nucleoprotein complexes. A direct interaction between …
WebThe F3 subdomain is a sandwich of two orthogonal antiparallel β sheets followed by an α helix; this fold is found in a number of structures, including the phosphotyrosine-binding (PTB) 1 and pleckstrin homology domains. In this study, we have localized a principal integrin β tail-binding site of talin to the predicted 96-residue PTB-like ... truth and reconciliation day a stat holidayWebThe Phosphotyrosine Binding (PTB) domain is one of the recently described domains involved in protein-protein interactions. truth and reconciliation day calgaryIn molecular biology, Phosphotyrosine-binding domains are protein domains which bind to phosphotyrosine. The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to … See more APBA1; APBA2; APBA3; APPL1; EPS8; EPS8L1; EPS8L2; EPS8L3; TENC1; TNS; TNS1; TNS3; TNS4; DOK1; DOK2; DOK3; DOK4; DOK5; DOK6; DOK7; FRS2; FRS3; IRS1; IRS2; IRS4; NOS1AP; TLN1; TLN2 See more • SH2 domains also bind phosphorylated tyrosines See more • Eukaryotic Linear Motif resource motif class LIG_PTB_Phospho_1 See more philips cpap masks wispWebJun 11, 2014 · Hakai acts through its phosphotyrosine-binding (HYB) domain, which bears a dimeric fold that recognizes the phosphotyrosine motifs of E-cadherin, cortactin, DOK1, … truth and reconciliation day bc 2022WebOct 6, 2006 · The RET receptor tyrosine kinase is important for several different biological functions during development. The recruitment at the phosphorylated Tyr1062 site in RET of a number of different … truth and reconciliation day 2023 statWebAug 17, 2024 · Bound to the intracellular juxtamembrane region of each FGFR chain is the phosphotyrosine-binding (PTB) domain of FGF receptor substrate 2α (FRS2α). philips cpap recall cancer typeWebDec 7, 1995 · The PTB domain is structurally similar to pleckstrin homology domains (a β-sandwich capped by an α-helix) and binds to acidic phospholipids, suggesting a possible … philips cpap penrith