|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

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

Search results 1301 to 1400 out of 1557 for Tpr

<< First    < Previous  |  Next >    Last >>
0.059s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Protein
Q6PES1
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
•
•
•
•
•
Protein
Q8C027
Organism: Mus musculus/domesticus
Length: 813  
Fragment?: false
•
•
•
•
•
Protein
E0CY15
Organism: Mus musculus/domesticus
Length: 903  
Fragment?: false
•
•
•
•
•
Protein
Q3V3C0
Organism: Mus musculus/domesticus
Length: 1069  
Fragment?: true
•
•
•
•
•
Protein
E9PWD9
Organism: Mus musculus/domesticus
Length: 1133  
Fragment?: false
•
•
•
•
•
Protein Coding Gene
MGI:2385621 | Nup153
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1916732 | Nup35
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:2443003 | Pcid2
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Publication
34048282 | J:312131
First Author: Mitchell R
Year: 2021
Journal: Am J Physiol Heart Circ Physiol
Title: Ifetroban reduces coronary artery dysfunction in a mouse model of Duchenne muscular dystrophy.
Volume: 321
Issue: 1
Pages: H52-H58
•
•
•
•
•
Publication
12172320 | J:106000
First Author: Kubis N
Year: 2002
Journal: J Hypertens
Title: Role of microvascular rarefaction in the increased arterial pressure in mice lacking for the endothelial nitric oxide synthase gene (eNOS3pt-/- ).
Volume: 20
Issue: 8
Pages: 1581-7
•
•
•
•
•
Publication
29934347 | J:264331
     
First Author: Lizama BN
Year: 2018
Journal: J Neurosci
Title: Neuronal Preconditioning Requires the Mitophagic Activity of C-terminus of HSC70-Interacting Protein.
•
•
•
•
•
Protein
Q9ERU9
Organism: Mus musculus/domesticus
Length: 3053  
Fragment?: false
•
•
•
•
•
Protein
D3YY23
Organism: Mus musculus/domesticus
Length: 762  
Fragment?: false
•
•
•
•
•
Protein
Q9D4H7
Organism: Mus musculus/domesticus
Length: 753  
Fragment?: false
•
•
•
•
•
Protein
A0A182DWE6
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
•
•
•
•
•
Protein
E9PWW6
Organism: Mus musculus/domesticus
Length: 970  
Fragment?: false
•
•
•
•
•
Protein
Q3UBH9
Organism: Mus musculus/domesticus
Length: 970  
Fragment?: false
•
•
•
•
•
Protein
Q3TIQ4
Organism: Mus musculus/domesticus
Length: 970  
Fragment?: false
•
•
•
•
•
Protein
F6ZE64
Organism: Mus musculus/domesticus
Length: 754  
Fragment?: false
•
•
•
•
•
Publication
18329369 | J:137430
First Author: Pohl C
Year: 2008
Journal: Cell
Title: Final stages of cytokinesis and midbody ring formation are controlled by BRUCE.
Volume: 132
Issue: 5
Pages: 832-45
•
•
•
•
•
Publication
28242696 | -
First Author: Weijman JF
Year: 2017
Journal: Proc Natl Acad Sci U S A
Title: Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1.
Volume: 114
Issue: 11
Pages: E2096-E2105
•
•
•
•
•
Publication
17525332 | -
First Author: Matsuoka S
Year: 2007
Journal: Science
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
Volume: 316
Issue: 5828
Pages: 1160-6
•
•
•
•
•
Protein
F6VIR4
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: true
•
•
•
•
•
Protein
Q9JLI8
Organism: Mus musculus/domesticus
Length: 962  
Fragment?: false
•
•
•
•
•
Protein
Q9CWR2
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
•
•
•
•
•
Protein
Q68FD5
Organism: Mus musculus/domesticus
Length: 1675  
Fragment?: false
•
•
•
•
•
Protein
Q8R5A0
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: false
•
•
•
•
•
Protein
Q5KU39
Organism: Mus musculus/domesticus
Length: 853  
Fragment?: false
•
•
•
•
•
Protein
P97443
Organism: Mus musculus/domesticus
Length: 490  
Fragment?: false
•
•
•
•
•
Protein
P56695
Organism: Mus musculus/domesticus
Length: 890  
Fragment?: false
•
•
•
•
•
Protein
Q8BTK5
Organism: Mus musculus/domesticus
Length: 799  
Fragment?: false
•
•
•
•
•
Protein
Q3UN10
Organism: Mus musculus/domesticus
Length: 814  
Fragment?: false
•
•
•
•
•
Protein
Q3TDI2
Organism: Mus musculus/domesticus
Length: 890  
Fragment?: false
•
•
•
•
•
Protein
Q3UMA8
Organism: Mus musculus/domesticus
Length: 890  
Fragment?: false
•
•
•
•
•
Protein
Q3UQT9
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
•
•
•
•
•
Protein
Q5SXR6
Organism: Mus musculus/domesticus
Length: 1679  
Fragment?: false
•
•
•
•
•
Protein
Q3TR55
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
•
•
•
•
•
Protein
G5E8R7
Organism: Mus musculus/domesticus
Length: 456  
Fragment?: false
•
•
•
•
•
Protein
Q3TIF7
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
•
•
•
•
•
Protein
Q80UI9
Organism: Mus musculus/domesticus
Length: 890  
Fragment?: false
•
•
•
•
•
Protein
Q80U89
Organism: Mus musculus/domesticus
Length: 1684  
Fragment?: true
•
•
•
•
•
Protein
D3Z5H1
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
•
•
•
•
•
Publication
28076793 | J:254044
First Author: Burikhanov R
Year: 2017
Journal: Cell Rep
Title: Chloroquine-Inducible Par-4 Secretion Is Essential for Tumor Cell Apoptosis and Inhibition of Metastasis.
Volume: 18
Issue: 2
Pages: 508-519
•
•
•
•
•
Protein
Q8K284
Organism: Mus musculus/domesticus
Length: 2101  
Fragment?: false
•
•
•
•
•
Protein
Q3UTP3
Organism: Mus musculus/domesticus
Length: 1286  
Fragment?: false
•
•
•
•
•
Protein
Q3UHL0
Organism: Mus musculus/domesticus
Length: 2101  
Fragment?: false
•
•
•
•
•
Protein
Q3UPZ9
Organism: Mus musculus/domesticus
Length: 1233  
Fragment?: true
•
•
•
•
•
Protein
A0A0U1RPD8
Organism: Mus musculus/domesticus
Length: 2005  
Fragment?: false
•
•
•
•
•
Protein
Q3UY03
Organism: Mus musculus/domesticus
Length: 634  
Fragment?: true
•
•
•
•
•
Protein
Q3UQ70
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: true
•
•
•
•
•
Publication
15569936 | -
First Author: Chan C
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: Structural basis of activity and allosteric control of diguanylate cyclase.
Volume: 101
Issue: 49
Pages: 17084-9
•
•
•
•
•
Publication
3187531 | -
First Author: Aggarwal AK
Year: 1988
Journal: Science
Title: Recognition of a DNA operator by the repressor of phage 434: a view at high resolution.
Volume: 242
Issue: 4880
Pages: 899-907
•
•
•
•
•
Publication
11972345 | -
First Author: Steinmetzer K
Year: 2002
Journal: Nucleic Acids Res
Title: CopR binds and bends its target DNA: a footprinting and fluorescence resonance energy transfer study.
Volume: 30
Issue: 9
Pages: 2052-60
•
•
•
•
•
Publication
11545737 | -
First Author: Fairall L
Year: 2001
Journal: Mol Cell
Title: Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2.
Volume: 8
Issue: 2
Pages: 351-61
•
•
•
•
•
Publication
9034194 | -
First Author: Cooper JP
Year: 1997
Journal: Nature
Title: Regulation of telomere length and function by a Myb-domain protein in fission yeast.
Volume: 385
Issue: 6618
Pages: 744-7
•
•
•
•
•
Publication
21525244 | -
First Author: Scrivens PJ
Year: 2011
Journal: Mol Biol Cell
Title: C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking.
Volume: 22
Issue: 12
Pages: 2083-93
•
•
•
•
•
Publication
8127861 | -
First Author: L'Etoile ND
Year: 1994
Journal: Proc Natl Acad Sci U S A
Title: Human transcription factor IIIC box B binding subunit.
Volume: 91
Issue: 5
Pages: 1652-6
•
•
•
•
•
Publication
31525467 | -
First Author: Silva NSM
Year: 2020
Journal: Biochim Biophys Acta Proteins Proteom
Title: Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities.
Volume: 1868
Issue: 1
Pages: 140282
•
•
•
•
•
Protein Domain
IPR043969 | MAP3K_PH
Type: Domain
Description: Apoptosis signal-regulating kinases (ASK1/2/3 or MAP3K5/6/15) are mitogen-activated protein kinase kinase kinases (MAP3Ks) that mediate cellular responses to redox stress and inflammatory cytokines and play a key role in innate immunity and viral infection. This kind of signalling kinases are regulated by oligomerization and regulatory domains. In its N-terminal there is a thioredoxin-binding domain that negatively regulates activity and a TNF receptor-associated factors (TRAFs)-binding domain which triggers ASK activation and kinase activity. TRAFs-binding domain is composed by 14 helices, which form seven tetratricopeptide repeats (TPRs), followed by a PH-like domain to complete de central regulatory domain of ASK. The central regulatory region promotes ASK1 activity via its PH domain but also facilitates ASK1 autoinhibition by bringing the thioredoxin-binding and kinase domains into close proximity. The PH-like domain, adjacent to the kinase domain, is required together with an intact TPR region for ASK1 activity.The major role of the central regulatory region is to bring the thioredoxin-binding domain into close proximity to the kinase domain to inhibit its activity [].This PH-like domain is found in the regulatory region of ASK1/2/3 (also known as MAP3K5/6/15). The central regulatory region of ASK1 mediates a compact arrangement of the kinase and thioredoxin-binding domains which allows the binding of substrates for phosphorylation. This PH-like domain adopts the typical form of two antiparallel β-sheets followed by a C-terminal amphipathic helix [].
•
•
•
•
•
Protein Domain
IPR005631 | SDH
Type: Family
Description: This family includes the highly conserved mitochondrial and bacterial proteins Sdh5/SDHAF2/SdhE.Both yeast and human Sdh5/SDHAF2 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Mutational inactivation of Sdh5 confers tumor susceptibility in humans []. Bacterial homologues of Sdh5, termed SdhE, are functionally conserved being required for the flavinylation of SdhA and succinate dehydrogenase activity. Like Sdh5, SdhE interacts with SdhA. Furthermore, SdhE was characterised as a FAD co-factor chaperone that directly binds FAD to facilitate the flavinylation of SdhA. Phylogenetic analysis demonstrates that SdhE/Sdh5 proteins evolved only once in an ancestral alpha-proteobacteria prior to the evolution of the mitochondria and now remain in subsequent descendants including eukaryotic mitochondria and the alpha, beta and gamma proteobacteria [].This family was previously annotated in Pfam as being a divergent TPR repeat but structural evidence has indicated this is not true.
•
•
•
•
•
Protein Domain
IPR024111 | PEX5/PEX5L
Type: Family
Description: Peroxisomal proteins catalyse metabolic reactions. The import of proteins from the cytosol into the peroxisomes matrix depends on more than a dozen peroxin (PEX) proteins, among which PEX5 and PEX7 serve as receptors that shuttle proteins bearing one of two peroxisome-targeting signals (PTSs) into the organelle. PEX5 is the PTS1 receptor, while PEX7 is the PTS2 receptor. In plants, PEX7 depends on PEX5 binding to deliver PTS2 cargo into the peroxisome, and PEX7 also facilitates PEX5 accumulation and import of PTS1 cargo into peroxisomes [, ]. This entry include PEX5 (also known as PTS1R) from animals, fungi and plants. This entry also includes PEX5L from vertebrates. PEX5 binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import [, , ]. Based on subcellular localization and binding properties mammalian PEX5 may function as a regulator in an early step of the PTS1 protein import process []. PEX5L acts as an accessory subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, regulating their cell-surface expression and cyclic nucleotide dependence [, ]. Interestingly, although PEX5 and PEX5L have structurally similar binding at their TPR domains, they bind to different substrates in vivo [].
•
•
•
•
•
Protein Domain
IPR036507 | Telomere_rpt-bd_fac_dimer_sf
Type: Homologous_superfamily
Description: Telomeres function to shield chromosome ends from degradation and end-to-end fusions, as well as preventing the activation of DNA damage checkpoints. Telomeric repeat binding factor (TRF) proteins TRF1 and TRF2 are major components of vertebrate telomeres required for regulation of telomere stability. TRF1 and TRF2 bind to telomeric DNA as homodimers. Dimerisation involves the TRF homology (TRFH) subdomain contained within the dimerisation domain. The TRFH subdomain is important not only for dimerisation, but for DNA binding, telomere localisation, and interactions with other telomeric proteins. The dimerisation domains of TRF1 and TRF2 show the same multi-helical structure, arranged in a solenoid conformation similar to TPR repeats, which can be divided into an α-α superhelix and a long alpha hairpin [].The two related human TRF proteins hTRF1 and hTRF2 form homodimers and bind directly to telomeric TTAGGG repeats via the myb DNA binding domain at the carboxy terminus []. TRF1 is implicated in telomere length regulation and TRF2 in telomere protection []. Other telomere complex associated proteins are recruited through their interaction with either TRF1 or TRF2. The fission yeast protein Taz1p (telomere-associated in Schizosaccharomyces pombe (Fission yeast) has similarity to both hTRF1 and hTRF2 and may perform the dual functions of TRF1 and TRF2 at fission yeast telomeres []. This entry represents the dimerisation domain.
•
•
•
•
•
Protein Domain
IPR046874 | MAPK5/6/15
Type: Family
Description: Apoptosis signal-regulating kinases (ASK1/2/3 or MAP3K5/6/15) are mitogen-activated protein kinase kinase kinases (MAP3Ks) that mediate cellular responses to redox stress and inflammatory cytokines and play a key role in innate immunity and viral infection. This kind of signalling kinases are regulated by oligomerization and regulatory domains. In its N-terminal there is a thioredoxin-binding domain that negatively regulates activity and a TNF receptor-associated factors (TRAFs)-binding domain which triggers ASK activation and kinase activity. TRAFs-binding domain is composed by 14 helices, which form seven tetratricopeptide repeats (TPRs), followed by a PH-like domain to complete de central regulatory domain of ASK. The central regulatory region promotes ASK1 activity via its PH domain but also facilitates ASK1 autoinhibition by bringing the thioredoxin-binding and kinase domains into close proximity. The PH-like domain, adjacent to the kinase domain, is required together with an intact TPR region for ASK1 activity.The major role of the central regulatory region is to bring the thioredoxin-binding domain into close proximity to the kinase domain to inhibit its activity [].
•
•
•
•
•
Protein Domain
IPR046873 | HisK-N-like
Type: Domain
Description: Apoptosis signal-regulating kinases (ASK1/2/3 or MAP3K5/6/15) are mitogen-activated protein kinase kinase kinases (MAP3Ks) that mediate cellular responses to redox stress and inflammatory cytokines and play a key role in innate immunity and viral infection. This kind of signalling kinases are regulated by oligomerization and regulatory domains. In its N-terminal there is a thioredoxin-binding domain that negatively regulates activity and a TNF receptor-associated factors (TRAFs)-binding domain which triggers ASK activation and kinase activity. TRAFs-binding domain is composed by 14 helices, which form seven tetratricopeptide repeats (TPRs), followed by a PH-like domain to complete de central regulatory domain of ASK. The central regulatory region promotes ASK1 activity via its PH domain but also facilitates ASK1 autoinhibition by bringing the thioredoxin-binding and kinase domains into close proximity. The PH-like domain, adjacent to the kinase domain, is required together with an intact TPR region for ASK1 activity.The major role of the central regulatory region is to bring the thioredoxin-binding domain into close proximity to the kinase domain to inhibit its activity [].This domain represents a predicted non-heme-binding version of the globin domain identified in ASK1/2/3. It displays strongest affinities to the HisK-N family of sensor domains, which inhibit histidine kinase activation required for sporulation in bacteria of the firmicutes lineage. This globin domain is predicted to represent an independent sensory element recognizing a fatty acid or a related membrane-derived molecule which regulates activity of the ASK signalosome in apoptosis [].
•
•
•
•
•
Protein Domain
IPR046872 | DRHyd-ASK
Type: Domain
Description: Apoptosis signal-regulating kinases (ASK1/2/3 or MAP3K5/6/15) are mitogen-activated protein kinase kinase kinases (MAP3Ks) that mediate cellular responses to redox stress and inflammatory cytokines and play a key role in innate immunity and viral infection. This kind of signalling kinases are regulated by oligomerization and regulatory domains. In its N-terminal there is a thioredoxin-binding domain that negatively regulates activity and a TNF receptor-associated factors (TRAFs)-binding domain which triggers ASK activation and kinase activity. TRAFs-binding domain is composed by 14 helices, which form seven tetratricopeptide repeats (TPRs), followed by a PH-like domain to complete de central regulatory domain of ASK. The central regulatory region promotes ASK1 activity via its PH domain but also facilitates ASK1 autoinhibition by bringing the thioredoxin-binding and kinase domains into close proximity. The PH-like domain, adjacent to the kinase domain, is required together with an intact TPR region for ASK1 activity.The major role of the central regulatory region is to bring the thioredoxin-binding domain into close proximity to the kinase domain to inhibit its activity [].This is an uncharacterised DRHyd domain observed in MAP3K5/6/15. It potentially generates nucleotide-derived signal recognised by the TPR-S domain found in the same proteins [].
•
•
•
•
•
Protein Domain
IPR017357 | TERF1/2
Type: Family
Description: This group represents telomeric repeat-binding factors 1 (TERF1, also known as TRF1).Telomeres function to shield chromosome ends from degradation and end-to-end fusions, as well as preventing the activation of DNA damage checkpoints. Telomeric repeat binding factor (TRF) proteins TRF1 and TRF2 are major components of vertebrate telomeres required for regulation of telomere stability. TRF1 and TRF2 bind to telomeric DNA as homodimers. Dimerisation involves the TRF homology (TRFH) subdomain contained within the dimerisation domain. The TRFH subdomain is important not only for dimerisation, but for DNA binding, telomere localisation, and interactions with other telomeric proteins. The dimerisation domains of TRF1 and TRF2 show the same multi-helical structure, arranged in a solenoid conformation similar to TPR repeats, which can be divided into an α-α superhelix and a long alpha hairpin [].The two related human TRF proteins hTRF1 and hTRF2 form homodimers and bind directly to telomeric TTAGGG repeats via the myb DNA binding domain at the carboxy terminus []. TRF1 is implicated in telomere length regulation and TRF2 in telomere protection []. Other telomere complex associated proteins are recruited through their interaction with either TRF1 or TRF2. The fission yeast protein Taz1p (telomere-associated in Schizosaccharomyces pombe (Fission yeast) has similarity to both hTRF1 and hTRF2 and may perform the dual functions of TRF1 and TRF2 at fission yeast telomeres [].
•
•
•
•
•
Protein Domain
IPR030657 | TERF2
Type: Family
Description: This entry represents telomeric repeat-binding factor 2 (TERF2, also known as TRF2).Telomeres function to shield chromosome ends from degradation and end-to-end fusions, as well as preventing the activation of DNA damage checkpoints. Telomeric repeat binding factor (TRF) proteins TRF1 and TRF2 are major components of vertebrate telomeres required for regulation of telomere stability. TRF1 and TRF2 bind to telomeric DNA as homodimers. Dimerisation involves the TRF homology (TRFH) subdomain contained within the dimerisation domain. The TRFH subdomain is important not only for dimerisation, but for DNA binding, telomere localisation, and interactions with other telomeric proteins. The dimerisation domains of TRF1 and TRF2 show the same multi-helical structure, arranged in a solenoid conformation similar to TPR repeats, which can be divided into an α-α superhelix and a long alpha hairpin [].The two related human TRF proteins hTRF1 and hTRF2 form homodimers and bind directly to telomeric TTAGGG repeats via the myb DNA binding domain at the carboxy terminus []. TRF1 is implicated in telomere length regulation and TRF2 in telomere protection []. Other telomere complex associated proteins are recruited through their interaction with either TRF1 or TRF2. The fission yeast protein Taz1p (telomere-associated in Schizosaccharomyces pombe (Fission yeast) has similarity to both hTRF1 and hTRF2 and may perform the dual functions of TRF1 and TRF2 at fission yeast telomeres [].
•
•
•
•
•
Protein Domain
IPR001387 | Cro/C1-type_HTH
Type: Domain
Description: The cro/C1-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50-60 residues present in transcriptional regulators. The domain is named after the transcriptional repressors cro and C1 of temperate bacteriophages 434 and lambda, respectively. Besides in bacteriophages, cro/C1-type regulators are present in prokaryotes and in eukaryotes. The helix-turn-helix DNA-binding motif is generally located in the N-terminal part of these transcriptional regulators. The C-terminal part may contain an oligomerization domain, e.g. C1 repressors and CopR act as dimers, while SinR is a tetramer. The cro/C1-type HTH domain also occurs in combination with the TPR repeat and the C-terminal part of C-5 cytosine-specific DNA methylases contains regions related to the enzymatic function.Several structures of cro/C1-type transcriptional repressors have been resolved and their DNA-binding domain encompasses five α-helices, of which the extremities are less conserved []. The helix-turn-helix motif comprises the second and third helices, the third being called the recognition helix. The HTH is involved in DNA-binding into the major groove, where the recognition helix makes most DNA-contacts. The bacteriophage repressors regulate lysogeny/lytic growth by binding with differential affinity to the operators. These operators show 2-fold symmetry and the repressors bind as dimers. Binding of the repressor to the operator positions the DNA backbone into a slightly bent twist [, ].
•
•
•
•
•
Protein Domain
IPR025136 | MAP3K_TRAF-bd
Type: Domain
Description: Apoptosis signal-regulating kinases (ASK1/2/3 or MAP3K5/6/15) are mitogen-activated protein kinase kinase kinases (MAP3Ks) that mediate cellular responses to redox stress and inflammatory cytokines and play a key role in innate immunity and viral infection. This kind of signalling kinases are regulated by oligomerization and regulatory domains. In its N-terminal there is a thioredoxin-binding domain that negatively regulates activity and a TNF receptor-associated factors (TRAFs)-binding domain which triggers ASK activation and kinase activity. TRAFs-binding domain is composed by 14 helices, which form seven tetratricopeptide repeats (TPRs), followed by a PH-like domain to complete de central regulatory domain of ASK. The central regulatory region promotes ASK1 activity via its PH domain but also facilitates ASK1 autoinhibition by bringing the thioredoxin-binding and kinase domains into close proximity. The PH-like domain, adjacent to the kinase domain, is required together with an intact TPR region for ASK1 activity.The major role of the central regulatory region is to bring the thioredoxin-binding domain into close proximity to the kinase domain to inhibit its activity [].This domain corresponds to the TRAFs-binding domain found at the N terminus of some MAP3Ks. This domain includes seven tetratricopeptide repeats (TPRs) and, together with th PH-like domain, constitutes the central regulatory domain of ASK1.
•
•
•
•
•
Protein Domain
IPR013867 | Telomere_rpt-bd_fac_dimer_dom
Type: Domain
Description: Telomeres function to shield chromosome ends from degradation and end-to-end fusions, as well as preventing the activation of DNA damage checkpoints. Telomeric repeat binding factor (TRF) proteins TRF1 and TRF2 are major components of vertebrate telomeres required for regulation of telomere stability. TRF1 and TRF2 bind to telomeric DNA as homodimers. Dimerisation involves the TRF homology (TRFH) subdomain contained within the dimerisation domain. The TRFH subdomain is important not only for dimerisation, but for DNA binding, telomere localisation, and interactions with other telomeric proteins. The dimerisation domains of TRF1 and TRF2 show the same multi-helical structure, arranged in a solenoid conformation similar to TPR repeats, which can be divided into an α-α superhelix and a long alpha hairpin [].The two related human TRF proteins hTRF1 and hTRF2 form homodimers and bind directly to telomeric TTAGGG repeats via the myb DNA binding domain at the carboxy terminus []. TRF1 is implicated in telomere length regulation and TRF2 in telomere protection []. Other telomere complex associated proteins are recruited through their interaction with either TRF1 or TRF2. The fission yeast protein Taz1p (telomere-associated in Schizosaccharomyces pombe (Fission yeast) has similarity to both hTRF1 and hTRF2 and may perform the dual functions of TRF1 and TRF2 at fission yeast telomeres []. This entry represents the dimerisation domain.
•
•
•
•
•
Publication
22576369 | J:241280
 
First Author: Sala V
Year: 2012
Journal: Mol Med
Title: Signaling to cardiac hypertrophy: insights from human and mouse RASopathies.
Volume: 18
Pages: 938-47
•
•
•
•
•
Protein Coding Gene
MGI:894323 | Ranbp2
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1930089 | Mcm3ap
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1097706 | Cetn3
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1919286 | Eny2
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1341857 | Mad1l1
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1860374 | Mad2l1
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:109404 | Nup98
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI:1347085 | Cetn2
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Publication
18094055 | J:200405
First Author: Yamamura R
Year: 2008
Journal: Mol Biol Cell
Title: The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions.
Volume: 19
Issue: 3
Pages: 971-83
•
•
•
•
•
Publication
23395375 | J:197848
First Author: van Spronsen M
Year: 2013
Journal: Neuron
Title: TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites.
Volume: 77
Issue: 3
Pages: 485-502
•
•
•
•
•
Publication
24213529 | J:211898
First Author: Sato T
Year: 2014
Journal: J Cell Sci
Title: Rab8a and Rab8b are essential for several apical transport pathways but insufficient for ciliogenesis.
Volume: 127
Issue: Pt 2
Pages: 422-31
•
•
•
•
•
Publication
22921120 | J:187364
First Author: Pilli M
Year: 2012
Journal: Immunity
Title: TBK-1 promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation.
Volume: 37
Issue: 2
Pages: 223-34
•
•
•
•
•
Protein
Q9JKK8
Organism: Mus musculus/domesticus
Length: 2635  
Fragment?: false
•
•
•
•
•
Protein
Q3HNM7
Organism: Mus musculus/domesticus
Length: 579  
Fragment?: false
•
•
•
•
•
Protein
Q3U1Y4
Organism: Mus musculus/domesticus
Length: 1499  
Fragment?: false
•
•
•
•
•
Protein
A6H8H2
Organism: Mus musculus/domesticus
Length: 1906  
Fragment?: false
•
•
•
•
•
Protein
Q9JLN9
Organism: Mus musculus/domesticus
Length: 2549  
Fragment?: false
•
•
•
•
•
Protein
Q91W86
Organism: Mus musculus/domesticus
Length: 941  
Fragment?: false
•
•
•
•
•
Protein
G3UW77
Organism: Mus musculus/domesticus
Length: 532  
Fragment?: false
•
•
•
•
•
Protein
A0A1L1SSL9
Organism: Mus musculus/domesticus
Length: 2641  
Fragment?: false
•
•
•
•
•
Protein
A0A0R4J172
Organism: Mus musculus/domesticus
Length: 1510  
Fragment?: false
•
•
•
•
•
Protein
E9Q449
Organism: Mus musculus/domesticus
Length: 1615  
Fragment?: false
•
•
•
•
•
Protein
E9QPK4
Organism: Mus musculus/domesticus
Length: 2635  
Fragment?: false
•
•
•
•
•
Protein
Q8CEE5
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
•
•
•
•
•
Protein
E9Q8V6
Organism: Mus musculus/domesticus
Length: 1869  
Fragment?: false
•
•
•
•
•
Protein
B9EKY0
Organism: Mus musculus/domesticus
Length: 1354  
Fragment?: false
•
•
•
•
•
Protein
Q8R2Q7
Organism: Mus musculus/domesticus
Length: 869  
Fragment?: false
•
•
•
•
•
Protein
B2RT44
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
•
•
•
•
•
Protein
Q6PIP5
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: false
•
•
•
•
•




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