|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 801 to 900 out of 8285 for C2

<< First    < Previous  |  Next >    Last >>
0.025s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Publication
37059290 | J:355534
 
First Author: Sener EF
Year: 2023
Journal: Prog Neuropsychopharmacol Biol Psychiatry
Title: Heterozygous Cc2d1a mice show sex-dependent changes in the Beclin-1/p62 ratio with impaired prefrontal cortex and hippocampal autophagy.
Volume: 125
Pages: 110764
•
•
•
•
•
Publication
31721010 | J:319512
First Author: Dana H
Year: 2020
Journal: Neuromolecular Med
Title: Disregulation of Autophagy in the Transgenerational Cc2d1a Mouse Model of Autism.
Volume: 22
Issue: 2
Pages: 239-249
•
•
•
•
•
Publication
22833682 | J:190401
First Author: Chen KR
Year: 2012
Journal: J Biol Chem
Title: TBK1-associated protein in endolysosomes (TAPE)/CC2D1A is a key regulator linking RIG-I-like receptors to antiviral immunity.
Volume: 287
Issue: 38
Pages: 32216-21
•
•
•
•
•
Protein Coding Gene
MGI:1261872 | Wwc2
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein
Q3UYK4
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: true
•
•
•
•
•
Protein
A0A1D5RLP0
Organism: Mus musculus/domesticus
Length: 61  
Fragment?: true
•
•
•
•
•
Protein
Q9DB19
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: false
•
•
•
•
•
Protein Domain
IPR038983 | C2CD5
Type: Family
Description: C2CD5, also known as CDP138 or KIAA0528, is a C2 domain-containing phosphoprotein. It is a substrate for protein kinase Akt2, and it may be involved in the regulation of GLUT4 vesicle-plasma membrane fusion in response to insulin. The C2 domain of C2CD5 was shown to be capable of binding Ca(2+) and lipid membranes []. Other studies indicate that C2CD5 is a CDK5- and FIBP-interacting protein, forming a complex with these proteins that is involved in cell proliferation and migration [].
•
•
•
•
•
HT Experiment
E-MEXP-1853 | Transcription profiling of mouse fetal and early adult liver
 
Experiment Type: transcription profiling by array
Study Type: Baseline
Source: ArrayExpress
•
•
•
•
•
HT Experiment
E-MTAB-9213 | RNA-Seq of pancreatic islets from whole body knockout of lncRNA Pax6os1 mice
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: ArrayExpress
•
•
•
•
•
Protein Domain
IPR043549 | C2C4C/C2C4D
Type: Family
Description: The function of C2 calcium-dependent domain-containing protein 4C/4D is not known. The C2 domain is a Ca2 -dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking.
•
•
•
•
•
Protein Domain
IPR030533 | C2CD4
Type: Family
Description: The function of C2 calcium-dependent domain-containing protein 4C is not known. The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking.
•
•
•
•
•
Protein
B7FAU1
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: true
•
•
•
•
•
Protein Coding Gene
MGI:2388637 | Wwc1
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Publication
33297935 | J:299152
First Author: Hiltunen AE
Year: 2020
Journal: Mol Med
Title: Variant in NHLRC2 leads to increased hnRNP C2 in developing neurons and the hippocampus of a mouse model of FINCA disease.
Volume: 26
Issue: 1
Pages: 123
•
•
•
•
•
Publication
10403379 | J:224747
First Author: Nakayama T
Year: 1999
Journal: FEBS Lett
Title: Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain protein family, with OS-9, the product of a gene frequently amplified in osteosarcoma.
Volume: 453
Issue: 1-2
Pages: 77-80
•
•
•
•
•
Protein Domain
IPR037720 | C2B_Ferlin
Type: Domain
Description: Ferlins are involved in vesicle fusion events []. Ferlins and other proteins, such as synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1).Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins [, , ].This entry represents the second C2 repeat of ferlins, C2B, which has a type-II topology.
•
•
•
•
•
Protein Domain
IPR037722 | C2C_Ferlin
Type: Domain
Description: Ferlins are involved in vesicle fusion events []. Ferlins and other proteins, such as synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1).Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins [, , ].This entry represents the third C2 repeat of ferlins, C2C, and has a type-II topology.
•
•
•
•
•
Protein Domain
IPR037723 | C2D_Ferlin
Type: Domain
Description: Ferlins are involved in vesicle fusion events []. Ferlins and other proteins, such as synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1).Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins [, , ].This entry represents the fourth C2 repeat of ferlins, C2D, which has a type-II topology.
•
•
•
•
•
Protein Domain
IPR037724 | C2E_Ferlin
Type: Domain
Description: Ferlins are involved in vesicle fusion events []. Ferlins and other proteins, such as synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1).Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins [, , ].This entry represents the fifth C2 repeat of ferlins, C2E, which has a type-II topology.
•
•
•
•
•
Protein Domain
IPR037725 | C2F_Ferlin
Type: Domain
Description: Ferlins are involved in vesicle fusion events []. Ferlins and other proteins, such as synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1).Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins [, , ].This entry represents the sixth C2 repeat of ferlins, C2E, which has a type-II topology.
•
•
•
•
•
Protein Domain
IPR037726 | C2A_Ferlin
Type: Domain
Description: Ferlins are involved in vesicle fusion events []. Ferlins and other proteins, such as synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1).Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins [, , ].This entry represents the first C2 repeat of ferlins, C2A, which has a type-II topology.
•
•
•
•
•
Protein Coding Gene
MGI:1921991 | C2cd5
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1922947 | C2cd4b
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:3645763 | C2cd4a
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Publication
31031595 | J:285509
 
First Author: Song L
Year: 2019
Journal: Front Cell Neurosci
Title: The Neuroprotection of KIBRA in Promoting Neuron Survival and Against Amyloid β-Induced Apoptosis.
Volume: 13
Pages: 137
•
•
•
•
•
Publication
35367771 | J:323105
 
First Author: Han X
Year: 2022
Journal: EBioMedicine
Title: KIBRA regulates amyloid β metabolism by controlling extracellular vesicles secretion.
Volume: 78
Pages: 103980
•
•
•
•
•
Publication
37347662 | J:348577
First Author: Quigley LD
Year: 2023
Journal: Cell Rep
Title: Experience alters hippocampal and cortical network communication via a KIBRA-dependent mechanism.
Volume: 42
Issue: 6
Pages: 112662
•
•
•
•
•
Publication
9804756 | J:50924
First Author: Nagano F
Year: 1998
Journal: J Biol Chem
Title: Interaction of Doc2 with tctex-1, a light chain of cytoplasmic dynein. Implication in dynein-dependent vesicle transport.
Volume: 273
Issue: 46
Pages: 30065-8
•
•
•
•
•
Publication
10851170 | -
First Author: Brose N
Year: 2000
Journal: Curr Opin Neurobiol
Title: Regulation of transmitter release by Unc-13 and its homologues.
Volume: 10
Issue: 3
Pages: 303-11
•
•
•
•
•
Publication
8816702 | J:35371
First Author: Südhof TC
Year: 1996
Journal: Neuron
Title: Synaptotagmins: C2-domain proteins that regulate membrane traffic.
Volume: 17
Issue: 3
Pages: 379-88
•
•
•
•
•
Publication
7826360 | -
First Author: Orita S
Year: 1995
Journal: Biochem Biophys Res Commun
Title: Doc2: a novel brain protein having two repeated C2-like domains.
Volume: 206
Issue: 2
Pages: 439-48
•
•
•
•
•
Protein Domain
IPR014638 | Doc2
Type: Family
Description: Neurotransmitter release from nerve termini in the brain is regulated by several families of Ca2+-binding proteins with tandem C2 domains () []. The C2 domain confers the ability to binding phospholipids in a Ca2+-dependent fashion.Doc2 (double C2-like domain-containing protein) has one Munc13-interacting domain (Munc13 is a peripheral membrane protein in the plasma membrane of nerve termini). The interaction between Doc2 and Munc13-1 is thought to underlie the molecular mechanism of phorbol ester enhancement of neurotransmitter release [].Doc2 consists of three isoforms, Doc2alpha, beta and gamma. Doc2alpha is specifically expressed in neuronal cells and has been implicated in Ca2+-dependent neurotransmitter release, whereas Doc2beta is ubiquitously expressed [, ]. In contrast to the other Doc2 isoforms, the C2 domains of Doc2gamma lacks the Ca2+-dependent phospholipid binding activity. The highest expression of Doc2gamma mRNA is found in the heart, but occurs ubiquitously, the same as Doc2beta. Doc2gamma may also function as an effector for Munc13-1 and may be involved in the regulation of vesicular trafficking [].
•
•
•
•
•
Protein Coding Gene
MGI:1916025 | Atp6v1c2
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Publication
8771209 | -
First Author: Ponting CP
Year: 1996
Journal: Protein Sci
Title: Extending the C2 domain family: C2s in PKCs delta, epsilon, eta, theta, phospholipases, GAPs, and perforin.
Volume: 5
Issue: 1
Pages: 162-6
•
•
•
•
•
Publication
17631528 | -
First Author: Yang H
Year: 2007
Journal: Plant Physiol
Title: The Arabidopsis BAP1 and BAP2 genes are general inhibitors of programmed cell death.
Volume: 145
Issue: 1
Pages: 135-46
•
•
•
•
•
Publication
23872431 | -
First Author: Kawarazaki T
Year: 2013
Journal: Biochim Biophys Acta
Title: A low temperature-inducible protein AtSRC2 enhances the ROS-producing activity of NADPH oxidase AtRbohF.
Volume: 1833
Issue: 12
Pages: 2775-2780
•
•
•
•
•
Protein Domain
IPR014020 | Tensin_C2-dom
Type: Domain
Description: Tensins constitute an eukaryotic family of lipid phosphatases that are defined by thepresence of two adjacent domains: a lipid phosphatase domain and a C2-like domain. The tensin-type C2 domain has a structure similar to the classical C2 domain (see ) that mediates the Ca2+-dependent membrane recruitment of several signalling proteins. However the tensin-type C2 domain lacks two of the three conserved loops that bind Ca2+, and in this respect it is similar to the C2 domains of PKC-type [, ]. The tensin-type C2 domain can bind phopholipid membranes in a Ca2+ independent manner []. In the tumour suppressor protein PTEN, the best characterised member of the family, the lipid phosphatase domain was shown to specifically dephosphorylate the D3 position of the inositol ring of the lipid second messenger, phosphatydilinositol-3-4-5-triphosphate (PIP3). The lipid phosphatase domain contains the signature motif HCXXGXXR present in the active sites of protein tyrosine phosphatases (PTPs) and dual specificity phosphatases (DSPs). Furthermore, two invariant lysines are found only in the tensin-type phosphatase motif (HCKXGKXR) and are suspected to interact with the phosphate group at position D1 and D5 of the inositol ring [, ]. The C2 domain is found at the C terminus of the tumour suppressor protein PTEN (phosphatidyl-inositol triphosphate phosphatase). This domain may include a CBR3 loop, indicating a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc suggesting that the C2 domain productively positions the catalytic part of the protein on the membrane. The crystal structure of the PTEN tumour suppressor has been solved []. The lipid phosphatase domain has a structure similar to the dual specificity phosphatase (see ). However, PTEN has a larger active site pocket that could be important to accommodate PI(3,4,5)P3. Proteins known to contain a phosphatase and a C2 tensin-type domain are listed below: Tensin, a focal-adhesion molecule that binds to actin filaments. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton.Phosphatase and tensin homologue deleted on chromosome 10 protein (PTEN). It antagonizes PI 3-kinase signalling by dephosphorylating the 3-position of the inositol ring of PI(3,4,5)P3 and thus inactivates downstream signalling. It plays major roles both during development and in the adult to control cell size, growth, and survival.Auxilin. It binds clathrin heavy chain and promotes its assembly into regular cages.Cyclin G-associated kinase or auxilin-2. It is a potential regulator of clathrin-mediated membrane trafficking.
•
•
•
•
•
Protein Domain
IPR044750 | C2_SRC2/BAP
Type: Domain
Description: This is the C2 domain found in plant proteins, including SRC2 (Soybean genes Regulated by Cold 2) and BAP1/2 (BON1-associated protein 1/2), which are involved in defence responses [, ]. SRC2 is induced after pathogen infiltration and in cold conditions. Arabidopsis SRC2 homologue functions as a calcium-dependent activator of the NADPH oxidase AtRbohF, that mediates reactive oxygen species (ROS) production after cold induction. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding []. BAP1/2 are negative regulators of cell death and defense responses, as they repress the activity of disease resistance (R) genes [].
•
•
•
•
•
Publication
17018531 | J:127209
First Author: Liou HL
Year: 2006
Journal: J Biol Chem
Title: NPC2, the protein deficient in Niemann-Pick C2 disease, consists of multiple glycoforms that bind a variety of sterols.
Volume: 281
Issue: 48
Pages: 36710-23
•
•
•
•
•
Publication
20007703 | J:161675
First Author: Goldman SD
Year: 2010
Journal: J Biol Chem
Title: Niemann-Pick C1 functions independently of Niemann-Pick C2 in the initial stage of retrograde transport of membrane-impermeable lysosomal cargo.
Volume: 285
Issue: 7
Pages: 4983-94
•
•
•
•
•
Protein
Q8CHZ7
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
•
•
•
•
•
Protein
A0A1L1SSP2
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: true
•
•
•
•
•
Publication
12559952 | -
First Author: Kremerskothen J
Year: 2003
Journal: Biochem Biophys Res Commun
Title: Characterization of KIBRA, a novel WW domain-containing protein.
Volume: 300
Issue: 4
Pages: 862-7
•
•
•
•
•
Publication
24682284 | -
First Author: Wennmann DO
Year: 2014
Journal: Mol Biol Evol
Title: Evolutionary and molecular facts link the WWC protein family to Hippo signaling.
Volume: 31
Issue: 7
Pages: 1710-23
•
•
•
•
•
Publication
28815883 | -
First Author: Zhang Y
Year: 2017
Journal: J Cell Mol Med
Title: WWC2 is an independent prognostic factor and prevents invasion via Hippo signalling in hepatocellular carcinoma.
Volume: 21
Issue: 12
Pages: 3718-3729
•
•
•
•
•
Protein Domain
IPR039934 | C2CD2/C2CD2L
Type: Family
Description: This entry includes C2 domain-containing protein 2 (C2CD2) and C2CD2-like (C2CD2L) proteins. C2CD2L, also known as TMEM24, is an endoplasmic reticulum (ER)-anchored membrane protein that binds lipids and transports the phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2]precursor phosphatidylinositol between bilayers, allowing replenishment of PI(4,5)P2 hydrolyzed during signaling []. The function of C2CD2 is not known.
•
•
•
•
•
Protein Domain
IPR037771 | C2_WWC
Type: Domain
Description: The WWC (WW-and-C2-domain-containing protein) family negatively regulates cell proliferation and organ growth by suppressing the transcriptional activityof YAP, a major effector of the Hippo pathway. They activate large tumour suppressor 1 and 2 kinases (LATS1/2), which in turn phosphorylates the transcriptional co-activator YAP [, ]. Their two amino terminal WW domains mediate binding to target proteins, whereas the internal C2 domain is required for membrane association. WWC family members include WWC1 (also known as KIBRA), WWC2 and WWC3 [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Whereas the majority of known C2 domains have a role in Ca2+-dependent vesicle membrane association, these protein modules are also involved in Ca2+-insensitive membrane targeting as well as in intracellular protein-protein interactions. The C2 domain of KIBRA has been shown to have Ca2+-dependent-binding specificity for monophosphorylated phosphatidylinositols [].
•
•
•
•
•
GO Term
GO:0071020 | post-spliceosomal complex
•
•
•
•
•
Publication
29378832 | J:284780
 
First Author: Zhou QL
Year: 2018
Journal: Mol Cell Biol
Title: Membrane Trafficking Protein CDP138 Regulates Fat Browning and Insulin Sensitivity through Controlling Catecholamine Release.
Volume: 38
Issue: 8
•
•
•
•
•
Publication
17185389 | J:159145
First Author: Dawe HR
Year: 2007
Journal: Hum Mol Genet
Title: The Meckel-Gruber Syndrome proteins MKS1 and meckelin interact and are required for primary cilium formation.
Volume: 16
Issue: 2
Pages: 173-86
•
•
•
•
•
Publication
19515853 | J:151414
First Author: Tammachote R
Year: 2009
Journal: Hum Mol Genet
Title: Ciliary and centrosomal defects associated with mutation and depletion of the Meckel syndrome genes MKS1 and MKS3.
Volume: 18
Issue: 17
Pages: 3311-23
•
•
•
•
•
Protein Domain
IPR041847 | C2_cPLA2
Type: Domain
Description: This entry represents the C2 domain found in cytosolic phospholipase A2 (cPLA2), which hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. The cooperative binding of two Ca(2+) ions to the C2 domain of cPLA2-alpha induces docking to phosphatidylcholine (PC) membranes []. This domain have a type-II C2 domain topology. C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions [, ].
•
•
•
•
•
Publication
14573689 | J:86279
First Author: Erb KJ
Year: 2003
Journal: Infect Immun
Title: Mice deficient in nuclear factor of activated T-cell transcription factor c2 mount increased Th2 responses after infection with Nippostrongylus brasiliensis and decreased Th1 responses after mycobacterial infection.
Volume: 71
Issue: 11
Pages: 6641-7
•
•
•
•
•
Publication
8674414 | J:33548
First Author: Kaestner KH
Year: 1996
Journal: Development
Title: Clustered arrangement of winged helix genes fkh-6 and MFH-1: possible implications for mesoderm development.
Volume: 122
Issue: 6
Pages: 1751-8
•
•
•
•
•
Publication
34048600 | J:347777
First Author: Pond HL
Year: 2021
Journal: J Neurosci Res
Title: Digging behavior discrimination test to probe burrowing and exploratory digging in male and female mice.
Volume: 99
Issue: 9
Pages: 2046-2058
•
•
•
•
•
Publication
39208980 | J:353955
 
First Author: Vahid-Ansari F
Year: 2024
Journal: Neuropharmacology
Title: Rapid reorganization of serotonin projections and antidepressant response to 5-HT1A-biased agonist NLX-101 in fluoxetine-resistant cF1ko mice.
Volume: 261
Pages: 110132
•
•
•
•
•
Publication
38050173 | J:358827
 
First Author: Vahid-Ansari F
Year: 2024
Journal: J Neurosci
Title: Chronic Desipramine Reverses Deficits in Cell Activity, Norepinephrine Innervation, and Anxiety-Depression Phenotypes in Fluoxetine-Resistant cF1ko Mice.
Volume: 44
Issue: 3
•
•
•
•
•
Protein
Q3UJG0
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: false
•
•
•
•
•
Regulatory Region
MGI:7119820 | Rr231598
Type: CTCF_binding_site
Organism: mouse, laboratory
•
•
•
•
•
Allele
Chchd2<em1Dpn> | MGI:7532638
Name: coiled-coil-helix-coiled-coil-helix domain containing 2; endonuclease-mediated mutation 1, Derek P Narendra
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
•
•
•
•
•
Regulatory Region
MGI:6955355 | Rr67133
Type: CTCF_binding_site
Organism: mouse, laboratory
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: CMHD Targeted Library C2 (Tcp) C57BL/6N L1L2_NTARU-1
Creator: CMHD
Vector Type: Not Specified
Vector: L1L2_NTARU-1
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: CMHD Targeted Library C2 (Tcp) C57BL/6N L1L2_NTARU-0
Creator: CMHD
Vector Type: Not Specified
Vector: L1L2_NTARU-0
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: CMHD Targeted Library C2 (Tcp) C57BL/6N L1L2_NTARU-2
Creator: CMHD
Vector Type: Not Specified
Vector: L1L2_NTARU-2
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: CMHD Targeted Library C2 (Tcp) C57BL/6N L1L2_GOHANU
Creator: CMHD
Vector Type: Not Specified
Vector: L1L2_GOHANU
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: CMHD Targeted Library C2 (Tcp) C57BL/6N L1L2_NTARU-K
Creator: CMHD
Vector Type: Not Specified
Vector: L1L2_NTARU-K
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: MFGC Targeted Library C2 (Tcp) C57BL/6N L1L2_NTARU-2
Creator: MFGC
Vector Type: Not Specified
Vector: L1L2_NTARU-2
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: MFGC Targeted Library C2 (Tcp) C57BL/6N L1L2_NTARU-1
Creator: MFGC
Vector Type: Not Specified
Vector: L1L2_NTARU-1
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: MFGC Targeted Library C2 (Tcp) C57BL/6N L1L2_NTARU-0
Creator: MFGC
Vector Type: Not Specified
Vector: L1L2_NTARU-0
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: MFGC Targeted Library C2 (Tcp) C57BL/6N L1L2_GOHANU
Creator: MFGC
Vector Type: Not Specified
Vector: L1L2_GOHANU
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: MFGC Targeted Library C2 (Tcp) C57BL/6N L1L2_NTARU-K
Creator: MFGC
Vector Type: Not Specified
Vector: L1L2_NTARU-K
•
•
•
•
•
Cell Line Derivation
Cell Line Derivation
Derivation Type: Targeted
Name: MFGC Targeted Library C2 (Tcp) C57BL/6N L1L2_MFGC3
Creator: MFGC
Vector Type: Not Specified
Vector: L1L2_MFGC3
•
•
•
•
•
Protein
Q91YQ3
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: false
•
•
•
•
•
Protein
Q9D485
Organism: Mus musculus/domesticus
Length: 750  
Fragment?: false
•
•
•
•
•
Protein
D3YTN0
Organism: Mus musculus/domesticus
Length: 38  
Fragment?: true
•
•
•
•
•
Protein
A0A2R8VHB0
Organism: Mus musculus/domesticus
Length: 44  
Fragment?: true
•
•
•
•
•
Protein
A0A140LHZ2
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: true
•
•
•
•
•
Protein
A0A2R8VK06
Organism: Mus musculus/domesticus
Length: 30  
Fragment?: true
•
•
•
•
•
Protein
A0A338P709
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
•
•
•
•
•
Protein
Q80UG7
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: false
•
•
•
•
•
Protein
A0A1D5RLH0
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: true
•
•
•
•
•
Protein
A0A1Y7VJ89
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
•
•
•
•
•
Protein
Q8C6J4
Organism: Mus musculus/domesticus
Length: 414  
Fragment?: true
•
•
•
•
•
Protein
Q3U4B9
Organism: Mus musculus/domesticus
Length: 319  
Fragment?: false
•
•
•
•
•
Protein
V9GWV8
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: true
•
•
•
•
•
Protein
S4R212
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: true
•
•
•
•
•
Protein
A0A140LI21
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
•
•
•
•
•
Protein
Q8C8C0
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
•
•
•
•
•
Protein
Q8C944
Organism: Mus musculus/domesticus
Length: 125  
Fragment?: false
•
•
•
•
•
Publication
10361272 | -
First Author: Heinisch JJ
Year: 1999
Journal: Mol Microbiol
Title: The protein kinase C-mediated MAP kinase pathway involved in the maintenance of cellular integrity in Saccharomyces cerevisiae.
Volume: 32
Issue: 4
Pages: 671-80
•
•
•
•
•
Publication
15643058 | -
First Author: Denis V
Year: 2005
Journal: Eukaryot Cell
Title: Molecular analysis reveals localization of Saccharomyces cerevisiae protein kinase C to sites of polarized growth and Pkc1p targeting to the nucleus and mitotic spindle.
Volume: 4
Issue: 1
Pages: 36-45
•
•
•
•
•
Publication
29069410 | -
 
First Author: Heinisch JJ
Year: 2018
Journal: FEMS Microbiol Rev
Title: Protein kinase C in fungi-more than just cell wall integrity.
Volume: 42
Issue: 1
•
•
•
•
•
Protein Domain
IPR037778 | C2_fungal_PKC
Type: Domain
Description: Protein kinase C (PKC) is a member of a family of Ser/Thr phosphotransferases that are involved in many cellular signaling pathways. Fungi have only one or two PKCs in contrast to mammals, which have at least 9 []. Saccharomyces cerevisiae contains a single PKC isozyme, Pkc1p, which contains all of the regulatory motifs found in mammalian PKCs []. In addition to its main function in maintaining cell integrity, fungi PKCs have been implicated in the regulation of diverse processes such as the organization of the actin cytoskeleton, autophagy and apoptosis, cell cycle control, cytokinesis and genetic stability [, ]. PKC has two antiparallel coiled-coiled regions (ACC finger domain) known as HR1 (PKC homology region 1/ Rho binding domain) upstream of the C2 domain and two C1 domains downstream.The C2 domain was first identified in PKC. C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains, like those of PKC, are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions [, , , , ].This entry represents the C2 domain of fungal PKC-like proteins.
•
•
•
•
•
Protein Domain
IPR027007 | C2_DOCK-type_domain
Type: Domain
Description: Rho guanosine triphosphatases (GTPases) are critical regulators of cell motility, polarity, adhesion, cytoskeletal organisation, proliferation, geneexpression, and apoptosis. Conversion of these biomolecular switches to the activated GTP-bound state is controlled by two families of guanine nucleotide exchanges factors (GEFs). DH-PH proteins are a large group of Rho GEFs comprising a catalytic Dbl homology (DH) domain with an adjacent pleckstrin homology (PH) domain within the context of functionally diverse signalling modules. The evolutionarily distinct andsmaller family of DOCK (dedicator of cytokinesis) or CDM (CED-5, DOCK1180, Myoblast city) proteins activate either Rac or Cdc42 to control cell migration, morphogenesis, and phagocytosis. DOCK proteins share the DOCK-type C2 domain (also termed the DOCK-homology region (DHR)-1 or CDM-zizimin homology 1 (CZH1) domain and the DHR-2 domain (also termed the CZH2 or DOCKER domain), [, , , , , ].The ~200 residue DOCK-type C2 domain is located toward the N terminus. It adopts a C2-like architecture and interacts with phosphatidylinositol3,4,5-trisphosphate []to mediate signalling and membrane localization. The central core of the DOCK-type C2 domain domain adopts an antiparallel β-sandwich with the "type II"C2 domain fold (a circular permutation of the more common "type I"topology), in which two 4-stranded sheets with strand order 6-5-2-3 and 7-8-1-4 create convex- and concave-exposed faces, respectively [].Some DOCK proteins are listed below:Mammalian Mammalian dedicator of cytokinesis 180 (DOCK180 or DOCK1),important for cell migration.Mammalian DOCK2, important for lymphocyte development, homong, activation,adhesion, polarization and migration processes.Mammalian DOCK3 (also known as MOCA), is expressed predominantly in neuronsand resides in growth cones and membrane ruffles.Mammalian DOCK4, possesses tumor suppressor properties.Mammalian DOCK9 (zizimin1), plays an important role in dendrite growth inhippocampal neurons through activation of Cdc42.Drosophila melanogaster Myoblast city.Caenorhabditis elegans CED-5.
•
•
•
•
•
Publication
21943600 | J:178552
First Author: Makuch L
Year: 2011
Journal: Neuron
Title: Regulation of AMPA receptor function by the human memory-associated gene KIBRA.
Volume: 71
Issue: 6
Pages: 1022-9
•
•
•
•
•
Gene
288908 | Cc2d1a
Type: gene
Organism: rat
•
•
•
•
•
Gene
116456 | Dnajc2
Type: gene
Organism: rat
•
•
•
•
•
Gene
29684 | Klrc2
Type: gene
Organism: rat
•
•
•
•
•
Gene
293148 | C2cd3
Type: gene
Organism: rat
•
•
•
•
•




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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom