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Search results 501 to 600 out of 635 for Cbl

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Type Details Score
Publication
18602463 | -
First Author: Nonis D
Year: 2008
Journal: Cell Signal
Title: Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking.
Volume: 20
Issue: 10
Pages: 1725-39
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Protein Coding Gene
MGI:104686 | Crkl
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P47941
Organism: Mus musculus/domesticus
Length: 303  
Fragment?: false
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Protein Domain
IPR035771 | CIN85_SH3_2
Type: Domain
Description: CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1), CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins [, , ]. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others []. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This entry represents the second SH3 domain (SH3B) of CIN85. SH3B has been shown to bind Cbl proline-rich peptides and ubiquitin [].
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Protein
D3YV42
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
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Publication
26853145 | J:233034
First Author: Quarato G
Year: 2016
Journal: Mol Cell
Title: Sequential Engagement of Distinct MLKL Phosphatidylinositol-Binding Sites Executes Necroptosis.
Volume: 61
Issue: 4
Pages: 589-601
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Publication
28827318 | -
First Author: Liu S
Year: 2017
Journal: Proc Natl Acad Sci U S A
Title: MLKL forms disulfide bond-dependent amyloid-like polymers to induce necroptosis.
Volume: 114
Issue: 36
Pages: E7450-E7459
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Publication
26337687 | -
First Author: Czabotar PE
Year: 2015
Journal: FEBS J
Title: A tale of two domains - a structural perspective of the pseudokinase, MLKL.
Volume: 282
Issue: 22
Pages: 4268-78
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Protein Domain
IPR014741 | Adaptor_Cbl_EF_hand-like
Type: Domain
Description: Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface.The N-terminal region of Cbl contains a Cbl-type phosphotyrosine-binding (Cbl-PTB) domain, which is composed of three evolutionarily conserved domains: an N-terminal four-helix bundle (4H) domain, an EF hand-like calcium-binding domain, and a divergent SH2-like domain. The calcium-bound EF-hand wedges between the 4H and SH2 domains, and roughly determines their relative orientation. The Cbl-PTB domain has also been named Cbl N-terminal (Cbl-N) or tyrosine kinase binding (TKB) domain [, ].The N-terminal 4H domain contains four long α-helices. The C andD helices in this domain pack against the adjacent EF-hand-like domain, and a highly conserved loop connecting the A and B helices contacts the SH2-like domain. The EF-hand motif is similar to classical EF-hand proteins. The SH2-likedomain retains the general helix-sheet-helix architecture of the SH2 fold, but lacks the secondary β-sheet, comprising β-strands D', E and F, and also a prominent BG loop [].This entry represents the EF hand-like domain.
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Protein Domain
IPR014742 | Adaptor_Cbl_SH2-like
Type: Domain
Description: Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface.The N-terminal region of Cbl contains a Cbl-type phosphotyrosine-binding (Cbl-PTB) domain, which is composed of three evolutionarily conserved domains: an N-terminal four-helix bundle (4H) domain, an EF hand-like calcium-binding domain, and a divergent SH2-like domain. The calcium-bound EF-hand wedges between the 4H and SH2 domains, and roughly determines their relative orientation. The Cbl-PTB domain has also been named Cbl N-terminal (Cbl-N) or tyrosine kinase binding (TKB) domain [, ].The N-terminal 4H domain contains four long α-helices. The C and D helices in this domain pack against the adjacent EF-hand-like domain, and a highly conserved loop connecting the A and B helices contacts the SH2-like domain. The EF-hand motif is similar to classical EF-hand proteins. The SH2-likedomain retains the general helix-sheet-helix architecture of the SH2 fold, but lacks the secondary β-sheet, comprising β-strands D', E and F, and also a prominent BG loop [].This entry represents the SH2-like domain.
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Protein Domain
IPR024159 | Cbl_PTB
Type: Domain
Description: Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface.The N-terminal region of Cbl contains a Cbl-type phosphotyrosine-binding (Cbl-PTB) domain, which is composed of three evolutionarily conserved domains: an N-terminal four-helix bundle (4H) domain, an EF hand-like calcium-binding domain, and a divergent SH2-like domain. The calcium-bound EF-hand wedges between the 4H and SH2 domains, and roughly determines their relative orientation. The Cbl-PTB domain has also been named Cbl N-terminal (Cbl-N) or tyrosine kinase binding (TKB) domain [, ].The N-terminal 4H domain contains four long α-helices. The C and D helices in this domain pack against the adjacent EF-hand-like domain, and a highly conserved loop connecting the A and B helices contacts the SH2-like domain. The EF-hand motif is similar to classical EF-hand proteins. The SH2-likedomain retains the general helix-sheet-helix architecture of the SH2 fold, but lacks the secondary β-sheet, comprising β-strands D', E and F, and also a prominent BG loop [].This entry represents the Cbl-PTB domain.
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Protein Domain
IPR036537 | Adaptor_Cbl_N_dom_sf
Type: Homologous_superfamily
Description: Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface.The N-terminal region of Cbl contains a Cbl-type phosphotyrosine-binding (Cbl-PTB) domain, which is composed of three evolutionarily conserved domains: an N-terminal four-helix bundle (4H) domain, an EF hand-like calcium-binding domain, and a divergent SH2-like domain. The calcium-bound EF-hand wedges between the 4H and SH2 domains, and roughly determines their relative orientation. The Cbl-PTB domain has also been named Cbl N-terminal (Cbl-N) or tyrosine kinase binding (TKB) domain [, ].The N-terminal 4H domain contains four long α-helices. The C and D helices in this domain pack against the adjacent EF-hand-like domain, and a highly conserved loop connecting the A and B helices contacts the SH2-like domain. The EF-hand motif is similar to classical EF-hand proteins. The SH2-likedomain retains the general helix-sheet-helix architecture of the SH2 fold, but lacks the secondary β-sheet, comprising β-strands D', E and F, and also a prominent BG loop [].This entry represents the N-terminal four-helical bundle domain superfamily. This domain can also be found in the N terminus of mammalian MLKL, a pseudokinase essential for TNF-alpha-induced necroptosis []. The four-helical bundle (NB) domain of MLK is involved in oligomerization to facilitate plasma membrane targeting through the low-affinity binding of NB to phosphorylated inositol polar head groups of phosphatidylinositol phosphate (PIP) phospholipids [, ].
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Protein Domain
IPR003153 | Adaptor_Cbl_N_hlx
Type: Domain
Description: Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface.The N-terminal region of Cbl contains a Cbl-type phosphotyrosine-binding (Cbl-PTB) domain, which is composed of three evolutionarily conserved domains: an N-terminal four-helix bundle (4H) domain, an EF hand-like calcium-binding domain, and a divergent SH2-like domain. The calcium-bound EF-hand wedges between the 4H and SH2 domains, and roughly determines their relative orientation. The Cbl-PTB domain has also been named Cbl N-terminal (Cbl-N) or tyrosine kinase binding (TKB) domain [, ].The N-terminal 4H domain contains four long α-helices. The C and D helices in this domain pack against the adjacent EF-hand-like domain, and a highly conserved loop connecting the A and B helices contacts the SH2-like domain. The EF-hand motif is similar to classical EF-hand proteins. The SH2-likedomainretains the general helix-sheet-helix architecture of the SH2 fold, but lacks the secondary β-sheet, comprising β-strands D', E and F, and also a prominent BG loop [].This entry represents the N-terminal four-helical bundle domain.
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Publication
22262777 | -
First Author: Niiro H
Year: 2012
Journal: Blood
Title: CIN85 is required for Cbl-mediated regulation of antigen receptor signaling in human B cells.
Volume: 119
Issue: 10
Pages: 2263-73
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Publication
12177062 | -
First Author: Szymkiewicz I
Year: 2002
Journal: J Biol Chem
Title: CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases.
Volume: 277
Issue: 42
Pages: 39666-72
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Publication
12354621 | -
First Author: Dikic I
Year: 2002
Journal: FEBS Lett
Title: CIN85/CMS family of adaptor molecules.
Volume: 529
Issue: 1
Pages: 110-5
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Publication
20331533 | -
First Author: Havrylov S
Year: 2010
Journal: Traffic
Title: Emerging roles of Ruk/CIN85 in vesicle-mediated transport, adhesion, migration and malignancy.
Volume: 11
Issue: 6
Pages: 721-31
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Protein Domain
IPR037408 | Cbl_PBP2
Type: Domain
Description: Cbl is a member of the LysR transcriptional regulators that comprise the largest family of prokaryotic transcription factor. Cbl shows high sequence similarity to CysB, the LysR-type transcriptional activator of genes involved in sulfate and thiosulfate transport, sulfate reduction, and cysteine synthesis []. In Escherichia coli, the function of Cbl is required for expression of sulfate starvation-inducible (ssi) genes, coupled with the biosynthesis of cysteine from the organic sulfur sources (sulfonates). The ssi genes include the ssuEADCB and tauABCD operons encoding uptake systems for organosulfur compounds, aliphatic sulfonates, and taurine []. The genes in these operons encode an ABC-type transport system required for uptake of aliphatic sulfonates and a desulfonation enzyme. Both Cbl and CysB require expression of the tau and ssu genes. Like many other members of the LTTR family, the Cbl is composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor []. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2).The PBP2 are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate- binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction [, , ].
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Publication
11162497 | J:66945
First Author: Fiore F
Year: 2001
Journal: Biochem Biophys Res Commun
Title: Characterization of the mouse Cblc/Cbl3 gene.
Volume: 280
Issue: 1
Pages: 182-7
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Protein Coding Gene
MGI:104580 | Rapgef1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098211 | Pik3cd
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:99147 | Yes1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
O35904
Organism: Mus musculus/domesticus
Length: 1043  
Fragment?: false
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Protein
Q04736
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
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Protein
Q3UHC1
Organism: Mus musculus/domesticus
Length: 1224  
Fragment?: false
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Publication
11230129 | -
First Author: Albrecht V
Year: 2001
Journal: EMBO J
Title: The NAF domain defines a novel protein-protein interaction module conserved in Ca2+-regulated kinases.
Volume: 20
Issue: 5
Pages: 1051-63
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Publication
15539077 | -
First Author: Sutcliffe IC
Year: 2004
Journal: FEMS Microbiol Rev
Title: Lipoproteins of Mycobacterium tuberculosis: an abundant and functionally diverse class of cell envelope components.
Volume: 28
Issue: 5
Pages: 645-59
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Publication
31471317 | -
First Author: Melly GC
Year: 2019
Journal: J Biol Chem
Title: Structural and functional evidence that lipoprotein LpqN supports cell envelope biogenesis in Mycobacterium tuberculosis.
Volume: 294
Issue: 43
Pages: 15711-15723
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Publication
30118676 | -
First Author: Eoh H
Year: 2018
Journal: Mol Cell
Title: Bacterial Protein Reshapes Host Defense toward Antiviral Responses.
Volume: 71
Issue: 4
Pages: 483-484
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Protein Domain
IPR019674 | Lipoprotein_LpqN/LpqT-like
Type: Family
Description: This protein is conserved in Mycobacteriaceae and is likely to be a lipoprotein []. lpqN is involved in cell envelope lipid changes during biofilm maturation. It interacts with periplasmic loop domains of the MmpL3 and MmpL11 transporters that export mycolic acid-containing cell envelope lipids. It also interacts with secreted cell envelope biosynthetic enzymes such as Ag85A []. It has been shown to interact with host CBL, a host ubiquitin ligase, and probably blocks the normal functions of CBL and disturbs CBL-mediated antibacterial activity [].This entry also includes LpqT and Mtc28. Their function is not clear.
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Protein Domain
IPR015130 | Lys-AminoMut_A
Type: Domain
Description: This domain is found in proteins involved in the 1,2 rearrangement of the terminal amino group of DL-lysine and of L-beta-lysine, using adenosylcobalamin (AdoCbl) and pyridoxal-5'-phosphate as cofactors. The structure is predominantly a PLP-binding TIM barrel domain, with several additional α-helices and β-strands at the N and C termini. These helices and strands form an intertwined accessory clamp structure that wraps around the sides of the TIM barrel and extends up toward the Ado ligand of the Cbl cofactor, providing most of the interactions observed between the protein and the Ado ligand of the Cbl, suggesting that its role is mainly in stabilising AdoCbl in the precatalytic resting state.
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Protein Domain
IPR037086 | Lys-AminoMut_asu_sf
Type: Homologous_superfamily
Description: This domain superfamily is found in proteins involved in the 1,2 rearrangement of the terminal amino group of DL-lysine and of L-beta-lysine, using adenosylcobalamin (AdoCbl) and pyridoxal-5'-phosphate as cofactors. The structure is predominantly a PLP-binding TIM barrel domain, with several additional α-helices and β-strands at the N and C termini. These helices and strands form an intertwined accessory clamp structure that wraps around the sides of the TIM barrel and extends up toward the Ado ligand of the Cbl cofactor, providing most of the interactions observed between the protein and the Ado ligand of the Cbl, suggesting that its role is mainly in stabilising AdoCbl in the precatalytic resting state.
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Publication
21863050 | J:176241
First Author: Lipkowitz S
Year: 2011
Journal: Nat Rev Cancer
Title: RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis.
Volume: 11
Issue: 9
Pages: 629-43
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Publication
18769463 | -
First Author: Jozic D
Year: 2008
Journal: Nat Struct Mol Biol
Title: Reply to "The binding stoichiometry of CIN85 SH3 domain A and Cbl-b".
Volume: 15
Issue: 9
Pages: 891-2
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Protein Domain
IPR035770 | CIN85_SH3_1
Type: Domain
Description: CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1), CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins [, , ]. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others []. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This entry represents the first SH3 domain (SH3A) of CIN85; SH3A binds to internal proline-rich motifs within the proline-rich region. This intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. SH3A has also been shown to bind ubiquitin and to an atypical PXXXPR motif at the C terminus of Cbl and the cytoplasmic end of the cell adhesion protein CD2 [].
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Protein Coding Gene
MGI:88508 | Crk
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:99515 | Syk
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:109277 | Pik3r3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P48025
Organism: Mus musculus/domesticus
Length: 629  
Fragment?: false
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Protein
Q64010
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: false
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Protein
Q64143
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: false
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Publication
10506196 | -
First Author: van Der Ploeg JR
Year: 1999
Journal: J Biol Chem
Title: The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl.
Volume: 274
Issue: 41
Pages: 29358-65
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Publication
11402167 | -
First Author: Guo Y
Year: 2001
Journal: Plant Cell
Title: Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance.
Volume: 13
Issue: 6
Pages: 1383-400
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Protein Domain
IPR018451 | NAF/FISL_domain
Type: Domain
Description: The NAF domain is a 24 amino acid domain that is found in a plant-specific subgroup of serine-threonine protein kinases (CIPKs), that interact with calcineurin B-like calcium sensor proteins (CBLs). Whereas the N-terminal part of CIPKs comprises a conserved catalytic domain typical of Ser-Thr kinases, the much less conserved C-terminal domain appears to be unique to this subgroup of kinases. The only exception is the NAF domain that forms an 'island of conservation' in this otherwise variable region. The NAF domain has been named after the prominent conserved amino acids Asn-Ala-Phe. It represents a minimum protein interaction module that is both necessary and sufficient to mediate the interaction with the CBL calcium sensor proteins [].The secondary structure of the NAF domain is currently not known, but secondary structure computation of the C-terminal region of Arabidopsis thaliana CBL-interacting protein kinase 1 revealed a long helical structure [].The NAF domain has also been named FISL motif for its conserved amino acid residues [].
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Protein Domain
IPR004041 | NAF_dom
Type: Domain
Description: The NAF domain is a 24 amino acid domain that is found in a plant-specific subgroup of serine-threonine protein kinases (CIPKs), that interact with calcineurin B-like calcium sensor proteins (CBLs). Whereas the N-terminal part of CIPKs comprises a conserved catalytic domain typical of Ser-Thr kinases, the much less conserved C-terminal domain appears to be unique to this subgroup of kinases. The only exception is the NAF domain that forms an 'island of conservation' in this otherwise variable region. The NAF domain has been named after the prominent conserved amino acids Asn-Ala-Phe. It represents a minimum protein interaction module that is both necessary and sufficient to mediate the interaction with the CBL calcium sensor proteins [].The secondary structure of the NAF domain is currently not known, but secondary structure computation of the C-terminal region of Arabidopsis thaliana CBL-interacting protein kinase 1 revealed a long helical structure [].
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Protein Domain
IPR035772 | CIN85_SH3_3
Type: Domain
Description: CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1), CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins [, , ]. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others []. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This entry represents the third SH3 domain (SH3C) of CIN85. SH3C has been shown to bind ubiquitin [].
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Publication
15255893 | -
First Author: Lochowska A
Year: 2004
Journal: Mol Microbiol
Title: Identification of activating region (AR) of Escherichia coli LysR-type transcription factor CysB and CysB contact site on RNA polymerase alpha subunit at the cysP promoter.
Volume: 53
Issue: 3
Pages: 791-806
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Publication
18456803 | -
First Author: Kouzuma A
Year: 2008
Journal: J Bacteriol
Title: Transcription factors CysB and SfnR constitute the hierarchical regulatory system for the sulfate starvation response in Pseudomonas putida.
Volume: 190
Issue: 13
Pages: 4521-31
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Protein Domain
IPR037423 | CysB_PBP2
Type: Domain
Description: CysB is a transcriptional activator of genes involved in sulfate and thiosulfate transport, sulfate reduction, and cysteine synthesis. In Escherichia coli, the regulation of transcription in response to sulfur source is attributed to two transcriptional regulators, CysB and Cbl []. CysB, in association with Cbl, downregulates the expression of ssuEADCB operon which is required for the utilization of sulfur from aliphatic sulfonates, in the presence of cysteine []. Also, Cbl and CysB together directly function as transcriptional activators of tauABCD genes, which are required for utilization of taurine as sulfur source for growth []. Like many other members of the LTTR family, CysB is composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins []. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor []. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2).The PBP2 are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate- binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction [, , ].
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Publication
12771181 | J:120692
First Author: Sohn HW
Year: 2003
Journal: J Exp Med
Title: Cbl-b negatively regulates B cell antigen receptor signaling in mature B cells through ubiquitination of the tyrosine kinase Syk.
Volume: 197
Issue: 11
Pages: 1511-24
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Publication
26507128 | J:246188
First Author: Martin-Blanco N
Year: 2016
Journal: Int Immunol
Title: CD3ε recruits Numb to promote TCR degradation.
Volume: 28
Issue: 3
Pages: 127-37
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Publication
23430977 | J:199961
First Author: Lai SC
Year: 2013
Journal: FASEB J
Title: The transcobalamin receptor knockout mouse: a model for vitamin B12 deficiency in the central nervous system.
Volume: 27
Issue: 6
Pages: 2468-75
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Publication
21708930 | J:176805
First Author: Kometani K
Year: 2011
Journal: J Exp Med
Title: CIN85 drives B cell responses by linking BCR signals to the canonical NF-kappaB pathway.
Volume: 208
Issue: 7
Pages: 1447-57
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Publication
30057274 | J:270534
First Author: Calabretta S
Year: 2018
Journal: Dev Cell
Title: Loss of PRMT5 Promotes PDGFRα Degradation during Oligodendrocyte Differentiation and Myelination.
Volume: 46
Issue: 4
Pages: 426-440.e5
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Publication
11894095 | J:335500
First Author: Soubeyran P
Year: 2002
Journal: Nature
Title: Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors.
Volume: 416
Issue: 6877
Pages: 183-7
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Publication
10979970 | J:64604
First Author: Heisterkamp N
Year: 2000
Journal: Blood
Title: Reduced oncogenicity of p190 Bcr/Abl F-actin-binding domain mutants.
Volume: 96
Issue: 6
Pages: 2226-32
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Publication
18539136 | J:137761
First Author: Tsyba L
Year: 2008
Journal: Biochem Biophys Res Commun
Title: Alternative splicing affecting the SH3A domain controls the binding properties of intersectin 1 in neurons.
Volume: 372
Issue: 4
Pages: 929-34
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Protein Coding Gene
MGI:95602 | Fyn
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98923 | Vav1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1922019 | Pik3cb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:96892 | Lyn
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P25911
Organism: Mus musculus/domesticus
Length: 512  
Fragment?: false
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Protein
P39688
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q8BTI9
Organism: Mus musculus/domesticus
Length: 1064  
Fragment?: false
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Protein
P27870
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Publication
9309218 | -
First Author: Tyrrell R
Year: 1997
Journal: Structure
Title: The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement.
Volume: 5
Issue: 8
Pages: 1017-32
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Publication
9442882 | -
 
First Author: Thomas SM
Year: 1997
Journal: Annu Rev Cell Dev Biol
Title: Cellular functions regulated by Src family kinases.
Volume: 13
Pages: 513-609
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Publication
19359362 | -
First Author: Ortega-Roldan JL
Year: 2009
Journal: Nucleic Acids Res
Title: Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex.
Volume: 37
Issue: 9
Pages: e70
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Protein Domain
IPR035850 | Lck_SH2
Type: Domain
Description: Lck is a member of the Src non-receptor type tyrosine kinase family of proteins. CD4 and CD8 directly couple with Lck, and cross-linking of these receptors leads to Lck activation [, ]. The N-terminal tail of Lck is myristoylated and palmitoylated and it tethers the protein to the plasma membrane of the cell. Lck also contains an SH3 domain, an SH2 domain, and a C-terminal tyrosine kinase domain. Lck has 2 phosphorylation sites, the first an autophosphorylation site that is linked to activation of the protein and the second which is phosphorylated by Csk, which inhibits it. Lck is also inhibited by SHP-1 dephosphorylation and by Cbl ubiquitin ligase, which is part of the ubiquitin-mediated pathway []. This entry represents the SH2 domain of Lck.The Src non-receptor type tyrosine kinase (SFK) family members have an unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail. The SH2 domain of SFKs is involved in kinase autoinhibition and T-cell receptor signaling. The binding SH2 domains to phosphotyrosine (pY) sites is critical for the autoinhibition and substrate recognition of the SFKs [].
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Protein
Q8R550
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q3TA88
Organism: Mus musculus/domesticus
Length: 665  
Fragment?: false
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Protein Coding Gene
MGI:1206581 | Pik3ca
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098772 | Pik3r2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
O08908
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
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Protein
P42337
Organism: Mus musculus/domesticus
Length: 1068  
Fragment?: false
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Publication
9872323 | J:52472
First Author: Liu SK
Year: 1998
Journal: Oncogene
Title: Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc.
Volume: 17
Issue: 24
Pages: 3073-82
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Publication
14560016 | J:86267
First Author: Griffiths EK
Year: 2003
Journal: Mol Cell Biol
Title: Cbl-3-deficient mice exhibit normal epithelial development.
Volume: 23
Issue: 21
Pages: 7708-18
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Publication
11891219 | J:76854
First Author: Pandey A
Year: 2002
Journal: J Biol Chem
Title: A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling.
Volume: 277
Issue: 21
Pages: 19131-8
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Publication
19190244 | J:148122
First Author: Alcázar I
Year: 2009
Journal: Blood
Title: p85beta phosphoinositide 3-kinase regulates CD28 coreceptor function.
Volume: 113
Issue: 14
Pages: 3198-208
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Publication
19897579 | J:157792
First Author: Beedholm-Ebsen R
Year: 2010
Journal: Blood
Title: Identification of multidrug resistance protein 1 (MRP1/ABCC1) as a molecular gate for cellular export of cobalamin.
Volume: 115
Issue: 8
Pages: 1632-9
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Publication
20595514 | J:165878
First Author: Orinska Z
Year: 2010
Journal: Blood
Title: I787 provides signals for c-Kit receptor internalization and functionality that control mast cell survival and development.
Volume: 116
Issue: 15
Pages: 2665-75
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Publication
33340762 | J:305597
 
First Author: Shahnur A
Year: 2021
Journal: Biochem Biophys Res Commun
Title: A potential defense mechanism against amyloid deposition in cerebellum.
Volume: 535
Pages: 25-32
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Publication
28351841 | J:247839
First Author: Arora K
Year: 2017
Journal: FASEB J
Title: Maternofetal transport of vitamin B12: role of TCblR/CD320 and megalin.
Volume: 31
Issue: 7
Pages: 3098-3106
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Publication
30303736 | J:284947
First Author: Arora K
Year: 2019
Journal: FASEB J
Title: Neuropathology of vitamin B12 deficiency in the Cd320-/- mouse.
Volume: 33
Issue: 2
Pages: 2563-2573
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Publication
30016500 | J:266662
First Author: Battaglia-Hsu SF
Year: 2018
Journal: Nucleic Acids Res
Title: Inherited disorders of cobalamin metabolism disrupt nucleocytoplasmic transport of mRNA through impaired methylation/phosphorylation of ELAVL1/HuR.
Volume: 46
Issue: 15
Pages: 7844-7857
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Publication
19257814 | J:169514
First Author: Nakajima A
Year: 2009
Journal: J Bone Miner Res
Title: Loss of Cbl-b increases osteoclast bone-resorbing activity and induces osteopenia.
Volume: 24
Issue: 7
Pages: 1162-72
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Publication
20400514 | J:164469
First Author: Daniel JL
Year: 2010
Journal: J Biol Chem
Title: Cbl-b is a novel physiologic regulator of glycoprotein VI-dependent platelet activation.
Volume: 285
Issue: 23
Pages: 17282-91
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Publication
16549761 | J:107654
First Author: Tan DP
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Enhancement of long-term memory retention and short-term synaptic plasticity in cbl-b null mice.
Volume: 103
Issue: 13
Pages: 5125-30
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Publication
19009524 | J:141390
First Author: Raberger J
Year: 2008
Journal: Eur J Immunol
Title: Impaired T-cell development in the absence of Vav1 and Itk.
Volume: 38
Issue: 12
Pages: 3530-42
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Publication
26799654 | J:257394
First Author: Zhang Y
Year: 2016
Journal: PLoS One
Title: Decreased Brain Levels of Vitamin B12 in Aging, Autism and Schizophrenia.
Volume: 11
Issue: 1
Pages: e0146797
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Publication
20308550 | J:159321
First Author: Vivanco I
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: The phosphatase and tensin homolog regulates epidermal growth factor receptor (EGFR) inhibitor response by targeting EGFR for degradation.
Volume: 107
Issue: 14
Pages: 6459-64
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Publication
11489945 | J:259938
First Author: Engels N
Year: 2001
Journal: J Exp Med
Title: Epstein-Barr virus latent membrane protein 2A (LMP2A) employs the SLP-65 signaling module.
Volume: 194
Issue: 3
Pages: 255-64
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Publication
32006024 | J:301361
First Author: Kodama T
Year: 2020
Journal: Int Immunol
Title: Ubiquitination of IgG1 cytoplasmic tail modulates B-cell signalling and activation.
Volume: 32
Issue: 6
Pages: 385-395
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Publication
34062268 | J:311423
 
First Author: Barbera S
Year: 2021
Journal: Matrix Biol
Title: The C-type lectin CD93 controls endothelial cell migration via activation of the Rho family of small GTPases.
Volume: 99
Pages: 1-17
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Publication
26965285 | J:231912
First Author: Akutagawa J
Year: 2016
Journal: Leukemia
Title: Targeting the PI3K/Akt pathway in murine MDS/MPN driven by hyperactive Ras.
Volume: 30
Issue: 6
Pages: 1335-43
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Publication
16164598 | J:108456
First Author: Kaneko T
Year: 2005
Journal: Genes Cells
Title: Rho mediates endocytosis of epidermal growth factor receptor through phosphorylation of endophilin A1 by Rho-kinase.
Volume: 10
Issue: 10
Pages: 973-87
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Publication
22642810 | J:328869
First Author: Froese DS
Year: 2012
Journal: Biochemistry
Title: Structure of MMACHC reveals an arginine-rich pocket and a domain-swapped dimer for its B12 processing function.
Volume: 51
Issue: 25
Pages: 5083-90
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Publication
9307287 | J:42736
First Author: McLean GR
Year: 1997
Journal: Cancer Res
Title: Cobalamin analogues modulate the growth of leukemia cells in vitro.
Volume: 57
Issue: 18
Pages: 4015-22
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Publication
16116204 | J:113210
First Author: Davanture S
Year: 2005
Journal: J Immunol
Title: Selective defect in antigen-induced TCR internalization at the immune synapse of CD8 T cells bearing the ZAP-70(Y292F) mutation.
Volume: 175
Issue: 5
Pages: 3140-9
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Publication
16212556 | J:117559
First Author: Thien CB
Year: 2005
Journal: Biochem J
Title: c-Cbl and Cbl-b ubiquitin ligases: substrate diversity and the negative regulation of signalling responses.
Volume: 391
Issue: Pt 2
Pages: 153-66
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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