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Search results 101 to 200 out of 243 for Ipp

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Type Details Score
Publication
27626380 | J:236599
First Author: Dickinson ME
Year: 2016
Journal: Nature
Title: High-throughput discovery of novel developmental phenotypes.
Volume: 537
Issue: 7621
Pages: 508-514
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Publication
- | J:188991
     
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
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Publication
- | J:94790
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Mouse Synonym Curation
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Publication
24194600 | J:228563
First Author: Koscielny G
Year: 2014
Journal: Nucleic Acids Res
Title: The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data.
Volume: 42
Issue: Database issue
Pages: D802-9
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Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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Publication
- | J:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
17062755 | -
First Author: Miyawaki K
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Roles of Arabidopsis ATP/ADP isopentenyltransferases and tRNA isopentenyltransferases in cytokinin biosynthesis.
Volume: 103
Issue: 44
Pages: 16598-603
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Protein Domain
IPR018022 | IPT
Type: Family
Description: tRNA dimethylallyltransferase alternative names include delta(2)-isopentenylpyrophosphate transferase, IPP transferral and 2-methylthio-N6-isopentyladenosine tRNA modification enzyme. This enzyme catalyses the first step in the modification of an adenosine near the anticodon to 2-methylthio-N6-isopentyladenosine [].Plants have two classes of isopentenyltransferases (IPTs): ATP/ADP isopentenyltransferases (IPT1, 3, 4-8) and tRNA IPTs (IPT2 and 9) []. Both types are included in this family.
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UniProt Feature
UniProt Feature
Begin: 1
Description: Actin-binding protein IPP
Type: chain
End: 584
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Publication
3031456 | -
First Author: Dihanich ME
Year: 1987
Journal: Mol Cell Biol
Title: Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae.
Volume: 7
Issue: 1
Pages: 177-84
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Publication
11536049 | -
First Author: VanHouten JN
Year: 2001
Journal: Oncogene
Title: Cloning and characterization of ectopically expressed transcripts for the actin-binding protein MIPP in mouse mammary carcinomas.
Volume: 20
Issue: 38
Pages: 5366-72
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Protein
P49442
Organism: Mus musculus/domesticus
Length: 396  
Fragment?: false
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Protein
Q80UN9
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
P58044
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
Q8BFZ6
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Publication
15522220 | -
First Author: Takahashi K
Year: 2004
Journal: Biochem Biophys Res Commun
Title: Cellular signaling mediated by calphoglin-induced activation of IPP and PGM.
Volume: 325
Issue: 1
Pages: 203-14
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GO Term
GO:0170045 | isopentenyl pyrophosphate transmembrate transporter activity
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GO Term
GO:0046490 | isopentenyl diphosphate metabolic process
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Protein
Q80UN9-2
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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GO Term
GO:0004452 | isopentenyl-diphosphate delta-isomerase activity
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Pathway
R-MMU-446388 | Regulation of cytoskeletal remodeling and cell spreading by IPP complex components
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GO Term
GO:1990065 | Dxr protein complex
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GO Term
GO:0009240 | isopentenyl diphosphate biosynthetic process
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Protein Coding Gene
MGI:1195263 | Lims1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2153063 | Parvb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:103040 | Rsu1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1201675 | Tesk1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9ES46
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: false
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Protein
Q99JW4
Organism: Mus musculus/domesticus
Length: 325  
Fragment?: false
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Protein
Q01730
Organism: Mus musculus/domesticus
Length: 277  
Fragment?: false
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Protein
O70146
Organism: Mus musculus/domesticus
Length: 627  
Fragment?: false
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Protein Coding Gene
MGI:1931144 | Parva
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9EPC1
Organism: Mus musculus/domesticus
Length: 372  
Fragment?: false
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Protein Coding Gene
MGI:2137706 | Actn1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q7TPR4
Organism: Mus musculus/domesticus
Length: 892  
Fragment?: false
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Publication
15009187 | -
First Author: Yamashita S
Year: 2004
Journal: Eur J Biochem
Title: Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.
Volume: 271
Issue: 6
Pages: 1087-93
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Publication
12798687 | -
First Author: Steinbacher S
Year: 2003
Journal: J Mol Biol
Title: Crystal structure of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Bacillus subtilis.
Volume: 329
Issue: 5
Pages: 973-82
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Protein Domain
IPR011179 | IPdP_isomerase
Type: Family
Description: This entry represents the bacterial and archaeal isopentenyl-diphosphate delta-isomerase (IPP isomerase). IPP isomerase catalyses the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), and is a key enzyme in the biosynthesis of isoprenoids via the mevalonate pathway. The bacterial and archaeal IPP isomerase (type 2 enzyme) differs from that found in eukaryotes (type 1 enzyme), and requires NADPH, magnesium, and FMN for activity [, ].
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Protein Coding Gene
MGI:108295 | Pxn
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q8VI36
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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HT Experiment
GSE106413 | RNA sequencing analysis of PINCH mutant sciatic nerves
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Publication
9228075 | J:41959
First Author: Paton VG
Year: 1997
Journal: J Biol Chem
Title: Cloning and subcellular localization of hamster and rat isopentenyl diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif targets the enzyme to peroxisomes.
Volume: 272
Issue: 30
Pages: 18945-50
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Protein Coding Gene
MGI:1920591 | Arhgef6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q8K4I3
Organism: Mus musculus/domesticus
Length: 771  
Fragment?: false
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Protein Domain
IPR001441 | UPP_synth-like
Type: Family
Description: In prokaryotes, undecaprenyl diphosphate synthase (UPP synthase, di-trans-poly-cis-decaprenylcistransferase or ditrans,polycis-undecaprenyl-diphosphate synthase ()), catalyzes the formation of the carrier lipid undecaprenyl pyrophosphate (UPP) in bacterial cell wall peptidoglycan biosynthesis from isopentenyl pyrophosphate (IPP) [, , , , , , , , , , , , , ]. Cis (Z)-Isoprenyl diphosphate synthase (cis-IPPS) catalyzes the successive 1'-4 condensation of the IPP molecule to trans,trans-farnesyl diphosphate (FPP) or to cis,trans-FPP to form long-chain polyprenyl diphosphates. A few can also catalyze the condensation of IPP to trans-geranyl diphosphate to form the short-chain cis,trans- FPP. cis-IPPS form homodimers and are mechanistically and structurally distinct from trans-IPPS, which lack the DDXXD motifs, yet require Mg2+for activity. Homologues are also found in archaebacteria and include a number of uncharacterised proteins including some from yeasts.This entry also matches related enzymes that transfer alkyl groups, such as dehydrodolichyl diphosphate synthase from eukaryotes, which catalyzes the formation of the polyisoprenoid glycosyl carrier lipid dolichyl monophosphate.
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Publication
9677368 | -
First Author: Shimizu N
Year: 1998
Journal: J Biol Chem
Title: Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases.
Volume: 273
Issue: 31
Pages: 19476-81
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Publication
16900467 | -
First Author: Takahashi S
Year: 2006
Journal: Chem Rec
Title: Structure and function of cis-prenyl chain elongating enzymes.
Volume: 6
Issue: 4
Pages: 194-205
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Publication
23134568 | -
First Author: Akhtar TA
Year: 2013
Journal: Plant J
Title: The tomato cis-prenyltransferase gene family.
Volume: 73
Issue: 4
Pages: 640-52
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Publication
12636086 | -
First Author: Kharel Y
Year: 2003
Journal: Nat Prod Rep
Title: Molecular analysis of cis-prenyl chain elongating enzymes.
Volume: 20
Issue: 1
Pages: 111-8
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Publication
22471620 | -
First Author: Teng KH
Year: 2012
Journal: Mol Membr Biol
Title: Undecaprenyl diphosphate synthase, a cis-prenyltransferase synthesizing lipid carrier for bacterial cell wall biosynthesis.
Volume: 29
Issue: 7
Pages: 267-73
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Publication
11076526 | -
First Author: Pan JJ
Year: 2000
Journal: Biochemistry
Title: Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis.
Volume: 39
Issue: 45
Pages: 13856-61
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Publication
11346651 | -
First Author: Kharel Y
Year: 2001
Journal: J Biol Chem
Title: Identification of Significant residues for homoallylic substrate binding of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase.
Volume: 276
Issue: 30
Pages: 28459-64
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Publication
10908715 | -
First Author: Cunillera N
Year: 2000
Journal: FEBS Lett
Title: Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis.
Volume: 477
Issue: 3
Pages: 170-4
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Publication
10586494 | -
First Author: Koyama T
Year: 1999
Journal: Biosci Biotechnol Biochem
Title: Molecular analysis of prenyl chain elongating enzymes.
Volume: 63
Issue: 10
Pages: 1671-6
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Publication
1181565 | -
First Author: Bednarzewski J
Year: 1975
Journal: Pol Tyg Lek
Title: [Myocardial infarct mortality and cigarette smoking in the records of Myocardial Infarct Registries in the City of Warsaw and in Lublin].
Volume: 30
Issue: 42
Pages: 1737-9
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Publication
11442630 | -
First Author: Sato M
Year: 2001
Journal: Genes Cells
Title: Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis.
Volume: 6
Issue: 6
Pages: 495-506
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Publication
10816587 | -
First Author: Schulbach MC
Year: 2000
Journal: J Biol Chem
Title: Identification of a short (C15) chain Z-isoprenyl diphosphate synthase and a homologous long (C50) chain isoprenyl diphosphate synthase in Mycobacterium tuberculosis.
Volume: 275
Issue: 30
Pages: 22876-81
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Publication
9736763 | -
First Author: Sun Z
Year: 1998
Journal: Proc Natl Acad Sci U S A
Title: Differential expression of two isopentenyl pyrophosphate isomerases and enhanced carotenoid accumulation in a unicellular chlorophyte.
Volume: 95
Issue: 19
Pages: 11482-8
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Publication
9418296 | -
First Author: Ramos-Valdivia AC
Year: 1997
Journal: Nat Prod Rep
Title: Isopentenyl diphosphate isomerase: a core enzyme in isoprenoid biosynthesis. A review of its biochemistry and function.
Volume: 14
Issue: 6
Pages: 591-603
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Protein Domain
IPR011876 | IsopentenylPP_isomerase_typ1
Type: Family
Description: This entry represents type 1 of two non-homologous families of the enzyme isopentenyl-diphosphate delta-isomerase (IPP isomerase; ). IPP isomerase is a member of the Nudix hydrolase superfamily, and is a key enzyme in the isoprenoid biosynthetic pathway. It catalyses the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate. Dimethylallyl phosphate is the initial substrate for the biosynthesis of carotenoids and other long chain isoprenoids []. IPP is an essential building block for many compounds, including enzyme cofactors, sterols, and prenyl groups. This enzyme interconverts isopentenyl diphosphate and dimethylallyl diphosphate. The enzyme requires one Mn2+ or Mg2+ ion in its active site to fold into an active conformation and also contains the Nudix motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. The metal binding site is present within the active site and plays structural and catalytical roles. IPP isomerase is well represented in several bacteria, archaebacteria and eukaryotes, including fungi, mammals and plants. Despite sequence variations (mainly at the N terminus), the core structure is highly conserved [].
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Publication
9655509 | J:48284
First Author: Acharya JK
Year: 1998
Journal: Neuron
Title: Synaptic defects and compensatory regulation of inositol metabolism in inositol polyphosphate 1-phosphatase mutants.
Volume: 20
Issue: 6
Pages: 1219-29
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Protein
Q99KU1
Organism: Mus musculus/domesticus
Length: 333  
Fragment?: false
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Protein
Q99LJ8
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
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Protein
A3KGL2
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Protein
A3KGL3
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: true
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Protein
A3KGL0
Organism: Mus musculus/domesticus
Length: 299  
Fragment?: false
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Protein
A3KGK9
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
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Publication
9882662 | -
First Author: Apfel CM
Year: 1999
Journal: J Bacteriol
Title: Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene.
Volume: 181
Issue: 2
Pages: 483-92
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Protein Domain
IPR001228 | IspD
Type: Family
Description: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) catalyses the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) in the deoxyxylulose pathway of isopentenyl diphosphate (IPP) biosynthesis []. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. The isoprenoid pathway is a well known target for anti-infective drug development [, ]. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein.
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Protein Domain
IPR036424 | UPP_synth-like_sf
Type: Homologous_superfamily
Description: In prokaryotes, undecaprenyl diphosphate synthase (UPP synthase or di-trans-poly-cis-decaprenylcistransferase ()), catalyzes the formation of the carrier lipid undecaprenyl pyrophosphate (UPP) in bacterial cell wall peptidoglycan biosynthesis from isopentenyl pyrophosphate (IPP) [, , , , , , , , , , , , , ]. Cis (Z)-Isoprenyl diphosphate synthase (cis-IPPS) catalyzes the successive 1'-4 condensation of the IPP molecule to trans,trans-farnesyl diphosphate (FPP) or to cis,trans-FPP to form long-chain polyprenyl diphosphates. A few can also catalyze the condensation of IPP to trans-geranyl diphosphate to form the short-chain cis,trans- FPP. cis-IPPS form homodimers and are mechanistically and structurally distinct from trans-IPPS, which lack the DDXXD motifs, yet require Mg2+for activity. Homologues are also found in archaebacteria and include a number of uncharacterised proteins including some from yeasts.The structure of diphosphate synthase has three layers (alpha/beta/alpha) with parallel β-sheet of six strands.This entry also matches related enzymes that transfer alkyl groups, such as dehydrodolichyl diphosphate synthase from eukaryotes, which catalyzes the formation of the polyisoprenoid glycosyl carrier lipid dolichyl monophosphate.
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Publication
27207548 | J:249466
First Author: Kang L
Year: 2016
Journal: Diabetes
Title: Integrin-Linked Kinase in Muscle Is Necessary for the Development of Insulin Resistance in Diet-Induced Obese Mice.
Volume: 65
Issue: 6
Pages: 1590-600
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Publication
25609703 | J:223845
First Author: Karaköse E
Year: 2015
Journal: J Cell Sci
Title: The focal adhesion protein PINCH-1 associates with EPLIN at integrin adhesion sites.
Volume: 128
Issue: 5
Pages: 1023-33
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Publication
29282838 | J:260812
First Author: Chakraborty A
Year: 2018
Journal: Biol Rev Camb Philos Soc
Title: The inositol pyrophosphate pathway in health and diseases.
Volume: 93
Issue: 2
Pages: 1203-1227
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Publication
11714808 | J:72826
First Author: Daubenberger CA
Year: 2001
Journal: J Immunol
Title: Functional and structural similarity of V gamma 9V delta 2 T cells in humans and Aotus monkeys, a primate infection model for Plasmodium falciparum malaria.
Volume: 167
Issue: 11
Pages: 6421-30
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Publication
19435803 | J:150585
First Author: Stanchi F
Year: 2009
Journal: J Cell Sci
Title: Molecular dissection of the ILK-PINCH-parvin triad reveals a fundamental role for the ILK kinase domain in the late stages of focal-adhesion maturation.
Volume: 122
Issue: Pt 11
Pages: 1800-11
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Publication
35616334 | J:330429
 
First Author: Paes de Faria J
Year: 2022
Journal: Development
Title: Pinch2 regulates myelination in the mouse central nervous system.
Volume: 149
Issue: 13
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Publication
20005845 | -
First Author: Fukuda K
Year: 2009
Journal: Mol Cell
Title: The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions.
Volume: 36
Issue: 5
Pages: 819-30
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Publication
20033063 | -
First Author: Wickström SA
Year: 2010
Journal: EMBO J
Title: The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!
Volume: 29
Issue: 2
Pages: 281-91
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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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