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Search results 1501 to 1600 out of 4706 for Coil

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Type Details Score
Protein
C0LQ87
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
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Protein
O35656
Organism: Mus musculus/domesticus
Length: 636  
Fragment?: false
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Protein
D3YUF7
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
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Protein
Q05CE2
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
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Protein
A0MTM0
Organism: Mus musculus/domesticus
Length: 55  
Fragment?: true
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Protein
J3QJZ1
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: false
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Protein
A0A2R8VKR9
Organism: Mus musculus/domesticus
Length: 48  
Fragment?: true
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Protein
F6VMG1
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: true
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Protein
D6RH90
Organism: Mus musculus/domesticus
Length: 372  
Fragment?: false
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Protein
C0LQ88
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q3TBQ1
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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Publication
28101862 | -
 
First Author: Guzenko D
Year: 2017
Journal: Subcell Biochem
Title: Crystallographic Studies of Intermediate Filament Proteins.
Volume: 82
Pages: 151-170
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Protein Domain
IPR039008 | IF_rod_dom
Type: Domain
Description: Intermediate filaments (IF) [, ]are proteins which are primordialcomponents of the cytoskeleton and the nuclear envelope. They generally formfilamentous structures 8 to 14 nm wide. IF proteins are members of a verylarge multigene family of proteins which has been subdivided in six types:Type I: Acidic cytokeratins.Type II: Basic cytokeratins.Type III: Vimentin, desmin, glial fibrillary acidic protein (GFAP),peripherin, and plasticin.Type IV: Neurofilaments L, H and M, alpha-internexin and nestin.Type V: Nuclear lamins A, B1, B2 and C.Type VI: 'Orphan' IF proteins, which are more distant in terms of theiramino acid sequences.All IF proteins are structurally similar in that they consist of: a centralrod domain comprising some 300 to 350 residues which is arranged in coiled-coiled α-helices, with at least two short characteristic interruptions; aN-terminal non-helical domain (head) of variable length; and a C-terminaldomain (tail) which is also non-helical, and which shows extreme lengthvariation between different IF proteins.While IF proteins are evolutionary and structurally related, they have limitedsequence homologies except in several regions of the rod domain. The IF roddomain is approximately 310 residues long in all cytoplasmic IF proteins andclose to 350 residues in the nuclear ones. The IF rod domain exhibits aninterrupted α-helical conformation and reveals apronouncedseven-residue periodicity in the distribution of apolar residues.The heptad periodicity within the rod domain is interrupted in several places,which generates four consecutive α-helical segments: 1A and 1B, whichtogether form the so-called coil 1, and 2A and 2B, which form coil 2. The fourα-helical segments are interconnected by relatively short, variablelinkers L1, L12 and L2 [, ].IF proteins have a very strong tendency to dimerize via the formation of anα-helical coiled coil (CC) by their rod domains [].
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Protein Domain
IPR018039 | IF_conserved
Type: Conserved_site
Description: Intermediate filaments (IF) []are proteins which are primordial components of the cytoskeleton and the nuclear envelope. They generally form filamentous structures 8 to 14 nm wide. IF proteins are members of a very large multigene family of proteins, which has been subdivided in six major subgroups: Type I: Acidic cytokeratins. Type II: Basic cytokeratins. Type III: Vimentin, desmin, glial fibrillary acidic protein (GFAP), peripherin, and plasticin. Type IV: Neurofilaments L, H and M, alpha-internexin and nestin. Type V: Nuclear lamins A, B1, B2 and C. Type VI: 'Orphan' IF proteins, which are more distant in terms of their amino acid sequences. All IF proteins are structurally similar in that they consist of: a centralrod domain comprising some 300 to 350 residues which is arranged in coiled-coiled α-helices, with at least two short characteristic interruptions; aN-terminal non-helical domain (head) of variable length; and a C-terminaldomain (tail) which is also non-helical, and which shows extreme lengthvariation between different IF proteins.While IF proteins are evolutionary and structurally related, they have limited sequence homologies except in several regions of the rod domain. The IF rod domain is approximately 310 residues long in all cytoplasmic IF proteins andclose to 350 residues in the nuclear ones. The IF rod domain exhibits aninterrupted α-helical conformation and reveals apronounced seven-residue periodicity in the distribution of apolar residues.The heptad periodicity within the rod domain is interrupted in several places,which generates four consecutive α-helical segments: 1A and 1B, whichtogether form the so-called coil 1, and 2A and 2B, which form coil 2. The fourα-helical segments are interconnected by relatively short, variablelinkers L1, L12 and L2 [, ].IF proteins have a very strong tendency to dimerize via the formation of anα-helical coiled coil (CC) by their rod domains [].This entry represents a conserved region situated at the very end of the 2B segment, which is critically involved in specific dimer-dimer interactions within the mature filament [].
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Protein
Q8CAQ8
Organism: Mus musculus/domesticus
Length: 757  
Fragment?: false
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Protein
O35658
Organism: Mus musculus/domesticus
Length: 278  
Fragment?: false
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Protein
Q61908
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
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Protein
Q8R5L1
Organism: Mus musculus/domesticus
Length: 279  
Fragment?: false
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Protein
A6H604
Organism: Mus musculus/domesticus
Length: 268  
Fragment?: true
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Protein
A3KGA5
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
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Protein
Q3U7N2
Organism: Mus musculus/domesticus
Length: 741  
Fragment?: false
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Protein
A0A0U1RP81
Organism: Mus musculus/domesticus
Length: 488  
Fragment?: false
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Protein
E9QAY6
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
E9Q800
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: false
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Protein
Q2YDW0
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: true
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Protein
Q3TZK4
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: true
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Protein
Q6P8Y5
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: true
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Protein
A0A1B0GX08
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: true
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Protein
D6RJK7
Organism: Mus musculus/domesticus
Length: 784  
Fragment?: false
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Protein
Q3TEY5
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: false
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Protein
Q3TVZ5
Organism: Mus musculus/domesticus
Length: 741  
Fragment?: false
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Protein
A0A0U1RQ14
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: true
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Protein
Q3TQL4
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: true
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Protein
E9PVS5
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: true
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Publication
10097078 | J:54130
First Author: Jiang J
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein.
Volume: 96
Issue: 7
Pages: 3572-7
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Publication
9559539 | -
First Author: Seytter T
Year: 1998
Journal: Yeast
Title: Mam33p, an oligomeric, acidic protein in the mitochondrial matrix of Saccharomyces cerevisiae is related to the human complement receptor gC1q-R.
Volume: 14
Issue: 4
Pages: 303-10
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Publication
18511074 | -
First Author: Kauko A
Year: 2008
Journal: J Mol Biol
Title: Coils in the membrane core are conserved and functionally important.
Volume: 380
Issue: 1
Pages: 170-80
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Publication
16306995 | -
First Author: Schumacher MA
Year: 2005
Journal: Nature
Title: Structures of ParB bound to DNA reveal mechanism of partition complex formation.
Volume: 438
Issue: 7067
Pages: 516-9
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Publication
15647377 | -
First Author: John GB
Year: 2005
Journal: Mol Biol Cell
Title: The mitochondrial inner membrane protein mitofilin controls cristae morphology.
Volume: 16
Issue: 3
Pages: 1543-54
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Publication
8206833 | -
First Author: Heruth DP
Year: 1994
Journal: J Bacteriol
Title: Characterization of genetic determinants for R body synthesis and assembly in Caedibacter taeniospiralis 47 and 116.
Volume: 176
Issue: 12
Pages: 3559-67
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Publication
15785846 | -
First Author: Jeblick J
Year: 2005
Journal: J Mol Evol
Title: Sequence, transcription activity, and evolutionary origin of the R-body coding plasmid pKAP298 from the intracellular parasitic bacterium Caedibacter taeniospiralis.
Volume: 60
Issue: 2
Pages: 164-73
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Publication
1409643 | -
First Author: Garcia JA
Year: 1992
Journal: Proc Natl Acad Sci U S A
Title: Cloning and chromosomal mapping of a human immunodeficiency virus 1 "TATA" element modulatory factor.
Volume: 89
Issue: 20
Pages: 9372-6
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Publication
12778115 | -
First Author: Morais MC
Year: 2003
Journal: Nat Struct Biol
Title: Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly.
Volume: 10
Issue: 7
Pages: 572-6
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Publication
9405159 | -
First Author: Barthe P
Year: 1997
Journal: J Mol Biol
Title: Solution structure of human p8MTCP1, a cysteine-rich protein encoded by the MTCP1 oncogene, reveals a new alpha-helical assembly motif.
Volume: 274
Issue: 5
Pages: 801-15
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Publication
10850804 | -
First Author: Barthe P
Year: 2000
Journal: Protein Sci
Title: Synthesis and NMR solution structure of an alpha-helical hairpin stapled with two disulfide bridges.
Volume: 9
Issue: 5
Pages: 942-55
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Publication
8361760 | -
First Author: Stern MH
Year: 1993
Journal: Oncogene
Title: MTCP-1: a novel gene on the human chromosome Xq28 translocated to the T cell receptor alpha/delta locus in mature T cell proliferations.
Volume: 8
Issue: 9
Pages: 2475-83
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Publication
8596442 | -
First Author: Shankar S
Year: 1995
Journal: Mol Microbiol
Title: Regulation of nucleoside diphosphate kinase and an alternative kinase in Escherichia coli: role of the sspA and rnk genes in nucleoside triphosphate formation.
Volume: 17
Issue: 5
Pages: 935-43
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Publication
12022893 | -
First Author: Del Rizzo PA
Year: 2002
Journal: Biochemistry
Title: The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain.
Volume: 41
Issue: 21
Pages: 6875-84
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Publication
23791107 | -
First Author: Guo Y
Year: 2013
Journal: Am J Hum Genet
Title: Dissecting disease inheritance modes in a three-dimensional protein network challenges the "guilt-by-association" principle.
Volume: 93
Issue: 1
Pages: 78-89
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Protein Domain
IPR031925 | TBCC_N
Type: Domain
Description: Tubulin binding cofactor C (TBCC) is a post-chaperonin involved in folding pathways that lead to the final release of alpha beta native heterodimers incorporated in microtubules. TBCC is organised into three different domains: N-terminal, CARP and C-terminal [].This entry represents the N-terminal domain of TBCC. The N-terminal comprises a structured coiled coil and a highly dynamic N-terminal region which concentrates 80% of charged and polar residues and is believed to be important in interaction with tubulin []. Overall, the N-terminal domain of TBCC is responsible for its interaction with components of the centrosome by its N-terminal domain.
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Protein Domain
IPR026034 | MreD_proteobac
Type: Family
Description: The MreD (murein formation D) protein is involved in bacterial cell shape determination [, ]. Most rod-shaped bacteria depend on MreB and RodA to achieve either a rod shape or some other non-spherical morphology such as coil or stalk formation. MreD is encoded in an operon with MreB, and often with RodA and PBP-2 as well. It is highly hydrophobic (therefore somewhat low-complexity) and highly divergent, and therefore cannot always be identified on the basis of sequence similarity.This entry represents the proteobacterial MreD proteins.
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Protein Domain
IPR028987 | ATP_synth_B-like_membr_sf
Type: Homologous_superfamily
Description: The b subunit of the E. coli F-type ATP synthase is present as a dimer and links the peripheral F(1) subunits to the membrane-integral F(0) portion. The dimerisation domain of the b subunit consists of an α-helical coiled-coil structure. In the dimer the two helices form a coiled coil with a right-handed superhelical twist. Analysis of b sequences from other prokaryotes indicates conservation of an undecad repeat in this domain []. This superfamily represents a membrane domain that covers most of the dimerisation domain of the b subunit of the E. coli F-type ATP synthase.
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Protein Domain
IPR038397 | TBCC_N_sf
Type: Homologous_superfamily
Description: Tubulin binding cofactor C (TBCC) is a post-chaperonin involved in folding pathways that lead to the final release of alpha beta native heterodimers incorporated in microtubules. TBCC is organised into three different domains: N-terminal, CARP and C-terminal [].This entry represents the N-terminal domain of TBCC. The N-terminal comprises a structured coiled coil and a highly dynamic N-terminal region which concentrates 80% of charged and polar residues and is believed to be important in interaction with tubulin []. Overall, the N-terminal domain of TBCC is responsible for its interaction with components of the centrosome by its N-terminal domain.
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Protein Domain
IPR024128 | T-cell_CD3_zeta
Type: Family
Description: The TCR complex of T-lymphocytes consists of either a TCR alpha/beta or TCR gamma/delta heterodimer co-expressed at the cell surface with the invariant subunits of CD3 labelled gamma, delta, epsilon, zeta, and eta []. The zeta subunit forms either homodimers or heterodimers with eta [], but eta homodimers have not been observed. The structure of the zetazeta transmembrane dimer consists of a left-handed coiled coil with polar contacts. Two aspartic acids are critical for zetazeta dimerisation and assembly with TCR []. This family includes the zeta subunit from the CD3 T-Cell co-receptor.
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Protein Domain
IPR036172 | ApoA-II_sf
Type: Homologous_superfamily
Description: Apolipoprotein A-II (ApoA-II) is the second major apolipoprotein of high density lipoprotein in human plasma. Mature ApoA-II is present as a dimer of two 77-amino acid chains joined by a disulphide bridge []. ApoA-II regulates many steps in HDL metabolism, and its role in coronary heart disease is unclear []. In bovine serum, the ApoA-II homologue is present in almost free form. Bovine ApoA-II shows antimicrobial activity against Escherichia coli and yeasts in phosphate buffered saline (PBS) [].ApoA-II structure presents a segmented tetrameric parallel coiled coil fold.
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Protein Domain
IPR014884 | ParB_fam_C
Type: Domain
Description: ParB is a component of the par system which mediates accurate DNA partition during cell division. It recognises A-box and B-box DNA motifs. ParB forms an asymmetric dimer with 2 extended helix-turn-helix (HTH) motifs that bind to A-boxes. The HTH motifs emanate from a beta sheet coiled coil DNA binding module []. Both DNA binding elements are free to rotate around a flexible linker, this enables them to bind to complex arrays of A- and B-box elements on adjacent DNA arms of the looped partition site [].
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Protein Domain
IPR036486 | AsiA_sf
Type: Homologous_superfamily
Description: Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. It is an all-helical protein, composed of six helical segments and intervening loops and turns, as well as a helix-turn-helix DNA binding motif, although neither free anti-sigma factor nor anti-sigma factor bound to sigma-70 has been shown to interact directly with DNA. In solution, the protein forms a symmetric dimer of small (10.59kDa) protomers, which are composed of helix and coil regions and are devoid of β-strand/sheet secondary structural elements [].
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Protein Domain
IPR022091 | TMF_TATA-bd
Type: Domain
Description: This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes []. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs []. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organisation in animal []and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family [].
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Protein Domain
IPR022092 | TMF_DNA-bd
Type: Family
Description: This is the middle region of a family of TATA element modulatory factor 1 (TMF1) proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organisation in animal []and plant []cells.
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Protein Domain
IPR036876 | UVR_dom_sf
Type: Homologous_superfamily
Description: During the process of Escherichia coli nucleotide excision repair, DNA damagerecognition and processing are achieved by the action of the uvrA, uvrB,and uvrC gene products []. UvrB and UvrC share a common domain of around 35amino acids, the so called UVR domain. This domain in UvrB can interact withthe homologous domain in UvrC throughout a putative coiled coil structure.This interaction is important for the incision of the damaged strand [].A conserved region similar to the UVR domain is also found in the ATP-binding subunit of bacterial and chloroplastic Clp ATPases [], which suggest that the UVR domain is not only involved in the interaction between uvrB and uvrC.
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Protein Domain
IPR019133 | Mt-IM_prot_Mitofilin
Type: Family
Description: Mitofilin (also known as MICOS complex subunit MIC60) is a component of the MICOS complex which controls mitochondrial cristae morphology, maintenance of junctions, inner membrane architecture, and formation of contact sites to the outer membrane [, ]. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex []. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence (residues 1-43) rich in positive-charged and hydroxylated residues and a membrane anchor domain (residues 47-66). In addition, it has three centrally located coiled coil domains (residues 200-240, 280-310 and 400-420) [].
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Protein Domain
IPR007385 | Scp_MukE
Type: Family
Description: MukE is involved in the segregation and condensation of prokaryotic chromosomes. MukE along with MukF () interact with MukB () in vivo forming a complex, which is required for chromosome condensation and segregation in Escherichia coli []. The Muk complex appears to be similar to the SMC-ScpA-ScpB complex in other prokaryotes where MukB is the homologue of SMC []. ScpA () and ScpB () have little sequence similarity to MukE or MukF, though they are predicted to be structurally similar, being predominantly α-helical with coiled coil regions.
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Protein Domain
IPR017225 | Cell_shape_determin_MreD_prd
Type: Family
Description: The MreD (murein formation D) protein is involved in bacterial cell shape determination. Most rod-shaped bacteria depend on MreB and RodA to achieve either a rod shape or some other non-spherical morphology such as coil or stalk formation. MreD is encoded in an operon with MreB, and often with RodA and PBP-2 as well. It is highly hydrophobic (therefore somewhat low-complexity) and highly divergent, and therefore cannot always be identified on the basis of sequence similarity.This group represents predicted MreD proteins found primarily in Clostridium and Treponema species.
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Protein Domain
IPR042037 | MukE_C
Type: Homologous_superfamily
Description: MukE is involved in the segregation and condensation of prokaryotic chromosomes. MukE along with MukF () interact with MukB () in vivo forming a complex, which is required for chromosome condensation and segregation in Escherichia coli []. The Muk complex appears to besimilar to the SMC-ScpA-ScpB complex in other prokaryotes where MukB is the homologue of SMC []. ScpA () and ScpB () have little sequence similarity to MukE or MukF, though they are predicted to be structurally similar, being predominantly α-helical with coiled coil regions. This superfamily represents the MukE C-terminal domain. Structurally, it consists of 4 helices and 3 small beta strands.
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Protein Domain
IPR042038 | MukE_N
Type: Homologous_superfamily
Description: MukE is involved in the segregation and condensation of prokaryotic chromosomes. MukE along with MukF () interact with MukB () in vivo forming a complex, which is required for chromosome condensation and segregation in Escherichia coli []. The Muk complex appears to be similar to the SMC-ScpA-ScpB complex in other prokaryotes where MukB is the homologue of SMC []. ScpA () and ScpB () have little sequence similarity to MukE or MukF, though they are predicted to be structurally similar, being predominantly α-helical with coiled coil regions. This superfamily represents the MukE N-terminal domain. Structurally, it consists of 3 helices and 2 small beta strands.
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Protein Domain
IPR005625 | PepSY-ass_TM
Type: Family
Description: This family contains proteins of up to five transmembranes helices found in bacterial species, some of which carry a nested PepSY domain. Coil residues are significantly more conserved than other residues and are frequently found within channels and transporters, where they introduce the flexibility and polarity required for transport across the membrane [].PepSY (peptidase (M4) and YpeB of subtilis) is a repeated region first identified in Thermoanaerobacter tengcongensis. The PepSY domain functions in the control of M4 peptidases through their propeptide and in the germination of spores. It may also play a part in regulating protease activity [].
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Protein Domain
IPR005582 | Chromosome_partition_MukF
Type: Family
Description: This family contains MukF, which are proteins involved in chromosome condensation, segregation and cell cycle progression. MukE along with MukF interact with MukB in vivo forming a complex, which is required for chromosome condensation and segregation in Escherichia coli []. The Muk complex appears to be similar to the SMC-ScpA-ScpB complex in other prokaryotes where MukB is the homologue of SMC []. ScpA and ScpB have little sequence similarity to MukE or MukF, though they are predicted to be structurally similar, being predominantly α-helical with coiled coil regions. The structure of MuKF has been revealed [].
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Protein Domain
IPR027179 | MTCP1
Type: Family
Description: Proteins in this family adopt a coiled coil structure, with two antiparallel α-helices that are tightly strapped together by two disulfide bridges at each end. The protein sequence shows a cysteine motif, required for the stabilisation of the coiled-coil-like structure. Additional inter-helix hydrophobic contacts impart stability to this scaffold [].The precise function of this family is, as yet, unknown []. MTCP1 is found in mitochondria. Mature-T-Cell Proliferation is the first gene unequivocally identified in the group of uncommon leukemias with a mature phenotype [].
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Protein Domain
IPR042699 | TRIM58_RING-HC
Type: Domain
Description: TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to 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, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain [].
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Protein Domain
IPR015100 | AsiA
Type: Family
Description: Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. It is an all-helical protein, composed of six helical segments and intervening loops and turns, as well as a helix-turn-helix DNA binding motif, although neither free anti-sigma factor nor anti-sigma factor bound to sigma-70 has been shown to interact directly with DNA. In solution, the protein forms a symmetric dimer of small (10.59kDa) protomers, which are composed of helix and coil regions and are devoid of β-strand/sheet secondary structural elements [].
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Protein Domain
IPR042765 | TRIM42_RING-HC
Type: Domain
Description: Tripartite motif-containing protein 42 (TRIM42) belongs to the C-III 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, Bbox1 and Bbox2, and a coiled coil domain. It also has a novel cysteine-rich motif N-terminal to the RBCC domain, as well as a COS (carboxyl-terminal subgroup one signature) box and a fibronectin type-III (FN3) domain positioned C-terminal to the RBCC domain. TRIM42 can interact with TRIM27, a known cancer-associated protein. Its precise biological function remains unclear [, ].
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Protein Domain
IPR040655 | TIAM1_CC-Ex
Type: Domain
Description: Tiam1 is a guanine exchange factor (GEF) for CDC42 and the Rho-family GTPase Rac1, which plays an important role in cell-matrix adhesion and in cell migration [, ]. Tiam1 is involved in multiple steps of tumorigenesis [].This entry represents the CC and Ex subdomain found in the PH-CC-Ex globular domain of the Tiam1 and Tiam2 proteins (T-lymphoma invasion and metastasis). The CC subdomain forms an antiparallel coiled coil with two long α-helices, together with the C-terminal Ex subdomain they form a small globular domain comprising three α-helices. The CC subdomain of the Tiam2 PHCCEx domain follows the C-terminal alpha1 helix of the PH subdomain through a four-residue linker [].
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Protein Domain
IPR040749 | BRCC36_C
Type: Domain
Description: This is the C-terminal domain of BRCC36, a Zn2+ dependent deubiquitinating enzyme, present in Camponotus floridanus. BRCC36 hydrolyzes lysine linked ubiquitin chains as part of macromolecular complexes that participate in either interferon signalling or DNA-damage recognition. The domain consists of 2 non canonical helices. The domain interacts hydrophobically with helices alpha 4 and alpha 5 of KIAA0157 in the form of a coiled coil helical bundle. This interaction helps establish the association of BRCC36 with KIAA0157, a pseudo-DUB MPN- protein that is essential for theactivity of BRCC36 [].
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Protein Domain
IPR001943 | UVR_dom
Type: Domain
Description: During the process of Escherichia coli nucleotide excision repair, DNA damagerecognition and processing are achieved by the action of the uvrA, uvrB,and uvrC gene products []. UvrB and UvrC share a common domain of around 35amino acids, the so called UVR domain. This domain in UvrB can interact withthe homologous domain in UvrC throughout a putative coiled coil structure.This interaction is important for the incision of the damaged strand [].A conserved region similar to the UVR domain is also found in the ATP-binding subunit of bacterial and chloroplastic Clp ATPases [], which suggest that the UVR domain is not only involved in the interaction between uvrB and uvrC.
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Protein Domain
IPR021070 | Killing_trait_RebB
Type: Family
Description: R-bodies are highly insoluble protein ribbons which coil into cylindrical structures in the cell and the genes for their synthesis and assembly are encoded on a plasmid. One of these three proteins is RebB, which this entry represents.RebB is one of three proteins necessary for the production of R- bodies, refractile inclusion bodies produced by a small number of bacterial species, essential for the expression of the killing trait of the endosymbiont bacteria that produce them for attack upon the host Paramecium. Note that many members are uncharacterised proteins [, ].
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Publication
20206616 | J:160493
First Author: Dy P
Year: 2010
Journal: Dev Biol
Title: Synovial joint morphogenesis requires the chondrogenic action of Sox5 and Sox6 in growth plate and articular cartilage.
Volume: 341
Issue: 2
Pages: 346-59
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Protein Coding Gene
MGI:2686151 | Kif28
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:109318 | Myl6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1917789 | Myl6b
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1339709 | Myh3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1339713 | Myh4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1339712 | Myh8
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:109187 | Kifc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:3710243 | Myh7b
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098232 | Kif12
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098237 | Kif9
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098258 | Kif15
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
B9EKI3
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
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Protein
Q2V056
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
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Protein
A0A0G2JFK4
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: false
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Protein
Q3U008
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: true
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Protein
Q3TZQ9
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: false
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Publication
8466476 | -
First Author: Van Houten B
Year: 1993
Journal: Bioessays
Title: Mechanism of action of the Escherichia coli UvrABC nuclease: clues to the damage recognition problem.
Volume: 15
Issue: 1
Pages: 51-9
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Publication
8530482 | -
First Author: Moolenaar GF
Year: 1995
Journal: J Biol Chem
Title: The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3'-incision.
Volume: 270
Issue: 51
Pages: 30508-15
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Publication
15554981 | -
First Author: Frees D
Year: 2004
Journal: Mol Microbiol
Title: Clp ATPases are required for stress tolerance, intracellular replication and biofilm formation in Staphylococcus aureus.
Volume: 54
Issue: 5
Pages: 1445-62
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Publication
9724625 | -
First Author: Jenkins J
Year: 1998
Journal: J Struct Biol
Title: Structure and evolution of parallel beta-helix proteins.
Volume: 122
Issue: 1-2
Pages: 236-46
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Publication
11927603 | -
First Author: Shorter J
Year: 2002
Journal: J Cell Biol
Title: Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115.
Volume: 157
Issue: 1
Pages: 45-62
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Publication
2687239 | -
First Author: Wachi M
Year: 1989
Journal: J Bacteriol
Title: New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells.
Volume: 171
Issue: 12
Pages: 6511-6
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Publication
11830637 | -
First Author: Urbauer JL
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: Solution structure and stability of the anti-sigma factor AsiA: implications for novel functions.
Volume: 99
Issue: 4
Pages: 1831-5
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Publication
15128430 | -
 
First Author: Fridmann-Sirkis Y
Year: 2004
Journal: BMC Cell Biol
Title: TMF is a golgin that binds Rab6 and influences Golgi morphology.
Volume: 5
Pages: 18
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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