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Search results 1701 to 1800 out of 4706 for Coil

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Type Details Score
Publication
23965929 | J:214362
 
First Author: Yi JS
Year: 2013
Journal: Nat Commun
Title: MG53-induced IRS-1 ubiquitination negatively regulates skeletal myogenesis and insulin signalling.
Volume: 4
Pages: 2354
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Publication
25740648 | -
First Author: Kang HA
Year: 2015
Journal: Nucleic Acids Res
Title: Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.
Volume: 43
Issue: 7
Pages: 3841-56
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Publication
11560955 | -
First Author: Billaut-Mulot O
Year: 2001
Journal: J Clin Invest
Title: SS-56, a novel cellular target of autoantibody responses in Sjögren syndrome and systemic lupus erythematosus.
Volume: 108
Issue: 6
Pages: 861-9
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Publication
18451177 | -
First Author: Miyajima N
Year: 2008
Journal: Cancer Res
Title: TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells.
Volume: 68
Issue: 9
Pages: 3486-94
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Publication
24999993 | -
First Author: Wynne C
Year: 2014
Journal: PLoS One
Title: TRIM68 negatively regulates IFN-β production by degrading TRK fused gene, a novel driver of IFN-β downstream of anti-viral detection systems.
Volume: 9
Issue: 7
Pages: e101503
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Publication
19212346 | -
First Author: Baek Sørensen R
Year: 2009
Journal: J Invest Dermatol
Title: Melanoma inhibitor of apoptosis protein (ML-IAP) specific cytotoxic T lymphocytes cross-react with an epitope from the auto-antigen SS56.
Volume: 129
Issue: 8
Pages: 1992-9
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Protein Domain
IPR028041 | WDCP
Type: Family
Description: This family includes WD repeat and coiled-coil-containing protein (WDCP, previously known as C2orf44), which is found in eukaryotes and consists of around 721 amino acids. The N-terminal contains two WD (tryptophan-aspartic acid) repeats (WD1 and WD2). WD repeats may be involved in a range of biological functions including apoptosis, transcriptional regulation and signal transduction. The C-terminal contains a proline-rich sequence (PPRLPQR), and is predicted to have leucine-rich coiled coil region (CC) [].WDCP was identified in a proteomic screen to find signalling components that interact with Hck (hematopoietic cell kinase), a non-receptor tyrosine kinase. WDCP was shown to bind tightly and specifically to the SH3 domain of Hck in U937 human monocytic cells. WDCP was also shown to exist as an oligomer when expressed in mammalian cells. While the function of WDCP is unknown, it has been identified in a gene fusion event with anaplastic lymphoma kinase (ALK) in colorectal cancer patients [].
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Protein Domain
IPR006955 | Uso1_p115_C
Type: Domain
Description: This domain identifies a group of proteins, which are described as: General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein. This myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerisation, and a short C-terminal acidic region []. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the Golgi stack. This domain is found in the acidic C-terminal region, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another [].
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Protein Domain
IPR006953 | Vesicle_Uso1_P115_head
Type: Domain
Description: This domain identifies a group of proteins, which are described as: General vesicular transport factor, Transcytosis associated protein (TAP) or Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerisation, and a short C-terminal acidic region []. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the Golgi stack. This domain is found in the head region. The head region is highly conserved, but its function is unknown. It does not seem to be essential for vesicle tethering []. The N-terminal part of the head region contains context-detected Armadillo/beta-catenin-like repeats.
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Protein Domain
IPR018973 | MZB
Type: Domain
Description: This is the C-terminal MrfA (Mitomycin repair factor A, also known as YprA in Bacillus subtilis) Zn+2-binding domain (MZB, also referred to as DUF1998) which contains a conserved four-cysteine signature motif. These four Cys reside in a short coil between two α-helices and form a metal ion-binding site []. This domain is frequently found at the C-terminal of ndNTPases, however, it is also found encoded in a standalone gene, downstream of putative helicase domain-encoding genes associated with bacterial anti-phage defense system DISARM. MrfA is a DNA helicase that supports repair of mitomycin C-induced DNA damage. MrfA homologues are widely distributed in bacteria and are also present in archaea, fungi and plants. The MrfA-homologue in yeast, Hrq1, also reduces mitomycin C sensitivity. Hrq1 has high similarity to human RecQ4 and was therefore assigned to the RecQ-like helicase family []. MrfA homologues appear to be missing in Enterobacteria, however, certain pathogenic Escherichia coli and Salmonella strains harbour Z5898-like helicases with this domain [].
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Protein Domain
IPR014828 | NSP7_CoV
Type: Domain
Description: Non-structural protein NSP7 has been implicated in viral RNA replication and is predominantly α-helical in structure. Its central core is an N-terminal helical bundle (HB), with helices HB1, HB2 and HB3, forming a triple-stranded antiparallel coiled coil with a right-handed superhelical pitch. It is part of the RNA-dependent RNA polymerase (RdRp) heterotetramer which consists of one NSP7, two NSP8 molecules and the catalytic NSP12, defined as the minimal core component for mediating coronavirus RNA synthesis [, , , , , ]. NSP7 and NSP8 forms a complex that adopts a hollow cylinder-like structure []. The dimensions of the central channel and positive electrostatic properties of the cylinder imply that it confers processivity on RNA-dependent RNA polymerase []. NSP7 and NSP8 play a role in the stabilisation of NSP12 regions involved in RNA binding, and are essential for a highly active NSP12 polymerase complex [, , , ].
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Protein Domain
IPR036274 | HR1_rpt_sf
Type: Homologous_superfamily
Description: HR1 was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN) []. The first two of these repeats were later shown to bind the small G protein rho [, ]known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. This domain contains two long alpha helices forming a left-handed antiparallel coiled-coil fold termed the antiparallel coiled- coil (ACC) finger domain. The two long helices encompass the basic region and the leucine repeat region, which are identified as the Rho-binding region [, , ].
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Protein Domain
IPR009012 | GrpE_head
Type: Homologous_superfamily
Description: In prokaryotes, the nucleotideexchange factor GrpE and the chaperone DnaJ are required for nucleotide binding of the molecular chaperone DnaK []. The DnaK reaction cycle involves rapid peptide binding and release, which is dependent upon nucleotide binding. DnaJ accelerates the hydrolysis of ATP by DnaK, which enables the ADP-bound DnaK to tightly bind peptide. GrpE catalyses the release of ADP from DnaK, which is required for peptide release. In eukaryotes, GrpE is essential for mitochondrial Hsp70 function, however the cytosolic Hsp70 homologues are GrpE-independent.GrpE binds as a homodimer to the ATPase domain of DnaK, and may interact with the peptide-binding domain of DnaK. GrpE accomplishes nucleotide exchange by opening the nucleotide-binding cleft of DnaK. GrpE is comprised of two domains, the N-terminal coiled coil domain, which may facilitate peptide release, and the C-terminal head domain, which forms part of the contact surface with the ATPase domain of DnaK. The head domain is comprised of six short beta strands with a limited hydrophobic core.
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Protein Domain
IPR034743 | RH1
Type: Domain
Description: The RH1 (RILP homology 1) protein-protein interaction domain is found in thefollowing animal Rab36-binding proteins:Rab interacting lysosomal proteins (RILP),RILP-like 1 (RILP-L1),RILP-like 2 (RILP-L2),JNK-interacting protein 3 (JIP3),JNK-interacting protein 4 (JIP4).It binds to the myosin Va globular tail domain (MyoVa-GTD) in mainlyhydrophobic interactions.The RH1 domain adopts an all-helical structure and forms ahomodimer with a four-helix bundle conformation to interact with MyoVa-GTD.The RH1 homodimer is structurally separated into two parts, the N-terminalfour-helix bundle formed by alpha2 and alpha3N and the C-terminal coiled-coilformed by alpha3C. The four-helix bundle in the RH1 dimer is mainly stabilizedby forming a hydrophobic core. The N-terminal small helix (alpha1) and itsfollowing loop pack on alpha2 from the same molecule and alpha3 from theneighbouring molecule and thus contribute to the bundle stability. The RH1homodimer is further strengthened by a coiled coil formed by the C-terminalhalf of the alpha3-helix [].This entry represents the entire RH1 domain.
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Protein Domain
IPR042656 | TRIM68_RING-HC
Type: Domain
Description: TRIM68 is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems []. It also functions as a cofactor for androgen receptor-mediated transcription through regulating ligand-dependent transcription of androgen receptor in prostate cancer cells []. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogren"s syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE [, ]. TRIM68 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. This entry represents the C3HC4-type RING-HC finger found in TRIM68.
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Protein Domain
IPR027739 | EB1_Meta
Type: Family
Description: Microtubule-associated protein RP/EB family member 1 (EB1) belongs to the RP/EB family, which consists of MAPRE1 (EB1), MAPRE2 (RP1, also known as EB2) and MAPRE3 (EBF3, also known as EB3). EB1 binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. EB1 contains an N-terminal calponin homology (CH) domain that is responsible for the interaction with microtubules (MTs), and a C-terminal coiled coil domain that extends into a four-helix bundle, required for dimer formation []. Through their C-terminal sequences, EBs interact with most other known +TIPs (plus end tracking proteins) and recruit many of them to the growing MT ends [, ]. EB1 is involved in MT anchoring at the centrosome and cell migration [].
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Protein Domain
IPR027356 | NPH3_dom
Type: Domain
Description: The NRL (for NPH3/RPT2-Like) family is formed by signaling molecules specificto higher plants. Several regions of sequence and predicted structuralconservation define members of the NRL family, with three domains being mostnotable: an N-terminal BTB domain, a centrally located NPH3domain, and a C-terminal coiled coil domain. The function of the NPH3 domainis not yet known [, , , , , , , ].Some proteins known to contain a NPH3 domain include:Arabidopsis non-phototropic hypocotyl 3 (NPH3), may function as an adapteror scaffold protein in plants.Arabidopsis root-phototropisme 2 (RPT2), a signal transducer involved inphototropic response and stomatal opening in association with phototropin 1(phot1).Oriza coleoptile phototropism 1 (CPT1), the rice ortholog of NPH3. It isrequired for phototropism of coleoptiles and lateral translocation ofauxin.This entry represents the NPH3 domain.
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Protein Domain
IPR040661 | LZ3wCH
Type: Domain
Description: This domain is found at the C-terminal region of Hop2 and Mnd1 proteins. In meiotic DNA recombination, the Hop2-Mnd1 complex promotes Dmc1-mediated single-stranded DNA (ssDNA) invasion into homologous chromosomes to form a synaptic complex. Hop2 (for homologous pairing; also known as TBPIP) is expressed specifically during meiosis, same as Mnd1 (for meiotic nuclear divisions 1). The C-terminal region of both Hop2 and Mnd1, folds into three α-helices that are interrupted by two short non-helical regions. These α-helices of the two proteins together form a parallel coiled coil that provides the major interface for heterodimer formation. The non-helical regions form substantially kinked junctions between adjacent leucine zippers: the LZ1-LZ2 and LZ2-LZ3 junctions.This domain is the C-terminal segment of Hop2 and Mnd1 which folds back onto the C-terminal leucine zipper (LZ3) to form a helical bundle-like structure, hence designated LZ3wCH (for LZ3 with capping helices). The LZ3wCH region plays a role in interacting with the Dmc1 nucleofilament [].
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Protein Domain
IPR037204 | NSP7_sf_CoV
Type: Homologous_superfamily
Description: Non-structural protein NSP7 has been implicated in viral RNA replication and is predominantly α-helical in structure. Its central core is an N-terminal helical bundle (HB), with helices HB1, HB2 and HB3, forming a triple-stranded antiparallel coiled coil with a right-handed superhelical pitch. It is part of the RNA-dependent RNA polymerase (RdRp) heterotetramer which consists of one NSP7, two NSP8 molecules and the catalytic NSP12, defined as the minimal core component for mediating coronavirus RNA synthesis [, , , , , ]. NSP7 and NSP8 forms a complex that adopts a hollow cylinder-like structure []. The dimensions of the central channel and positive electrostatic properties of the cylinder imply that it confers processivity on RNA-dependent RNA polymerase []. NSP7 and NSP8 play a role in the stabilisation of NSP12 regions involved in RNA binding, and are essential for a highly active NSP12 polymerase complex [, , , ].
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Protein Domain
IPR013134 | Zn_hook_RAD50
Type: Domain
Description: The MRN complex (Mre11-Rad50-Nbs1) plays an important role in many DNA metabolic events that involve DNA double-stranded breaks. MRN is one of the first factors to be localised to DNA lesions where it might have a structural role by tethering and stabilising broken chromosomes [, ]. Rad50 is a split ABC-type ATPase; its centre contains a long heptad repeat that folds into an antiparallel coiled coil, bringing the N-terminal (Walker A) and the C-terminal (Walker B) domains in close proximity []. The apex of the coiled coil contains a dimerization interface, a conserved Cys-X-X-Cys motif in a hook-shaped domain that dimerizes with a second hook domain via cysteine-mediated zinc ion coordination. This zinc dependent dimerization event allows the formation of a complex that has appropriate lengths and conformational proporties to link sister chromatids in homologous recombination and DNA ends in non-homologous end-joining.
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Protein Domain
IPR001393 | Calsequestrin
Type: Family
Description: Calsequestrin is the principal calcium-binding protein present in thesarcoplasmic reticulum of cardiac and skeletal muscle []. It is a highly acidic protein that is able to bind over 40 calcium ions and acts as an internalcalcium store in muscle. Sequence analysis has suggested that calcium isnot bound in distinct pockets via EF-hand motifs, but rather via presentation of a charged protein surface. Two forms of calsequestrinhave been identified. The cardiac form is present in cardiac and slowskeletal muscle and the fast skeletal form is found in fast skeletal muscle.The release of calsequestrin-bound calcium (through a a calciumrelease channel) triggers muscle contraction.The active protein is not highly structured, more than 50% ofit adopting a random coil conformation []. When calcium binds there is a structural change wherebythe α-helical content of the protein increases from 3 to 11% [].Both forms of calsequestrin are phosphorylated by casein kinase II, butthe cardiac form is phosphorylated more rapidly and to a higher degree [].
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Protein Domain
IPR011050 | Pectin_lyase_fold/virulence
Type: Homologous_superfamily
Description: Microbial pectin and pectate lyases are virulence factors that degrade the pectic components of the plant cell wall []. When the backbone of pectin is methylated it is known as pectin and is cleaved by pectin lyase, and when it is demethylated it is known as pectate and is cleaved by pectate lyase. Pectin lyase from Aspergillus niger displays a single-stranded, right-handed parallel β-helix topology (), where each coil contains three β-strands and three turn regions. Several other virulence factors share this β-helix topology, although they vary in the number of coils, including bacterial pectate lyases, fungal and bacterial galacturonases (such as rhamnogalacturonase and polygalacturonase), chrondroitinase B from Flavobacterium sp., iota-carrageenase from Alteromonas sp., pectin methylesterase (PemA), P22 tailspike protein from Enterobacteria phage P22, and the virulence factor P.69 pertactin from Bordetella pertussis that mediates adhesion to target mammalian cells [].
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Protein Domain
IPR035038 | TRIM72
Type: Family
Description: TRIM72, also known as MG53, is a cardiac and skeletal muscle-specific TRIM protein. It is involved in cardiac and skeletal muscle membrane repair []. TRIM72 initiates the assembly of cell membrane repair machinery at sarcolemmal membrane injury sites in response to entry of the extracellular oxidative environment []. As an E3 ligase, it negatively regulates skeletal myogenesis and insulin signalling by targeting insulin receptor substrate 1 (IRS-1) [].Tripartite Motif (TRIM) family members share a common domain architecture characterised by the presence of a modular N-terminal RBCC motif, also called the TRIM, which consists of a RING domain, followed by one or two B-box domains and a long coiled coil (CC) region. The RBCC motif is followed by C-terminal functional domains that are often used to categorise family members into subgroups [].TRIM72 C terminus consists of the distinct N-terminal PRY subdomain followed by the SPRY subdomain.
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Protein Domain
IPR013805 | GrpE_coiled_coil
Type: Homologous_superfamily
Description: In prokaryotes, the nucleotide exchange factor GrpE and the chaperone DnaJ are required for nucleotide binding of the molecular chaperone DnaK []. The DnaK reaction cycle involves rapid peptide binding and release, which is dependent upon nucleotide binding. DnaJ accelerates the hydrolysis of ATP by DnaK, which enables the ADP-bound DnaK to tightly bind peptide. GrpE catalyses the release of ADP from DnaK, which is required for peptide release. In eukaryotes, GrpE is essential for mitochondrial Hsp70 function, however the cytosolic Hsp70 homologues are GrpE-independent.GrpE binds as a homodimer to the ATPase domain of DnaK, and may interact with the peptide-binding domain of DnaK. GrpE accomplishes nucleotide exchange by opening the nucleotide-binding cleft of DnaK. GrpE is comprised of two domains, the N-terminal coiled coil domain, which may facilitate peptide release, and the C-terminal head domain, which forms part of the contact surface with the ATPase domain of DnaK. This superfamily represents the N-terminal coiled-coil domain.
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Protein Domain
IPR013859 | Ssr4_N
Type: Domain
Description: This is the N-terminal domain of the SWI/SNF and RSC complexes subunit Ssr4 from S. pombe, a member of the chromatin structure remodeling complex (RSC) and the SWI/SNF complex [, ]. RSC is involved in transcription regulation and nucleosome positioning which controls, particularly, membrane and organelle development genes. The ATP-dependent chromatin remodelling complex SWI/SNF is required for the positive and negative regulation of gene expression of a large number of genes through the regulation of nucleosome remodelling [].The structure of this domain revealed that it has a novel fold comprising an antiparallel β-sheet of seven strands with α-helices on one side and random coil on the other []. It contains the highly conserved motif WxxxxxPxxGxxxxxxxxxxxxxxxDG.
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Protein Domain
IPR043097 | PProtein_oligomer_dom1
Type: Homologous_superfamily
Description: Phosphoprotein P, an indispensable subunit of the viral polymerase complex, is a modular protein organised into two moieties that are both functionally and structurally distinct: a well-conserved C-terminal moiety that contains all the regions required for transcription, and a poorly conserved, intrinsically unstructured N-terminal moiety that provides several additional functions required for replication. The N-terminal moiety is responsible for binding to newly synthesised free N(0) (nucleoprotein that has not yet bound RNA), in order to prevent the binding of N(0) to cellular RNA. The C-terminal moiety consists of an oligomerisation domain, an N-RNA (nucleoprotein-RNA)-binding domain and an L polymerase-binding domain [, ]. The oligomerisation domain reveals a homotetrameric coiled coil structure with many details that are different from classic coiled coils with canonical hydrophobic heptad repeats [].This superfamily represents domain 1 of the phosphoprotein P oligomerisation domain from Sendai virus as well as from close family members.
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Protein Domain
IPR018233 | Calsequestrin_CS
Type: Conserved_site
Description: Calsequestrin is the principal calcium-binding protein present in thesarcoplasmic reticulum of cardiac and skeletal muscle []. It is a highly acidic protein that is able to bind over 40 calcium ions and acts as an internalcalcium store in muscle. Sequence analysis has suggested that calcium isnot bound in distinct pockets via EF-hand motifs, but rather via presentation of a charged protein surface. Two forms of calsequestrinhave been identified. The cardiac form is present in cardiac and slowskeletal muscle and the fast skeletal form is found in fast skeletal muscle.The release of calsequestrin-bound calcium (through a a calciumrelease channel) triggers muscle contraction.The active protein is not highly structured, more than 50% ofit adopting a random coil conformation []. When calcium binds there is a structural change wherebythe α-helical content of the protein increases from 3 to 11% [].Both forms of calsequestrin are phosphorylated by casein kinase II, butthe cardiac form is phosphorylated more rapidly and to a higher degree [].
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Publication
20080746 | J:156525
First Author: Ikenouchi J
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: FRMD4A regulates epithelial polarity by connecting Arf6 activation with the PAR complex.
Volume: 107
Issue: 2
Pages: 748-53
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Publication
15311282 | -
First Author: Wen Y
Year: 2004
Journal: Nat Cell Biol
Title: EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration.
Volume: 6
Issue: 9
Pages: 820-30
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Protein
Q9CQA6
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: false
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Publication
9287130 | J:51112
First Author: Wagener R
Year: 1997
Journal: FEBS Lett
Title: Primary structure of matrilin-3, a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin-1) and von Willebrand factor.
Volume: 413
Issue: 1
Pages: 129-34
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Protein
P24161
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: false
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Protein
Q8K0C8
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: false
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Protein
Q8BT51
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: false
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Protein
Q9DCJ5
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
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Protein
Q3UU54
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: false
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Protein
S4R231
Organism: Mus musculus/domesticus
Length: 63  
Fragment?: true
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Protein
Q8CEX1
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: true
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Protein
J3QMU3
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
A0A1S6GWI0
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: false
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Protein
A2MZG6
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: false
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Publication
9687364 | -
First Author: Zuccola HJ
Year: 1998
Journal: Structure
Title: Structural basis of the oligomerization of hepatitis delta antigen.
Volume: 6
Issue: 7
Pages: 821-30
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Publication
17921300 | -
First Author: Grosskinsky U
Year: 2007
Journal: J Bacteriol
Title: A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport.
Volume: 189
Issue: 24
Pages: 9011-9
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Publication
9103205 | -
First Author: Harrison CJ
Year: 1997
Journal: Science
Title: Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.
Volume: 276
Issue: 5311
Pages: 431-5
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Publication
9065385 | -
First Author: Jin C
Year: 1997
Journal: Curr Genet
Title: Cloning and characterization of MRP10, a yeast gene coding for a mitochondrial ribosomal protein.
Volume: 31
Issue: 3
Pages: 228-34
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Publication
9860297 | J:51782
First Author: Triepels R
Year: 1998
Journal: Hum Genet
Title: The nuclear-encoded human NADH:ubiquinone oxidoreductase NDUFA8 subunit: cDNA cloning, chromosomal localization, tissue distribution, and mutation detection in complex-I-deficient patients.
Volume: 103
Issue: 5
Pages: 557-63
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Publication
15177562 | -
First Author: Westerman BA
Year: 2004
Journal: Genomics
Title: C2360, a nuclear protein expressed in human proliferative cytotrophoblasts, is a representative member of a novel protein family with a conserved coiled coil-helix-coiled coil-helix domain.
Volume: 83
Issue: 6
Pages: 1094-104
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Publication
7851406 | -
First Author: Palmer RH
Year: 1995
Journal: Eur J Biochem
Title: Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family.
Volume: 227
Issue: 1-2
Pages: 344-51
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Publication
8647255 | -
First Author: Shibata H
Year: 1996
Journal: FEBS Lett
Title: Characterization of the interaction between RhoA and the amino-terminal region of PKN.
Volume: 385
Issue: 3
Pages: 221-4
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Publication
9446575 | -
First Author: Flynn P
Year: 1998
Journal: J Biol Chem
Title: Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif.
Volume: 273
Issue: 5
Pages: 2698-705
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Publication
14514689 | -
First Author: Owen D
Year: 2003
Journal: J Biol Chem
Title: Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1).
Volume: 278
Issue: 50
Pages: 50578-87
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Publication
27129201 | -
First Author: Watson JR
Year: 2016
Journal: J Biol Chem
Title: Investigation of the Interaction between Cdc42 and Its Effector TOCA1: HANDOVER OF Cdc42 TO THE ACTIN REGULATOR N-WASP IS FACILITATED BY DIFFERENTIAL BINDING AFFINITIES.
Volume: 291
Issue: 26
Pages: 13875-90
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Publication
16188992 | -
First Author: Peti W
Year: 2005
Journal: J Virol
Title: Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.
Volume: 79
Issue: 20
Pages: 12905-13
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Publication
16360038 | -
First Author: Rubin SM
Year: 2005
Journal: Cell
Title: Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release.
Volume: 123
Issue: 6
Pages: 1093-106
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Publication
17055436 | -
First Author: Call ME
Year: 2006
Journal: Cell
Title: The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor.
Volume: 127
Issue: 2
Pages: 355-68
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Publication
9072162 | -
First Author: Padlan EA
Year: 1997
Journal: Curr Biol
Title: T-cell receptors: feeling out the complex.
Volume: 7
Issue: 1
Pages: R17-20
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Publication
8112294 | J:19072
First Author: Koyasu S
Year: 1994
Journal: EMBO J
Title: Targeted disruption within the CD3 zeta/eta/phi/Oct-1 locus in mouse.
Volume: 13
Issue: 4
Pages: 784-97
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Publication
12388762 | -
First Author: Askham JM
Year: 2002
Journal: Mol Biol Cell
Title: Evidence that an interaction between EB1 and p150(Glued) is required for the formation and maintenance of a radial microtubule array anchored at the centrosome.
Volume: 13
Issue: 10
Pages: 3627-45
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Publication
18322465 | -
First Author: Akhmanova A
Year: 2008
Journal: Nat Rev Mol Cell Biol
Title: Tracking the ends: a dynamic protein network controls the fate of microtubule tips.
Volume: 9
Issue: 4
Pages: 309-22
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Publication
10542152 | -
First Author: Motchoulski A
Year: 1999
Journal: Science
Title: Arabidopsis NPH3: A NPH1 photoreceptor-interacting protein essential for phototropism.
Volume: 286
Issue: 5441
Pages: 961-4
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Publication
17493935 | -
First Author: Pedmale UV
Year: 2007
Journal: J Biol Chem
Title: Regulation of phototropic signaling in Arabidopsis via phosphorylation state changes in the phototropin 1-interacting protein NPH3.
Volume: 282
Issue: 27
Pages: 19992-20001
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Publication
20031912 | -
First Author: Inoue S
Year: 2008
Journal: Mol Plant
Title: Leaf positioning of Arabidopsis in response to blue light.
Volume: 1
Issue: 1
Pages: 15-26
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Publication
11846562 | -
First Author: Mo Y
Year: 2001
Journal: J Mol Biol
Title: Crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex.
Volume: 314
Issue: 3
Pages: 495-506
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Publication
11256070 | -
First Author: Ng M
Year: 2001
Journal: Nat Rev Genet
Title: Function and evolution of the plant MADS-box gene family.
Volume: 2
Issue: 3
Pages: 186-95
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Protein Domain
IPR041785 | FRMD4A/B_FERM_C
Type: Domain
Description: FERM domain-containing protein 4A (FRMD4A) is part of the Par-3/FRMD4A/cytohesin-1 complex that activates Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization. The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables. When primordial AJs are formed, Par-3 recruits scaffolding protein FRMD4A which connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1 [].FERM domain-containing protein 4B (FRMD4B, also called GRP1-binding protein, GRSP1) is a novel member of GRP1 signaling complexes that are recruited to plasma membrane ruffles in response to insulin receptor signaling. The GRSP1/FRMD4B protein contains a FERM protein domain as well as two coiled coil domains and may function as a scaffolding protein. GRP1 and GRSP1 interact through the coiled coil domains in the two proteins []. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites [, ].
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Protein Domain
IPR033897 | MADS_SRF-like
Type: Domain
Description: SRF-like/Type I subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor)) box family of eukaryotic transcriptional regulators []. Binds DNA and exists as hetero- and homo-dimers [, ]. Differs from the MEF-like/Type II subgroup mainly in position of the alpha 2 helix responsible for the dimerization interface. Important in homeotic regulation in plants and in immediate-early development in animals []. Also found in fungi [, ].Human serum response factor (SRF) is a ubiquitous nuclear protein important for cell proliferation and differentiation. SRF function is essential for transcriptional regulation of numerous growth-factor-inducible genes, such as c-fos oncogene and muscle-specific actin genes. A core domain of around 90 amino acids is sufficient for the activities of DNA-binding, dimerisation and interaction with accessory factors. Within the core is a DNA-binding region, designated the MADS box [], that is highly similar to many eukaryotic regulatory proteins: among these are MCM1, the regulator of cell type-specific genes in fission yeast; DSRF, a Drosophila trachea development factor; the MEF2 family of myocyte-specific enhancer factors; and the Agamous and Deficiens families of plant homeotic proteins.In SRF, the MADS box has been shown to be involved in DNA-binding and dimerisation []. Proteins belonging to the MADS family function as dimers, the primary DNA-binding element of which is an anti-parallel coiled coil of two amphipathic α-helices, one from each subunit. The DNA wraps around the coiled coil allowing the basic N-termini of the helices to fit into the DNA major groove. The chain extending from the helix N-termini reaches over the DNA backbone and penetrates into the minor groove. A 4-stranded, anti-parallel β-sheet packs against the coiled-coil face opposite the DNA and is the central element of the dimerisation interface. The MADS-box domain is commonly found associated with K-box region see ().
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Protein
P46660
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q6IFX2
Organism: Mus musculus/domesticus
Length: 452  
Fragment?: false
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Protein
Q62168
Organism: Mus musculus/domesticus
Length: 407  
Fragment?: false
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Protein
Q3UV17
Organism: Mus musculus/domesticus
Length: 594  
Fragment?: false
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Protein
P07744
Organism: Mus musculus/domesticus
Length: 525  
Fragment?: false
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Protein
P11679
Organism: Mus musculus/domesticus
Length: 490  
Fragment?: false
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Protein
Q61781
Organism: Mus musculus/domesticus
Length: 484  
Fragment?: false
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Protein
P05784
Organism: Mus musculus/domesticus
Length: 423  
Fragment?: false
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Protein
Q61765
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
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Protein
Q6IFZ9
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: false
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Protein
Q497I4
Organism: Mus musculus/domesticus
Length: 455  
Fragment?: false
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Protein
Q9D312
Organism: Mus musculus/domesticus
Length: 431  
Fragment?: false
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Protein
P03995
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
Q6IFZ6
Organism: Mus musculus/domesticus
Length: 572  
Fragment?: false
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Protein
Q9DCV7
Organism: Mus musculus/domesticus
Length: 457  
Fragment?: false
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Protein
Q922U2
Organism: Mus musculus/domesticus
Length: 580  
Fragment?: false
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Protein
P02535
Organism: Mus musculus/domesticus
Length: 570  
Fragment?: false
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Protein
Q6IFX4
Organism: Mus musculus/domesticus
Length: 482  
Fragment?: false
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Protein
Q99M73
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
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Protein
P50446
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
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Protein
Q6NXH9
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
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Protein
Q64291
Organism: Mus musculus/domesticus
Length: 487  
Fragment?: false
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Protein
Q3TTY5
Organism: Mus musculus/domesticus
Length: 707  
Fragment?: false
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Protein
Q9R0H5
Organism: Mus musculus/domesticus
Length: 524  
Fragment?: false
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Protein
Q6IME9
Organism: Mus musculus/domesticus
Length: 520  
Fragment?: false
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Protein
Q8VED5
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
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Protein
Q61897
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q99M74
Organism: Mus musculus/domesticus
Length: 516  
Fragment?: false
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Protein
Q99PS0
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q9Z2T6
Organism: Mus musculus/domesticus
Length: 507  
Fragment?: false
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Protein
P15331
Organism: Mus musculus/domesticus
Length: 475  
Fragment?: false
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Protein
Q9Z2K1
Organism: Mus musculus/domesticus
Length: 469  
Fragment?: false
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Protein
P04104
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: false
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Protein
Q6IMF0
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: false
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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