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Search results 101 to 200 out of 511 for Erp29

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Type Details Score
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
18696346 | J:140475
First Author: Verma V
Year: 2008
Journal: Curr Eye Res
Title: Constancy of ERp29 expression in cultured retinal pigment epithelial cells in the Ccl2/Cx3cr1 deficient mouse model of age-related macular degeneration.
Volume: 33
Issue: 8
Pages: 701-7
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Allele
Tg(Erp29-EGFP)KX108Gsat | MGI:4847033
Name: transgene insertion KX108, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Reporter
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Strain
MGI:5004215 | STOCK Tg(Erp29-EGFP)KX108Gsat/Mmucd
Attribute String: mutant stock, transgenic
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Protein Domain
IPR036356 | ERp29_C_sf
Type: Homologous_superfamily
Description: ERp29 (also known as ERp28 and ERp31) is a ubiquitously expressed endoplasmic reticulum protein found in mammals []. This protein has an N-terminal thioredoxin-like domain, which is homologous to the domain of human protein disulphide isomerase (PDI). ERp29 may help mediate the chaperone function of PDI. The C-terminal Erp29 domain has a 5-helical bundle fold. ERp29 is thought to form part of the thyroglobulin folding complex []. The Drosophila homologue, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe [].
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Protein Domain
IPR011679 | ERp29_C
Type: Domain
Description: ERp29 (also known as ERp28 and ERp31) is a ubiquitously expressed endoplasmic reticulum protein found in mammals []. This protein has an N-terminal thioredoxin-like domain, which is homologous to the domain of human protein disulphide isomerase (PDI). ERp29 may help mediate the chaperone function of PDI. The C-terminal Erp29 domain has a 5-helical bundle fold. ERp29 is thought to form part of the thyroglobulin folding complex []. The Drosophila homologue, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe [].
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Publication
18421225 | J:190363
First Author: Chan CC
Year: 2008
Journal: Ophthalmic Res
Title: Ccl2/Cx3cr1-deficient mice: an animal model for age-related macular degeneration.
Volume: 40
Issue: 3-4
Pages: 124-8
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Publication
36936785 | J:350827
First Author: Li J
Year: 2023
Journal: iScience
Title: Non-canonical function of DPP4 promotes cognitive impairment through ERp29-associated mitochondrial calcium overload in diabetes.
Volume: 26
Issue: 3
Pages: 106271
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Publication
10727933 | -
First Author: Hubbard MJ
Year: 2000
Journal: Eur J Biochem
Title: Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells. Evidence for a unique role in secretory-protein synthesis.
Volume: 267
Issue: 7
Pages: 1945-57
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Protein Domain
IPR012883 | ERp29_N
Type: Domain
Description: ERp29 () is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle [, ]. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organised into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI) []. However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that the function of ERp29 is similar to the chaperone function of PDI []. The N-terminal domain is exclusively responsible for the homodimerisation of the protein, without covalent linkages or additional contacts with other domains [].The Drosophila homologue, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase [].
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Publication
36302455 | J:331591
 
First Author: Hui Y
Year: 2023
Journal: Metabolism
Title: Nonenzymatic function of DPP4 promotes diabetes-associated cognitive dysfunction through IGF-2R/PKA/SP1/ERp29/IP3R2 pathway-mediated impairment of Treg function and M1 microglia polarization.
Volume: 138
Pages: 155340
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Publication
31156553 | J:288922
 
First Author: Xu C
Year: 2019
Journal: Front Endocrinol (Lausanne)
Title: Abnormal Glucose Metabolism and Insulin Resistance Are Induced via the IRE1α/XBP-1 Pathway in Subclinical Hypothyroidism.
Volume: 10
Pages: 303
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Protein
Q8R3W7
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Protein
O88312
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
Q9CQ75
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: false
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Protein
Q9D8U3
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: false
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Protein
Q9DB60
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Publication
15120624 | -
First Author: Nardini M
Year: 2004
Journal: Biochem Biophys Res Commun
Title: Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution.
Volume: 318
Issue: 2
Pages: 470-6
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Protein
Q91VW3
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: false
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Protein
Q9D1A0
Organism: Mus musculus/domesticus
Length: 226  
Fragment?: false
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Protein
Q9WUZ7
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: false
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Protein
Q9JJU8
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Protein
Q8BG73
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: false
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Protein
Q3U9A8
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Protein
Q8C0Z0
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: true
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Protein
Q3TGK4
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
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Protein
Q80W79
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
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Protein
Q3UKU2
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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Protein
Q9CT42
Organism: Mus musculus/domesticus
Length: 238  
Fragment?: true
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Protein
A0A494B9J5
Organism: Mus musculus/domesticus
Length: 33  
Fragment?: true
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Protein
E9Q2Q9
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
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Protein
Q3UFS2
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: true
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Protein
Q8R558
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: true
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Protein
Q8C0Z4
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: false
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Protein
Q3TGU8
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: true
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Protein
A2AV98
Organism: Mus musculus/domesticus
Length: 42  
Fragment?: true
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Protein
Q9CRQ1
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: true
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Protein
D6RGN4
Organism: Mus musculus/domesticus
Length: 29  
Fragment?: true
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Protein
A0A3B2WB97
Organism: Mus musculus/domesticus
Length: 299  
Fragment?: false
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Protein
A0A1Y7VJW5
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
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Protein
D3Z3Z9
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
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Protein
M0QWP9
Organism: Mus musculus/domesticus
Length: 59  
Fragment?: true
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Protein
A0A217FL55
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: true
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Protein
A0A1C7ZMY4
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
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Protein
Q05C23
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: true
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Protein
Q8C073
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: false
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Protein
A0A3B2WCC8
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
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Protein
D3Z2H4
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: true
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Protein
A0A0A6YVV3
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: false
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Protein
A0A087WQU5
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: false
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Protein
F6X737
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
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Protein
A0A1Y7VL91
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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Protein
A0A087WS96
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: false
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Protein
A0A1Y7VKZ8
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: true
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Protein
Q9D8Q5
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: false
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Publication
15862094 | -
 
First Author: Buchanan BB
Year: 2005
Journal: Annu Rev Plant Biol
Title: Redox regulation: a broadening horizon.
Volume: 56
Pages: 187-220
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Publication
10610776 | J:58887
First Author: Reuter K
Year: 1999
Journal: J Mol Biol
Title: Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein.
Volume: 294
Issue: 2
Pages: 515-25
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Publication
9300489 | -
First Author: Guddat LW
Year: 1997
Journal: Protein Sci
Title: Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
Volume: 6
Issue: 9
Pages: 1893-900
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Publication
1304339 | -
First Author: Xia TH
Year: 1992
Journal: Protein Sci
Title: NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Volume: 1
Issue: 3
Pages: 310-21
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Publication
12089152 | -
First Author: Yeh AP
Year: 2002
Journal: J Biol Chem
Title: High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus.
Volume: 277
Issue: 37
Pages: 34499-507
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Publication
12529327 | -
First Author: Kim SJ
Year: 2003
Journal: J Biol Chem
Title: The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteins.
Volume: 278
Issue: 12
Pages: 10790-8
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Publication
15341729 | -
First Author: Brockmann C
Year: 2004
Journal: Structure
Title: The oxidized subunit B8 from human complex I adopts a thioredoxin fold.
Volume: 12
Issue: 9
Pages: 1645-54
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Publication
10383197 | -
First Author: Kemmink J
Year: 1999
Journal: J Biomol NMR
Title: The structure in solution of the b domain of protein disulfide isomerase.
Volume: 13
Issue: 4
Pages: 357-68
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Publication
8898209 | -
First Author: Gaudet R
Year: 1996
Journal: Cell
Title: Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin.
Volume: 87
Issue: 3
Pages: 577-88
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Publication
2181145 | -
First Author: Katti SK
Year: 1990
Journal: J Mol Biol
Title: Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution.
Volume: 212
Issue: 1
Pages: 167-84
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Publication
16597834 | -
First Author: Téllez-Sanz R
Year: 2006
Journal: Protein Sci
Title: Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1.
Volume: 15
Issue: 5
Pages: 1093-105
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Protein Domain
IPR036249 | Thioredoxin-like_sf
Type: Homologous_superfamily
Description: Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2), where a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system, the NADP/thioredoxin system, and the glutathione/glutaredoxin system []. Several of these disulphide proteins share a common structure, consisting of a three-layer α/β/α core. Proteins that contain domains with a thioredoxin-like fold include:Arsenate reductase (ArsC) []Calsequestrin (contains three tandem repeats of this fold) []Circadian oscillation regulator KaiB []Disulphide bond isomerase DsbC and DsbG (C-terminal domain) [, ]Disulphide bond facilitator DsbA (contains an α-helical insertion) []Endoplasmic reticulum protein ERP29 (N-terminal domain) []Glutathione S-transferase (GST) (N-terminal domain) []Mitochondrial ribosomal protein L51/S25/CI-B8 domain (variable positions for Cys residues in active site) []Phosducin []Protein disulphide isomerase (PDI) (contains two tandem repeats of this fold) []Glutathione peroxidase-like enzymes []Selenoprotein W-related []SH3-binding glutamic acid-rich protein like (SH3BGR) (lacks both conserved Cys residues) []Spliceosomal protein U5-15Kd []Thioltransferases, including thioredoxin [], glutaredoxin [], hybrid peroxiredoxin hyPrx5 []Thioredoxin-like 2Fe-2S ferredoxin []
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Protein
Q8BVF2
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
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Protein
Q9CYH2
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
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Protein
Q9D125
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
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Protein
Q99N89
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
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Protein
Q8VC33
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Protein
Q9D531
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
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Protein
Q9CQM5
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
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Protein
Q8BUH1
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q78Y63
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
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Protein
P83877
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: false
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Protein
Q8VCH8
Organism: Mus musculus/domesticus
Length: 506  
Fragment?: false
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Protein
D3Z252
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: true
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Protein
Q925P6
Organism: Mus musculus/domesticus
Length: 26  
Fragment?: true
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Protein
Q3U125
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: false
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Protein
Q810B1
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: true
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Protein
D3Z0A8
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: true
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Protein
A0A0R4J078
Organism: Mus musculus/domesticus
Length: 506  
Fragment?: false
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Protein
Q8BPD3
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: false
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Protein
Q6KAU3
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
Q8BHV1
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: false
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Protein
F8WGE7
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: true
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Protein
A0A0A6YXV1
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
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Protein
Q78JM7
Organism: Mus musculus/domesticus
Length: 63  
Fragment?: false
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Protein
D3Z398
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
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Protein
Q6P060
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: true
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Protein
D3YYG8
Organism: Mus musculus/domesticus
Length: 174  
Fragment?: true
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Protein
Q5RL20
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
Q9CQ86
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
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Protein
Q3TDN2
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
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Protein
Q3UQA7
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
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Protein
P63300
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: false
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Protein
Q9ERR7
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
Q8BTV1
Organism: Mus musculus/domesticus
Length: 347  
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