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Search results 6801 to 6900 out of 8285 for C2

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Type Details Score
Publication
15031411 | -
First Author: Yang S
Year: 2004
Journal: Plant Cell
Title: A haplotype-specific Resistance gene regulated by BONZAI1 mediates temperature-dependent growth control in Arabidopsis.
Volume: 16
Issue: 4
Pages: 1060-71
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Publication
19522566 | -
First Author: Li Y
Year: 2009
Journal: Mol Plant Microbe Interact
Title: Multiple R-like genes are negatively regulated by BON1 and BON3 in arabidopsis.
Volume: 22
Issue: 7
Pages: 840-8
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Publication
14748705 | -
First Author: Sim RB
Year: 2004
Journal: Biochem Soc Trans
Title: Proteases of the complement system.
Volume: 32
Issue: Pt 1
Pages: 21-7
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Publication
12359063 | -
First Author: Perez P
Year: 2002
Journal: J Biochem
Title: Yeast protein kinase C.
Volume: 132
Issue: 4
Pages: 513-7
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Publication
11994162 | -
First Author: Schmitz HP
Year: 2002
Journal: Mol Microbiol
Title: Regulation of yeast protein kinase C activity by interaction with the small GTPase Rho1p through its amino-terminal HR1 domain.
Volume: 44
Issue: 3
Pages: 829-40
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Publication
15364579 | -
First Author: Harmat V
Year: 2004
Journal: J Mol Biol
Title: The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions.
Volume: 342
Issue: 5
Pages: 1533-46
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Publication
15117939 | -
First Author: Gregory LA
Year: 2004
Journal: J Biol Chem
Title: The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin.
Volume: 279
Issue: 28
Pages: 29391-7
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Publication
9475719 | -
First Author: Flick JS
Year: 1998
Journal: Genetics
Title: An essential function of a phosphoinositide-specific phospholipase C is relieved by inhibition of a cyclin-dependent protein kinase in the yeast Saccharomyces cerevisiae.
Volume: 148
Issue: 1
Pages: 33-47
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Publication
23913687 | -
First Author: Galdieri L
Year: 2013
Journal: J Biol Chem
Title: Yeast phospholipase C is required for normal acetyl-CoA homeostasis and global histone acetylation.
Volume: 288
Issue: 39
Pages: 27986-98
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Publication
11559854 | -
First Author: Koushika SP
Year: 2001
Journal: Nat Neurosci
Title: A post-docking role for active zone protein Rim.
Volume: 4
Issue: 10
Pages: 997-1005
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Publication
16473612 | -
 
First Author: Fukuda M
Year: 2005
Journal: Methods Enzymol
Title: Assay of the Rab-binding specificity of rabphilin and Noc2: target molecules for Rab27.
Volume: 403
Pages: 469-81
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Publication
27728837 | -
 
First Author: Dümmer M
Year: 2016
Journal: J Plant Physiol
Title: EHB1 and AGD12, two calcium-dependent proteins affect gravitropism antagonistically in Arabidopsis thaliana.
Volume: 206
Pages: 114-124
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Publication
9209068 | -
First Author: Li D
Year: 1997
Journal: J Bacteriol
Title: Purification and sequence analysis of a novel NADP(H)-dependent type III alcohol dehydrogenase from Thermococcus strain AN1.
Volume: 179
Issue: 13
Pages: 4433-7
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Publication
10491136 | -
First Author: Antoine E
Year: 1999
Journal: Eur J Biochem
Title: Cloning and over-expression in Escherichia coli of the gene encoding NADPH group III alcohol dehydrogenase from Thermococcus hydrothermalis. Characterization and comparison of the native and the recombinant enzymes.
Volume: 264
Issue: 3
Pages: 880-9
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Publication
10981690 | -
First Author: Holt PJ
Year: 2000
Journal: FEMS Microbiol Lett
Title: Cloning, sequencing and expression in Escherichia coli of the primary alcohol dehydrogenase gene from Thermoanaerobacter ethanolicus JW200.
Volume: 190
Issue: 1
Pages: 57-62
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Publication
19115036 | -
First Author: Ying X
Year: 2009
Journal: Extremophiles
Title: Molecular characterization of the recombinant iron-containing alcohol dehydrogenase from the hyperthermophilic Archaeon, Thermococcus strain ES1.
Volume: 13
Issue: 2
Pages: 299-311
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Protein Domain
IPR031462 | CTSRT
Type: Family
Description: Cation channel sperm-associated targeting subunit tau (CTSRT, also known as Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 11 and C2 calcium-dependent domain-containing protein 6) has been identified in mice as an auxiliary component of the CatSper complex, which is involved in sperm cell hyperactivation. Sperm cell hyperactivation is required for sperm motility, essential late in the preparation of sperm for fertilization []. This protein is key for CatSper flagellar targeting and trafficking into the quadrilinear nanodomains as it links the channel-carrying vesicles and motor proteins in elongating flagella.
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Protein Domain
IPR028696 | SYT14
Type: Family
Description: Synaptotagmin-14 (SYT14) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains (known as C2A and C2B domains). Most of the synaptotagmins have a unique N-terminal domain (transmembrane region) that is involved in membrane anchoring or specific ligand binding. In mammals, SYT14 is expressed in brain (especially in the cerebellum) []. Mutations in SYT14 gene cause spinocerebellar ataxia, autosomal recessive, 11 (SCAR11), which is a clinically and genetically heterogeneous group of cerebellar disorders []. This entry also includes synaptotagmin-14-like protein (SYT14L, also known as sytdep) from human, which is highly expressed in mature peripheral blood neutrophils [].
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Protein Domain
IPR041799 | TOLIP_CUE
Type: Domain
Description: Tollip (Toll-interacting protein) is a component of the IL-1RI pathway which contains an N-terminal C2 domain and a C-terminal CUE domain. Tollip binds to the cytoplasmic TIR domain of IL-1Rs after IL-1 stimulation. It is sufficient for recruitment of IRAK to IL-1Rs and negatively regulates IL-1-induced signaling by inhibiting IRAK phosphorylation. In addition, Tollip directly interacts with toll-like receptors TLR2 and TLR4, and plays an inhibitory role in TLR-mediated cell activation through suppressing phosphorylation and kinase activity of IRAK. Moreover, Tollip can associate with GAT domains of Tom1 and its related proteins Tom1L1 and Tom1L2, and facilitate the recruitment of clathrin onto endosomes [, ].
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Protein Domain
IPR028699 | SYT11
Type: Family
Description: Synaptotagmin-11 (SYT11) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains (known as C2A and C2B domains). Most of the synaptotagmins have a unique N-terminal domain (transmembrane region) that is involved in membrane anchoring or specific ligand binding. The SYT11 gene is located on a major susceptibility locus of familial schizophrenia []. The STY11 loci has also been linked to Parkinson's disease (PD) []. Parkin, a ubiquitin ligase, binds to the C2A and C2B domains of SYT11 resulting in the polyubiquitination of SYT11 [].
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Protein Domain
IPR028682 | SYT3
Type: Family
Description: Synaptotagmin-3 (SYT3) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains. Most of the synaptotagmins have a unique N-terminal domain that is involved in membrane anchoring or specific ligand binding. SYT3 is required for the formation and delivery of cargo to the perinuclear endocytic recycling compartment (ERC) []. Among synaptotagmins 1-11, SYT3 is the only one that is expressed in T cells. It is essential for chemokine receptor CXCR4 recycling in T cells and thereby affects CXCL12 chemokine-induced migration [].
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Protein Domain
IPR041857 | Noc2_FYVE
Type: Domain
Description: Rab effector Noc2 (also known as RPH3AL) is a Rab3 effector that mediates the regulation of secretory vesicle exocytosis in neurons and certain endocrine cells []. It also functions as a Rab27 effector and is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells [, ]. Noc2 contains an N-terminal Rab3A effector domain which harbors a conserved zinc finger, but lacks tandem C2 domains. The FYVE domain of Noc2 resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif [].
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Protein Domain
IPR038678 | Spondin_N_sf
Type: Homologous_superfamily
Description: Spondins are multi-domain extracellular matrix (ECM) protein as well as contact-repellent molecules that directs axon outgrowth and cell migration during development. Spondins are involved in patterning axonal growth trajectory through either inhibiting or promoting adhesion of embryonic nerve cells [].This superfamily represents a domain found in the N-terminal half of several Spondin proteins [], also called FS domain. It is found in F-spondins (spondin-1), mindins (spondin-2). Its homology to a common Ca2+- and lipid-binding C2 domain suggests that the F-spondin FS domain is responsible for part of the membrane targeting of F-spondin in its regulation of axon development [].
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Protein Domain
IPR009465 | Spondin_N
Type: Domain
Description: Spondins are multi-domain extracellular matrix (ECM) protein as well as contact-repellent molecules that directs axon outgrowth and cell migration during development. Spondins are involved in patterning axonal growth trajectory through either inhibiting or promoting adhesion of embryonic nerve cells [].This conserved region is found in the N-terminal half of several Spondin proteins [], also called FS domain. It is found in F-spondins (spondin-1), mindins (spondin-2). Its homology to a common Ca2+- and lipid-binding C2 domain suggests that the F-spondin FS domain is responsible for part of the membrane targeting of F-spondin in its regulation of axon development [].
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Protein Domain
IPR044518 | ARF_GAP_AGD11/12/13
Type: Family
Description: This entry represents a group of plant ADP-ribosylation factor GTPase-activating proteins (ArfGAPs), such as AGD11/12/13 from Arabidopsis. ArfGAPs are a family of proteins containing an ArfGAP catalytic domain that induces the hydrolysis of GTP bound to the small guanine nucleotide-binding protein Arf, a member of the Ras superfamily of GTPases. Of all known members belonging to the ARF-GAP protein family only AGD11, 12, and 13 possess a C2 domain enabling them to bind phospholipids, phosphoinositide and proteins in a calcium-dependent manner []. The C-terminal domain of AGD12 is structurally related to ENHANCED BENDING (EHB) 1, and both of them function as calcium-dependent proteins that affect gravitropism in Arabidopsis thaliana [].
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Protein Domain
IPR039032 | Rim-like
Type: Family
Description: RIM proteins are scaffolding proteins at the active zone which bind to several other presynaptic proteins. The long isoforms of RIM proteins, which contain N-terminal Rab3 and Munc13 interacting domains, as well as a central PDZ domain and two C-terminal C2 domains, are encoded by two genes, Rim1 and Rim2 []. They have multiple isoforms (alpha, beta, gamma) diverging in their structural composition, which mediate overlapping and distinct functions [, ]. These isoforms are involved in determining Ca2+ channel density and vesicle docking at the presynaptic active zone []. This entry includes Rim and related proteins. In Caenorhabditis elegans Rim acts after vesicle docking likely via regulating priming [].
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Protein Domain
IPR030539 | SYT15
Type: Family
Description: Synaptotagmin-15 (Syt15) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains (known as C2A and C2B domains). Most of the synaptotagmins have a unique N-terminal domain that is involved in membrane anchoring or specific ligand binding. Mammals contain 16 synaptotagmins; eight of these bind Ca2+ via their C2-domains (Syt1-Syt3, Syt5-7, Syt9, and Syt10), whereas the other eight, including Syt15, do not [].Unlike other synaptotagmins, the mouse and human Syt15 have an alternative splicing isoform that lacks the C-terminal portion of the C2B domain (named Syt15-b). Expression of Syt15 is mainly found in non-neuronal tissues [].
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Protein Domain
IPR030540 | SYT8
Type: Family
Description: Synaptotagmin-8 (Syt8) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains (known as C2A and C2B domains). Most of the synaptotagmins have a unique N-terminal domain that is involved in membrane anchoring or specific ligand binding. Mammals contain 16 synaptotagmins; eight of these bind Ca2+ via their C2-domains (Syt1-Syt3, Syt5-7, Syt9, and Syt10), whereas the other eight, including Syt8, do not [].Syt8 is expressed in neurons, neuroendocrine and endocrine cells []. It is involved in insulin secretion []and may function in acrosomal exocytosis [].
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Protein Domain
IPR045910 | AdhA-like
Type: Family
Description: This entry represents the long-chain primary alcohol dehydrogenase AdhA (ADHA) from Thermoanaerobacter ethanolicus (formerly known as Clostridium thermohydrosulfuricum). This enzyme is an alcohol dehydrogenase active against primary long-chain alcohols that catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor []. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. [, , ]. Members of this protein family are mainly found in bacteria and archaea.
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Protein Domain
IPR037571 | MASP2
Type: Family
Description: This entry represents mannan-binding lectin-associated serine peptidase 2 (MASP2; MEROPS identifier S01.229), a serine endopeptidase from family S1 (chymotrypsin family) which is a component in the activation of complement in the lectin pathway. MASP2 has trypsin-like specificity and it processes complement components C2 and C4 []. The fragments released, C2a and C4b, form the C3/C5 convertase. The specificity of MASP2 is identical to that of complement component C1s, but from the solved tertiary structure that enzyme-substrate interactions are different []. MASP2 is inhibited by C1 inhibitor []. MASP2 forms a homodimer, stabilized by two Ca2+ions, before it binds to mannose-binding protein C []. MASP2 autoactivates itself to a two-chain form.
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Protein Domain
IPR037312 | PKC-like_HR1
Type: Domain
Description: This entry represents the second HR1 domain found in fungal PKC-like proteins including Pkc1p from Saccharomyces cerevisiae, and Pck1p and Pck2p from Schizosaccharomyces pombe. The yeast PKC-like proteins play a critical role in regulating cell wall biosynthesis and maintaining cell wall integrity []. They contain two HR1 domains, C2 and C1 domains, and a kinase domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family []. The HR1 domains of Pck1p and Pck2p interact with GTP-bound Rho1p and Rho2p [].
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Protein Domain
IPR037755 | Plc1_PH
Type: Domain
Description: Saccharomyces cerevisiae Plc1 is a homologue of the delta isoform of mammalian phosphoinositide-specific phospholipase C (PI-PLC) []. It is required for the initial step of inositol polyphosphate (InsP) synthesis. It hydrolyzes phosphatidylinositol 4,5-biphosphate (PIP2) to generate the signaling molecules inositol 1,4,5-triphosphate (IP3) and 1,2-diacylglycerol (DAG) []. Plc1 contains an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, and a C-terminal C2 domain. This entry represents the PH domain found in Plc1 and its homologues from fungi.
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Protein Domain
IPR045052 | Copine
Type: Family
Description: Copines are a widely distributed class of Ca2+-dependent lipid-binding proteins. Most have a characteristic domain structure: two C2 domains in the N-terminal region and a von Willebrand A (VWA) domain in the C-terminal region. They are potentially involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth [, ]. In plants, they are known as BONZAI proteins []. The copine family in plants may have effects in promoting growth and development in addition to repressing cell death [, ]. Caenorhabditis elegans copine, also known as Nra1, is Involved in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine and levamisole [].
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Protein Domain
IPR031116 | BONZAI
Type: Family
Description: Copines are a widely distributed class of Ca2+-dependent lipid-binding proteins. Most have a characteristic domain structure: two C2 domains in the N-terminal region and a von Willebrand A (VWA) domain in the C-terminalregion.In Arabidopsis the copine family consist of BON1 (BONZAI 1), BON2 (BONZAI 2) and BON3 (BONZAI 3). The copine family in plants may have effects in promoting growth and development in addition to repressing cell death [, ]. BON1 and BON3 negatively regulate multiple resistance (R-like) genes; these are involved in plant responses to biotic attacks but need to be repressed in the absence of biotic stresses as their effects are detrimental to plant growth and development [, , ].
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Publication
17116687 | J:118168
First Author: Cho YJ
Year: 2007
Journal: Mol Cell Biol
Title: Abr and Bcr, two homologous Rac GTPase-activating proteins, control multiple cellular functions of murine macrophages.
Volume: 27
Issue: 3
Pages: 899-911
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Publication
21258343 | J:170600
First Author: Rooryck C
Year: 2011
Journal: Nat Genet
Title: Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome.
Volume: 43
Issue: 3
Pages: 197-203
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Publication
18940604 | J:155184
First Author: Kukimoto-Niino M
Year: 2008
Journal: Structure
Title: Structural basis for the exclusive specificity of Slac2-a/melanophilin for the Rab27 GTPases.
Volume: 16
Issue: 10
Pages: 1478-90
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Publication
18780722 | -
First Author: Oda A
Year: 2008
Journal: Int Immunol
Title: PKC eta directs induction of IRF-4 expression and Ig kappa gene rearrangement in pre-BCR signaling pathway.
Volume: 20
Issue: 11
Pages: 1417-26
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Publication
18025218 | J:155211
First Author: Cheng N
Year: 2007
Journal: J Immunol
Title: A critical role of protein kinase C delta activation loop phosphorylation in formyl-methionyl-leucyl-phenylalanine-induced phosphorylation of p47(phox) and rapid activation of nicotinamide adenine dinucleotide phosphate oxidase.
Volume: 179
Issue: 11
Pages: 7720-8
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Protein
Q60648
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
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Publication
15949469 | J:106401
First Author: Stawowy P
Year: 2005
Journal: Cardiovasc Res
Title: Protein kinase C epsilon mediates angiotensin II-induced activation of beta1-integrins in cardiac fibroblasts.
Volume: 67
Issue: 1
Pages: 50-9
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Publication
12062444 | -
First Author: Nagashima K
Year: 2002
Journal: FEBS Lett
Title: Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions.
Volume: 517
Issue: 1-3
Pages: 233-8
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Protein
Q5F1Z8
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
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Protein
M0QWC0
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: false
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Protein
M0QW56
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
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Protein
Q8C019
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
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Protein
A0A0J9YUZ7
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: true
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Protein
Q5D222
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
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Protein
M0QWI1
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Protein
H3BKY4
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: true
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Publication
11287656 | -
First Author: Tzarfati-Majar V
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: F-spondin is a contact-repellent molecule for embryonic motor neurons.
Volume: 98
Issue: 8
Pages: 4722-7
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Publication
19153605 | -
First Author: Li Y
Year: 2009
Journal: EMBO J
Title: Structure of the F-spondin domain of mindin, an integrin ligand and pattern recognition molecule.
Volume: 28
Issue: 3
Pages: 286-97
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Publication
21569239 | -
 
First Author: Tan K
Year: 2011
Journal: BMC Struct Biol
Title: The structure of the Ca²+-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein.
Volume: 11
Pages: 22
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Publication
11118617 | -
First Author: Caricasole A
Year: 2000
Journal: Biochim Biophys Acta
Title: Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1).
Volume: 1517
Issue: 1
Pages: 63-72
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Publication
25193662 | -
First Author: Charpentier TH
Year: 2014
Journal: J Biol Chem
Title: Membrane-induced allosteric control of phospholipase C-β isozymes.
Volume: 289
Issue: 43
Pages: 29545-57
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Publication
10475605 | -
First Author: Takayama Y
Year: 1999
Journal: Mol Immunol
Title: Gene structure of the P100 serine-protease component of the human Ra-reactive factor.
Volume: 36
Issue: 8
Pages: 505-14
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Publication
15355962 | -
First Author: Grohmanova K
Year: 2004
Journal: J Biol Chem
Title: Phosphorylation of IQGAP1 modulates its binding to Cdc42, revealing a new type of rho-GTPase regulator.
Volume: 279
Issue: 47
Pages: 48495-504
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Publication
18637121 | -
First Author: Shirai Y
Year: 2008
Journal: FEBS J
Title: Protein kinase Cepsilon: function in neurons.
Volume: 275
Issue: 16
Pages: 3988-94
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Publication
17971128 | -
First Author: Van Kolen K
Year: 2008
Journal: J Neurochem
Title: Nociceptive and behavioural sensitisation by protein kinase Cepsilon signalling in the CNS.
Volume: 104
Issue: 1
Pages: 1-13
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Publication
21681677 | -
First Author: Chen Y
Year: 2011
Journal: Front Med
Title: The role of protein kinase C epsilon in neural signal transduction and neurogenic diseases.
Volume: 5
Issue: 1
Pages: 70-6
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Publication
14643884 | -
First Author: Aksoy E
Year: 2004
Journal: Int J Biochem Cell Biol
Title: Protein kinase C epsilon: a new target to control inflammation and immune-mediated disorders.
Volume: 36
Issue: 2
Pages: 183-8
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Publication
17875639 | J:126967
First Author: Qi ZH
Year: 2007
Journal: J Biol Chem
Title: Protein kinase C epsilon regulates gamma-aminobutyrate type A receptor sensitivity to ethanol and benzodiazepines through phosphorylation of gamma2 subunits.
Volume: 282
Issue: 45
Pages: 33052-63
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Publication
11884385 | -
First Author: Numazaki M
Year: 2002
Journal: J Biol Chem
Title: Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cepsilon and identification of two target serine residues.
Volume: 277
Issue: 16
Pages: 13375-8
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Publication
20558593 | J:180551
First Author: Lee HK
Year: 2010
Journal: Mol Pharmacol
Title: Protein kinase C-eta and phospholipase D2 pathway regulates foam cell formation via regulator of G protein signaling 2.
Volume: 78
Issue: 3
Pages: 478-85
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Publication
15489897 | -
First Author: Aeder SE
Year: 2004
Journal: Oncogene
Title: PKC-eta mediates glioblastoma cell proliferation through the Akt and mTOR signaling pathways.
Volume: 23
Issue: 56
Pages: 9062-9
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Publication
11112424 | -
First Author: Akkaraju GR
Year: 2000
Journal: Biochem Biophys Res Commun
Title: Overexpression of protein kinase C-eta attenuates caspase activation and tumor necrosis factor-alpha-induced cell death.
Volume: 279
Issue: 1
Pages: 103-7
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Publication
15774464 | -
First Author: Okhrimenko H
Year: 2005
Journal: J Biol Chem
Title: Roles of tyrosine phosphorylation and cleavage of protein kinase Cdelta in its protective effect against tumor necrosis factor-related apoptosis inducing ligand-induced apoptosis.
Volume: 280
Issue: 25
Pages: 23643-52
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Publication
18092819 | -
First Author: Jiang K
Year: 2008
Journal: Biochemistry
Title: Identification of a novel antiapoptotic human protein kinase C delta isoform, PKCdeltaVIII in NT2 cells.
Volume: 47
Issue: 2
Pages: 787-97
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Publication
11877440 | -
First Author: Ren J
Year: 2002
Journal: J Biol Chem
Title: Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling.
Volume: 277
Issue: 20
Pages: 17616-22
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Publication
1748588 | -
First Author: Hubert W
Year: 1991
Journal: Int J Psychophysiol
Title: Autonomic, neuroendocrine, and subjective responses to emotion-inducing film stimuli.
Volume: 11
Issue: 2
Pages: 131-40
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Publication
16940418 | J:140440
First Author: Pula G
Year: 2006
Journal: Blood
Title: PKCdelta regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation.
Volume: 108
Issue: 13
Pages: 4035-44
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Publication
19587372 | J:153266
First Author: Chari R
Year: 2009
Journal: Blood
Title: Lyn, PKC-delta, SHIP-1 interactions regulate GPVI-mediated platelet-dense granule secretion.
Volume: 114
Issue: 14
Pages: 3056-63
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Publication
17558407 | -
First Author: Arts HH
Year: 2007
Journal: Nat Genet
Title: Mutations in the gene encoding the basal body protein RPGRIP1L, a nephrocystin-4 interactor, cause Joubert syndrome.
Volume: 39
Issue: 7
Pages: 882-8
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Publication
12874105 | -
First Author: Castagnet P
Year: 2003
Journal: Hum Mol Genet
Title: RPGRIP1s with distinct neuronal localization and biochemical properties associate selectively with RanBP2 in amacrine neurons.
Volume: 12
Issue: 15
Pages: 1847-63
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Publication
21685204 | -
First Author: Coene KL
Year: 2011
Journal: Hum Mol Genet
Title: The ciliopathy-associated protein homologs RPGRIP1 and RPGRIP1L are linked to cilium integrity through interaction with Nek4 serine/threonine kinase.
Volume: 20
Issue: 18
Pages: 3592-605
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Publication
18281315 | -
First Author: Devuyst O
Year: 2008
Journal: Nephrol Dial Transplant
Title: Mutations in RPGRIP1L: extending the clinical spectrum of ciliopathies.
Volume: 23
Issue: 5
Pages: 1500-3
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Publication
28559319 | -
First Author: Oberhofer A
Year: 2017
Journal: Proc Natl Acad Sci U S A
Title: Myosin Va's adaptor protein melanophilin enforces track selection on the microtubule and actin networks in vitro.
Volume: 114
Issue: 24
Pages: E4714-E4723
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Publication
15173169 | -
First Author: Junutula JR
Year: 2004
Journal: J Biol Chem
Title: Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins.
Volume: 279
Issue: 32
Pages: 33430-7
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Publication
19702578 | -
First Author: Kelly EE
Year: 2009
Journal: Biol Cell
Title: Class I Rab11-family interacting proteins are binding targets for the Rab14 GTPase.
Volume: 102
Issue: 1
Pages: 51-62
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14532427 | -
 
First Author: Prekeris R
Year: 2003
Journal: ScientificWorldJournal
Title: Rabs, Rips, FIPs, and endocytic membrane traffic.
Volume: 3
Pages: 870-80
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Protein Domain
IPR027436 | PKC_delta
Type: Family
Description: Protein kinase C, delta type is a member of the novel protein kinase C (nPKC) family. PKC delta plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis [], but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death []. PKC delta is also involves in tumor suppression [], required for oxygen radical production by NADPH oxidase [, ]and acts as positive or negative regulator in platelet functional responses [, ].PKC is a family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol [, ]. Members of this family play key regulatory roles in various cellular processes. Currently, there are ten isoforms of PKC which can be classified into classical (alpha, beta I, beta II, gamma), novel (delta, epsilon, eta, theta) and atypical (zeta, iota/lambda) types based on their primary structure and biochemical characteristics [, , ]. All PKCs contain a C-terminal kinase domain and an N-terminal regulatory domain.The N-terminal regulatory domain of nPKC consists of a C2 domain follows by a double C1 domain (C1A and C1B). The C2 domain does not respond to calcium which makes nPKC diacylglycerol-sensitive but calcium-independent [, , ].
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Protein Domain
IPR027274 | PKC_epsilon
Type: Family
Description: Protein kinase C, epsilon is a novel type of protein kinase C (nPKC). PKC epsilon plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion [], motility, migration []and cell cycle, functions in neuron growth [, , ]and ion channel regulation [, ], and is involved in immune response [], cancer cell invasion and regulation of apoptosis [, ].The N-terminal regulatory domain of nPKC consists of a C2 domain follows by a double C1 domain (C1A and C1B). The C2 domain does not respond to calcium which makes nPKC diacylglycerol-sensitive but calcium-independent [, , ].PKC is a family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol [, ]. Members of this family play key regulatory roles in various cellular processes. Currently, there are ten isoforms of PKC which can be classified into classical (alpha, beta I, beta II, gamma), novel (delta, epsilon, eta, theta) and atypical (zeta, iota/lambda) types based on their primary structure and biochemical characteristics [, , ]. All PKCs contain a C-terminal kinase domain and an N-terminal regulatory domain.
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Protein Domain
IPR027431 | PKC_eta
Type: Family
Description: Protein kinase C, eta type is a member of the novel protein kinase C (nPKC) family. It is involved in the regulation of cell differentiation in keratinocytes []and pre-B cell receptor []. PKC eta also mediates regulation of epithelial tight junction integrity []and foam cell formation []. In addition, it is required for glioblastoma proliferation []and apoptosis prevention in MCF-7 cells[].PKC is a family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol [, ]. Members of this family play key regulatory roles in various cellular processes. Currently, there are ten isoforms of PKC which can be classified into classical (alpha, beta I, beta II, gamma), novel (delta, epsilon, eta, theta) and atypical (zeta, iota/lambda) types based on their primary structure and biochemical characteristics [, , ]. All PKCs contain a C-terminal kinase domain and an N-terminal regulatory domain.The N-terminal regulatory domain of nPKC consists of a C2 domain follows by a double C1 domain (C1A and C1B). The C2 domain does not respond to calcium which makes nPKC diacylglycerol-sensitive but calcium-independent [, , ].
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Protein Domain
IPR024175 | Pept_S1A_C1r/C1S/mannan-bd
Type: Family
Description: These proteins belong to MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)), subfamily S1A.This family contains the mammalian mannan-binding lectin-associated serine proteases 1 and 2 (MASP1 and MASP2) and complement components C1s and C1r. The C1 complex, containing C1q, C1s, and C1r, triggers the classical complement pathway. When C1q interacts with antibody, C1r becomes autocatalytically activated. Activated C1r in turn activates C1s, which then cleaves C2 and C4 in the classical pathway.Mannose-binding lectin (MBL) complexes with MASP1, MASP2, and a smaller alternative splice product of the MASP2 gene. Binding of MBL to carbohydrates on the surface of microorganisms triggers activation of the associated MASPs. Then MASP1 activates C3 and C2, whereas MASP2 activates C4 and C2 []. Based on the fact that the gene structures of MASP1, C1r, and C1s are similar except that C1r and C1s lack introns in the region encoding the trypsin domain, it has been proposed that the MASP proteins evolved earlier than C1r and C1s []. The complement pathway is also involved in development [].These sequences typically contain a signal sequence, followed by a CUB domain, an EGF-like domain (which often is not detected), a second CUB domain, two sushi domains (sometimes only one is detected), and a trypsin domain.
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Protein Domain
IPR037442 | Melanophilin_FYVE-rel_dom
Type: Domain
Description: Melanophilin, also termed SlaC2-a, or exophilin-3, is a GTP-bound form of Rab27A-, myosin Va-, and actin-binding protein present on melanosomes. It is involved in the control of transferring of melanosomes from microtubules to actin filaments. It also functions as a melanocyte type myosin Va (McM5) binding partner and directly activates the actin-activated ATPase activity of McM5 through forming a tripartite protein complex with Rab27A and an actin-based motor myosin Va [,]. SlaC2-a belongs to the Slp homologue lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites []. The SHD1 and SHD2 of SlaC2-a are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-a has a middle myosin-binding domain and a C-terminal actin-binding domain [].
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Protein Domain
IPR037789 | FIP_classI
Type: Family
Description: Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11/Rab11-FIP5, RCP/RAB11FIP1, and FIP2) which contain a C2 domain after N terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes []. Class I FIPs, but not the class II FIPs, also interact with Rab14 [].The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. Recent studies have identified several Rab11-FIP complex-binding proteins that regulate distinct membrane traffic pathways [].This family consist of class I FIPs.
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Protein Domain
IPR031139 | RPGRIP1_fam
Type: Family
Description: RPGR-interacting protein 1 (RPGRIP1) is mutated in the eye disease Leber congenital amaurosis (LCA) and its structural homologue, RPGRIP1-like (RPGRIP1L, also called NPHP8 or fantom), is mutated in many different ciliopathies [, ]. Both are multidomain proteins that are predicted to interact with retinitis pigmentosa G-protein regulator (RPGR) []. Both consist of an N-terminal coiled coil domain, two C2 domains (C2N and C2C), and a C-terminal RPGR-interacting domain (RID). RID is a C2 domain with a canonical beta sandwich structure that does not bind Ca2+ and/or phospholipids and thus constitutes a unique type of protein-protein interaction module [].Both RPGRIP1 and RPGRIP1L interact with the ciliary transition zone protein nephrocystin 4 (NPHP4) via their C2C domain [, ]. An hypothesis is that RPGRIP1 and RPGRIP1L function as cilium-specific scaffolds that recruit a Nek4 signaling network which regulates cilium stability []. The expression of RPGRIP1 seems to be limited to photoreceptors and amacrine cells in the retina [], whereas RPGRIP1L is found in other tissues as well.
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Publication
23399561 | J:198986
First Author: Umebayashi H
Year: 2013
Journal: Biochem Biophys Res Commun
Title: Phospholipase C-related catalytically inactive protein, a novel microtubule-associated protein 1 light chain 3-binding protein, negatively regulates autophagosome formation.
Volume: 432
Issue: 2
Pages: 268-74
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Publication
22349825 | J:244534
First Author: Kikuchi K
Year: 2013
Journal: Oncogene
Title: Protein kinase C iota as a therapeutic target in alveolar rhabdomyosarcoma.
Volume: 32
Issue: 3
Pages: 286-95
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Publication
35859073 | J:326813
First Author: Georgieva AM
Year: 2022
Journal: Nat Commun
Title: Inactivation of Sirt6 ameliorates muscular dystrophy in mdx mice by releasing suppression of utrophin expression.
Volume: 13
Issue: 1
Pages: 4184
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Publication
18276788 | J:132272
First Author: Nagaraju K
Year: 2008
Journal: Am J Pathol
Title: Dysferlin deficiency enhances monocyte phagocytosis: a model for the inflammatory onset of limb-girdle muscular dystrophy 2B.
Volume: 172
Issue: 3
Pages: 774-85
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Publication
23281710 | J:211540
First Author: Singh RK
Year: 2013
Journal: FEBS J
Title: Distinct and opposing roles for Rab27a/Mlph/MyoVa and Rab27b/Munc13-4 in mast cell secretion.
Volume: 280
Issue: 3
Pages: 892-903
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Publication
25198651 | J:221523
First Author: Kanagawa M
Year: 2014
Journal: PLoS One
Title: Contribution of dysferlin deficiency to skeletal muscle pathology in asymptomatic and severe dystroglycanopathy models: generation of a new model for Fukuyama congenital muscular dystrophy.
Volume: 9
Issue: 9
Pages: e106721
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Publication
11447257 | J:79298
First Author: Polic B
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: How alpha beta T cells deal with induced TCR alpha ablation.
Volume: 98
Issue: 15
Pages: 8744-9
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Publication
32929010 | J:296273
First Author: Gupta S
Year: 2020
Journal: Proc Natl Acad Sci U S A
Title: Hemostasis vs. homeostasis: Platelets are essential for preserving vascular barrier function in the absence of injury or inflammation.
Volume: 117
Issue: 39
Pages: 24316-24325
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Publication
18086860 | J:130864
First Author: Zou X
Year: 2007
Journal: J Exp Med
Title: Heavy chain-only antibodies are spontaneously produced in light chain-deficient mice.
Volume: 204
Issue: 13
Pages: 3271-83
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Publication
24453992 | J:208787
First Author: Kikuchi K
Year: 2014
Journal: PLoS Genet
Title: Cell-cycle dependent expression of a translocation-mediated fusion oncogene mediates checkpoint adaptation in rhabdomyosarcoma.
Volume: 10
Issue: 1
Pages: e1004107
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Publication
18755982 | J:143800
First Author: Anderson KE
Year: 2008
Journal: Blood
Title: CD18-dependent activation of the neutrophil NADPH oxidase during phagocytosis of Escherichia coli or Staphylococcus aureus is regulated by class III but not class I or II PI3Ks.
Volume: 112
Issue: 13
Pages: 5202-11
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Publication
17080428 | J:116658
First Author: Schouwey K
Year: 2007
Journal: Dev Dyn
Title: Notch1 and Notch2 receptors influence progressive hair graying in a dose-dependent manner.
Volume: 236
Issue: 1
Pages: 282-9
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Publication
16024047 | J:128550
First Author: Heiman-Patterson TD
Year: 2005
Journal: J Neurol Sci
Title: Background and gender effects on survival in the TgN(SOD1-G93A)1Gur mouse model of ALS.
Volume: 236
Issue: 1-2
Pages: 1-7
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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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