|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 301 to 365 out of 365 for Cpa1

<< First    < Previous  |  Next >    Last >>
0.22s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Protein
Q9WUJ5
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
•
•
•
•
•
Protein
A2A464
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
•
•
•
•
•
Protein
Q69ZU9
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: true
•
•
•
•
•
Protein
M0QW97
Organism: Mus musculus/domesticus
Length: 520  
Fragment?: true
•
•
•
•
•
Protein
M0QWN6
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: true
•
•
•
•
•
Protein
Q3TM63
Organism: Mus musculus/domesticus
Length: 336  
Fragment?: false
•
•
•
•
•
Publication
11700351 | -
First Author: Verkhovskaya ML
Year: 2001
Journal: Microbiology
Title: Deletion of one of two Escherichia coli genes encoding putative Na+/H+ exchangers (ycgO) perturbs cytoplasmic alkali cation balance at low osmolarity.
Volume: 147
Issue: Pt 11
Pages: 3005-13
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:3506744
Assay Type: RNA in situ
Annotation Date: 2025-01-16
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3565020
Pattern: Regionally restricted
Stage: TS20
Assay Id: MGI:7852705
Age: embryonic day 12.5
Note: Expression was detected in the trunk and did not overlap with Cpa1 staining in the newly formed branches.
Specimen Label: 2H
Detected: true
Specimen Num: 2
•
•
•
•
•
Protein
Q61165
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: false
•
•
•
•
•
Protein
Q8BLV3
Organism: Mus musculus/domesticus
Length: 726  
Fragment?: false
•
•
•
•
•
Protein
Q8BZ00
Organism: Mus musculus/domesticus
Length: 644  
Fragment?: false
•
•
•
•
•
Protein
Q7TSV2
Organism: Mus musculus/domesticus
Length: 823  
Fragment?: false
•
•
•
•
•
Protein
B2RXE2
Organism: Mus musculus/domesticus
Length: 898  
Fragment?: false
•
•
•
•
•
Protein
Q3ZAS0
Organism: Mus musculus/domesticus
Length: 814  
Fragment?: false
•
•
•
•
•
Protein
Q9WUJ4
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: true
•
•
•
•
•
Protein
B0QZV3
Organism: Mus musculus/domesticus
Length: 670  
Fragment?: false
•
•
•
•
•
Protein
A8E634
Organism: Mus musculus/domesticus
Length: 644  
Fragment?: false
•
•
•
•
•
Protein
Q499E9
Organism: Mus musculus/domesticus
Length: 644  
Fragment?: false
•
•
•
•
•
Protein
Q80X31
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: false
•
•
•
•
•
Protein
D3Z0Q9
Organism: Mus musculus/domesticus
Length: 313  
Fragment?: true
•
•
•
•
•
Protein
Q3T994
Organism: Mus musculus/domesticus
Length: 644  
Fragment?: false
•
•
•
•
•
Protein
Q3TN68
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: true
•
•
•
•
•
Protein
Q3UDC9
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: false
•
•
•
•
•
Protein
Q8BTG0
Organism: Mus musculus/domesticus
Length: 702  
Fragment?: false
•
•
•
•
•
Protein
Q80U52
Organism: Mus musculus/domesticus
Length: 700  
Fragment?: true
•
•
•
•
•
Protein
Q3U3A6
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: false
•
•
•
•
•
Protein
A1L3P4
Organism: Mus musculus/domesticus
Length: 702  
Fragment?: false
•
•
•
•
•
Protein
Q8BUE1
Organism: Mus musculus/domesticus
Length: 797  
Fragment?: false
•
•
•
•
•
Protein
G3X939
Organism: Mus musculus/domesticus
Length: 829  
Fragment?: false
•
•
•
•
•
Protein
A0A286YD40
Organism: Mus musculus/domesticus
Length: 862  
Fragment?: false
•
•
•
•
•
Protein
Q6UJY2
Organism: Mus musculus/domesticus
Length: 1175  
Fragment?: false
•
•
•
•
•
Publication
2141606 | -
First Author: Orbach MJ
Year: 1990
Journal: J Biol Chem
Title: The Neurospora crassa arg-2 locus. Structure and expression of the gene encoding the small subunit of arginine-specific carbamoyl phosphate synthetase.
Volume: 265
Issue: 19
Pages: 10981-7
•
•
•
•
•
Protein Domain
IPR013203 | Leader_Arg2_CPA1
Type: Family
Description: In this family there are leader peptides involved in the regulation of the glutaminase subunit (small subunit) of arginine-specific carbamoyl phosphate synthetase. In Neurospora crassa it is a small upstream ORF of 24 codons above the arg-2 locus []. In yeast it is the leader peptide of the CPA1 gene. The 5' region of CPA1 mRNA contains a 25 codon upstream open reading frame. The leader peptide, the product of the upstream open reading frame, plays an essential, negative role in the specific repression of CPA1 by arginine [].
•
•
•
•
•
Publication
9537504 | -
First Author: Dibrov P
Year: 1998
Journal: FEBS Lett
Title: Comparative molecular analysis of Na+/H+ exchangers: a unified model for Na+/H+ antiport?
Volume: 424
Issue: 1-2
Pages: 1-5
•
•
•
•
•
Publication
9278382 | J:42741
First Author: Orlowski J
Year: 1997
Journal: J Biol Chem
Title: Na+/H+ exchangers of mammalian cells.
Volume: 272
Issue: 36
Pages: 22373-6
•
•
•
•
•
Publication
9507001 | -
First Author: Numata M
Year: 1998
Journal: J Biol Chem
Title: Identification of a mitochondrial Na+/H+ exchanger.
Volume: 273
Issue: 12
Pages: 6951-9
•
•
•
•
•
Publication
12027219 | -
 
First Author: Burckhardt G
Year: 2002
Journal: J Nephrol
Title: The Na+/H+ exchanger gene family.
Volume: 15 Suppl 5
Pages: S3-21
•
•
•
•
•
Publication
12502567 | -
 
First Author: Hayashi H
Year: 2002
Journal: Ann N Y Acad Sci
Title: Multiple modes of regulation of Na+/H+ exchangers.
Volume: 976
Pages: 248-58
•
•
•
•
•
Publication
16734752 | -
First Author: Alexander RT
Year: 2006
Journal: Acta Physiol (Oxf)
Title: Na+/H+ exchangers and the regulation of volume.
Volume: 187
Issue: 1-2
Pages: 159-67
•
•
•
•
•
Publication
17071327 | -
First Author: Bobulescu IA
Year: 2006
Journal: Semin Nephrol
Title: Na+/H+ exchangers in renal regulation of acid-base balance.
Volume: 26
Issue: 5
Pages: 334-44
•
•
•
•
•
Publication
16513813 | -
First Author: Pardo JM
Year: 2006
Journal: J Exp Bot
Title: Alkali cation exchangers: roles in cellular homeostasis and stress tolerance.
Volume: 57
Issue: 5
Pages: 1181-99
•
•
•
•
•
Publication
11187762 | -
First Author: Wakabayashi S
Year: 2000
Journal: Seikagaku
Title: [Structure function and regulation of the mammalian Na+/H+ exchangers].
Volume: 72
Issue: 11
Pages: 1329-34
•
•
•
•
•
Publication
17218973 | -
First Author: Malo ME
Year: 2006
Journal: Can J Physiol Pharmacol
Title: Physiological role and regulation of the Na+/H+ exchanger.
Volume: 84
Issue: 11
Pages: 1081-95
•
•
•
•
•
Publication
2982857 | -
First Author: Zalkin H
Year: 1985
Journal: J Biol Chem
Title: Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.
Volume: 260
Issue: 6
Pages: 3350-4
•
•
•
•
•
Protein Domain
IPR017926 | GATASE
Type: Domain
Description: Glutamine amidotransferase (GATase) enzymes catalyse the removal of the ammonia group from glutamine and then transfer this group to a substrate to form a new carbon-nitrogen group []. The GATase domain exists either as a separate polypeptidic subunit or as part of a larger polypeptide fused in different ways to a synthase domain. Two classes of GATase domains have been identified [, ]: class-I (also known as trpG-type or triad) and class-II (also known as purF-type or Ntn). Class-I (or type 1) GATase domains have been found in the following enzymes:The second component of anthranilate synthase (AS) []. AS catalyzes the biosynthesis of anthranilate from chorismate and glutamine. AS is generally a dimeric enzyme: the first component can synthesize anthranilate using ammonia rather than glutamine, whereas component II provides the GATase activity []. In some bacteria and in fungi the GATase component of AS is part of a multifunctional protein that also catalyzes other steps of the biosynthesis of tryptophan.The second component of 4-amino-4-deoxychorismate (ADC) synthase, a dimeric prokaryotic enzyme that functions in the pathway that catalyzes the biosynthesis of para-aminobenzoate (PABA) from chorismate and glutamine. The second component (gene pabA) provides the GATase activity [].CTP synthase. CTP synthase catalyzes the final reaction in the biosynthesis of pyrimidine, the ATP-dependent formation of CTP from UTP and glutamine. CTP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the C-terminal section [].GMP synthase (glutamine-hydrolyzing). GMP synthase catalyzes the ATP-dependent formation of GMP from xanthosine 5'-phosphate and glutamine. GMP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the N-terminal section [, ].Glutamine-dependent carbamoyl-phosphate synthase (GD-CPSase); an enzyme involved in both arginine and pyrimidine biosynthesis and which catalyzes the ATP-dependent formation of carbamoyl phosphate from glutamine and carbon dioxide. In bacteria GD-CPSase is composed of two subunits: the large chain (gene carB) provides the CPSase activity, while the small chain (gene carA) provides the GATase activity. In yeast the enzyme involved in arginine biosynthesis is also composed of two subunits: CPA1 (GATase), and CPA2 (CPSase). In most eukaryotes, the first three steps of pyrimidine biosynthesis are catalyzed by a large multifunctional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals). The GATase domain is located at the N-terminal extremity of this polyprotein [].Phosphoribosylformylglycinamidine synthase, an enzyme that catalyzes the fourth step in the de novo biosynthesis of purines. In some species of bacteria and rchaea, FGAM synthase II is composed of two subunits: a small chain (gene purQ) which provides the GATase activity and a large chain (gene purL) which provides the aminator activity. In eukaryotes and Gram-negative bacteria a single polypeptide (large type of purL) contains a FGAM synthethase domain and the GATase as the C-terminal domain [].Imidazole glycerol phosphate synthase subunit hisH, an enzyme that catalyzes the fifth step in the biosynthesis of histidine.A triad of conserved Cys-His-Glu forms the active site, wherein the catalytic cysteine is essential for the amidotransferase activity [, ]. Different structures show that the active site Cys of type 1 GATase is located at the tip of a nucleophile elbow.
•
•
•
•
•
Protein
A2AEQ5
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: false
•
•
•
•
•
Protein
Q3THK7
Organism: Mus musculus/domesticus
Length: 693  
Fragment?: false
•
•
•
•
•
Protein
P70698
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
•
•
•
•
•
Protein
P70303
Organism: Mus musculus/domesticus
Length: 586  
Fragment?: false
•
•
•
•
•
Protein
B2RRH9
Organism: Mus musculus/domesticus
Length: 693  
Fragment?: false
•
•
•
•
•
Publication
10449718 | -
First Author: Knöchel T
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
Volume: 96
Issue: 17
Pages: 9479-84
•
•
•
•
•
Publication
15301531 | -
First Author: Anand R
Year: 2004
Journal: Biochemistry
Title: Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography.
Volume: 43
Issue: 32
Pages: 10328-42
•
•
•
•
•
Publication
8548458 | -
First Author: Tesmer JJ
Year: 1996
Journal: Nat Struct Biol
Title: The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Volume: 3
Issue: 1
Pages: 74-86
•
•
•
•
•
Publication
2679363 | -
 
First Author: Crawford IP
Year: 1989
Journal: Annu Rev Microbiol
Title: Evolution of a biosynthetic pathway: the tryptophan paradigm.
Volume: 43
Pages: 567-600
•
•
•
•
•
Publication
3298209 | -
First Author: Weng ML
Year: 1987
Journal: J Bacteriol
Title: Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain.
Volume: 169
Issue: 7
Pages: 3023-8
•
•
•
•
•
Publication
6086650 | -
First Author: Nyunoya H
Year: 1984
Journal: J Biol Chem
Title: Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain.
Volume: 259
Issue: 15
Pages: 9790-8
•
•
•
•
•
Publication
4355768 | -
 
First Author: Buchanan JM
Year: 1973
Journal: Adv Enzymol Relat Areas Mol Biol
Title: The amidotransferases.
Volume: 39
Pages: 91-183
•
•
•
•
•
Publication
9575335 | -
First Author: Massière F
Year: 1998
Journal: Cell Mol Life Sci
Title: The mechanism of glutamine-dependent amidotransferases.
Volume: 54
Issue: 3
Pages: 205-22
•
•
•
•
•
Protein
Q7TN13
Organism: Mus musculus/domesticus
Length: 1019  
Fragment?: true
•
•
•
•
•
Protein
E9QAT6
Organism: Mus musculus/domesticus
Length: 971  
Fragment?: false
•
•
•
•
•
Publication
8098212 | -
First Author: Davidson JN
Year: 1993
Journal: Bioessays
Title: The evolutionary history of the first three enzymes in pyrimidine biosynthesis.
Volume: 15
Issue: 3
Pages: 157-64
•
•
•
•
•
Protein
Q8C196
Organism: Mus musculus/domesticus
Length: 1500  
Fragment?: false
•
•
•
•
•
Protein
B2RQC6
Organism: Mus musculus/domesticus
Length: 2225  
Fragment?: false
•
•
•
•
•
Protein
E9QAI5
Organism: Mus musculus/domesticus
Length: 2162  
Fragment?: false
•
•
•
•
•
Protein
G3UWN2
Organism: Mus musculus/domesticus
Length: 2164  
Fragment?: false
•
•
•
•
•




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