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Search results 401 to 500 out of 754 for Trio

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Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Protein
A0A1L1STP0
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Protein
A2AIT6
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: false
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Protein
Q8QZU5
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: true
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Protein
Q499J1
Organism: Mus musculus/domesticus
Length: 282  
Fragment?: true
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Protein
Q3U0U1
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
E9QME1
Organism: Mus musculus/domesticus
Length: 356  
Fragment?: false
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Protein
A8Y5P0
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: true
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Protein
Q3TTX3
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: true
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Protein
F8QPD5
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Publication
8349655 | -
First Author: Sato Y
Year: 1993
Journal: J Biol Chem
Title: Primary structure of alpha-tocopherol transfer protein from rat liver. Homology with cellular retinaldehyde-binding protein.
Volume: 268
Issue: 24
Pages: 17705-10
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Publication
9461221 | -
First Author: Sha B
Year: 1998
Journal: Nature
Title: Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein.
Volume: 391
Issue: 6666
Pages: 506-10
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Publication
2198263 | -
First Author: Salama SR
Year: 1990
Journal: J Bacteriol
Title: Cloning and characterization of Kluyveromyces lactis SEC14, a gene whose product stimulates Golgi secretory function in Saccharomyces cerevisiae.
Volume: 172
Issue: 8
Pages: 4510-21
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Publication
10829015 | J:113900
First Author: Zimmer S
Year: 2000
Journal: J Biol Chem
Title: A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization.
Volume: 275
Issue: 33
Pages: 25672-80
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Publication
12767229 | -
First Author: Panagabko C
Year: 2003
Journal: Biochemistry
Title: Ligand specificity in the CRAL-TRIO protein family.
Volume: 42
Issue: 21
Pages: 6467-74
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Publication
30704900 | J:274082
First Author: Zong D
Year: 2019
Journal: Mol Cell
Title: BRCA1 Haploinsufficiency Is Masked by RNF168-Mediated Chromatin Ubiquitylation.
Volume: 73
Issue: 6
Pages: 1267-1281.e7
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Publication
29955957 | J:309800
First Author: Schrauwen I
Year: 2018
Journal: Hum Genet
Title: De novo variants in GREB1L are associated with non-syndromic inner ear malformations and deafness.
Volume: 137
Issue: 6-7
Pages: 459-470
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Publication
39032134 | J:359420
     
First Author: Shen X
Year: 2024
Journal: Mol Oncol
Title: The genetic duet of concurrent RASAL1 and PTEN alterations promotes cancer aggressiveness by cooperatively activating the PI3K-AKT pathway.
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Publication
26131933 | J:225836
First Author: Schwarz LA
Year: 2015
Journal: Nature
Title: Viral-genetic tracing of the input-output organization of a central noradrenaline circuit.
Volume: 524
Issue: 7563
Pages: 88-92
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Publication
28832620 | J:245687
First Author: Seki Y
Year: 2017
Journal: PLoS One
Title: A novel splice site mutation of myosin VI in mice leads to stereociliary fusion caused by disruption of actin networks in the apical region of inner ear hair cells.
Volume: 12
Issue: 8
Pages: e0183477
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Publication
8896981 | J:33704
First Author: Southwood CM
Year: 1996
Journal: Dev Dyn
Title: Erythroid Krüppel-like factor exhibits an early and sequentially localized pattern of expression during mammalian erythroid ontogeny.
Volume: 206
Issue: 3
Pages: 248-59
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Publication
24421874 | J:211939
First Author: Aza-Carmona M
Year: 2014
Journal: PLoS One
Title: NPPB and ACAN, two novel SHOX2 transcription targets implicated in skeletal development.
Volume: 9
Issue: 1
Pages: e83104
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Publication
26020792 | J:237734
First Author: Gaskill BN
Year: 2015
Journal: PLoS One
Title: The Effect of Cage Space on Behavior and Reproduction in Crl:CD1(Icr) and C57BL/6NCrl Laboratory Mice.
Volume: 10
Issue: 5
Pages: e0127875
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Protein
B1B1A7
Organism: Mus musculus/domesticus
Length: 1403  
Fragment?: true
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Protein
Q9Z275
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
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Protein
Q52KR3
Organism: Mus musculus/domesticus
Length: 3084  
Fragment?: false
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Protein
A0A0U1RQ07
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: true
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Protein
Q8C7Z1
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: true
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Protein
Q544Y3
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
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Protein
A0A0U1RNL2
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: true
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Publication
32284351 | -
First Author: Mushegian A
Year: 2020
Journal: RNA
Title: An ancient evolutionary connection between Ribonuclease A and EndoU families.
Volume: 26
Issue: 7
Pages: 803-813
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Publication
25287301 | -
First Author: Schwarz DS
Year: 2014
Journal: J Cell Biol
Title: The calcium-dependent ribonuclease XendoU promotes ER network formation through local RNA degradation.
Volume: 207
Issue: 1
Pages: 41-57
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Publication
28139767 | -
 
First Author: Laneve P
Year: 2017
Journal: Sci Rep
Title: Drosophila CG3303 is an essential endoribonuclease linked to TDP-43-mediated neurodegeneration.
Volume: 7
Pages: 41559
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Publication
32049015 | -
First Author: Jia F
Year: 2020
Journal: Cell Rep
Title: Regulation of Nucleotide Metabolism and Germline Proliferation in Response to Nucleotide Imbalance and Genotoxic Stresses by EndoU Nuclease.
Volume: 30
Issue: 6
Pages: 1848-1861.e5
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Publication
21805647 | -
First Author: Ragno R
Year: 2011
Journal: ChemMedChem
Title: Identification of small-molecule inhibitors of the XendoU endoribonucleases family.
Volume: 6
Issue: 10
Pages: 1797-805
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Publication
24344237 | J:208364
First Author: Poe JC
Year: 2014
Journal: J Exp Med
Title: EndoU is a novel regulator of AICD during peripheral B cell selection.
Volume: 211
Issue: 1
Pages: 57-69
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Protein Domain
IPR018998 | EndoU_C
Type: Domain
Description: This entry represents the EndoU domain found at the C-terminal of EndoU endoribonucleases, which carries out a conserved RNA processing function. The EndoU domain cleaves RNA at uridylates and release 2',3'-cyclic phosphodiester ends. The EndoU domain is an α/β domain, that contains nine α-helices and three antiparallel β-sheets; the latter are clustered on one side of the domain, whereas the α-helices are largely on the other side []. It contains a conserved trio of catalytic residues, two histidines and a lysine.EndoU is a family of metal-dependent endoribonucleases that is broadly conserved among eukaryotes [, ]. EndoU family members have RNA-binding and endoribonuclease activities and appear to be involved in many aspects ofbiology, including small nucleolar RNA biogenesis, endoplasmic reticulum (ER) network formation, immune response, and neurodegeneration:Xenopus laevis endoribonuclease XendoU is responsible for processing the intron encoded U16 and U86 small nucleolar RNAs (snoRNAs) [, , ].Human EndoU, also known as PP11 (placental protein 11), has an endoribonuclease activity with placental tissue specificity [, , ].Drosophila melanogaster CG2145 and DendoU endoribonucleases [].Caenorhabditis elegans endu-2 regulates nucleotide metabolism and germ cell proliferation in response to nucleotide imbalance and other genotoxic stress [].
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Publication
33042997 | J:310766
 
First Author: Dunn AR
Year: 2020
Journal: Front Cell Dev Biol
Title: Identifying Mechanisms of Normal Cognitive Aging Using a Novel Mouse Genetic Reference Panel.
Volume: 8
Pages: 562662
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Protein
A0A2I3BRP6
Organism: Mus musculus/domesticus
Length: 1849  
Fragment?: false
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Protein
F6QYT9
Organism: Mus musculus/domesticus
Length: 2371  
Fragment?: true
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Protein
A0A2I3BS12
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: true
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Protein
Q5FWK3
Organism: Mus musculus/domesticus
Length: 439  
Fragment?: false
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Protein
Q9CXP4
Organism: Mus musculus/domesticus
Length: 425  
Fragment?: false
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Protein
A0A2X0SSA9
Organism: Mus musculus/domesticus
Length: 441  
Fragment?: true
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Protein
A2AH25
Organism: Mus musculus/domesticus
Length: 479  
Fragment?: false
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Protein
Q8C2P4
Organism: Mus musculus/domesticus
Length: 425  
Fragment?: false
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Protein
Q8C5A0
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
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Protein
A0A2X0U2B7
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: true
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Protein
Q8BQW4
Organism: Mus musculus/domesticus
Length: 479  
Fragment?: false
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Protein
E9Q4H6
Organism: Mus musculus/domesticus
Length: 57  
Fragment?: true
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Protein Domain
IPR020021 | Glycosyl_amidation-assoc_WbuZ
Type: Family
Description: This entry represents a protein highly similar to the HisF protein, but generally represents the second HisF homologue in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homologue of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in Escherichia coli [], IfnA in Pseudomonas aeruginosa []and PseA in Campylobacter jejuni []. Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologues are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when these are in low concentration []. WbuY (like HisH) is proposed to act as a glutaminase to release ammonium. In histidine biosynthesis this is also dispensable in the presence of exogenous ammonium ion. HisH and HisF form a complex such that the ammonium ion is passed directly to HisF where it is used in an amidation reaction causing a subsequent cleavage and cyclization. In the case of WbuYZ, the ammonium ion would be passed from WbuY to WbuZ. WbuZ, being non-essential and so similar to HisF that a sugar substrate is unlikely, would function instead as a ammonium channel to the WbuX protein which does the enzymatic work.
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Protein
A0A2I3BQT2
Organism: Mus musculus/domesticus
Length: 1424  
Fragment?: true
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Publication
- | J:27499
First Author: Lyon MF
Year: 1994
Journal: Mouse Genome
Title: Webbed toes as an effect of an allele of belted, btH
Volume: 92
Issue: 3
Pages: 503
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Protein
G3UYM8
Organism: Mus musculus/domesticus
Length: 757  
Fragment?: true
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Protein
B2XXT9
Organism: Mus musculus/domesticus
Length: 29  
Fragment?: true
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Protein
A0A0G2JEU6
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: true
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Protein
A0A1W2P7L9
Organism: Mus musculus/domesticus
Length: 143  
Fragment?: true
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Protein
E9PVB8
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein
E0CZ69
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: true
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Protein
E0CXB4
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
Q3V381
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
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Protein
S4R1A7
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: true
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Protein
A0A571BF98
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: false
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Protein
Q8BII0
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
D3YY99
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: true
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Protein
A0A494BAB2
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
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Protein
B2XXT3
Organism: Mus musculus/domesticus
Length: 29  
Fragment?: true
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Publication
16895992 | -
First Author: Renzi F
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication.
Volume: 103
Issue: 33
Pages: 12365-70
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Publication
18936097 | -
First Author: Laneve P
Year: 2008
Journal: J Biol Chem
Title: The tumor marker human placental protein 11 is an endoribonuclease.
Volume: 283
Issue: 50
Pages: 34712-9
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Publication
15755742 | -
First Author: Gioia U
Year: 2005
Journal: J Biol Chem
Title: Functional characterization of XendoU, the endoribonuclease involved in small nucleolar RNA biosynthesis.
Volume: 280
Issue: 19
Pages: 18996-9002
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Publication
28610924 | -
 
First Author: Lee HC
Year: 2017
Journal: Gene Expr Patterns
Title: Embryonic expression patterns of Eukaryotic EndoU ribonuclease family gene endouC in zebrafish.
Volume: 25-26
Pages: 66-70
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Protein Domain
IPR000219 | DH-domain
Type: Domain
Description: The Rho family GTPases Rho, Rac and CDC42 regulate a diverse array of cellular processes. Like all members of the Ras superfamily, the Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states.Activation of Rho proteins through release of bound GDP and subsequentbinding of GTP, is catalysed by guanine nucleotide exchange factors (GEFs) inthe Dbl family. The proteins encoded by members of the Dbl family share acommon domain, presented in this entry, of about 200 residues (designated the Dbl homology or DH domain) that has been shown to encode a GEF activity specific for a number of Rho family members. In addition, all family members possess a second, shared domain designated the pleckstrin homology (PH) domain (). Trio and its homologue UNC-73 are unique within the Dbl family insomuch as they encode two distinct DH/PH domain modules. The PH domain is invariably located immediately C-terminal to the DH domain and this invariant topography suggests a functional interdependence between these two structural modules. Biochemical data have established the role of the conserved DH domain in Rho GTPase interaction and activation, and the role of the tandem PH domain in intracellular targeting and/or regulation of DH domain function. The DH domain of Dbl has been shown to mediate oligomerisation that is mostly homophilic in nature. In addition to the tandem DH/PH domains Dbl family GEFs contain diverse structural motifs like serine/threonine kinase, RBD, PDZ, RGS, IQ, REM, Cdc25, RasGEF, CH, SH2, SH3, EF, spectrin or Ig.The DH domain is composed of three structurally conserved regions separated bymore variable regions. It does not share significant sequence homology withother subtypes of small G-protein GEF motifs such as the Cdc25 domain and theSec7 domain, which specifically interact with Ras and ARF family small GTPases, respectively, nor with other Rho protein interactive motifs, indicating that the Dbl family proteins are evolutionarily unique. The DH domain is composed of 11 alpha helices that are folded into a flattened, elongated α-helix bundle in which two of the three conserved regions, conserved region 1 (CR1) and conserved region 3 (CR3), are exposed near the centre of one surface. CR1 and CR3, together with a part of alpha-6 and the DH/PH junction site, constitute the Rho GTPase interacting pocket.
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Protein
Q9CWP6
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
A8Y5H7
Organism: Mus musculus/domesticus
Length: 715  
Fragment?: false
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Protein
Q99J08
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
Q8R0F9
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
Q5SQ27
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: false
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Protein
Q3UWW2
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
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Protein
B1AU74
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
B2RXM5
Organism: Mus musculus/domesticus
Length: 696  
Fragment?: false
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Protein
Q0KL02
Organism: Mus musculus/domesticus
Length: 3102  
Fragment?: false
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Protein
G3UXP9
Organism: Mus musculus/domesticus
Length: 1059  
Fragment?: false
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Protein
D3YUF4
Organism: Mus musculus/domesticus
Length: 1046  
Fragment?: false
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Protein
E9Q863
Organism: Mus musculus/domesticus
Length: 1067  
Fragment?: false
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Protein
Q5FWH6
Organism: Mus musculus/domesticus
Length: 849  
Fragment?: false
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Protein
Q8BW86
Organism: Mus musculus/domesticus
Length: 850  
Fragment?: false
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Protein
H3BKT3
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: true
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Protein
A2AWP4
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: true
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Protein
H3BL15
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: true
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Protein
A0A2I3BRJ9
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
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Protein
A0A140LJD4
Organism: Mus musculus/domesticus
Length: 861  
Fragment?: false
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Protein
F7AI27
Organism: Mus musculus/domesticus
Length: 932  
Fragment?: true
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Protein
Q3V3S7
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: true
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Protein
A0A1Y7VNM7
Organism: Mus musculus/domesticus
Length: 584  
Fragment?: false
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Protein
F7BCP8
Organism: Mus musculus/domesticus
Length: 579  
Fragment?: true
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Protein
H3BKV6
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
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Publication
15629947 | -
First Author: Feng L
Year: 2005
Journal: J Bacteriol
Title: Structural and genetic characterization of enterohemorrhagic Escherichia coli O145 O antigen and development of an O145 serogroup-specific PCR assay.
Volume: 187
Issue: 2
Pages: 758-64
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Publication
18156256 | -
First Author: King JD
Year: 2008
Journal: J Bacteriol
Title: lfnA from Pseudomonas aeruginosa O12 and wbuX from Escherichia coli O145 encode membrane-associated proteins and are required for expression of 2,6-dideoxy-2-acetamidino-L-galactose in lipopolysaccharide O antigen.
Volume: 190
Issue: 5
Pages: 1671-9
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Protein
Q04690
Organism: Mus musculus/domesticus
Length: 2841  
Fragment?: false
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Protein
Q9DBL2
Organism: Mus musculus/domesticus
Length: 498  
Fragment?: false
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Protein
A2AET8
Organism: Mus musculus/domesticus
Length: 944  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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