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Search results 201 to 300 out of 409 for Hpd

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Type Details Score
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:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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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
10789590 | J:62498
First Author: Bossu E
Year: 2000
Journal: Anticancer Drugs
Title: Determination of the maximal carcinoma/normal skin ratio after HpD or m-THPC administration in Hairless mice (SKH-1) by fluorescence spectroscopy.
Volume: 11
Issue: 2
Pages: 85-91
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Allele
Hpd<em1Smoc> | MGI:7290249
Name: 4-hydroxyphenylpyruvic acid dioxygenase; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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GO Term
GO:0008889 | glycerophosphodiester phosphodiesterase activity
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Interaction Experiment
Xie Y (2019)
Description: HPD degradation regulated by the TTC36-STK33-PELI1 signaling axis induces tyrosinemia and neurological damage.
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Protein
P49429
Organism: Mus musculus/domesticus
Length: 393  
Fragment?: false
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DO Term
DOID:0111362 | hawkinsinuria
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Protein Domain
IPR022105 | DUF3645
Type: Domain
Description: This domain family is found in eukaryotes, and is approximately 40 amino acids in length. There is a conserved HPD sequence motif.
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Protein Domain
IPR046486 | DUF6579
Type: Family
Description: This entry represents a family of proteins that is functionally uncharacterised. This family of proteins is found in Fungi. Proteins in this family are approximately 300 amino acids in length. There are some conserved motifs, HxFF, HPD and FHLLI.
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Protein Domain
IPR028031 | DUF4460
Type: Domain
Description: This domain of unknown function has a conserved HPD sequence motif. There are two completely conserved residues (N and F) that may be functionally important. The domain is found in eukaryotic proteins, including T-cell activation inhibitor which may have a role in regulation of T cell activation or apoptosis [, ].
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Protein
D6RHM0
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: false
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Publication
17456197 | -
First Author: Sawitzki B
Year: 2007
Journal: Am J Transplant
Title: Identification of gene markers for the prediction of allograft rejection or permanent acceptance.
Volume: 7
Issue: 5
Pages: 1091-102
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Publication
19684086 | J:187570
First Author: Keeren K
Year: 2009
Journal: J Immunol
Title: Expression of tolerance associated gene-1, a mitochondrial protein inhibiting T cell activation, can be used to predict response to immune modulating therapies.
Volume: 183
Issue: 6
Pages: 4077-87
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Protein
Q66JZ4
Organism: Mus musculus/domesticus
Length: 499  
Fragment?: false
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Protein
G3X983
Organism: Mus musculus/domesticus
Length: 509  
Fragment?: false
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Publication
11836248 | J:76352
First Author: Shen Y
Year: 2002
Journal: J Biol Chem
Title: Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress.
Volume: 277
Issue: 18
Pages: 15947-56
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Publication
22771762 | J:192397
First Author: Camacho A
Year: 2012
Journal: Exp Neurol
Title: Ablation of PGC1 beta prevents mTOR dependent endoplasmic reticulum stress response.
Volume: 237
Issue: 2
Pages: 396-406
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Publication
30076962 | J:270172
First Author: Pagliarani S
Year: 2018
Journal: Biochim Biophys Acta Mol Basis Dis
Title: Glucose-free/high-protein diet improves hepatomegaly and exercise intolerance in glycogen storage disease type III mice.
Volume: 1864
Issue: 10
Pages: 3407-3417
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Publication
18057094 | J:132294
First Author: Ropelle ER
Year: 2008
Journal: Diabetes
Title: A central role for neuronal AMP-activated protein kinase (AMPK) and mammalian target of rapamycin (mTOR) in high-protein diet-induced weight loss.
Volume: 57
Issue: 3
Pages: 594-605
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Publication
31961715 | J:302634
First Author: Björnson Granqvist A
Year: 2020
Journal: Am J Physiol Renal Physiol
Title: High-protein diet accelerates diabetes and kidney disease in the BTBRob/ob mouse.
Volume: 318
Issue: 3
Pages: F763-F771
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Publication
26914452 | J:249161
First Author: Shen ZJ
Year: 2016
Journal: PLoS One
Title: Phosphate-Induced Renal Fibrosis Requires the Prolyl Isomerase Pin1.
Volume: 11
Issue: 2
Pages: e0150093
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Publication
7588220 | J:29761
First Author: Zdanowicz MM
Year: 1995
Journal: Endocrinology
Title: Effect of insulin-like growth factor I in murine muscular dystrophy.
Volume: 136
Issue: 11
Pages: 4880-6
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Publication
10051657 | J:53361
First Author: Meech R
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: A binding site for homeodomain and Pax proteins is necessary for L1 cell adhesion molecule gene expression by Pax-6 and bone morphogenetic proteins.
Volume: 96
Issue: 5
Pages: 2420-5
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Publication
31028147 | J:276281
First Author: Kamada T
Year: 2019
Journal: Proc Natl Acad Sci U S A
Title: PD-1+ regulatory T cells amplified by PD-1 blockade promote hyperprogression of cancer.
Volume: 116
Issue: 20
Pages: 9999-10008
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Publication
22295104 | J:184296
First Author: Naville D
Year: 2012
Journal: PLoS One
Title: Link between intestinal CD36 ligand binding and satiety induced by a high protein diet in mice.
Volume: 7
Issue: 1
Pages: e30686
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Publication
35681705 | J:326610
 
First Author: Zhu L
Year: 2022
Journal: Cancers (Basel)
Title: Differential Effects of Dietary Macronutrients on the Development of Oncogenic KRAS-Mediated Pancreatic Ductal Adenocarcinoma.
Volume: 14
Issue: 11
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Protein
D3Z4I5
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: false
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Protein
A0A0G2JGN9
Organism: Mus musculus/domesticus
Length: 22  
Fragment?: true
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Protein
A0A087WSK1
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: false
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Protein
F6WN43
Organism: Mus musculus/domesticus
Length: 37  
Fragment?: true
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Protein Domain
IPR036869 | J_dom_sf
Type: Homologous_superfamily
Description: The hsp70 chaperone machine performs many diverse roles in the cell, including folding of nascent proteins, translocation of polypeptides across organelle membranes, coordinating responses to stress, and targeting selected proteins for degradation. DnaJ is a member of the hsp40 family of molecular chaperones, which is also called the J-protein family, the members of which regulate the activity of hsp70s. DnaJ (hsp40) binds to dnaK (hsp70) and stimulates its ATPase activity, generating the ADP-bound state of dnaK, which interacts stably with the polypeptide substrate [, ]. Structurally, the DnaJ protein consists of an N-terminal conserved domain (called 'J' domain) of about 70 amino acids, a glycine-rich region ('G' domain') of about 30 residues, a central domain containing four repeats of a CXXCXGXG motif ('CRR' domain) and a C-terminal region of 120 to 170 residues.Such a structure is shown in the following schematic representation:+------------+-+-------+-----+-----------+--------------------------------+| J-domain | | Gly-R | | CXXCXGXG | C-terminal |+------------+-+-------+-----+-----------+--------------------------------+The structure of the J-domain has been solved []. The J domain consists of four helices, the second of which has a charged surface that includes basic residues that are essential for interaction with the ATPase domain of hsp70 []. J-domains are found in many prokaryotic and eukaryotic proteins []. In yeast, three J-like proteins have been identified containing regions closely resembling a J-domain, but lacking the conserved HPD motif - these proteins do not appear to act as molecular chaperones [].
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Protein Domain
IPR001623 | DnaJ_domain
Type: Domain
Description: The hsp70 chaperone machine performs many diverse roles in the cell, including folding of nascent proteins, translocation of polypeptides across organelle membranes, coordinating responses to stress, and targeting selected proteins for degradation. DnaJ is a member of the hsp40 family of molecular chaperones, which is also called the J-protein family, the members of which regulate the activity of hsp70s. DnaJ (hsp40) binds to dnaK (hsp70) and stimulates its ATPase activity, generating the ADP-bound state of dnaK, which interacts stably with the polypeptide substrate [, ]. Structurally, the DnaJ protein consists of an N-terminal conserved domain (called 'J' domain) of about 70 amino acids, a glycine-rich region ('G' domain') of about 30 residues, a central domain containing four repeats of a CXXCXGXG motif ('CRR' domain) and a C-terminal region of 120 to 170 residues.Such a structure is shown in the following schematic representation:+------------+-+-------+-----+-----------+--------------------------------+| J-domain | | Gly-R | | CXXCXGXG | C-terminal |+------------+-+-------+-----+-----------+--------------------------------+The structure of the J-domain has been solved []. The J domain consists of four helices, the second of which has a charged surface that includes basic residues that are essential for interaction with the ATPase domain of hsp70 []. J-domains are found in many prokaryotic and eukaryotic proteins []. In yeast, three J-like proteins have been identified containing regions closely resembling a J-domain, but lacking the conserved HPD motif - these proteins do not appear to act as molecular chaperones [].
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Protein Domain
IPR018253 | DnaJ_domain_CS
Type: Conserved_site
Description: The hsp70 chaperone machine performs many diverse roles in the cell, including folding of nascent proteins, translocation of polypeptides across organelle membranes, coordinating responses to stress, and targeting selected proteins for degradation. DnaJ is a member of the hsp40 family of molecular chaperones, which is also called the J-protein family, the members of which regulate the activity of hsp70s. DnaJ (hsp40) binds to dnaK (hsp70) and stimulates its ATPase activity, generating the ADP-bound state of dnaK, which interacts stably with the polypeptide substrate [, ]. Structurally, the DnaJ protein consists of an N-terminal conserved domain (called 'J' domain) of about 70 amino acids, a glycine-rich region ('G' domain') of about 30 residues, a central domain containing four repeats of a CXXCXGXG motif ('CRR' domain) and a C-terminal region of 120 to 170 residues.Such a structure is shown in the following schematic representation:+------------+-+-------+-----+-----------+--------------------------------+| J-domain | | Gly-R | | CXXCXGXG | C-terminal |+------------+-+-------+-----+-----------+--------------------------------+The structure of the J-domain has been solved []. The J domain consists of four helices, the second of which has a charged surface that includes basic residues that are essential for interaction with the ATPase domain of hsp70 []. J-domains are found in many prokaryotic and eukaryotic proteins []. In yeast, three J-like proteins have been identified containing regions closely resembling a J-domain, but lacking the conserved HPD motif - these proteins do not appear to act as molecular chaperones []. This entry represents a conserved site found within the J-domain.
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Protein
Q9CQ94
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: false
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Protein
Q8VCE1
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
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Protein
Q78YY6
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q8CHS2
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
Q9D844
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: false
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Protein
Q921R4
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
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Protein
P59041
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
A2ALW5
Organism: Mus musculus/domesticus
Length: 357  
Fragment?: false
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Protein
Q6NZB0
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: false
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Protein
Q9R022
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: false
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Protein
Q9CQV7
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
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Protein
Q9CRX9
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
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Protein
A2ALF0
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
F6QIL6
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
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Protein
K3W4M1
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: false
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Protein
A0A0G2JEI3
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: false
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Protein
F6UL52
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Protein
F8WH68
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
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Protein
G3X8S1
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
Q9CY89
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: false
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Protein
Q9D5A2
Organism: Mus musculus/domesticus
Length: 226  
Fragment?: false
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Protein
E9Q1L7
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
D3Z0T8
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
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Protein
Q8C4S9
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
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Protein
A2ALF2
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: false
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Protein
A2ALF3
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
G5E8V6
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: false
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Protein
A0A087WPZ9
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: false
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Protein
Q6IS32
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: true
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Protein
Q8BLF3
Organism: Mus musculus/domesticus
Length: 678  
Fragment?: false
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Protein
F2Z3Z8
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
A0A1W2P8C3
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: true
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Protein
D3Z5K6
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: false
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Protein
F6TQL3
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: true
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Protein
D3Z032
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: true
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Protein
Q6P8Z3
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
Q04190
Organism: Mus musculus/domesticus
Length: 195  
Fragment?: false
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Protein
F6YK70
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Protein
Q04188
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
Q9DBI3
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
F2Z410
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: false
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Protein
Q7TMI2
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: true
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Protein
Q80ZP0
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
Q6GTN1
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
Q9CQV1
Organism: Mus musculus/domesticus
Length: 125  
Fragment?: false
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Protein
A0A1L1SQA2
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: false
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Protein
Q8CCS1
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: false
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Protein
O35723
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: false
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Protein
Q149L6
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
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Protein
Q9QYI8
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
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Protein
Q9QYI7
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
Q9QYI6
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: false
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Protein
Q91WN1
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: false
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Protein
Q9CZJ9
Organism: Mus musculus/domesticus
Length: 357  
Fragment?: false
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Protein
O54946
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: false
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Protein
P60904
Organism: Mus musculus/domesticus
Length: 198  
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