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Search results 2101 to 2200 out of 5471 for Tyr

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Type Details Score
Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tdo2/Tdo2 Tyr/Tyr
Background: STOCK Tdo2/J
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: C3H/HeJ
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: Not Specified
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: a/a Tyr/Tyr
Background: involves: C57BL/6J
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: a/a Lyst/Lyst Tyr/Tyr
Background: involves: C3H/Rl * C57BL/6J
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/H * C3H/HeH
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: BALB/c * C3H/HeH
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl * T-stock
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl * T-stock
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: (C57BL/6J x SJL/J)F1
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Mlana/Mlana Tyr/Tyr
Background: involves: 129S/SvEv * C57BL/6 * FVB/N * SJL
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: a/a Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: a/a Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: a/a Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: a/a Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: Swiss
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: BALB/cJ
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: Not Specified
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: NMRI/Han
Zygosity: hm
Has Mutant Allele: true
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Publication
19708029 | -
First Author: Del Mare S
Year: 2009
Journal: J Cell Biochem
Title: WWOX: its genomics, partners, and functions.
Volume: 108
Issue: 4
Pages: 737-45
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Publication
25538133 | -
First Author: Schrock MS
Year: 2015
Journal: Exp Biol Med (Maywood)
Title: WWOX: a fragile tumor suppressor.
Volume: 240
Issue: 3
Pages: 296-304
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Publication
9804843 | -
First Author: Beeler T
Year: 1998
Journal: J Biol Chem
Title: The Saccharomyces cerevisiae TSC10/YBR265w gene encoding 3-ketosphinganine reductase is identified in a screen for temperature-sensitive suppressors of the Ca2+-sensitive csg2Delta mutant.
Volume: 273
Issue: 46
Pages: 30688-94
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Publication
28575652 | -
First Author: Boyden LM
Year: 2017
Journal: Am J Hum Genet
Title: Mutations in KDSR Cause Recessive Progressive Symmetric Erythrokeratoderma.
Volume: 100
Issue: 6
Pages: 978-984
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Publication
21421810 | -
First Author: Chao DY
Year: 2011
Journal: Plant Cell
Title: Sphingolipids in the root play an important role in regulating the leaf ionome in Arabidopsis thaliana.
Volume: 23
Issue: 3
Pages: 1061-81
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Protein Domain
IPR045022 | KDSR-like
Type: Family
Description: This entry represents a group of 3-ketodihydrosphingosine reductases, including KDSR from animals and Tsc10 from yeasts and plants. They catalyse the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS) and are required for sphingolipid biosynthesis [, , ].Proteins in this entry show strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central β-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing [, , ].Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction [, , ].
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Protein Domain
IPR042732 | WWOX_SDR_c-like
Type: Domain
Description: This entry represents the classical-like SDR domain of human WWOX and related proteins. Proteins in this entry share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser [, ]. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central β-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction [, , , ].
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Publication
33158444 | J:298978
First Author: Espinoza S
Year: 2020
Journal: BMC Biol
Title: Neuronal surface P antigen (NSPA) modulates postsynaptic NMDAR stability through ubiquitination of tyrosine phosphatase PTPMEG.
Volume: 18
Issue: 1
Pages: 164
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Publication
10818261 | J:63539
First Author: Feuerbach D
Year: 2000
Journal: Neuropharmacology
Title: Cloning, expression and pharmacological characterisation of the mouse somatostatin sst(5) receptor.
Volume: 39
Issue: 8
Pages: 1451-62
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Publication
33763305 | J:307887
 
First Author: Munz M
Year: 2021
Journal: PeerJ
Title: In silico candidate variant and gene identification using inbred mouse strains.
Volume: 9
Pages: e11017
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Publication
- | J:11966
 
First Author: Womack JE
Year: 1989
Journal: Cytogenet Cell Genet
Title: Syntenic mapping of 37 loci in cattle. Chromosomal conservation with mouse and man.
Volume: 51
Pages: 1109 (Abstr.)
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Publication
16741970 | -
First Author: Bagella L
Year: 2006
Journal: J Cell Biochem
Title: Identification of murine cdk10: association with Ets2 transcription factor and effects on the cell cycle.
Volume: 99
Issue: 3
Pages: 978-85
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Publication
11684687 | -
First Author: Pursglove SE
Year: 2002
Journal: J Biol Chem
Title: The solution structure and intramolecular associations of the Tec kinase SRC homology 3 domain.
Volume: 277
Issue: 1
Pages: 755-62
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Publication
6130097 | -
First Author: Garcia E
Year: 1983
Journal: J Biol Chem
Title: Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII uridylyltransferase and uridylyl-removing enzyme.
Volume: 258
Issue: 4
Pages: 2246-53
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Publication
19393245 | -
First Author: Bonet R
Year: 2009
Journal: J Mol Biol
Title: NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding.
Volume: 389
Issue: 2
Pages: 230-7
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Publication
15489910 | -
First Author: Boggon TJ
Year: 2004
Journal: Oncogene
Title: Structure and regulation of Src family kinases.
Volume: 23
Issue: 48
Pages: 7918-27
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Publication
12573241 | -
First Author: Nore BF
Year: 2003
Journal: Biochim Biophys Acta
Title: Identification of phosphorylation sites within the SH3 domains of Tec family tyrosine kinases.
Volume: 1645
Issue: 2
Pages: 123-32
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Publication
15803148 | -
First Author: Schwartzberg PL
Year: 2005
Journal: Nat Rev Immunol
Title: TEC-family kinases: regulators of T-helper-cell differentiation.
Volume: 5
Issue: 4
Pages: 284-95
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Publication
15771581 | -
 
First Author: Berg LJ
Year: 2005
Journal: Annu Rev Immunol
Title: Tec family kinases in T lymphocyte development and function.
Volume: 23
Pages: 549-600
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Publication
15240663 | J:91916
First Author: Garçon F
Year: 2004
Journal: J Immunol
Title: Tec kinase migrates to the T cell-APC interface independently of its pleckstrin homology domain.
Volume: 173
Issue: 2
Pages: 770-5
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Publication
18242510 | -
First Author: Iorns E
Year: 2008
Journal: Cancer Cell
Title: Identification of CDK10 as an important determinant of resistance to endocrine therapy for breast cancer.
Volume: 13
Issue: 2
Pages: 91-104
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Publication
7664269 | -
First Author: Li S
Year: 1995
Journal: Cancer Res
Title: The cdc-2-related kinase, PISSLRE, is essential for cell growth and acts in G2 phase of the cell cycle.
Volume: 55
Issue: 18
Pages: 3992-5
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Publication
7812447 | -
 
First Author: Schouler C
Year: 1994
Journal: Microbiology (Reading)
Title: Sequence and organization of the lactococcal prolate-headed bIL67 phage genome.
Volume: 140 ( Pt 11)
Pages: 3061-9
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Protein Domain
IPR018227 | Amino_acid_transport_2
Type: Family
Description: Amino acid permeases are integral membrane proteins involved in the transportof amino acids into the cell. A number of such proteins have been found to beevolutionary related [, , ]. Aromatic amino acids are concentrated in the cytoplasm of Escherichia coli by 4 distinct transport systems: a general aromatic amino acid permease, and aspecific permease for each of the 3 types (Phe, Tyr and Trp) []. It has been shown []that some permeases in E. coli and related bacteria are evolutionary related.These permeases are proteins of about 400 to 420 amino acids and are located in the cytoplasmic membrane and, like bacterial sugar/cation transporters, are thought to contain 12 transmembrane (TM)regions []- hydropathy analysis, however, is inconclusive, suggesting thepossibility of 10 to 12 membrane-spanning domains []. The best conserved domain is a stretch of 20 residues which seems to be located in a cytoplasmic loop between thefirst and second transmembrane region.
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Protein Domain
IPR032835 | RhoGAP-FF1
Type: Domain
Description: This entry represents the FF domain of the Rho GTPase activating proteins (GAPs). These are the key proteins that make the switch between the active guanosine-triphosphate-bound form of Rho guanosine triphosphatases (GTPases) and the inactive guanosine-diphosphate-bound form. Rho guanosine triphosphatases (GTPases) are a family of proteins with key roles in the regulation of actin cytoskeleton dynamics.The RhoGAP-FF1 domain have been implicated in binding to the transcription factor TFII-I; and phosphorylation of Tyr308 within the first FF domain inhibits this interaction. The RhoGAP-FF1 domain constitutes the first solved structure of an FF domain that lacks the first of the two highly conserved Phe residues, but the substitution of Phe by Tyr does not affect the domain fold [].
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Protein Domain
IPR044093 | STKc_CDK10
Type: Domain
Description: Cyclin-dependent kinases (cdks) are the catalytic subunits of a large family of serine/threonine protein kinases (STKs). They are key regulators of eukaryotic cell cycle progression. CDK10 (also known as PISSLRE) is a cdc2-related kinase that contains the canonical regulatory Tyr and Thr residues present in all protein kinases and a PSTAIRE-like motif named PISSLRE []. CDK10 is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle []. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen [].
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Protein Domain
IPR010043 | UTase/UR
Type: Family
Description: This entry describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for signal-transduction protein PII, and acts as the sensory component of the nitrogen regulation (ntr) system [, ]. The ntr system modulates nitrogen metabolism in response to the prevailing nitrogen source and the requirements of the cell. During nitrogen fixation, ammonia and 2-oxoglutarate can be used to produce glutamate. The activity of the PII protein is stimulated by glutamine and inhibited by 2-oxoglutarate. Under glutamate-limiting conditions, PII is uridylylated by GlnD leading to the activation of glutamate synthetase and to the stimulation of NtrC-dependent promoters. Under high concentrations of fixed nitrogen, PII is de-uridylylated leading to the inactivation of the glutamate synthetase pathway and switching off NtrC-dependent promoters [].Not all homologues of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see ), but the modification site is preserved in the PII homologue of all species with a member of this family.
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Protein Domain
IPR046461 | TerL_ATPase
Type: Domain
Description: Terminase large subunit (TerL) from bacteriophages and evolutionarily related viruses, is an important component of the DNA packing machinery and comprises an ATPase domain, which powers DNA translocation and a nuclease domain that cuts concatemeric DNA [, ]. TerL forms pentamers in which the ATPase domains form a ring distal to the capsid. This is the ATPase domain which contains a C-terminal subdomain that sits above the ATPase active site, called the "Lid subdomain"with reference to analogous lid subdomains found in other ATPases []. It contains a hydrophobic patch (Trp and Tyr residues) that mediates critical interactions in the interface between adjacent ATPase subunits and assists the positioning of the arginine finger residue that catalyses ATP hydrolysis [, ]. This domain is also found in uncharacterised proteins encoded by bacterial prophages, including YmfN from Escherichia coli.
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Protein Domain
IPR007295 | DUF402
Type: Domain
Description: This β-barrel domain is found in FomD, a protein encoded in the fosfomycin biosynthesis gene cluster [, ], which hydrolyzes (S)-HPP-CMP to give (S)-HPP and CMP in the presence of Mn2 or Co2 []. FomD also hydrolyzes cytidylyl 2-hydroxyethylphosphonate (HEP-CMP), which is a biosynthetic intermediate before C-methylation. FomD structure revealed that it has a β-barrel fold consisting of a large twisted antiparallel β-sheet, a key feature of DUF402-containing proteins. The function of this domain is unknown. It has a conserved Tyr residue which activates a water molecule to promote nucleophilic attack on the phosphorus atom of the phosphonate moiety []. This domain has been also found in Ntdp (nucleoside tri- and diphosphatase, also known as Sa1684) from Staphylococcus aureus [].
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Protein Domain
IPR001663 | Rng_hydr_dOase-A
Type: Family
Description: Aromatic ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols []. The complex has both hydroxylase and electron transfer components. The hydroxylase component is itself composed of two subunits: an alpha-subunit of about 50kDa, and a beta-subunit of about 20kDa. The electron transfer component is either composed of two subunits: a ferredoxin and a ferredoxin reductase or by a single bifunctional ferredoxin/reductase subunit. Sequence analysis of hydroxylase subunits of ring hydroxylating systems (including toluene, benzene and napthalene 1,2-dioxygenases) suggests they are derived from a common ancestor []. The alpha-subunit binds both a Rieske-like 2Fe-2S cluster and an iron atom: conserved Cys and His residues in the N-terminal region may provide 2Fe-2S ligands, while conserved His and Tyr residues may coordinate the iron. The beta subunit may be responsible for the substrate specificity of the dioxygenase system [].
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Protein Domain
IPR013061 | Trp/try_permease_CS
Type: Conserved_site
Description: Amino acid permeases are integral membrane proteins involved in the transportof amino acids into the cell. A number of such proteins have been found to beevolutionary related [, , ].Aromatic amino acids are concentrated in the cytoplasm of Escherichia coli by 4 distinct transport systems: a general aromatic amino acid permease, and aspecific permease for each of the 3 types (Phe, Tyr and Trp) []. It has been shown []that some permeases in E. coli and related bacteria are evolutionary related.These permeases are proteins of about 400 to 420 amino acids and are located in the cytoplasmic membrane and, like bacterial sugar/cation transporters, are thought to contain 12 transmembrane (TM)regions []- hydropathy analysis, however, is inconclusive, suggesting thepossibility of 10 to 12 membrane-spanning domains []. The best conserved domain is a stretch of 20 residues which seems to be located in a cytoplasmic loop between thefirst and second transmembrane region.This entry represents a conserved site specific for tyryptophan and tyrosine permeases.
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Protein Domain
IPR035572 | Tec_SH3
Type: Domain
Description: This entry represents the SH3 domain of Tec [, ]. Tec is a cytoplasmic (or nonreceptor) tyrosine kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain []. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions []. It is more widely-expressed than other Tec subfamily kinases. Tec is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils [, ]. Tec is a key component of T-cell receptor (TCR) signaling, and is important in TCR-stimulated proliferation and phospholipase C-gamma1 activation [].
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Protein Domain
IPR035930 | FomD-like_sf
Type: Homologous_superfamily
Description: This β-barrel domain is found in FomD, a protein encoded in the fosfomycin biosynthesis gene cluster [, ], which hydrolyzes (S)-HPP-CMP to give (S)-HPP and CMP in the presence of Mn2 or Co2 []. FomD also hydrolyzes cytidylyl 2-hydroxyethylphosphonate (HEP-CMP), which is a biosynthetic intermediate before C-methylation. FomD structure revealed that it has a β-barrel fold consisting of a large twisted antiparallel β-sheet, a key feature of DUF402-containing proteins. The function of this domain is unknown. It has a conserved Tyr residue which activates a water molecule to promote nucleophilic attack on the phosphorus atom of the phosphonate moiety []. This domain has been also found in Ntdp (nucleoside tri- and diphosphatase, also known as Sa1684) from Staphylococcus aureus [].
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Protein Domain
IPR045593 | Atg11_middle
Type: Domain
Description: This domain represents a region comprised between residues 522 and 583 from fission yeast protein Atg11 (also known as Taz1-interacting factor 1). This domain is necessary and sufficient for Atg11 autophagy function and for supporting Atg1 kinase activity as it harbours an Atg1-binding domain at the N terminus and a homodimerization domain at the C terminus. The N-terminal part of this domain contains the conserved aromatic residues Phe and Tyr necessary for the direct and specific interaction with the tMIT domain of Atg1. This interaction is required for the autophagy function of Atg11. The C-terminal part of this domain, residues 546-583, is predicted to adopt a coiled-coil conformation which mediates Atg11 homodimerization []. Proteins containing this domain seem to be restricted to Schizosaccharomyces.
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Protein Domain
IPR008963 | Purple_acid_Pase-like_N
Type: Homologous_superfamily
Description: Purple acid phosphatases (PAPs) are ubiquitous binuclear metal-containing acid hydrolases characterised by their acidic pH optima and their intense purple colour due to a TyrO-to-FeIII charge-transfer transition. The amino acid residues coordinating the metal ions are conserved in all PAPs. Active PAPs contain an FeIII ion coordinated to Tyr O, a His N, and an Asp O2, in addition to a divalent metal ion (Fe, Zn, or Mn) coordinated by a His N, a His N, and an Asn O. A hydroxide ion and an Asp O2bridge the two metal ions []. These enzymes share a high degree of homology within their N-termini [].This entry also includes phospholipase D, the structure of which has been solved from Bacillus subtilis and shows a purple acid phosphatase-like fold [].
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Publication
9384560 | -
First Author: Sträter N
Year: 1997
Journal: Structure
Title: Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures.
Volume: 5
Issue: 11
Pages: 1437-52
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Publication
9665711 | -
First Author: MacBeath G
Year: 1998
Journal: Biochemistry
Title: A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii.
Volume: 37
Issue: 28
Pages: 10062-73
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Publication
8335631 | -
First Author: Xia T
Year: 1993
Journal: J Bacteriol
Title: The aroQ-encoded monofunctional chorismate mutase (CM-F) protein is a periplasmic enzyme in Erwinia herbicola.
Volume: 175
Issue: 15
Pages: 4729-37
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Publication
7500951 | -
First Author: Hidaka T
Year: 1995
Journal: Mol Gen Genet
Title: Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis.
Volume: 249
Issue: 3
Pages: 274-80
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Protein Domain
IPR002701 | CM_II_prokaryot
Type: Domain
Description: Chorismate mutase (CM) is a regulatory enzyme () required forbiosynthesis of the aromatic amino acids phenylalanine and tyrosine. CMcatalyzes the Claisen rearrangement of chorismate to prephenate, which cansubsequently be converted to precursors of either L-Phe or L-Tyr. Inbifunctional enzymes the CM domain can be fused to a prephenate dehydratase(P-protein for Phe biosynthesis), to a prephenatedehydrogenase (T-protein, for Tyr biosynthesis), or to3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase.Besides these prokaryotic bifunctional enzymes, monofunctional CMs occur inprokaryotes as well as in fungi, plants and nematode worms []. The sequence of monofunctional chorismate mutase aligns well with the N-terminal part of P-proteins [].The type II or AroQ class of CM has an all-helical 3Dstructure, represented by the CM domain of the bifunctional Escherichia coliP-protein. This type is named after the Enterobacteragglomerans monofunctional CM encoded by the aroQ gene []. All CM domainsfrom bifunctional enzymes as well as most monofunctional CMs belong to thisclass, including archaeal CM.Eukaryotic CM from plants and fungi form a separate subclass of AroQ,represented by the Baker's yeast allosteric CM. These enzymes show onlypartial sequence similarity to the prokaryotic CMs due to insertions ofregulatory domains, but the helix-bundle topology and catalytic residues areconserved and the 3D structure of the E. coli CM dimer resembles a yeast CMmonomer [, , ]. The E. coli P-protein CM domain consists of3 helices and lacks allosteric regulation. The yeast CM has evolved by geneduplication and dimerization and each monomer has 12 helices. Yeast CM isallosterically activated by Trp and inhibited by Tyr [].This entry represents the CM type 2 domain, mainly from prokaryotes. It does not include the CM from plants and or Baker's yeast.
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Protein Domain
IPR037039 | CM_AroQ_sf_eucaryotic
Type: Homologous_superfamily
Description: Chorismate mutase (CM) is a regulatory enzyme () required for biosynthesis of the aromatic amino acids phenylalanine and tyrosine. CM catalyzes the Claisen rearrangement of chorismate to prephenate, which can subsequently be converted to precursors of either L-Phe or L-Tyr. In bifunctional enzymes the CM domain can be fused to a prephenate dehydratase (P-protein for Phe biosynthesis), to a prephenate dehydrogenase (T-protein, for Tyr biosynthesis), or to 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase (). Besides these prokaryotic bifunctional enzymes, monofunctional CMs occur in prokaryotes as well as in fungi, plants and nematode worms [].The type I or AroH class of CM is represented by Bacillus subtilis aroH, a monofunctional, nonallosteric, homotrimeric enzyme characterized by its pseudo-alpha/β-barrel 3D structure. Each monomer folds into a 5-stranded mixed β-sheet packed against an α-helix and a 3-10 helix. The core is formed by a closed barrel of mixed β-sheets surrounded by helices. The interfaces between adjacent subunits form three equivalent clefts that harbor the active sites [].The type II or AroQ class of CM has a completely different all-helical 3D structure, represented by the CM domain of the bifunctional Escherichia coli P-protein. This type is named after the Enterobacter agglomerans monofunctional CM encoded by the aroQ gene []. All CM domains from bifunctional enzymes as well as most monofunctional CMs belong to this class, including archaeal CM.Eukaryotic CM from plants and fungi form a separate subclass of AroQ, represented by the Baker's yeast allosteric CM []. These enzymes show only partial sequence similarity to the prokaryotic CMs due to insertions of regulatory domains, but the helix-bundle topology and catalytic residues are conserved and the 3D structure of the E. coli CM dimer resembles a yeast CM monomer [, , ]. The E. coli P-protein CM domain consists of 3 helices and lacks allosteric regulation. The yeast CM has evolved by gene duplication and dimerization and each monomer has 12 helices. Yeast CM is allosterically activated by Trp and inhibited by Tyr [].
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Protein Domain
IPR008238 | Chorismate_mutase_AroQ_euk
Type: Family
Description: Chorismate mutase (CM) is a regulatory enzyme () required for biosynthesis of the aromatic amino acids phenylalanine and tyrosine. CM catalyzes the Claisen rearrangement of chorismate to prephenate, which can subsequently be converted to precursors of either L-Phe or L-Tyr. In bifunctional enzymes the CM domain can be fused to a prephenate dehydratase (P-protein for Phe biosynthesis), to a prephenate dehydrogenase (T-protein, for Tyr biosynthesis), or to 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase (). Besides these prokaryotic bifunctional enzymes, monofunctional CMs occur in prokaryotes as well as in fungi, plants and nematode worms [].The type I or AroH class of CM is represented by Bacillus subtilis aroH, a monofunctional, nonallosteric, homotrimeric enzyme characterized by its pseudo-alpha/β-barrel 3D structure. Each monomer folds into a 5-stranded mixed β-sheet packed against an α-helix and a 3-10 helix. The core is formed by a closed barrel of mixed β-sheets surrounded by helices. The interfaces between adjacent subunits form three equivalent clefts that harbor the active sites [].The type II or AroQ class of CM has a completely different all-helical 3D structure, represented by the CM domain of the bifunctional Escherichia coli P-protein. This type is named after the Enterobacter agglomerans monofunctional CM encoded by the aroQ gene []. All CM domains from bifunctional enzymes as well as most monofunctional CMs belong to this class, including archaeal CM.Eukaryotic CM from plants and fungi form a separate subclass of AroQ, represented by the Baker's yeastallosteric CM []. These enzymes show only partial sequence similarity to the prokaryotic CMs due to insertions of regulatory domains, but the helix-bundle topology and catalytic residues are conserved and the 3D structure of the E. coli CM dimer resembles a yeast CM monomer [, , ]. The E. coli P-protein CM domain consists of 3 helices and lacks allosteric regulation. The yeast CM has evolved by gene duplication and dimerization and each monomer has 12 helices. Yeast CM is allosterically activated by Trp and inhibited by Tyr [].This entry represents chorismate mutase from eukaryotes.
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Publication
12368099 | -
First Author: Kleiger G
Year: 2002
Journal: J Mol Biol
Title: GXXXG and GXXXA motifs stabilize FAD and NAD(P)-binding Rossmann folds through C(alpha)-H... O hydrogen bonds and van der waals interactions.
Volume: 323
Issue: 1
Pages: 69-76
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Strain
MGI:5512982 | STOCK T(2;8)2Wa/H
Attribute String: chromosome aberration, translocation, mutant stock
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Strain
MGI:2164972 | STOCK Tyr<c> Ednrb<s> Tyrp1<b> Hr<hr>
Attribute String: mutant stock
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Strain
MGI:5318083 | STOCK Tmem98<Rwhs>/H
Attribute String: chemically induced mutation, mutant stock
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Strain
MGI:2164847 | CTA/Idr
Attribute String: inbred strain, spontaneous mutation, mutant strain
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Strain
MGI:2176276 | STOCK A Tyr<c> Sha/J
Attribute String: mutant stock, spontaneous mutation
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: 101/Rl * C3H/Rl
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: AKR/J * DBA/2J
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr
Background: involves: SELH/Bc * SWV/Bc
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tyr/Tyr<+> Del(7)Tyr/?
Background: involves: 101/H * C3H/HeH
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: A/? Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: A/? Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: A/? Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: A/? Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: A/? Tyr/Tyr
Background: involves: C57BL/6 * FVB
Zygosity: cx
Has Mutant Allele: true
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Publication
29584722 | J:262141
First Author: Liggins MC
Year: 2018
Journal: PLoS Genet
Title: PIKfyve regulates melanosome biogenesis.
Volume: 14
Issue: 3
Pages: e1007290
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Publication
29311329 | J:260599
First Author: Bélanger C
Year: 2018
Journal: Proc Natl Acad Sci U S A
Title: Dysregulation of cotranscriptional alternative splicing underlies CHARGE syndrome.
Volume: 115
Issue: 4
Pages: E620-E629
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Publication
24597867 | J:238828
First Author: Caburet S
Year: 2014
Journal: N Engl J Med
Title: Mutant cohesin in premature ovarian failure.
Volume: 370
Issue: 10
Pages: 943-949
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Publication
25233132 | J:218054
 
First Author: Blum B
Year: 2014
Journal: Elife
Title: Reversal of β cell de-differentiation by a small molecule inhibitor of the TGFβ pathway.
Volume: 3
Pages: e02809
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Publication
35044447 | J:340541
First Author: Liang W
Year: 2022
Journal: Diabetes
Title: Pathogenic Role of Diabetes-Induced Overexpression of Kallistatin in Corneal Wound Healing Deficiency Through Inhibition of Canonical Wnt Signaling.
Volume: 71
Issue: 4
Pages: 747-761
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Publication
33667344 | J:303708
First Author: McKimpson WM
Year: 2021
Journal: Dev Cell
Title: Conversion of the death inhibitor ARC to a killer activates pancreatic β cell death in diabetes.
Volume: 56
Issue: 6
Pages: 747-760.e6
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Publication
31624141 | J:287848
First Author: Tan SM
Year: 2020
Journal: Diabetes
Title: Complement C5a Induces Renal Injury in Diabetic Kidney Disease by Disrupting Mitochondrial Metabolic Agility.
Volume: 69
Issue: 1
Pages: 83-98
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Publication
29654303 | J:263120
First Author: Zhao XP
Year: 2018
Journal: Sci Rep
Title: Hedgehog Interacting Protein Promotes Fibrosis and Apoptosis in Glomerular Endothelial Cells in Murine Diabetes.
Volume: 8
Issue: 1
Pages: 5958
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Publication
25249008 | J:324511
First Author: Mohamed R
Year: 2014
Journal: J Mol Med (Berl)
Title: Urinary semaphorin 3A correlates with diabetic proteinuria and mediates diabetic nephropathy and associated inflammation in mice.
Volume: 92
Issue: 12
Pages: 1245-56
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