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Search results 2101 to 2200 out of 2368 for Tpr

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Type Details Score
Publication
11463335 | J:188908
First Author: Amery L
Year: 2001
Journal: Biochem J
Title: Identification of PEX5p-related novel peroxisome-targeting signal 1 (PTS1)-binding proteins in mammals.
Volume: 357
Issue: Pt 3
Pages: 635-46
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Publication
32189562 | -
First Author: Han Y
Year: 2020
Journal: Channels (Austin)
Title: The structure and function of TRIP8b, an auxiliary subunit of hyperpolarization-activated cyclic-nucleotide gated channels.
Volume: 14
Issue: 1
Pages: 110-122
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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
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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
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Publication
20118938 | -
First Author: Schneider M
Year: 2010
Journal: Nat Struct Mol Biol
Title: Human PRP4 kinase is required for stable tri-snRNP association during spliceosomal B complex formation.
Volume: 17
Issue: 2
Pages: 216-21
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Publication
26586833 | -
First Author: Sun L
Year: 2016
Journal: Plant Physiol
Title: Arabidopsis PHL2 and PHR1 Act Redundantly as the Key Components of the Central Regulatory System Controlling Transcriptional Responses to Phosphate Starvation.
Volume: 170
Issue: 1
Pages: 499-514
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Publication
30327661 | -
 
First Author: Wang Z
Year: 2018
Journal: Front Plant Sci
Title: Functional Characterization of Arabidopsis PHL4 in Plant Response to Phosphate Starvation.
Volume: 9
Pages: 1432
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Publication
2125516 | -
First Author: Cassingena R
Year: 1990
Journal: Biol Cell
Title: Methionine-independence, tumorigenicity and oncogene expression of rat hepatocarcinoma cells.
Volume: 69
Issue: 2
Pages: 113-8
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Publication
26082401 | -
First Author: Guo M
Year: 2015
Journal: Plant Physiol
Title: Integrative Comparison of the Role of the PHOSPHATE RESPONSE1 Subfamily in Phosphate Signaling and Homeostasis in Rice.
Volume: 168
Issue: 4
Pages: 1762-76
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Publication
28969789 | -
 
First Author: Hu S
Year: 2017
Journal: Plant Sci
Title: OsMYB45 plays an important role in rice resistance to cadmium stress.
Volume: 264
Pages: 1-8
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Publication
28708834 | -
First Author: Zhang Y
Year: 2017
Journal: PLoS One
Title: OsMPH1 regulates plant height and improves grain yield in rice.
Volume: 12
Issue: 7
Pages: e0180825
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Publication
32680975 | -
First Author: Ren D
Year: 2020
Journal: Plant Physiol
Title: MORE FLORET1 Encodes a MYB Transcription Factor That Regulates Spikelet Development in Rice.
Volume: 184
Issue: 1
Pages: 251-265
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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 ��-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 [, ].
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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 ��-sheets followed by a C-terminal amphipathic helix [].
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Protein Domain
IPR024111 | PEX5/PEX5L
Type: Family
Description: 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 [].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 [, ].
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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 ��-�� superhelix and a long �� 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 [].
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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 ��-�� superhelix and a long �� hairpin [].The two related human TRF proteins hTRF1 and hTRF2 formhomodimers 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 [].
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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.
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Protein Domain
IPR059087 | RESC10
Type: Domain
Description: This domain is found in RESC10 (). RESC10 is predicted to adopt an all-helical structure with a disordered N-terminal region (of about 118 amino acids) that is predicted with low confidence. The rest of the protein is predicted with high confidence and shows a helical repeat structure that resembles proteins containing Armadillo (ARM)/��-catenin-like repeats and tetratricopeptide (TPR) repeats. Both ARM and TPR repeats are implicated in mediating protein-protein interactions.RNA-editing substrate-binding complex 10 protein (RESC10) is a component of RESC which, together with RECC forms the editosome that orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs []. RESC stabilises gRNAs and engages mRNAs. The RNA-editing catalytic complex (RECC) fulfills gRNA-programmed mRNA cleavage, uridine insertion or deletion, and religation reactions. RESC is a heterogenous assembly of ~18 proteins that enclose gRNAs and mRNAs. RESC10 is composed of HEAT repeats. RESC10 is integral to maintaining the structural and functional integrity of RESC, acting upstream of other RESC proteins to orchestrate their organisation and interactions. Besides, the gRNA 3' nucleotides interact with RESC10 [].
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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 ��-�� superhelix and a long �� 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.
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Protein Domain
IPR056167 | A-sol_ELP1
Type: Domain
Description: This entry represents the ��-solenoid domain found within the C-terminal dimerisation domain of Elongator complex protein 1 (ELP1) from eukaryotes. Residues within the ��-14-helix are highly conserved from yeast to human and act as a kink to maintain the TPR-like domain and ��-solenoid domain at nearly a 90-degree angle.Elongator is a conserved protein complex implicated in multiple processes including regulation of transcription, alpha-tubulin acetylation and tRNA modification. Mutations in the ELP1 gene have been shown to cause the neurodegenerative disease familial dysautonomia []. The C-terminal dimerisation domain consists of 28 ��-helices organised in three domains: an elongated ��-solenoid domain (helices 1 to 14); a TPR domain, formed by six double-helix repeats (helices 15 to 26); and a three-helix bundle, C-terminal cap (helices 26 to 28) []. ELP1 self-association contributes to its stability and is important for Elongator assembly []. ELP1 is considered to function both as a scaffold, for Elongator complex ELP2 and ELP3 binding, and as a docking site for various factors that regulate Elongator activity [, , ]. Also known as IKAP, ELP1 acts as a regulator of IkB kinase complex involved in proinflammatory cytokine signalling [].
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Protein Domain
IPR046955 | PHR1-like
Type: Family
Description: This family of plant proteins includes Myb family transcription factor protein PHOSPHATE STARVATION RESPONSE 1 from Arabidopsis thaliana (PHR1) and similar proteins from plants, including PHLs from A.thaliana and MPH1/MOF1 from rice. They belong to a family of MYB-CC transcription factors and are regarded as the key components of the central regulatory system controlling plant transcriptional responses to phosphate (Pi) starvation [, , ].PHR1 is a transcription factor and a master regulator of phosphate starvation responses (PSRs) [].PHL1 (PHR1-LIKE 1), PHL2, and perhaps also PHL3, act redundantly with PHR1 to regulate plant Pi starvation responses []. However, PHL4 has only a minor role in the regulation of plant responses to Pi starvation []. PHL10 (also known as MYR1) acts redundantly with PHL9 (also known as MYR2) as a repressor of flowering and organ elongation under decreased light intensity [].MPH1 is likely a transcription factor involved in the regulation of plant height by elongating internode cell length []. It is involved in the positive regulation of grain yield []. MPH may play a role in the regulation of genes related to cell elongation and cell wall synthesis, which are associated with plant height and yield phenotypes []. It also plays a role in tolerance to cadmium stress [].MOF1 is a transcriptional repressor that plays a role in the regulation of organ identity and spikelet meristem determinacy []. It interacts with the TPR corepressors to possibly repress the expression of downstream target genes [].
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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 [].
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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 [].
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Protein Domain
IPR056424 | Beta-prop_GEMI5_2nd
Type: Domain
Description: This entry represents the second ��-propeller found in Gem-associated protein 5 (GEMI5) from vertebrates and its orthologue from Drosophila melanogaster, Protein rigor mortis (RIG). The ��-propellers in GEMI5 bind small nuclear RNAs (snRNAs) playing a critical role in the assembly of the heptameric Sm protein core on snRNAs and the biogenesis of small nuclear ribonucleoproteins (snRNPs) [, ]. Apart of being a component of the survival motor neuron (SMN) complex, it is a nuclear receptor-interacting protein required for the response to steroid hormone ecdysone during larval development in which this domain acts as a specific protein-protein interaction domain [].GEMI5 is a component of the survival of motor neurons (SMN) complex, that binds small nuclear RNAs (snRNAs). The SMN complex assembles the heptameric Sm protein core on snRNAs playing a critical role in the biogenesis of small nuclear ribonucleoproteins (snRNPs) [, ]. GEMI5 is also implicated in translation control, and gene expression reprogramming []. GEMI5 from animals share a domain architecture consisting of two N-terminal ��-propellers followed by a TPR domain and a C-terminal RNA-binding domain.
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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 ��-�� superhelix and a long �� 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.
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Protein Domain
IPR057853 | Beta-prop_WDR11_2nd
Type: Domain
Description: This entry represents the second ��-propeller found in WD repeat-containing protein 11 (WDR11) from animals and similar eukaryotic proteins.Members of the WDR11 family share a domain architecture consisting of two ��-propellers followed by a TPR domain. WDR11 has been implicated in human developmental genetic disorders characterised by delayed puberty and infertility. WDR11 modulates the Hedgehog (Hh) signalling pathway and is essential for adequate ciliogenesis []. The ��-propellers in WDR11 are involved in protein-protein interaction. This are essential for proper interaction with EMX1, a homeodomain transcription factor involved in the development of olfactory neurons. Impaired pubertal development is suggested to result from a deficiency of productive WDR11 protein interaction []. WDR11 is also involved in vesicle traffic as it binds TBC1D23, a vesicle-golgin adaptor required for endosome-to-Golgi trafficking []. WDR11 is part of the WDR11 complex (consisting of WDR11, C17orf75 and FAM91A) that facilitates the tethering of AP-1-derived vesicles []. Mutations of the WDR11 gene have been linked to congenital hypogonadotropic hypogonadism (CHH) and Kallmann syndrome (KS), human developmental genetic disorders defined by delayed puberty and infertility [].
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Protein Domain
IPR057852 | Beta-prop_WDR11_1st
Type: Domain
Description: This entry represents the first ��-propeller found at the N-terminal end of WD repeat-containing protein 11 (WDR11) from animals and similar eukaryotic proteins.Members of the WDR11 family share a domain architecture consisting of two ��-propellers followed by a TPR domain. WDR11 has been implicated in human developmental genetic disorders characterised by delayed puberty and infertility. WDR11 modulates the Hedgehog (Hh) signalling pathway and is essential for adequate ciliogenesis []. The ��-propellers in WDR11 are involved in protein-protein interaction. This are essential for proper interaction with EMX1, a homeodomain transcription factor involved in the development of olfactory neurons. Impaired pubertal development is suggested to result from a deficiency of productive WDR11 protein interaction []. WDR11 is also involved in vesicle traffic as it binds TBC1D23, a vesicle-golgin adaptor required for endosome-to-Golgi trafficking []. WDR11 is part of the WDR11 complex (consisting of WDR11, C17orf75 and FAM91A) that facilitates the tethering of AP-1-derived vesicles []. Mutations of the WDR11 gene have been linked to congenital hypogonadotropic hypogonadism (CHH) and Kallmann syndrome (KS), human developmental genetic disorders defined by delayed puberty and infertility [].
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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
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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
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Publication
23857772 | J:201644
First Author: Chen Y
Year: 2013
Journal: J Cell Biol
Title: Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport.
Volume: 202
Issue: 2
Pages: 351-64
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Protein Coding Gene
MGI:1347085 | Cetn2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q3HNM7
Organism: Mus musculus/domesticus
Length: 579  
Fragment?: false
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Protein
Q5KU39
Organism: Mus musculus/domesticus
Length: 853  
Fragment?: false
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Protein
Q68FD5
Organism: Mus musculus/domesticus
Length: 1675  
Fragment?: false
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Protein
Q91W86
Organism: Mus musculus/domesticus
Length: 941  
Fragment?: false
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Publication
12748172 | J:84931
First Author: Ouyang T
Year: 2003
Journal: J Biol Chem
Title: Identification and characterization of a nuclear interacting partner of anaplastic lymphoma kinase (NIPA).
Volume: 278
Issue: 32
Pages: 30028-36
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Protein
Q5SXR6
Organism: Mus musculus/domesticus
Length: 1679  
Fragment?: false
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Protein
D3Z267
Organism: Mus musculus/domesticus
Length: 532  
Fragment?: false
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Protein
A0A0U1RQ40
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: true
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Protein
B2RT44
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
F7A814
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
Q3TDR2
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
Q3TS83
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
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Protein
Q8CEE5
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
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Protein
Q8R2Q7
Organism: Mus musculus/domesticus
Length: 869  
Fragment?: false
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Publication
18212739 | -
First Author: Wilson JB
Year: 2008
Journal: Oncogene
Title: FANCG promotes formation of a newly identified protein complex containing BRCA2, FANCD2 and XRCC3.
Volume: 27
Issue: 26
Pages: 3641-52
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Publication
9192069 | J:40791
First Author: Jia Z
Year: 1997
Journal: Biochem Cell Biol
Title: Protein phosphatases: structures and implications.
Volume: 75
Issue: 1
Pages: 17-26
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Publication
8896463 | -
First Author: Venema J
Year: 1996
Journal: EMBO J
Title: RRP5 is required for formation of both 18S and 5.8S rRNA in yeast.
Volume: 15
Issue: 20
Pages: 5701-14
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Publication
17654514 | -
First Author: Sweet T
Year: 2008
Journal: J Cell Physiol
Title: Evidence for involvement of NFBP in processing of ribosomal RNA.
Volume: 214
Issue: 2
Pages: 381-8
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Publication
23382868 | -
First Author: Missbach S
Year: 2013
Journal: PLoS One
Title: 40S ribosome biogenesis co-factors are essential for gametophyte and embryo development.
Volume: 8
Issue: 1
Pages: e54084
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Protein Domain
IPR012935 | NuBaID_N
Type: Domain
Description: This entry represents the N-terminal zinc finger domain (formerly ZnF-C3HC) of Zinc finger C3HC-type protein 1 (ZC3HC1, also known as Nuclear-interacting partner of ALK (NIPA)), pre-mRNA leakage protein 39 (Pml39), mRNA export factor Rsm1 and related eukaryotic proteins. Pml39 and Rsm1 are ZC3HC1 homologues from S. cerevisiae and S. pombe, respectively [, ]. This domain contains three highly conserved cysteine residues, two of which evolutionarily invariant, followed by an invariant pair of histidine and cysteine residues []. This zinc finger domain is often found repeated and the second repeat domain () can harbour a large insert located after the first three cysteine residues. Both domains coordinate zinc ion via two cysteines and the histidine-cysteine pair, in a mode similar to the presumably related BIR domains () [, ].Rsm1 protein (), containing this domain, is involved in mRNA export from the nucleus []. Recently, Pml39 was found to be required for the retention of unspliced mRNA []. ZC3HC1 was formerly described as Nuclear-interacting partner of ALK (NIPA), with a proposed role in cell cycle regulation as a component of an SCF complex specifically targeting cyclin B1 []. These findings were recently refuted []. In contrast, ZC3HC1 was identified as a nuclear envelope-associated protein residing at the NPC-attached nuclear basket (NB) of Xenopus laevis oocytes and cultured human cells []. It was shown that ZC3HC1 is a constituent structural component of the NB essential for recruitment, positioning and linkage of a subpopulation of the NB scaffold protein TPR [, ]. Furthermore, it was demonstrated that the Pml39 is a functional homologue of ZC3HC1 and, similarly, is capable of interconnecting Mlp1 polypeptide, the corresponding homologue of TPR in S. cerevisiae []. Both N- (this entry) and C-terminal []zinc finger domains were found to be essential for binding TPR/Mlp1 and therefore denoted as the nuclear basket-interaction domain (NuBaID), representing an evolutionary conserved integral functional unit [].Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead, they bind other metals, such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog); however, they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g., some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation,epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
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Protein Domain
IPR013909 | NuBaID_C
Type: Domain
Description: This entry represents the C-terminal zinc finger domain of Zinc finger C3HC-type protein 1 (ZC3HC1, also known as Nuclear-interacting partner of ALK (NIPA)) and mRNA export factor Rsm1 which is a homologue from S. pombe. These proteins contain a C3HC-type zinc finger () at the N terminus followed by the domain represented in this entry. These N- and C-terminal zinc finger domains are homologous and both are related to BIR domains () [, ]. Contrary to the nomenclature, one of the cysteines is evolutionarily not conserved and the zinc ion coordination occurs exclusively via four invariant amino acids (C2HC), in a mode similar to the BIR domains () [, ]. This domain can harbour a large insert (several hundred residues long) after the first two conserved cysteine residues, which is probably intrinsically disordered []. However, some homologues, like Pml39 from S. cerevisiae, harbour only a very short linker between the conserved two cysteines and the histidine-cysteine pair [].Rsm1protein (), containing this domain, is involved in mRNA export from the nucleus []. Recently, Pml39 was found to be required for the retention of unspliced mRNA []. ZC3HC1 was formerly described as Nuclear-interacting partner of ALK (NIPA), with a proposed role in cell cycle regulation as a component of an SCF complex specifically targeting cyclin B1 []. These findings were recently refuted []. In contrast, ZC3HC1 was identified as a nuclear envelope-associated protein residing at the NPC-attached nuclear basket (NB) of Xenopus laevis oocytes and cultured human cells []. It was shown that ZC3HC1 is a constituent structural component of the NB essential for recruitment, positioning and linkage of a subpopulation of the NB scaffold protein TPR [, ]. Furthermore, it was demonstrated that the Pml39 is a functional homologue of ZC3HC1 and, similarly, capable of interconnecting Mlp1 polypeptide, the corresponding homologue of TPR in S. cerevisiae []. Both N- []and C-terminal (this entry) zinc finger domains were found to be essential for binding TPR/Mlp1 and therefore denoted as the nuclear basket-interaction domain (NuBaID), representing an evolutionary conserved integral functional unit [].Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead, they bind other metals, such as iron, or no metal at all. For example, some family members form salt bridgesto stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog); however, they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g., some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
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Protein
Q9R0Q7
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein
Q80YV2
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q8K284
Organism: Mus musculus/domesticus
Length: 2101  
Fragment?: false
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Protein
Q9D9A7
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: false
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Protein
Q6PIP5
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: false
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Protein
D3Z7C6
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
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Protein
Q3TJG6
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein
E0CYQ2
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: false
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Protein
Q3TI64
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q3UTP3
Organism: Mus musculus/domesticus
Length: 1286  
Fragment?: false
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Protein
Q8C806
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
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Protein
Q8C9B6
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
Q9CRH1
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: false
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Protein
A0A0U1RPD8
Organism: Mus musculus/domesticus
Length: 2005  
Fragment?: false
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Protein
A0A2K6EDK3
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
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Protein
A2A4P5
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
B2RUL0
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: false
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Protein
D3Z3D0
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
H3BKM2
Organism: Mus musculus/domesticus
Length: 459  
Fragment?: false
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Protein
Q3UHL0
Organism: Mus musculus/domesticus
Length: 2101  
Fragment?: false
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Protein
Q3UPZ9
Organism: Mus musculus/domesticus
Length: 1233  
Fragment?: true
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Protein
Q3UQ70
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: true
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Protein
Q3UY03
Organism: Mus musculus/domesticus
Length: 634  
Fragment?: true
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Protein
Q9CRG3
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
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Publication
15357289 | -
First Author: Yoon JH
Year: 2004
Journal: J Microbiol
Title: Schizosaccharomyces pombe rsm1 genetically interacts with spmex67, which is involved in mRNA export.
Volume: 42
Issue: 1
Pages: 32-6
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Publication
16009132 | -
First Author: Bassermann F
Year: 2005
Journal: Cell
Title: NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry.
Volume: 122
Issue: 1
Pages: 45-57
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Publication
34440706 | -
 
First Author: Gunkel P
Year: 2021
Journal: Cells
Title: ZC3HC1 Is a Novel Inherent Component of the Nuclear Basket, Resident in a State of Reciprocal Dependence with TPR.
Volume: 10
Issue: 8
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Publication
36857168 | -
First Author: Gunkel P
Year: 2023
Journal: Mol Biol Cell
Title: An evolutionarily conserved bimodular domain anchors ZC3HC1 and its yeast homologue Pml39p to the nuclear basket.
Volume: 34
Issue: 5
Pages: ar40
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Publication
36271106 | -
First Author: Hashimoto H
Year: 2022
Journal: Sci Rep
Title: Structure of the pre-mRNA leakage 39-kDa protein reveals a single domain of integrated zf-C3HC and Rsm1 modules.
Volume: 12
Issue: 1
Pages: 17691
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Publication
16162818 | -
First Author: Palancade B
Year: 2005
Journal: Mol Biol Cell
Title: Pml39, a novel protein of the nuclear periphery required for nuclear retention of improper messenger ribonucleoparticles.
Volume: 16
Issue: 11
Pages: 5258-68
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Publication
15316005 | -
First Author: Ye JZ
Year: 2004
Journal: J Biol Chem
Title: TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres.
Volume: 279
Issue: 45
Pages: 47264-71
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Publication
23636326 | -
First Author: Yang H
Year: 2013
Journal: Nature
Title: mTOR kinase structure, mechanism and regulation.
Volume: 497
Issue: 7448
Pages: 217-23
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Publication
11833360 | -
 
First Author: Heizmann CW
Year: 2002
Journal: Methods Mol Biol
Title: The multifunctional S100 protein family.
Volume: 172
Pages: 69-80
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Publication
25271326 | -
First Author: Puga MI
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: SPX1 is a phosphate-dependent inhibitor of Phosphate Starvation Response 1 in Arabidopsis.
Volume: 111
Issue: 41
Pages: 14947-52
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Publication
14621295 | J:86686
First Author: Okazaki N
Year: 2003
Journal: DNA Res
Title: Prediction of the coding sequences of mouse homologues of KIAA gene: III. the complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.
Volume: 10
Issue: 4
Pages: 167-80
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Protein
Q9JKK8
Organism: Mus musculus/domesticus
Length: 2635  
Fragment?: false
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Protein
A0A1L1SSL9
Organism: Mus musculus/domesticus
Length: 2641  
Fragment?: false
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Protein
E9QPK4
Organism: Mus musculus/domesticus
Length: 2635  
Fragment?: false
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Publication
17055430 | J:116097
First Author: Roux I
Year: 2006
Journal: Cell
Title: Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse.
Volume: 127
Issue: 2
Pages: 277-89
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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
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Publication
29311115 | J:317069
First Author: L?pez-Dom?nech G
Year: 2018
Journal: EMBO J
Title: Miro proteins coordinate microtubule- and actin-dependent mitochondrial transport and distribution.
Volume: 37
Issue: 3
Pages: 321-336
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Protein
P70371
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
E9QM06
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
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Protein
Q3V252
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: false
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Protein
Q7TSK8
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
A0A0A0MQ74
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: false
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Protein
O35144
Organism: Mus musculus/domesticus
Length: 541  
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.

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© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
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