|  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 501 to 600 out of 1932 for Tat

<< First    < Previous  |  Next >    Last >>
0.033s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Allele
Gabrr1<em1Rah> | MGI:5907202
 
Name: gamma-aminobutyric acid type A receptor subunit rho 1; endonuclease-mediated mutation 1, R Adron Harris
Allele Type: Endonuclease-mediated
•
•
•
•
•
Allele
Col1a1<tm1(RHOA*Y42C)Abass> | MGI:6393676
Name: collagen, type I, alpha 1; targeted mutation 1, Adam Bass
Allele Type: Targeted
Attribute String: Conditional ready, Humanized sequence, Inserted expressed sequence
•
•
•
•
•
GO Term
GO:0015627 | type II protein secretion system complex
•
•
•
•
•
Protein Coding Gene
MGI:1926953 | Ctdp1
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Domain
IPR006311 | TAT_signal
Type: Conserved_site
Description: The twin-arginine translocation (Tat) pathway serves the role of transporting folded proteins across energy-transducing membranes []. Homologues of the genes that encode the transport apparatus occur in archaea, bacteria, chloroplasts, and plant mitochondria []. In bacteria, the Tat pathway catalyses the export of proteins from the cytoplasm across the inner/cytoplasmic membrane. In chloroplasts, the Tat components are found in the thylakoid membrane and direct the import of proteins from the stroma. The Tat pathway acts separately from the general secretory (Sec) pathway, which transports proteins in an unfolded state [].It is generally accepted that the primary role of the Tat system is to translocate fully folded proteins across membranes. An example of proteins that need to be exported in their 3D conformation are redox proteins that have acquired complex multi-atom cofactors in the bacterial cytoplasm (or the chloroplast stroma or mitochondrial matrix). They include hydrogenases, formate dehydrogenases, nitrate reductases, trimethylamine N-oxide (TMAO) reductases and dimethyl sulphoxide (DMSO) reductases [, ]. The Tat system can also export whole heteroligomeric complexes in which some proteins have no Tat signal. This is the case of the DMSO reductase or formate dehydrogenase complexes. But there are also other cases where the physiological rationale for targeting a protein to the Tat signal is less obvious. Indeed, there are examples of homologous proteins that are in some cases targeted to the Tat pathway and in other cases to the Sec apparatus. Some examples are: copper nitrite reductases, flavin domains of flavocytochrome c and N-acetylmuramoyl-L-alanine amidases [].In halophilic archaea such as Halobacterium almost all secreted proteins appear to be Tat targeted. It has been proposed to be a response to the difficulties these organisms would otherwise face in successfully folding proteins extracellularly at high ionic strength [].The Tat signal peptide consists of three motifs: the positively charged N-terminal motif, the hydrophobic region and the C-terminal region that generally ends with a consensus short motif (A-x-A) specifying cleavage by signal peptidase. Sequence analysis revealed that signal peptides capable of targeting the Tat protein contain the consensus sequence [ST]-R-R-x-F-L-K. The nearly invariant twin-arginine gave rise to the pathway's name. In addition the h-region of Tat signal peptides is typically less hydrophobic than that of Sec-specific signal peptides [, ].This entry represents the Tat signal, from the methionine to the A-x-A short motif.
•
•
•
•
•
Protein Domain
IPR001831 | IV_Tat
Type: Family
Description: Like other lentiviruses, Human immunodeficiency virus 1 (HIV-1) encodes a trans-activating regulatory protein (Tat), which is essential for efficient transcription of the viral genome [, ]. Tat acts by binding to an RNA stem-loop structure, the trans-activating response element (TAR), found at the 5' ends of nascent HIV-1 transcripts. In binding to TAR, Tat alters the properties of the transcription complex, recruits a positive transcription elongation complex (P-TEFb) and hence increases the production of full-length viral RNA []. Tat protein also associates with RNA polymerase II complexes during early transcription elongation afterthe promoter clearance and before the synthesis of full-length TAR RNA transcript. This interaction of Tat with RNA polymerase II elongationcomplexes is P-TEFb-independent. There are two Tat binding sites on each transcription elongation complex; one is located onTAR RNA and the other one on RNA polymerase II near the exit site for nascent mRNA transcripts which suggests that two Tat molecules areinvolved in performing various functions during a single round of HIV-1 mRNA synthesis []. The minimum Tat sequence that can mediate specific TAR binding in vitrohas been mapped to a basic domain of 10 amino acids, comprising mostly Arg and Lys residues. Regulatory activity, however, also requires the 47 N-terminal residues, which interact with components of the transcription complex and function as a transcriptional activation domain [, , ].
•
•
•
•
•
Protein Domain
IPR019546 | TAT_signal_bac_arc
Type: Conserved_site
Description: The twin-arginine translocation (Tat) pathway serves the role of transporting folded proteins across energy-transducing membranes []. Homologues of the genes that encode the transport apparatus occur in archaea, bacteria, chloroplasts, and plant mitochondria []. In bacteria, the Tat pathway catalyses the export of proteins from the cytoplasm across the inner/cytoplasmic membrane. In chloroplasts, the Tat components are found in the thylakoid membrane and direct the import of proteins from the stroma. The Tat pathway acts separately from the general secretory (Sec) pathway, which transports proteins in an unfolded state [].It is generally accepted that the primary role of the Tat system is to translocate fully folded proteins across membranes. An example of proteins that need to be exported in their 3D conformation are redox proteins that have acquired complex multi-atom cofactors in the bacterial cytoplasm (or the chloroplast stroma or mitochondrial matrix). They include hydrogenases, formate dehydrogenases, nitrate reductases, trimethylamine N-oxide (TMAO) reductases and dimethyl sulphoxide (DMSO) reductases [, ]. The Tat system can also export whole heteroligomeric complexes in which some proteins have no Tat signal. This is the case of the DMSO reductase or formate dehydrogenase complexes. But there are also other cases where the physiological rationale for targeting a protein to the Tat signal is less obvious. Indeed, there are examples of homologous proteins that are in some cases targeted to the Tat pathway and in other cases to the Sec apparatus. Some examples are: copper nitrite reductases, flavin domains of flavocytochrome c and N-acetylmuramoyl-L-alanine amidases [].In halophilic archaea such as Halobacterium almost all secreted proteins appear to be Tat targeted. It has been proposed to be a response to the difficulties these organisms would otherwise face in successfully folding proteins extracellularly at high ionic strength [].The Tat signal peptide consists of three motifs: the positively charged N-terminal motif, the hydrophobic region and the C-terminal region that generally ends with a consensus short motif (A-x-A) specifying cleavage by signal peptidase. Sequence analysis revealed that signal peptides capable of targeting the Tat protein contain the consensus sequence [ST]-R-R-x-F-L-K. The nearly invariant twin-arginine gave rise to the pathway's name. In addition the h-region of Tat signal peptides is typically less hydrophobic than that of Sec-specific signal peptides [, ].
•
•
•
•
•
Protein Domain
IPR030912 | RK_trnsloc_Pase
Type: Family
Description: The Sec-independent protein export system TAT, or twin-arginine translocation, is composed of TatA, TatB, and TatC. The TAT system is unusual in Leptospira, with Lys replacing Arg in the second position of the twin-Arg motif. This protein, restricted to Leptospira and showing distant homology to the phosphoserine phosphatases RsbU and SpoIIE, is always encoded immediately downstream of the tatC gene and appears to be part of the variant TAT system. It lacks a TAT signal itself, and so is more likely to be part of the Sec-independent translocation machinery than to be a substrate. The suggested symbol is rktP, for RK-Translocation Phosphatase.
•
•
•
•
•
Allele
Tg(Camk2a-Fyn-531)1Nko | MGI:2446470
Name: transgene insertion 1, Nobuhiko Kojima
Allele Type: Transgenic
Attribute String: Constitutively active, Inserted expressed sequence
•
•
•
•
•
Allele
Flt3<tm2.1Dosm> | MGI:5565506
Name: FMS-like tyrosine kinase 3; targeted mutation 2.1, Donald Small
Allele Type: Targeted
Attribute String: Constitutively active
•
•
•
•
•
Allele
Flt3<tm2Dosm> | MGI:5565509
Name: FMS-like tyrosine kinase 3; targeted mutation 2, Donald Small
Allele Type: Targeted
Attribute String: Conditional ready, Constitutively active
•
•
•
•
•
Strain
MGI:5907203 | C57BL/6J-Gabrr1<em1Rah>/J
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
•
•
•
•
•
Allele
App<em1Adiuj> | MGI:6164022
Name: amyloid beta precursor protein; endonuclease-mediated mutation 1, MODEL-AD Center
Allele Type: Endonuclease-mediated
Attribute String: Humanized sequence
•
•
•
•
•
Strain
MGI:6393677 | B6.Cg-Col1a1<tm1(RHOA*Y42C)Abass>/J
Attribute String: mutant strain, congenic, targeted mutation
•
•
•
•
•
Allele
Tnfaip3<em1Mpa> | MGI:7484798
 
Name: tumor necrosis factor, alpha-induced protein 3; endonuclease-mediated mutation 1, Manolis Pasparakis
Allele Type: Endonuclease-mediated
•
•
•
•
•
Publication
16322447 | -
First Author: Wickner W
Year: 2005
Journal: Science
Title: Protein translocation across biological membranes.
Volume: 310
Issue: 5753
Pages: 1452-6
•
•
•
•
•
Publication
12029389 | -
First Author: Yen MR
Year: 2002
Journal: Arch Microbiol
Title: Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system.
Volume: 177
Issue: 6
Pages: 441-50
•
•
•
•
•
Publication
16092521 | -
First Author: Stephenson K
Year: 2005
Journal: Mol Membr Biol
Title: Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).
Volume: 22
Issue: 1-2
Pages: 17-28
•
•
•
•
•
Publication
16756481 | -
 
First Author: Lee PA
Year: 2006
Journal: Annu Rev Microbiol
Title: The bacterial twin-arginine translocation pathway.
Volume: 60
Pages: 373-95
•
•
•
•
•
Publication
15546663 | -
First Author: Robinson C
Year: 2004
Journal: Biochim Biophys Acta
Title: Tat-dependent protein targeting in prokaryotes and chloroplasts.
Volume: 1694
Issue: 1-3
Pages: 135-47
•
•
•
•
•
Publication
15802249 | -
First Author: Berks BC
Year: 2005
Journal: Curr Opin Microbiol
Title: Protein targeting by the bacterial twin-arginine translocation (Tat) pathway.
Volume: 8
Issue: 2
Pages: 174-81
•
•
•
•
•
Publication
12427925 | -
First Author: Bolhuis A
Year: 2002
Journal: Microbiology
Title: Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?
Volume: 148
Issue: Pt 11
Pages: 3335-46
•
•
•
•
•
Protein Domain
IPR006376 | Cu-R_CopA
Type: Family
Description: These sequences represent the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechanism of resistance by packaging and export.
•
•
•
•
•
Publication
25114049 | -
First Author: Chen YC
Year: 2014
Journal: Nucleic Acids Res
Title: Structure and function of TatD exonuclease in DNA repair.
Volume: 42
Issue: 16
Pages: 10776-85
•
•
•
•
•
Protein Coding Gene
MGI:1328366 | Smarcb1
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Publication
31298381 | -
First Author: Yu XY
Year: 2019
Journal: Eur Rev Med Pharmacol Sci
Title: TATDN1 promotes the development and progression of breast cancer by targeting microRNA-140-3p.
Volume: 23
Issue: 12
Pages: 5293-5300
•
•
•
•
•
Publication
23187801 | -
First Author: Yang H
Year: 2012
Journal: Cell Cycle
Title: The DNase domain-containing protein TATDN1 plays an important role in chromosomal segregation and cell cycle progression during zebrafish eye development.
Volume: 11
Issue: 24
Pages: 4626-32
•
•
•
•
•
Publication
33412752 | -
First Author: Seo D
Year: 2020
Journal: Genomics Inform
Title: The ceRNA network of lncRNA and miRNA in lung cancer.
Volume: 18
Issue: 4
Pages: e36
•
•
•
•
•
Publication
33192097 | -
 
First Author: Long Q
Year: 2020
Journal: Cancer Manag Res
Title: Overexpression of lncRNA TATDN1 Promotes Cancer Cell Proliferation in Triple Negative Breast Cancer by Regulating miR-26b Methylation.
Volume: 12
Pages: 11403-11410
•
•
•
•
•
Protein Domain
IPR001130 | TatD-like
Type: Family
Description: This protein family includes 3'-5' ssDNA/RNA exonuclease TatD and many uncharacterised deoxyribonucleases and metal-dependent hydrolases. The family is related to a large superfamily of metalloenzymes []. TatD has been shown to be a 3'-5' exonuclease that processes single-stranded DNA in DNA repair [, ].In E. coli TatD, which adopts a TIM-barrel fold, is encoded by a operon that encodes Tat proteins, including TatA, TatB, and TatC, for protein transport via the Tat (Twin-Arginine Translocation) pathway. However, TatD is not involved in the protein export in the Tat pathway [].Deoxyribonuclease TATDN1 from Danio rerio (Zebrafish) catalyses (in vitro) the decatenation of kinetoplast DNA producing linear DNA molecules. It is involved in chromosomal segregation and cell cycle progression during eye development []. TATDN1 has been related to several types of cancer [, , ].
•
•
•
•
•
Protein Coding Gene
MGI:87904 | Actb
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Publication
10747959 | -
First Author: Wexler M
Year: 2000
Journal: J Biol Chem
Title: TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export.
Volume: 275
Issue: 22
Pages: 16717-22
•
•
•
•
•
Publication
21115974 | J:170371
First Author: Fu J
Year: 2011
Journal: Blood
Title: The tumor suppressor gene WWOX links the canonical and noncanonical NF-κB pathways in HTLV-I Tax-mediated tumorigenesis.
Volume: 117
Issue: 5
Pages: 1652-61
•
•
•
•
•
Strain
MGI:3693370 | B6.Cg-Tg(Camk2a-Fyn-531)1Nko
Attribute String: congenic, mutant strain, transgenic
•
•
•
•
•
Strain
MGI:3761391 | B6.Cg-Tg(Camk2a-Fyn-531)1Nko/NkoRbrc
Attribute String: mutant strain, transgenic
•
•
•
•
•
Publication
12399115 | J:79980
First Author: Stork O
Year: 2002
Journal: Brain Res Mol Brain Res
Title: Resistance to alcohol withdrawal-induced behaviour in Fyn transgenic mice and its reversal by ifenprodil.
Volume: 105
Issue: 1-2
Pages: 126-35
•
•
•
•
•
Strain
MGI:5565710 | B6.129(C)-Flt3<tm2.1Dosm>
Attribute String: congenic, mutant strain, targeted mutation
•
•
•
•
•
Strain
MGI:6369609 | B6(SJL)-Apoe<em2(APOE*)Adiuj> App<em1Adiuj>/J
Attribute String: endonuclease-mediated mutation, mutant strain
•
•
•
•
•
Strain
MGI:6441012 | B6.Cg-App<em1Adiuj>/J
Attribute String: congenic, endonuclease-mediated mutation, mutant strain
•
•
•
•
•
Allele
Fgfr2<tm5.1Sor> | MGI:6477576
 
Name: fibroblast growth factor receptor 2; targeted mutation 5.1, Philippe Soriano
Allele Type: Targeted
•
•
•
•
•
Allele
Klhl3<em1Slin> | MGI:7506979
Name: kelch-like 3; endonuclease-mediated mutation 1, Shih-Hua Lin
Allele Type: Endonuclease-mediated
Attribute String: Humanized sequence
•
•
•
•
•
Genotype
Genotype
Symbol: Tg(Camk2a-Fyn-531)1Nko/?
Background: involves: 129S7/SvEvBrd * C57BL/6 * CBA
Zygosity: ot
Has Mutant Allele: true
•
•
•
•
•
Genotype
Genotype
Symbol: Tg(Camk2a-Fyn-531)1Nko/?
Background: B6.Cg-Tg(Camk2a-Fyn-531)1Nko
Zygosity: ot
Has Mutant Allele: true
•
•
•
•
•
Genotype
Genotype
Symbol: Flt3/Flt3<+>
Background: B6.129(C)-Flt3
Zygosity: ht
Has Mutant Allele: true
•
•
•
•
•
Protein Domain
IPR036560 | MADH/AADH_L_sf
Type: Homologous_superfamily
Description: Aralkylamine dehydrogenase light chain and methylamine dehydrogenase light chain are aromatic amine dehydrogenases that form heterotetramers with their respective heavy chains, and catalyse the oxidative deamination of amines to their corresponding aldehydes.The light subunit possesses an apparent Tat signal peptide. This subunit is dominated by beta structure [].
•
•
•
•
•
Protein Domain
IPR022507 | Metallophosphoesterase_RPA4764
Type: Family
Description: This entry describes a small collection of probable metallophosphoresterases, related to . Members of this protein family usually have a Sec-independent TAT (twin-arginine translocation) signal sequence, N-terminal to the region modeled by this HMM. This model and divide a narrow clade of -related enzymes.
•
•
•
•
•
Protein Domain
IPR022506 | Metallophosphoesterase_PPA1498
Type: Family
Description: This entry describes a small collection of probable metallophosphoresterases, related to but with long inserts separating some of the shared motifs such that the homology is apparent only through multiple sequence alignment. Members of this protein family, in general, have a Sec-independent TAT (twin-arginine translocation) signal sequence, N-terminal to the region modeled by this HMM. Members include YP_056203.1 from Propionibacterium acnes KPA171202.
•
•
•
•
•
Protein Domain
IPR040461 | Hop2
Type: Family
Description: Homologous-pairing protein 2 (Hop2) is required for proper homologous pairing and efficient cross-over and intragenic recombination during meiosis [, , ].The mammalian HOP2 homologue, TBPIP, was first identified as a factor interacting with TBP-1, which binds to the human immunodeficiency virus, type 1 Tat protein []. Later, TBPIP was found to be an activator that specifically stimulates the homologous pairing catalyzed by DMC1 [].
•
•
•
•
•
Protein Domain
IPR023644 | NO_Rdtase
Type: Family
Description: Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide. NosZ, one of the members of this family, is the nitrous-oxide reductase structural protein, with an N-terminal twin-arginine translocation (TAT) signal sequence. The TAT system replaces the Sec system for export of proteins with bound cofactor [].
•
•
•
•
•
Protein Coding Gene
MGI:1270129 | Dnaja1
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Publication
36109497 | J:328990
First Author: Patel T
Year: 2022
Journal: Nat Commun
Title: Transcriptional dynamics of murine motor neuron maturation in vivo and in vitro.
Volume: 13
Issue: 1
Pages: 5427
•
•
•
•
•
Publication
15192114 | J:92384
First Author: Enomoto R
Year: 2004
Journal: J Biol Chem
Title: Positive role of the mammalian TBPIP/HOP2 protein in DMC1-mediated homologous pairing.
Volume: 279
Issue: 34
Pages: 35263-72
•
•
•
•
•
Publication
9708739 | -
First Author: Leu JY
Year: 1998
Journal: Cell
Title: The meiosis-specific Hop2 protein of S. cerevisiae ensures synapsis between homologous chromosomes.
Volume: 94
Issue: 3
Pages: 375-86
•
•
•
•
•
Publication
11447128 | -
First Author: Nabeshima K
Year: 2001
Journal: EMBO J
Title: A novel meiosis-specific protein of fission yeast, Meu13p, promotes homologous pairing independently of homologous recombination.
Volume: 20
Issue: 14
Pages: 3871-81
•
•
•
•
•
Protein Domain
IPR002033 | TatC
Type: Family
Description: Proteins encoded by the mttABC operon (formerly yigTUW), mediate a novel Sec-independent membrane targeting and translocation system in Escherichia coli that interacts with cofactor-containing redox proteins having a S/TRRXFLK "twin arginine"leader motif. This family contains the E. coli mttB gene (TATC) [].A functional Tat system or Delta pH-dependent pathway requires three integral membrane proteins: TatA/Tha4, TatB/Hcf106 and TatC/cpTatC. The TatC protein is essential for the function of both pathways. It might be involved in twin-arginine signal peptide recognition, protein translocation and proton translocation. Sequence analysis predicts that TatC contains six transmembrane helices (TMHs), and experimental data confirmed that N and C termini of TatC or cpTatC are exposed to the cytoplasmic or stromal face of the membrane. The cytoplasmic N terminus and the first cytoplasmic loop region of the E. coli TatC protein are essential for protein export. At least two TatC molecules co-exist within each Tat translocon [, ].
•
•
•
•
•
Protein Domain
IPR019820 | Sec-indep_translocase_CS
Type: Conserved_site
Description: Proteins encoded by the mttABC operon (formerly yigTUW), mediate a novel Sec-independent membrane targeting and translocation system in Escherichia coli that interacts with cofactor-containing redox proteins having a S/TRRXFLK "twin arginine"leader motif. This family contains the E. coli mttB gene (TATC) [].A functional Tat system or Delta pH-dependent pathway requires three integral membrane proteins: TatA/Tha4, TatB/Hcf106 and TatC/cpTatC. The TatC protein is essential for the function of both pathways. It might be involved in twin-arginine signal peptide recognition, protein translocation and proton translocation. Sequence analysis predicts that TatC contains six transmembrane helices (TMHs), and experimental data confirmed that N and C termini of TatC or cpTatC are exposed to the cytoplasmic or stromal face of the membrane. The cytoplasmic N terminus and the first cytoplasmic loop region of the E. coli TatC protein are essential for protein export. At least two TatC molecules co-exist within each Tat translocon [, ].This entry represents a conserved site from the central section of these proteins.
•
•
•
•
•
Publication
20634377 | J:165866
First Author: Swaims AY
Year: 2010
Journal: Blood
Title: Immune activation induces immortalization of HTLV-1 LTR-Tax transgenic CD4+ T cells.
Volume: 116
Issue: 16
Pages: 2994-3003
•
•
•
•
•
Publication
38722890 | J:348293
First Author: Song X
Year: 2024
Journal: PLoS One
Title: NF-κB1 deficiency promotes macrophage-derived adrenal tumors but decreases neurofibromas in HTLV-I LTR-Tax transgenic mice.
Volume: 19
Issue: 5
Pages: e0303138
•
•
•
•
•
Publication
28623169 | J:242963
 
First Author: Blednov YA
Year: 2017
Journal: Neuropharmacology
Title: Mutation of the inhibitory ethanol site in GABAA ρ1 receptors promotes tolerance to ethanol-induced motor incoordination.
Volume: 123
Pages: 201-209
•
•
•
•
•
Allele
Tg(HIV)26Aln | MGI:3771187
Name: transgene insertion 26, Abner Louis Notkins
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•
Allele
Tg(SMN1-SMN2*)16Cll | MGI:5490785
Name: transgene insertion 16, Christian L Lorson
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
•
•
•
•
•
Strain
MGI:6477577 | 129S4/SvJae-Fgfr2<tm5.1Sor>/Mmjax
Attribute String: coisogenic, mutant strain, targeted mutation
•
•
•
•
•
Publication
35621709 | J:335611
First Author: Lin CM
Year: 2022
Journal: FASEB J
Title: Generation and analysis of pseudohypoaldosteronism type II knock-in mice caused by a nonsense KLHL3 mutation in the Kelch domain.
Volume: 36
Issue: 6
Pages: e22363
•
•
•
•
•
Allele
Cd79b<tm1.1Rein> | MGI:7666002
Name: CD79B antigen; targeted mutation 1.1, H Christian Reinhardt
Allele Type: Targeted
Attribute String: Conditional ready, Humanized sequence
•
•
•
•
•
Genotype
Genotype
Symbol: Fyn/Fyn<+> Tg(Camk2a-Fyn-531)1Nko/?
Background: involves: 129S7/SvEvBrd * C57BL/6 * CBA
Zygosity: cx
Has Mutant Allele: true
•
•
•
•
•
Publication
9546395 | -
First Author: Weiner JH
Year: 1998
Journal: Cell
Title: A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins.
Volume: 93
Issue: 1
Pages: 93-101
•
•
•
•
•
Publication
12163163 | -
First Author: Gouffi K
Year: 2002
Journal: FEBS Lett
Title: Topology determination and functional analysis of the Escherichia coli TatC protein.
Volume: 525
Issue: 1-3
Pages: 65-70
•
•
•
•
•
Publication
9813127 | -
First Author: Dos Santos JP
Year: 1998
Journal: J Mol Biol
Title: Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species.
Volume: 284
Issue: 2
Pages: 421-33
•
•
•
•
•
Protein Domain
IPR011887 | TorA
Type: Family
Description: This very narrowly defined family represents trimethylamine-N-oxide (TMAO) reductase TorA. TorA typically is located in the periplasm, has a Tat (twin-arginine translocation)-dependent signal sequence, and is encoded in a torCAD operon. TorA reduces TMAO into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions [, ]. The torC gene, located upstream from torA encodes a pentahemic c-type cytochrome, likely to be involved in electron transfer to the TorA terminal reductase [].
•
•
•
•
•
Protein Domain
IPR010181 | CGCAxxGCC_motif
Type: Family
Description: This entry represents a putative redox-active protein of about 140 residues, with four perfectly conserved Cys residues. It includes a CGAXXG motif. Most members are found within one or two loci of transporter or oxidoreductase genes. A member from Geobacter sulfurreducens, located in a molybdenum transporter operon, has a TAT (twin-arginine translocation) signal sequence for Sec-independent transport across theplasma membrane, a hallmark of bound prosthetic groups such as FeS clusters.
•
•
•
•
•
Protein Domain
IPR010776 | Hop2_WH_dom
Type: Domain
Description: Homologous-pairing protein 2 (Hop2) is required for proper homologous pairing and efficient cross-over and intragenic recombination during meiosis [, , ].The mammalian HOP2 homologue, TBPIP, was first identified as a factor interacting with TBP-1, which binds to the human immunodeficiency virus, type 1 Tat protein []. Later, TBPIP was found to be an activator that specifically stimulates the homologous pairing catalyzed by DMC1 []. This entry represents the winged helix domain found in Hop2.
•
•
•
•
•
Protein Domain
IPR011715 | Tyr_aminoTrfase_ubiquitination
Type: Domain
Description: This region contains a probable site of ubiquitination that ensures rapid degradation of tyrosine aminotransferase in rats. The half life of the enzyme in vivois about 2-4 hours. The enzyme contains at least 2 phosphorylation sites including CAPK at Ser29 and, at the other end of the protein, a casein kinase II site at S*QEECDK. This region of TAT is probably primarily related to regulatory events. Most other transaminases are much more stable and are not phosphorylated.
•
•
•
•
•
Protein
Q3U1C6
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
•
•
•
•
•
Protein
Q6P8M1
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
•
•
•
•
•
Protein
D3Z0V5
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
•
•
•
•
•
Protein
F8VQE6
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
•
•
•
•
•
Protein
A0A0R4J1E8
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
•
•
•
•
•
Protein
A0A571BEN9
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: true
•
•
•
•
•
Protein
F7CWI0
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
•
•
•
•
•
Protein
Q3U179
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
•
•
•
•
•
Protein
D3YXH9
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: false
•
•
•
•
•
Protein
F6W3K2
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
•
•
•
•
•
Protein
Q571H2
Organism: Mus musculus/domesticus
Length: 796  
Fragment?: true
•
•
•
•
•
Protein
Q3UJK8
Organism: Mus musculus/domesticus
Length: 735  
Fragment?: true
•
•
•
•
•
Protein
E9QL22
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
•
•
•
•
•
Protein
B7ZNL9
Organism: Mus musculus/domesticus
Length: 783  
Fragment?: false
•
•
•
•
•
Protein Domain
IPR018448 | TatB
Type: Family
Description: Translocation of proteins across the two membranes of Gram-negative bacteriacan be carried out via a number of routes. Most proteins marked for export carry a secretion signal at their N terminus, and are secreted by the general secretory pathway. The signal peptide is cleaved as they pass through the outer membrane. Other secretion systems include the type III system found in a select group of Gram-negative plant and animal pathogens, and the CagA system of Helicobacter pylori [].In some bacterial species, however, there exists a system that operates independently of the Sec pathway []. It selectively translocates periplasmic-bound molecules that are synthesised with, or are in close association with, "partner"proteins bearing an (S/T)RRXFLK twin arginine motif at the N terminus. The pathway is therefore termed the Twin-Arginine Translocation or TAT system. Surprisingly, the four components that make up the TAT system are structurally and mechanistically related to a pH-dependent import system in plant chloroplast thylakoid membranes []. Thegene products responsible for the Sec-independent pathway are called TatA,TatB, TatC and TatE.This entry represents Sec-independent protein translocase protein TatB (TatB) and similar proteins predominantly found in Proteobacteria. TatB is essential for the secretion of large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. It may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation []. It may form a circular arrangement with TatC [].
•
•
•
•
•
Publication
17891141 | J:152657
First Author: Martindill DM
Year: 2007
Journal: Nat Cell Biol
Title: Nucleolar release of Hand1 acts as a molecular switch to determine cell fate.
Volume: 9
Issue: 10
Pages: 1131-41
•
•
•
•
•
Publication
15207726 | J:169910
First Author: Mizugishi K
Year: 2004
Journal: Biochem Biophys Res Commun
Title: Myogenic repressor I-mfa interferes with the function of Zic family proteins.
Volume: 320
Issue: 1
Pages: 233-40
•
•
•
•
•
Publication
9649434 | -
First Author: Sargent F
Year: 1998
Journal: EMBO J
Title: Overlapping functions of components of a bacterial Sec-independent protein export pathway.
Volume: 17
Issue: 13
Pages: 3640-50
•
•
•
•
•
Publication
16280085 | J:103338
 
First Author: Stefan M
Year: 2005
Journal: BMC Genomics
Title: Genetic mapping of putative Chrna7 and Luzp2 neuronal transcriptional enhancers due to impact of a transgene-insertion and 6.8 Mb deletion in a mouse model of Prader-Willi and Angelman syndromes.
Volume: 6
Pages: 157
•
•
•
•
•
Publication
19381020 | J:149674
First Author: Papeta N
Year: 2009
Journal: J Clin Invest
Title: Susceptibility loci for murine HIV-associated nephropathy encode trans-regulators of podocyte gene expression.
Volume: 119
Issue: 5
Pages: 1178-88
•
•
•
•
•
Allele
Tg(CD4-HIV)F21380Pjo | MGI:2388572
Name: transgene insertion F21380, Paul Jolicoeur
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•
Allele
Tg(CD4-HIV)F21388Pjo | MGI:2388573
Name: transgene insertion F21388, Paul Jolicoeur
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•
Allele
Tg(CD4-HIV)F26985Pjo | MGI:2388585
Name: transgene insertion F26985, Paul Jolicoeur
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•
Allele
Tg(CD4-HIV)F27011Pjo | MGI:2388587
Name: transgene insertion F27011, Paul Jolicoeur
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•
Allele
Tg(CD4-HIV)F27367Pjo | MGI:2388588
Name: transgene insertion F27367, Paul Jolicoeur
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•
Allele
Tg(CD4-HIV)F27372Pjo | MGI:2388590
Name: transgene insertion F27372, Paul Jolicoeur
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•
Allele
Tg(CD4-HIV)F21407Pjo | MGI:2388592
Name: transgene insertion F21407, Paul Jolicoeur
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•
Allele
Tg(CD4-HIV)F26990Pjo | MGI:2450582
Name: transgene insertion F26990, Paul Jolicoeur
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
•
•
•
•
•




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