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Search results 1101 to 1200 out of 8285 for C2

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Type Details Score
Publication
15527968 | -
First Author: Warton K
Year: 2004
Journal: Gene
Title: A novel gene family induced by acute inflammation in endothelial cells.
Volume: 342
Issue: 1
Pages: 85-95
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Protein Domain
IPR039208 | C2_Ca-dependent_4
Type: Family
Description: C2 calcium-dependent domain-containing protein 4A (NLF1) and 4B (NLF2) are nuclear factors highly expressed in endothelial cells and induced by acute inflammation. They may have a role in regulating genes that control cellular architecture and adhesion [].
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GXD Expression
GXD Expression
 
Probe: MGI:18501
Assay Type: RNA in situ
Annotation Date: 2009-06-01
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1755021
Pattern: Regionally restricted
Stage: TS21
Assay Id: MGI:3846220
Age: embryonic day 13.5
Note: Expression in areas C1 and C2 and the area postrema.
Specimen Label: not shown E13.5
Detected: true
Specimen Num: 18
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Protein Domain
IPR037784 | C2_PKN
Type: Domain
Description: PKN is a lipid-activated serine/threonine kinase. It is a member of the protein kinase C (PKC) superfamily, but lacks a C1 domain. There are at least 3 different isoforms of PKN (PRK1/PKNalpha/PAK1; PKNbeta, and PRK2/PAK2/PKNgamma). The C-terminal region contains the Ser/Thr type protein kinase domain, while the N-terminal region of PKN contains three antiparallel coiled-coil (ACC) finger domains which are relatively rich in charged residues and contain a leucine zipper-like sequence. These domains binds to the small GTPase RhoA. Following these domains is a C2-like domain. Its C-terminal part functions as an auto-inhibitory region. PKNs are not activated by classical PKC activators such as diacylglycerol, phorbol ester or Ca2+, but instead are activated by phospholipids and unsaturated fatty acids [].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 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 [, , ,].
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Protein Coding Gene
MGI:1915344 | Smarcc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1918491 | Dmrtc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR037752 | C2C_KIAA1228
Type: Domain
Description: The extended-synaptotagmins derive their name from their partial domain structure similarity to the synaptotagmins, characterised by an N-terminal membrane anchor and cytosolically exposed C2 domains. Additionally they contain an SMP (synaptotagmin-like mitochondrial-lipid-binding protein) domain and multiple C2 domains (five in E-Syt1 and three in E-Syt2 and E-Syt3). However, the function of extended-synaptotagmins is different to that of synaptotagmins, which are involved in secretory vesicle tethering to the plasma membrane and exocytosis. The extended-synaptotagmins are located to the endoplasmic reticulum (ER), and tether this organelle to the plasma membrane via their C2 domains. They transport glycerolipids between the two bilayers via their lipid-harboring SMP domains. Ca2+ regulates their membrane tethering and lipid transport function [, , ].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. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry represents the C-terminal C2 domain in extendend synaptotagmins, which have a type-I topology [].
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Publication
39504361 | J:359114
First Author: Chen KR
Year: 2024
Journal: Sci Adv
Title: Endosomes serve as signaling platforms for RIG-I ubiquitination and activation.
Volume: 10
Issue: 45
Pages: eadq0660
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Protein
Q78T81
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: false
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Protein
Q8BQS4
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
A2ASZ7
Organism: Mus musculus/domesticus
Length: 73  
Fragment?: true
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Protein
E9Q4R1
Organism: Mus musculus/domesticus
Length: 370  
Fragment?: false
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Protein
A0A158RFU0
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: false
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Protein Domain
IPR021656 | C2-C2_1
Type: Domain
Description: This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins [].
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Protein Coding Gene
MGI:2444115 | Hecw1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR037786 | C2A_Tac2-N
Type: Domain
Description: Tac2-N (tandem C2 protein in nucleus) contains two C2 domains and a short C terminus including a WHXL motif, which are key in stabilizing transport vesicles to the plasma membrane by binding to a plasma membrane. However, unlike the usual carboxyl-terminal-type (C-type) tandem C2 proteins, it lacks a transmembrane domain, a Slp-homology domain, and a Munc13-1-interacting domain. Homology search analysis indicate that no known protein motifs are located in its N terminus, making Tac2-N a novel class of Ca2+-independent, C-type tandem C2 proteins [].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 [, ].This entry represents the first C2 domain of Tac2-N.
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Protein Domain
IPR037788 | C2B_Tac2-N
Type: Domain
Description: Tac2-N (tandem C2 protein in nucleus) contains two C2 domains and a short C terminus including a WHXL motif, which are key in stabilizing transport vesicles to the plasma membrane by binding to a plasma membrane. However, unlike the usual carboxyl-terminal-type (C-type) tandem C2 proteins, it lacks a transmembrane domain, a Slp-homology domain, and a Munc13-1-interacting domain. Homology search analysis indicate that no known protein motifs are located in its N terminus, making Tac2-N a novel class of Ca2+-independent, C-type tandem C2 proteins [].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 [, ].This entry represents the second C2 domain of Tac2-N.
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Publication
39388350 | J:358155
First Author: Dunham TL
Year: 2024
Journal: Cell Rep
Title: WWC2 modulates GABA(A)-receptor-mediated synaptic transmission, revealing class-specific mechanisms of synapse regulation by WWC family proteins.
Volume: 43
Issue: 10
Pages: 114841
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Protein Coding Gene
MGP_129S1SvImJ_G0020024 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0019980 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0019956 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0019966 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0019768 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1921663 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0020415 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0019314 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0019740 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0019851 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0019840 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0019927 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0020444 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0019077 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0019368 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0029787 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0018873 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
36465112 | J:332010
First Author: Mendoza ML
Year: 2022
Journal: iScience
Title: KIBRA regulates activity-induced AMPA receptor expression and synaptic plasticity in an age-dependent manner.
Volume: 25
Issue: 12
Pages: 105623
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Interaction Experiment
Fukuda M (2001)
Description: Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins.
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Interaction Experiment
Kuroda TS (2002)
Description: Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains.
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Interaction Experiment
Nakatani Y (2000)
Description: Identification of a cellular protein that functionally interacts with the C2 domain of cytosolic phospholipase A(2)alpha.
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Publication
15159548 | J:90669
First Author: Matsumoto M
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: Noc2 is essential in normal regulation of exocytosis in endocrine and exocrine cells.
Volume: 101
Issue: 22
Pages: 8313-8
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Publication
34919125 | J:316788
 
First Author: Yang F
Year: 2022
Journal: Development
Title: C2CD6 regulates targeting and organization of the CatSper calcium channel complex in sperm flagella.
Volume: 149
Issue: 2
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Publication
19232397 | -
First Author: Storch J
Year: 2009
Journal: Biochim Biophys Acta
Title: Niemann-Pick C2 (NPC2) and intracellular cholesterol trafficking.
Volume: 1791
Issue: 7
Pages: 671-8
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Protein
Q8CGW9
Organism: Mus musculus/domesticus
Length: 370  
Fragment?: false
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Protein Coding Gene
MGI:1891883 | C2cd2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR029402 | TGT_C2
Type: Domain
Description: Domain C2 of tRNA-guanine transglycosylase is formed by a four-stranded anti-parallel β-sheet lined with two alpha helices. It has conserved basic residues on the surface of the β-sheets as does the C-terminal domain PUA (). The catalytic domain of TGT has conserved basic residues on the outer surface of the N-terminal three-stranded beta sheet, which closes the barrel. It is postulated that these basic residues from the three domains form a continuous, positively charged patch to which the tRNA binds [].
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Publication
30967557 | J:285941
First Author: Song L
Year: 2019
Journal: Nat Commun
Title: KIBRA controls exosome secretion via inhibiting the proteasomal degradation of Rab27a.
Volume: 10
Issue: 1
Pages: 1639
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Publication
11341920 | -
First Author: Laich A
Year: 2001
Journal: Biochim Biophys Acta
Title: Complement C4bC2 complex formation: an investigation by surface plasmon resonance.
Volume: 1544
Issue: 1-2
Pages: 96-112
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Publication
9642242 | -
First Author: Rawal N
Year: 1998
Journal: J Biol Chem
Title: C5 convertase of the alternative pathway of complement. Kinetic analysis of the free and surface-bound forms of the enzyme.
Volume: 273
Issue: 27
Pages: 16828-35
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Publication
3546307 | -
First Author: Kam CM
Year: 1987
Journal: J Biol Chem
Title: Human complement proteins D, C2, and B. Active site mapping with peptide thioester substrates.
Volume: 262
Issue: 8
Pages: 3444-51
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Protein
Q0VEJ0
Organism: Mus musculus/domesticus
Length: 659  
Fragment?: false
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Protein
Q1A6V0
Organism: Mus musculus/domesticus
Length: 866  
Fragment?: false
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Protein
O35681
Organism: Mus musculus/domesticus
Length: 587  
Fragment?: false
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Protein
Q9R0N5
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
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Protein
Q9R0N8
Organism: Mus musculus/domesticus
Length: 511  
Fragment?: false
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Protein
Q9R0N6
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
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Protein
Q7TN83
Organism: Mus musculus/domesticus
Length: 639  
Fragment?: false
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Protein
Q9R0N4
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
Q9R0N3
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
Q3UY13
Organism: Mus musculus/domesticus
Length: 342  
Fragment?: false
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Protein
Q80U82
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: true
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Protein
S4R1M8
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: true
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Protein
Q3TPH5
Organism: Mus musculus/domesticus
Length: 429  
Fragment?: false
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Protein
Q8QZS8
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
Q3TPW8
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: true
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Protein
Q6P1H9
Organism: Mus musculus/domesticus
Length: 426  
Fragment?: false
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Protein
Q496Q4
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
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Protein
Q3TYC4
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
Q05BE2
Organism: Mus musculus/domesticus
Length: 444  
Fragment?: false
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Protein
D3YWW9
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: false
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Protein
A0A5F8MPS8
Organism: Mus musculus/domesticus
Length: 529  
Fragment?: false
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Protein
Q9JM86
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: true
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Protein
Q496Q3
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
G3X9Y1
Organism: Mus musculus/domesticus
Length: 587  
Fragment?: false
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Protein
Q059J3
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
F2Z3W8
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
Q8C8S6
Organism: Mus musculus/domesticus
Length: 438  
Fragment?: false
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Protein Domain
IPR038250 | TGT_C2_sf
Type: Homologous_superfamily
Description: Archaeosine tRNA-guanine transglycosylase (ArcTGT) is made of an N-terminal catalytic domain and a C-terminal region with unidentified functions. The C-terminal region is divided into three domains, C1, C2, and C3. The catalytic domain of TGT has conserved basic residues on the outer surface of the N-terminal three-stranded beta sheet, which closes the barrel. It is postulated that these basic residues from the three domains form a continuous, positively charged patch to which the tRNA binds [].This superfamily represents domain C2 of ArcTGT, formed by a four-stranded anti-parallel β-sheet lined with two alpha helices. It has conserved basic residues on the surface of the β-sheets as does the C-terminal domain PUA () [].
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Publication
24184645 | -
 
First Author: Lyakhova TA
Year: 2014
Journal: Chem Phys Lipids
Title: The C2 domains of granuphilin are high-affinity sensors for plasma membrane lipids.
Volume: 182
Pages: 29-37
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Publication
15851033 | -
First Author: Benes CH
Year: 2005
Journal: Cell
Title: The C2 domain of PKCdelta is a phosphotyrosine binding domain.
Volume: 121
Issue: 2
Pages: 271-80
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Publication
15971254 | J:101649
First Author: Zohn IE
Year: 2005
Journal: Birth Defects Res A Clin Mol Teratol
Title: Using genomewide mutagenesis screens to identify the genes required for neural tube closure in the mouse.
Volume: 73
Issue: 9
Pages: 583-90
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Protein
Q3TSE2
Organism: Mus musculus/domesticus
Length: 933  
Fragment?: true
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Publication
10748113 | J:72471
First Author: Wang Y
Year: 2000
Journal: J Biol Chem
Title: The RIM/NIM family of neuronal C2 domain proteins. Interactions with Rab3 and a new class of Src homology 3 domain proteins.
Volume: 275
Issue: 26
Pages: 20033-44
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Publication
21887293 | J:176152
First Author: Dixit SS
Year: 2011
Journal: PLoS One
Title: Loss of Niemann-Pick C1 or C2 protein results in similar biochemical changes suggesting that these proteins function in a common lysosomal pathway.
Volume: 6
Issue: 8
Pages: e23677
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Publication
- | J:4484
First Author: Holmes RS
Year: 1981
Journal: Dev Genet
Title: Genetic regulation of alcohol dehydrogenase C2 in the mouse. Developmental consequences of the temporal locus (Adh-3t) and positioning of Adh-3 on chromosome 3.
Volume: 2
Issue: 1
Pages: 89-98
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Publication
18344988 | -
First Author: Sanchez-Diaz A
Year: 2008
Journal: Nat Cell Biol
Title: Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast.
Volume: 10
Issue: 4
Pages: 395-406
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Publication
18522821 | -
First Author: Mendoza M
Year: 2008
Journal: Curr Biol
Title: Cytokinesis: keeping ring and membrane together.
Volume: 18
Issue: 11
Pages: R479-80
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Publication
19139265 | -
First Author: Roberts-Galbraith RH
Year: 2009
Journal: J Cell Biol
Title: The SH3 domains of two PCH family members cooperate in assembly of the Schizosaccharomyces pombe contractile ring.
Volume: 184
Issue: 1
Pages: 113-27
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Protein Domain
IPR037791 | C2_fungal_Inn1
Type: Domain
Description: Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis []. The C2 domain of Inn1, located at the N terminus, is required for ingression of the plasma membrane. The C terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3 [, ]. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow []. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane []. S. pombe Inn1 is also involved in the ingression of the plasma membrane during cytokinesis. However, it does not play an essential role, probably because the actinomyosin ring is connected to the cell cortex by many more proteins [].
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Pathway
R-MMU-166786 | Creation of C4 and C2 activators
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Publication
19745154 | -
First Author: Yang J
Year: 2009
Journal: Science
Title: Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor.
Volume: 325
Issue: 5946
Pages: 1398-402
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Protein
Q6I6G8
Organism: Mus musculus/domesticus
Length: 1578  
Fragment?: false
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Protein
Q8K4P8
Organism: Mus musculus/domesticus
Length: 1604  
Fragment?: false
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Publication
27349930 | J:235223
First Author: Omori H
Year: 2016
Journal: FEBS Lett
Title: Changes in expression of C2cd4c in pancreatic endocrine cells during pancreatic development.
Volume: 590
Issue: 16
Pages: 2584-93
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Protein
Q9EQT6
Organism: Mus musculus/domesticus
Length: 426  
Fragment?: false
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Gene
316395 | Hecw2
Type: gene
Organism: rat
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Gene
459844 | HECW2
Type: gene
Organism: chimpanzee
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Gene
291209 | Hecw1
Type: gene
Organism: rat
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Gene
463367 | HECW1
Type: gene
Organism: chimpanzee
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Gene
475868 | HECW1
Type: gene
Organism: dog, domestic
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Gene
514243 | HECW1
Type: gene
Organism: cattle
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