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Search results 6601 to 6700 out of 8321 for Src

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0.049s

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Type Details Score
Publication
10782093 | -
First Author: Odorizzi G
Year: 2000
Journal: Trends Biochem Sci
Title: Phosphoinositide signaling and the regulation of membrane trafficking in yeast.
Volume: 25
Issue: 5
Pages: 229-35
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Publication
9428629 | J:44758
First Author: Haffner C
Year: 1997
Journal: FEBS Lett
Title: Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15.
Volume: 419
Issue: 2-3
Pages: 175-80
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Publication
10542231 | -
First Author: Cestra G
Year: 1999
Journal: J Biol Chem
Title: The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity.
Volume: 274
Issue: 45
Pages: 32001-7
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Publication
21932368 | -
First Author: Takaichi R
Year: 2012
Journal: J Neurosci Res
Title: Inhibitory effect of NAP-22 on the phosphatase activity of synaptojanin-1.
Volume: 90
Issue: 1
Pages: 21-7
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Publication
21316588 | -
First Author: Chang-Ileto B
Year: 2011
Journal: Dev Cell
Title: Synaptojanin 1-mediated PI(4,5)P2 hydrolysis is modulated by membrane curvature and facilitates membrane fission.
Volume: 20
Issue: 2
Pages: 206-18
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Publication
23277200 | -
First Author: Barrett A
Year: 2013
Journal: Cell Signal
Title: p130Cas: a key signalling node in health and disease.
Volume: 25
Issue: 4
Pages: 766-77
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Protein
Q62225
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: false
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Protein
Q60787
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: false
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Protein
Q9QXT1
Organism: Mus musculus/domesticus
Length: 280  
Fragment?: false
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Protein
Q91ZA6
Organism: Mus musculus/domesticus
Length: 436  
Fragment?: false
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Protein
O09039
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
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Protein
O35718
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
O35717
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: false
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Protein
Q6P549
Organism: Mus musculus/domesticus
Length: 1257  
Fragment?: false
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Protein
Q9JLY0
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: false
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Protein
Q8R0L1
Organism: Mus musculus/domesticus
Length: 411  
Fragment?: false
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Protein
Q61140
Organism: Mus musculus/domesticus
Length: 874  
Fragment?: false
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Protein
O35716
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
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Protein
Q8BZ33
Organism: Mus musculus/domesticus
Length: 696  
Fragment?: false
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Protein
O54928
Organism: Mus musculus/domesticus
Length: 536  
Fragment?: false
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Protein
Q8VHQ2
Organism: Mus musculus/domesticus
Length: 579  
Fragment?: false
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Protein
Q3TLY3
Organism: Mus musculus/domesticus
Length: 874  
Fragment?: false
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Protein
E9Q796
Organism: Mus musculus/domesticus
Length: 901  
Fragment?: false
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Protein
A0A087WRI1
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
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Protein
Q3U5Y3
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: false
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Protein
A0A140LIY1
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: true
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Protein
Q3UK44
Organism: Mus musculus/domesticus
Length: 280  
Fragment?: false
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Protein
Q3UL29
Organism: Mus musculus/domesticus
Length: 280  
Fragment?: false
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Protein
Q3TIT7
Organism: Mus musculus/domesticus
Length: 874  
Fragment?: false
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Protein
Q3TJP4
Organism: Mus musculus/domesticus
Length: 874  
Fragment?: false
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Protein
A0A1L1SR46
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
A2AV92
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
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Protein
D6RGA0
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
A0A087WPY9
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: true
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Protein
Q5U469
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
F6RVG2
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
Q8BNW5
Organism: Mus musculus/domesticus
Length: 290  
Fragment?: true
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Protein
A0A571BEJ5
Organism: Mus musculus/domesticus
Length: 648  
Fragment?: false
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Protein
Q99MW4
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
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Protein
B1AVB1
Organism: Mus musculus/domesticus
Length: 825  
Fragment?: false
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Protein
Q3TXP6
Organism: Mus musculus/domesticus
Length: 874  
Fragment?: false
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Protein
D3Z3Y5
Organism: Mus musculus/domesticus
Length: 538  
Fragment?: false
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Protein
B1ATD1
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
B1AVB5
Organism: Mus musculus/domesticus
Length: 905  
Fragment?: false
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Protein
A0A1L1STA1
Organism: Mus musculus/domesticus
Length: 139  
Fragment?: true
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Protein
S4R1A0
Organism: Mus musculus/domesticus
Length: 44  
Fragment?: false
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Protein
B1AVB4
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q8BYC8
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
B1AVB2
Organism: Mus musculus/domesticus
Length: 827  
Fragment?: false
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Protein
Q8CAS1
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
D6REG6
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: false
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Protein
A0A087WQM2
Organism: Mus musculus/domesticus
Length: 174  
Fragment?: true
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Protein
A0A338P675
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: true
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Protein
Q3TJB5
Organism: Mus musculus/domesticus
Length: 874  
Fragment?: false
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Protein
Q3U9J8
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
A7VK13
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: false
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Protein
Q548Q7
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: false
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Publication
10025422 | -
First Author: Antoine JC
Year: 1999
Journal: Arch Neurol
Title: Antiamphiphysin antibodies are associated with various paraneoplastic neurological syndromes and tumors.
Volume: 56
Issue: 2
Pages: 172-7
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Publication
34018922 | J:311392
   
First Author: Zhang X
Year: 2021
Journal: Elife
Title: Amphiphysin I cleavage by asparagine endopeptidase leads to tau hyperphosphorylation and synaptic dysfunction.
Volume: 10
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Publication
15611048 | -
First Author: Puertollano R
Year: 2005
Journal: J Biol Chem
Title: Interactions of TOM1L1 with the multivesicular body sorting machinery.
Volume: 280
Issue: 10
Pages: 9258-64
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Publication
14563850 | J:148073
First Author: Yamakami M
Year: 2003
Journal: J Biol Chem
Title: Tom1, a VHS domain-containing protein, interacts with tollip, ubiquitin, and clathrin.
Volume: 278
Issue: 52
Pages: 52865-72
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Publication
15056867 | -
First Author: Yamakami M
Year: 2004
Journal: Biol Pharm Bull
Title: Tom1 (target of Myb 1) is a novel negative regulator of interleukin-1- and tumor necrosis factor-induced signaling pathways.
Volume: 27
Issue: 4
Pages: 564-6
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Publication
12732142 | -
First Author: Groemping Y
Year: 2003
Journal: Cell
Title: Molecular basis of phosphorylation-induced activation of the NADPH oxidase.
Volume: 113
Issue: 3
Pages: 343-55
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Publication
17177976 | -
First Author: Maruyama T
Year: 2007
Journal: Clin Exp Immunol
Title: Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells.
Volume: 147
Issue: 1
Pages: 164-75
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Publication
16221668 | -
First Author: Ceccarelli DF
Year: 2006
Journal: J Biol Chem
Title: Crystal structure of the FERM domain of focal adhesion kinase.
Volume: 281
Issue: 1
Pages: 252-9
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Publication
17574028 | -
First Author: Lietha D
Year: 2007
Journal: Cell
Title: Structural basis for the autoinhibition of focal adhesion kinase.
Volume: 129
Issue: 6
Pages: 1177-87
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Publication
19244237 | -
First Author: Han S
Year: 2009
Journal: J Biol Chem
Title: Structural characterization of proline-rich tyrosine kinase 2 (PYK2) reveals a unique (DFG-out) conformation and enables inhibitor design.
Volume: 284
Issue: 19
Pages: 13193-201
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Publication
25380750 | -
First Author: Yoon H
Year: 2015
Journal: J Histochem Cytochem
Title: Understanding the roles of FAK in cancer: inhibitors, genetic models, and new insights.
Volume: 63
Issue: 2
Pages: 114-28
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Publication
29891810 | -
 
First Author: Naser R
Year: 2018
Journal: Cancers (Basel)
Title: Endogenous Control Mechanisms of FAK and PYK2 and Their Relevance to Cancer Development.
Volume: 10
Issue: 6
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Protein Domain
IPR041784 | FAK1/PYK2_FERM_C
Type: Domain
Description: FAK1 (focal adhesion kinase 1) is a non-receptor tyrosine kinase that localizes to focal adhesions in adherent cells. It has been implicated in diverse cellular roles including cell locomotion, mitogen response and cell survival []. The N-terminal region of FAK1 contains a FERM domain, a linker, a kinase domain, and a C-terminal FRNK (FAK-related-non-kinase) domain. Three subdomains of FERM: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), form a cloverleaf fold, similar to those of known FERM structures despite the low sequence conservation. The phosphoinositide-binding site found in ERM family proteins is not present in the FERM domain of FAK1 []. The adjacent Src SH3 and SH2 binding sites in the linker of FAK1 associates with the F3 and F1 lobes and are thought to be involved in regulation. The FERM domain of FAK1 can inhibit enzymatic activity and repress FAK signaling. In an inactive state of FAK1, the FERM domain is thought to interact with the catalytic domain of FAK1 to repress its activity. Upon activation this interaction is disrupted and its kinase activity restored. The FRNK domain is thought to function as a negative regulator of kinase activity. This entry represents the C-lobe/F3 domain, which is the third structural domain within the FERM domain. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites [, ]. Proteins containing this domain also include protein-tyrosine kinase 2-beta (also known as PYK2), which is a cytoplasmic, non-receptor tyrosine kinase implicated in multiple signaling pathways []. PYK2 is a close paralogue to FAK in vertebrates that can often functionally compensate for loss of FAK [].
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Protein Domain
IPR014645 | TOM1
Type: Family
Description: Tom1 (target of Myb 1) and its related proteins (Tom1L1 and Tom1L2) constitute a protein family and share an N-terminal VHS (Vps27p/Hrs/Stam) domain followed by a GAT (GGA and Tom1) domain.VHS domains are found at the N termini of select proteins involved in intracellular membrane trafficking and are often localized to membranes. The three dimensional structure of human TOM1 VHS domain reveals eight helices arranged in a superhelix. The surface of the domain has two main features: (1) a basic patch on one side due to several conserved positively charged residues on helix 3 and (2) a negatively charged ridge on the opposite side, formed by residues on helix 2 []. The basic patch is thought to mediate membrane binding.It was demonstrated that the GAT domain of both Tom1 and Tom1L1 binds ubiquitin, suggesting that these proteins might participate in the sorting of ubiquitinated proteins into multivesicular bodies (MVB) []. Moreover, Tom1L1 interacts with members of the MVB sorting machinery. Specifically, the VHS domain of Tom1L1 interacts with Hrs (hepatocyte growth factor-regulated tyrosine kinase substrate), whereas a PTAP motif, located between the VHS and GAT domains of Tom1L1, is responsible for binding to TSG101 (tumour susceptibility gene 101). Myc epitope-tagged Tom1L1 is recruited to endosomes following Hrs expression. In addition, Tom1L1 possesses several tyrosine motifs at the C-terminal region that mediate interactions with members of the Src family kinases and other signalling proteins such as Grb2 and p85. Expression of a constitutively active form of Fyn kinase promotes the recruitment of Tom1L1 to enlarged endosomes. It is proposed that Tom1L1 could act as an intermediary between the signalling and degradative pathways [].Over expression of Tom1 suppresses activation of the transcription factors NF-kappaB and AP-1, induced by either IL-1beta or tumour necrosis factor (TNF)-alpha, and the VHS domain of Tom1 is indispensable for this suppressive activity. This suggests that Tom1 is a common negative regulator of signalling pathways induced by IL-1beta and TNF-alpha [].
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Protein Domain
IPR003017 | Amphiphysin_1
Type: Family
Description: Amphiphysins belong to the expanding BAR (Bin-Amphiphysin-Rvsp) family proteins, all members of which share a highly conserved N-terminal BAR domain, which has predicted coiled-coil structures required for amphiphysin dimerisation and plasma membrane interaction []. Almost all members also share a conserved C-terminal Src homology 3 (SH3) domain, which mediates their interactions with the GTPase dynamin and the inositol-5'-phosphatase synaptojanin 1 in vertebrates and with actin in yeast. The central region of all these proteins is most variable. In mammals, the central region of amphiphysin I and amphiphysin IIa contains a proline-arginine-rich region for endophilin binding and a CLAP domain, for binding to clathrin and AP-2. The interactions mediated by both the central and C-terminal domains are believed to be modulated by protein phosphorylation [, ].Amphiphysins are proteins involved in clathrin-mediated endocytosis clathrin-mediated endocytosis, actin function, and signalling pathways [, ].Amphiphysin 1 was first identified in 1992 as a brain protein that was partially-associated with synaptic vesicles. Following its cloning, it was also realised to be a human auto-antigen that is detected in a rare neurological disease, Stiff-Man Syndrome, and also in certain types of cancer []. Amphiphysin 1 senses and facilitates membrane curvature to mediate synaptic vesicles invagination and fission during newly retrieved presynaptic vesicle formation and also acts as a linker protein binding with dynamin, clathrin, Amphiphysin II, and other dephosphins in the clathrin-coated complex. Amphiphysin 1 is cleaved an asparagine endopeptidase (AEP), which generates afragment that increases with aging. This fragment disrupts the normal endocytic function of Amphiphysin 1, leading to synaptic dysfunction, as it activates CDK5 inducing tau hyperphosphorylation. Therefore, Amphiphysin 1 posttranslational modification contributes to pathogenesis of Alzheimer's disease, being the AEP a therapeutic target [].
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Publication
10559861 | -
First Author: Takei K
Year: 1999
Journal: Nat Cell Biol
Title: Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis.
Volume: 1
Issue: 1
Pages: 33-9
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Publication
9720601 | -
First Author: Wigge P
Year: 1998
Journal: Trends Neurosci
Title: The amphiphysin family of proteins and their role in endocytosis at the synapse.
Volume: 21
Issue: 8
Pages: 339-44
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Publication
12047553 | -
First Author: Zhang B
Year: 2002
Journal: Traffic
Title: Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics. Bin-Amphiphysin-Rvsp.
Volume: 3
Issue: 7
Pages: 452-60
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Protein Coding Gene
MGP_CAROLIEiJ_G0015246 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0017151 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0017128 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0017088 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0017091 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0016911 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_95602 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0017549 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0016490 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0016885 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0016990 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0016985 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0017067 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0017015 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0017586 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0016271 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0016553 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0030663 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0016055 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
2488273 | J:37401
First Author: Cooke MP
Year: 1989
Journal: New Biol
Title: Expression of a novel form of the fyn proto-oncogene in hematopoietic cells.
Volume: 1
Issue: 1
Pages: 66-74
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Publication
1361685 | J:3417
First Author: Grant SG
Year: 1992
Journal: Science
Title: Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice.
Volume: 258
Issue: 5090
Pages: 1903-10
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Publication
21872217 | J:176593
 
First Author: Babus LW
Year: 2011
Journal: Brain Res
Title: Decreased dendritic spine density and abnormal spine morphology in Fyn knockout mice.
Volume: 1415
Pages: 96-102
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Publication
7628441 | J:243407
First Author: Takemoto Y
Year: 1995
Journal: EMBO J
Title: LckBP1, a proline-rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56lck.
Volume: 14
Issue: 14
Pages: 3403-14
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Publication
1387588 | J:2242
First Author: Stein PL
Year: 1992
Journal: Cell
Title: pp59fyn mutant mice display differential signaling in thymocytes and peripheral T cells.
Volume: 70
Issue: 5
Pages: 741-50
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Publication
8864276 | J:35216
First Author: Schafe GE
Year: 1996
Journal: Behav Neurosci
Title: Taste aversion learning in fyn mutant mice.
Volume: 110
Issue: 4
Pages: 845-8
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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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