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Search results 1901 to 2000 out of 2368 for Tpr

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0.12s

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Hits by Strain

Type Details Score
Protein
F6YFR7
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: true
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Protein
F7D926
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: true
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Protein
Q3THG2
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q3TXN6
Organism: Mus musculus/domesticus
Length: 715  
Fragment?: true
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Protein
Q3UK65
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
Q3UWW9
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q3UYM1
Organism: Mus musculus/domesticus
Length: 614  
Fragment?: false
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Protein
Q3V3N6
Organism: Mus musculus/domesticus
Length: 450  
Fragment?: false
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Protein
Q497E8
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q5BKQ9
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q7TMI0
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: true
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Protein
Q8BK73
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q8C0Z6
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: true
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Protein
Q8C1T5
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
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Protein
Q8K2N7
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: true
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Protein
Q9CXX1
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
Q9D1J2
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: false
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Protein
Q9JLP4
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: true
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Protein
Z4YLI8
Organism: Mus musculus/domesticus
Length: 1302  
Fragment?: false
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Protein
A0A338P7I7
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: true
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Protein
A0JLP6
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: true
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Protein
A0PJ90
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: true
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Protein
A2AQE4
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
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Protein
D6RHL2
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
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Protein
F6R2A2
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: true
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Protein
F6TM12
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: true
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Protein
F6Z1R4
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: true
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Protein
F8VPV8
Organism: Mus musculus/domesticus
Length: 1318  
Fragment?: false
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Protein
Q05CS8
Organism: Mus musculus/domesticus
Length: 687  
Fragment?: true
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Protein
Q32P08
Organism: Mus musculus/domesticus
Length: 785  
Fragment?: true
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Protein
Q3TJ98
Organism: Mus musculus/domesticus
Length: 306  
Fragment?: true
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Protein
Q3TZB5
Organism: Mus musculus/domesticus
Length: 819  
Fragment?: true
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Protein
Q8BU18
Organism: Mus musculus/domesticus
Length: 681  
Fragment?: true
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Protein
Q8BX21
Organism: Mus musculus/domesticus
Length: 586  
Fragment?: true
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Protein
Q8C1T2
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
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Protein
Q8CE71
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
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Protein
Q8K2I5
Organism: Mus musculus/domesticus
Length: 504  
Fragment?: true
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Protein
Q9JIK6
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: true
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Publication
11551174 | -
First Author: Andrade MA
Year: 2001
Journal: J Struct Biol
Title: Protein repeats: structures, functions, and evolution.
Volume: 134
Issue: 2-3
Pages: 117-31
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Protein Domain
IPR060204 | FANCG_N
Type: Domain
Description: This entry represents the N-terminal TPR domain of Fanconi anemia group G protein (FANCG). FANCG contains four tetratricopeptide repeat (TPR) domains that mediate protein-protein interactions. The specific function of this N-terminal TPR domain remains to be determined.Fanconi anemia (FA) is a human disorder characterised by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. This entry represents FANCG, which is part of the FA core complex required for the monoubiquitylation of FANCD2 and the FANCI heterodimer. FANCG is a DNA repair protein that operates in interstrand DNA cross-link repair and maintenance of normal chromosome stability [, ]. The protein belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL and FANCM. The protein localises to the nucleus and is highly expressed in testis and thymus. Mutations in FANCG cause Fanconi anemia complementation group G. The FA complex coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination []. Besides being part of the FA complex, FANCG also promotes formation of a protein complex containing BRCA2, FANCD2 and XRCC3 [].
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Protein
Q6NS46
Organism: Mus musculus/domesticus
Length: 1862  
Fragment?: false
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Protein
A2ALS3
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: true
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Publication
29271416 | -
First Author: Rao Q
Year: 2018
Journal: Cell Res
Title: Cryo-EM structure of human ATR-ATRIP complex.
Volume: 28
Issue: 2
Pages: 143-156
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Protein Coding Gene
MGI:1930089 | Mcm3ap
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2385621 | Nup153
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1097706 | Cetn3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1916732 | Nup35
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
18772196 | J:384688
First Author: Heidrych P
Year: 2008
Journal: Hum Mol Genet
Title: Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form.
Volume: 17
Issue: 23
Pages: 3814-21
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Publication
18329369 | J:137430
First Author: Pohl C
Year: 2008
Journal: Cell
Title: Final stages of cytokinesis and midbody ring formation are controlled by BRUCE.
Volume: 132
Issue: 5
Pages: 832-45
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Publication
9016560 | J:38553
First Author: Bovia F
Year: 1997
Journal: Nucleic Acids Res
Title: The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog.
Volume: 25
Issue: 2
Pages: 318-26
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Publication
29934347 | J:264331
First Author: Lizama BN
Year: 2018
Journal: J Neurosci
Title: Neuronal Preconditioning Requires the Mitophagic Activity of C-terminus of HSC70-Interacting Protein.
Volume: 38
Issue: 31
Pages: 6825-6840
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Publication
34048282 | J:312131
First Author: Mitchell R
Year: 2021
Journal: Am J Physiol Heart Circ Physiol
Title: Ifetroban reduces coronary artery dysfunction in a mouse model of Duchenne muscular dystrophy.
Volume: 321
Issue: 1
Pages: H52-H58
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Publication
12172320 | J:106000
First Author: Kubis N
Year: 2002
Journal: J Hypertens
Title: Role of microvascular rarefaction in the increased arterial pressure in mice lacking for the endothelial nitric oxide synthase gene (eNOS3pt-/- ).
Volume: 20
Issue: 8
Pages: 1581-7
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Protein
O70145
Organism: Mus musculus/domesticus
Length: 525  
Fragment?: false
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Publication
25457167 | -
First Author: Saksouk N
Year: 2014
Journal: Mol Cell
Title: Redundant mechanisms to form silent chromatin at pericentromeric regions rely on BEND3 and DNA methylation.
Volume: 56
Issue: 4
Pages: 580-94
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Protein
A0A1C7CYV2
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
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Protein
A0A1L1SSB5
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Protein
A0A1L1SU50
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
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Protein
A0A494B8X4
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
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Publication
14761955 | -
First Author: Lee YT
Year: 2004
Journal: J Biol Chem
Title: Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain.
Volume: 279
Issue: 16
Pages: 16511-7
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Publication
12372593 | -
First Author: Garcia-Ranea JA
Year: 2002
Journal: FEBS Lett
Title: p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families.
Volume: 529
Issue: 2-3
Pages: 162-7
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Publication
14576278 | -
First Author: Sickmann A
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: The proteome of Saccharomyces cerevisiae mitochondria.
Volume: 100
Issue: 23
Pages: 13207-12
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Publication
26100909 | -
First Author: Khan A
Year: 2015
Journal: Proc Natl Acad Sci U S A
Title: BEND3 represses rDNA transcription by stabilizing a NoRC component via USP21 deubiquitinase.
Volume: 112
Issue: 27
Pages: 8338-43
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Publication
21914818 | -
First Author: Sathyan KM
Year: 2011
Journal: J Cell Sci
Title: A BEN-domain-containing protein associates with heterochromatin and represses transcription.
Volume: 124
Issue: Pt 18
Pages: 3149-63
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Publication
26507581 | -
First Author: Khan A
Year: 2015
Journal: Transcription
Title: BEND3 mediates transcriptional repression and heterochromatin organization.
Volume: 6
Issue: 5
Pages: 102-5
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Publication
28977671 | -
First Author: Pitchai GP
Year: 2017
Journal: Nucleic Acids Res
Title: A novel TPR-BEN domain interaction mediates PICH-BEND3 association.
Volume: 45
Issue: 19
Pages: 11413-11424
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Publication
26060179 | -
 
First Author: Male G
Year: 2015
Journal: Nat Commun
Title: Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly.
Volume: 6
Pages: 7387
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Publication
12538866 | -
First Author: Sinars CR
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes.
Volume: 100
Issue: 3
Pages: 868-73
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Publication
20145257 | -
First Author: Roudier F
Year: 2010
Journal: Plant Cell
Title: Very-long-chain fatty acids are involved in polar auxin transport and developmental patterning in Arabidopsis.
Volume: 22
Issue: 2
Pages: 364-75
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Publication
11350175 | -
First Author: Pirkl F
Year: 2001
Journal: J Mol Biol
Title: Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40.
Volume: 308
Issue: 4
Pages: 795-806
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Publication
12857804 | -
First Author: Harrar Y
Year: 2003
Journal: Plant Physiol
Title: Hormonal control of cell proliferation requires PASTICCINO genes.
Volume: 132
Issue: 3
Pages: 1217-27
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Publication
21730050 | -
First Author: Gallo LI
Year: 2011
Journal: J Biol Chem
Title: The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress.
Volume: 286
Issue: 34
Pages: 30152-60
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Publication
26101251 | -
First Author: Romano S
Year: 2015
Journal: Nucleic Acids Res
Title: FKBP51 employs both scaffold and isomerase functions to promote NF-?B activation in melanoma.
Volume: 43
Issue: 14
Pages: 6983-93
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Publication
28147277 | -
First Author: Yu J
Year: 2017
Journal: Cell Rep
Title: Regulation of Serine-Threonine Kinase Akt Activation by NAD(+)-Dependent Deacetylase SIRT7.
Volume: 18
Issue: 5
Pages: 1229-1240
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Publication
28363942 | -
First Author: Luo K
Year: 2017
Journal: EMBO J
Title: USP49 negatively regulates tumorigenesis and chemoresistance through FKBP51-AKT signaling.
Volume: 36
Issue: 10
Pages: 1434-1446
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Publication
31434731 | -
 
First Author: DeDiego ML
Year: 2019
Journal: J Virol
Title: Novel Functions of IFI44L as a Feedback Regulator of Host Antiviral Responses.
Volume: 93
Issue: 21
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Publication
24945353 | -
First Author: Fournier G
Year: 2014
Journal: PLoS Pathog
Title: Recruitment of RED-SMU1 complex by Influenza A Virus RNA polymerase to control Viral mRNA splicing.
Volume: 10
Issue: 6
Pages: e1004164
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Publication
8553072 | -
First Author: Sanchez Y
Year: 1996
Journal: Science
Title: Regulation of RAD53 by the ATM-like kinases MEC1 and TEL1 in yeast cell cycle checkpoint pathways.
Volume: 271
Issue: 5247
Pages: 357-60
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Publication
11095737 | -
First Author: Mallory JC
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Protein kinase activity of Tel1p and Mec1p, two Saccharomyces cerevisiae proteins related to the human ATM protein kinase.
Volume: 97
Issue: 25
Pages: 13749-54
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Publication
16365046 | -
First Author: Ma JL
Year: 2006
Journal: J Biol Chem
Title: Activation of the checkpoint kinase Rad53 by the phosphatidyl inositol kinase-like kinase Mec1.
Volume: 281
Issue: 7
Pages: 3954-63
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Publication
15369670 | -
First Author: Lisby M
Year: 2004
Journal: Cell
Title: Choreography of the DNA damage response: spatiotemporal relationships among checkpoint and repair proteins.
Volume: 118
Issue: 6
Pages: 699-713
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Publication
9512710 | -
First Author: Koulich D
Year: 1998
Journal: J Mol Biol
Title: Distinct functions of N and C-terminal domains of GreA, an Escherichia coli transcript cleavage factor.
Volume: 276
Issue: 2
Pages: 379-89
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Publication
33169019 | -
First Author: Tannous EA
Year: 2021
Journal: Nat Struct Mol Biol
Title: Mechanism of auto-inhibition and activation of Mec1(ATR) checkpoint kinase.
Volume: 28
Issue: 1
Pages: 50-61
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Publication
31743518 | -
First Author: Xu H
Year: 2020
Journal: Mol Microbiol
Title: BB0326 is responsible for the formation of periplasmic flagellar collar and assembly of the stator complex in Borrelia burgdorferi.
Volume: 113
Issue: 2
Pages: 418-429
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Publication
19763088 | -
First Author: Liu Y
Year: 2009
Journal: EMBO J
Title: A longevity protein, Lag2, interacts with SCF complex and regulates SCF function.
Volume: 28
Issue: 21
Pages: 3366-77
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Publication
19942853 | -
First Author: Siergiejuk E
Year: 2009
Journal: EMBO J
Title: Cullin neddylation and substrate-adaptors counteract SCF inhibition by the CAND1-like protein Lag2 in Saccharomyces cerevisiae.
Volume: 28
Issue: 24
Pages: 3845-56
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Protein Domain
IPR000160 | GGDEF_dom
Type: Domain
Description: The GGDEF domain, which has been named after the conserved central sequence pattern GG[DE][DE]F is widespread in prokaryotes. It is typically present in multidomain proteins containing regulatory domains of signalling pathways or protein-protein or protein-ligand interaction modules, such as the response regulatory domain, the PAS/PAC domain, the HAMP domain, the GAF domain, the FHA domain or the TPR repeat. However a few single-domain proteins are also known. The GGDEF domain is involved in signal transduction and is likely to catalyse synthesis or hydrolysis of cyclic diguanylate (c-diGMP, bis(3',5')-cyclic diguanylic acid), an effector molecule that consists of two cGMP moieties bound head-to-tail [, , ].Structural studies of PleD from Caulobacter crescentus show that this domain forms a five-stranded ��-sheet surrounded by helices, similar to the catalytic core of adenylate cyclase [].
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Protein Domain
IPR048058 | Rrp5_S1_rpt_hs11_sc8
Type: Domain
Description: This entry represents the S1 repeat 11 from Homo sapiens Rrp5 (hs11) and S1 repeat 8 in S. cerevisiae (sc8).Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2.Rrp5 is involved in the biogenesis of rRNA. It is required for formation of both 18S and 5.8S rRNA in budding yeasts []. In humans, it is also known as NFBP, which is essential for the generation of 18S rRNA []. In Arabidopsis, it is essential for normal development of female gametophytes [].
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Protein Domain
IPR048059 | Rrp5_S1_rpt_hs1_sc1
Type: Domain
Description: This entry represents the first S1 from both Homo sapiens Rrp5 (hs1) and S. cerevisiae (sc1).Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2.Rrp5 is involved in the biogenesis of rRNA. It is required for formation of both 18S and 5.8S rRNA in budding yeasts []. In humans, it is also known as NFBP, which is essential for the generation of 18S rRNA []. In Arabidopsis, it is essential for normal development of female gametophytes [].
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Protein Domain
IPR007052 | CS_dom
Type: Domain
Description: The bipartite CS domain, which was named after CHORD-containing proteins and SGT1 [], is a ~100-residue protein-protein interaction module. The CS domain can be found in stand-alone form, as well as fused with other domains, such as CHORD (), SGS (), TPR (), cytochrome b5 () or b5 reductase, in multidomain proteins [].The CS domain has a compact antiparallel ��-sandwich fold consisting of seven ��-strands [, ].Some proteins known to contain a CS domain are listed below []:Eukaryotic proteins of the SGT1 family.Eukaryotic Rar1, related to pathogenic resistance in plants, and to development in animals.Eukaryotic nuclear movement protein nudC.Eukaryotic proteins of the p23/wos2 family, which act as co-chaperone.Animal b5+b5R flavo-hemo cytochrome NAD(P)H oxydoreductase type B.Mammalian integrin beta-1-binding protein 2 (melusin).
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Protein Domain
IPR039694 | WDR11
Type: Family
Description: Members of the WDR11 family share a domain architecture consisting of two ��-propellers followed by a TPR domain. WDR11 has been implicated in human developmental genetic disorders characterised by delayed puberty and infertility. WDR11 modulates the Hedgehog (Hh) signalling pathway and is essential for adequate ciliogenesis []. The ��-propellers in WDR11 are involved in protein-protein interaction. This are essential for proper interaction with EMX1, a homeodomain transcription factor involved in the development of olfactory neurons. Impaired pubertal development is suggested to result from a deficiency of productive WDR11 protein interaction []. WDR11 is also involved in vesicle traffic as it binds TBC1D23, a vesicle-golgin adaptor required for endosome-to-Golgi trafficking []. WDR11 is part of the WDR11 complex (consisting of WDR11, C17orf75 and FAM91A) that facilitates the tethering of AP-1-derived vesicles []. Mutations of the WDR11 gene have been linked to congenital hypogonadotropic hypogonadism (CHH) and Kallmann syndrome (KS), human developmental genetic disorders defined by delayed puberty and infertility [].
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Protein Domain
IPR049125 | FAN1-like_WH
Type: Domain
Description: This entry represents the WH domain of FAN1 and similar proteins mainly from eukaryotes and proteobacteria.Fanconi-associated nuclease 1 (FAN1) is a DNA structure-specific nuclease involved in the processing of DNA interstrand crosslinks (ICLs). It maintains genomic stability and prevents tissue decline in several organs. This protein possesses preferential endonuclease activity toward 5' flap structures. FAN1 is present in most eukaryotes and some bacterial sequences. It consists of four characterised domains: UBZ, SAP, TPR and VRR nuclease (). However, monocellular eukaryote and bacterial homologues lack the UBZ domain []. The N-terminal helical domain of FAN1 can be subdivided in a winged-helix (WH) DNA-binding domain, represented in this entry, and a SAP domain (bacterial and eukaryotic ) [, , , , ].
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Protein Domain
IPR050754 | FKBP4/5/8-like
Type: Family
Description: This family of proteins includes immunophilins with peptidyl-prolyl cis-trans isomerase (PPIase) and co-chaperone activities such as Peptidyl-prolyl cis-trans isomerase FKBP4/5 [, ]. FKBP4/5 are also involved in the intracellular trafficking of steroid hormone receptors and play a role in maintaining these receptors in the cytoplasm when unliganded []. FKBP4/5 regulate Akt/AKT1 activity by promoting interaction with PHLPP1, enhancing Akt/AKT1 dephosphorylation and activation [, ]. They also interact with components of the NF-kappaB signaling pathway, influencing kinase activity and IFN production [, ]. FKBP4 plays a role in microtubule dynamics, neuronal growth cone regulation, and may protect against oxidative stress in mitochondria []. Others are involved in protein folding, cell division, adhesion, elongation, and hormonal control of plant development, such as Peptidyl-prolyl cis-trans isomerase PASTICCINO1 from Arabidopsis [, ]. The family is characterised by the presence of TPR repeats and FKBP-type domains.
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Protein Domain
IPR051134 | PPP_phosphatase
Type: Family
Description: The PPP phosphatase family is involved in a variety of cellular processes including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels, circadian rhythms, and phototransduction. Members of the family dephosphorylate a wide range of proteins such as kinases, nuclear receptors, SMAD proteins, and TAU/MAPT, influencing signaling pathways related to steroid and thyroid hormones, calcium, fatty acids, TGF-beta, oxidative and genotoxic stresses. They participate in DNA damage response mechanisms, checkpoint activation, and DNA damage repair. Some members regulate adipogenesis and circadian rhythms, while others are implicated in the regulation of the Hsp90 chaperone machinery and photoreceptor function. The family includes subfamilies such as PP-5 (PP-T) and PP-7, with some members possessing TPR repeats for protein-protein interactions and autoinhibition, or EF-hands for calcium activation.
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Protein Domain
IPR051476 | Bac_ResReg_Asp_Phosphatase
Type: Family
Description: The Rap family proteins are bacterial response regulators with diverse roles in cellular processes such as sporulation and competence development. Members of the family act as aspartate phosphatases, targeting specific response regulators like Spo0F, thereby modulating sporulation initiation. Some Rap proteins also bind to the transcriptional factor ComA, inhibiting its DNA-binding activity and affecting the development of genetic competence. The family is characterized by a conserved domain architecture, including an N-terminal 3-helix bundle domain and a C-terminal TPR domain, which is involved in substrate and inhibitor interactions. Regulatory activity of Rap proteins is often modulated by specific peptide inhibitors, such as Phr peptides, which induce conformational changes that affect their binding and phosphatase activities.
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Protein Domain
IPR051727 | DnaJ_C3_Co-chaperones
Type: Family
Description: The DnaJ homolog subfamily C member 3 protein family is involved in various stress response mechanisms, particularly the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Family members act as co-chaperones, interacting with molecular chaperones such as HSPA8/HSC70 to stimulate ATPase activity and assist in protein folding. They play roles in inhibiting the phosphorylation of eIF-2-alpha, thus regulating protein synthesis under stress conditions. Some members are implicated in cold adaptation, virulence factor production, and ER homeostasis. They may also participate in nuclear membrane fusion during mating and contribute to cell wall architecture maintenance. The family is characterized by the presence of TPR repeats, which mediate interaction with unfolded polypeptides, and a J domain essential for chaperone activity enhancement.
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Protein Domain
IPR051864 | NCF2_NOXA1
Type: Family
Description: The NCF2/NOXA1 family comprises proteins that play a crucial role in the activation of NADPH oxidases, which are enzymes responsible for the production of superoxide and other reactive oxygen species (ROS). These ROS are involved in various biological processes, including host defense mechanisms, hormone biosynthesis, oxygen sensing, and signal transduction. Members of the NCF2/NOXA1 family typically contain domains such as OPR/PB1, SH3, and TPR repeats, which facilitate interactions with other proteins in the NADPH oxidase complex, such as NCF1, NCF4/p40-PHOX, and RAC1. The coordinated action of these proteins is essential for the activation of the latent NADPH oxidase complex, leading to the generation of superoxide, which is necessary for microbial killing and cellular signaling.
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Protein Domain
IPR056159 | Beta-prop_IFT121_TULP_N
Type: Domain
Description: This entry represents a ��-propeller domain found at the N-terminal of IFT121 (which corresponds to the first one) and TULP4 proteins. TULP4 may be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex. IFT-A polymerises and interacts with IFT-B, and uses an array of ��-propeller and TPR domains to create 'carriages' of the IFT train that engage TULP adaptor proteins []. Proteins in this entry are part of the non-core subcomplex, together with IFT43 and IFT139 [, ].IFT121 (also known as WDR35) is a component of the IFT complex A (IFT-A), which is required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors that is involved in ciliogenesis and ciliary protein trafficking [, , ]. This protein plays a role in cilia assembly and maintenance [, , ]. IFT121 contains a zinc finger with rubredoxin-like fold []. Knock-out IFT121 cells showed defective retrograde trafficking within cilia [].
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Protein Domain
IPR056153 | IFT122/SMU1_beta-prop
Type: Domain
Description: This entry represents a ��-propeller found at the N-terminal end of IFT122 and at the C-terminal of SMU1. Members of this group are found in eukaryotes and bacteria.Intraflagellar transport protein 122 homolog (IFT122) is one of the core components (together with WDR19/IFT144 and IFT140) of the IFT-A complex which is required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), being involved in cilia function and/or assembly [, ]. IFT-A polymerises interacts with IFT-B, and uses an array of ��-propeller and TPR domains to create 'carriages' of the IFT train that engage TULP adaptor proteins [].Human WD40 repeat-containing protein SMU1 is involved in pre-mRNA splicing as a component of the spliceosome [], and is required for normal accumulation of IK [].
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Protein Domain
IPR056169 | HB_ELP1
Type: Domain
Description: This entry represents the helical bundle domain found within the C-terminal dimerisation domain of Elongator complex protein 1 (ELP1), from eukaryotes.Elongator is a conserved protein complex implicated in multiple processes including regulation of transcription, alpha-tubulin acetylation and tRNA modification. Mutations in the ELP1 gene have been shown to cause the neurodegenerative disease familial dysautonomia []. The C-terminal dimerisation domain consists of 28 ��-helices organised in three domains: an elongated ��-solenoid domain (helices 1 to 14); a TPR domain, formed by six double-helix repeats (helices 15 to 26); and a three-helix bundle, C-terminal cap (helices 26 to 28) []. ELP1 self-association contributes to its stability and is important for Elongator assembly []. ELP1 is considered to function both as a scaffold, for Elongator complex ELP2 and ELP3 binding, and as a docking site for various factors that regulate Elongator activity [, , ]. Also known as IKAP, ELP1 acts as a regulator of IkB kinase complex involved in proinflammatory cytokine signalling [].
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