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Search results 1801 to 1900 out of 12470 for Impact

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Hits by Strain

Type Details Score
HT Experiment
GSE169351 | Atlas of the aging mouse intestine
 
Experiment Type: RNA-Seq
Study Type: Baseline
Source: GEO
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HT Experiment
E-GEOD-53511 | Characterization and comparison of lactating mouse and bovine mammary gland miRNomes
Series Id: GSE53511
Experiment Type: RNA-Seq
Study Type: Baseline
Source: ArrayExpress
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HT Experiment
GSE77715 | Dissecting the Effect of Genetic Variation on the Hepatic Expression of Drug Disposition Genes across the Collaborative Cross Mouse Strains
 
Experiment Type: RNA-Seq
Study Type: Baseline
Source: GEO
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HT Experiment
GSE131377 | SPOCD1 is a novel executor of piRNA-directed DNA methylation that links MIWI2 to the de novo DNA methylation machinery
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE201181 | ELAC2 is a prostate cancer rheostat that regulates nuclear and mitochondrial RNA metabolism (miRNA-Seq)
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE217964 | Neddylation is required for perinatal cardiac development through stimulation of metabolic maturation
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE216375 | The essential roles of FXR in diet and aging affected metabolic changes and liver disease development: a multi-omics study
 
Experiment Type: RNA-Seq
Study Type: Baseline
Source: GEO
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HT Experiment
GSE193582 | Transient Polycomb activity represses developmental genes in growing oocytes.
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE198686 | Nucleoside-Diphosphate Kinase 1 and 2 are master regulators of a liver protective response to high fat diet [RNA-seq]
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Protein
Q9JLG4
Organism: Mus musculus/domesticus
Length: 621  
Fragment?: false
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Publication
29567962 | J:283187
First Author: Su Q
Year: 2018
Journal: Nat Commun
Title: Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1.
Volume: 9
Issue: 1
Pages: 1192
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Protein
Q3V2I4
Organism: Mus musculus/domesticus
Length: 520  
Fragment?: true
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Protein
A0A1D5RLT9
Organism: Mus musculus/domesticus
Length: 816  
Fragment?: true
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Protein
Q3V056
Organism: Mus musculus/domesticus
Length: 621  
Fragment?: false
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Publication
8643665 | -
First Author: Ward CJ
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: Polycystin, the polycystic kidney disease 1 protein, is expressed by epithelial cells in fetal, adult, and polycystic kidney.
Volume: 93
Issue: 4
Pages: 1524-8
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Publication
8650545 | J:48348
First Author: Mochizuki T
Year: 1996
Journal: Science
Title: PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein.
Volume: 272
Issue: 5266
Pages: 1339-42
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Publication
9326320 | -
First Author: Veldhuisen B
Year: 1997
Journal: Am J Hum Genet
Title: A spectrum of mutations in the second gene for autosomal dominant polycystic kidney disease (PKD2).
Volume: 61
Issue: 3
Pages: 547-55
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Protein
Q8C0Z9
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: true
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Publication
11013137 | -
First Author: Bassi MT
Year: 2000
Journal: Am J Hum Genet
Title: Cloning of the gene encoding a novel integral membrane protein, mucolipidin-and identification of the two major founder mutations causing mucolipidosis type IV.
Volume: 67
Issue: 5
Pages: 1110-20
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Publication
12459486 | -
First Author: LaPlante JM
Year: 2002
Journal: FEBS Lett
Title: Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway.
Volume: 532
Issue: 1-2
Pages: 183-7
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Publication
14749347 | -
First Author: Raychowdhury MK
Year: 2004
Journal: Hum Mol Genet
Title: Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel.
Volume: 13
Issue: 6
Pages: 617-27
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Publication
18656177 | -
First Author: Bonnefont J
Year: 2008
Journal: Am J Hum Genet
Title: Evolutionary forces shape the human RFPL1,2,3 genes toward a role in neocortex development.
Volume: 83
Issue: 2
Pages: 208-18
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Publication
10683446 | -
First Author: Radcliffe PA
Year: 2000
Journal: FEBS Lett
Title: A conserved small GTP-binding protein Alp41 is essential for the cofactor-dependent biogenesis of microtubules in fission yeast.
Volume: 468
Issue: 1
Pages: 84-8
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Publication
32443810 | -
 
First Author: Romano M
Year: 2020
Journal: Cells
Title: A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping.
Volume: 9
Issue: 5
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Publication
30383829 | -
First Author: Saberi A
Year: 2018
Journal: PLoS Pathog
Title: A planarian nidovirus expands the limits of RNA genome size.
Volume: 14
Issue: 11
Pages: e1007314
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Publication
28174054 | -
 
First Author: Posthuma CC
Year: 2017
Journal: Virus Res
Title: Nidovirus RNA polymerases: Complex enzymes handling exceptional RNA genomes.
Volume: 234
Pages: 58-73
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Publication
26304538 | -
First Author: Lehmann KC
Year: 2015
Journal: Nucleic Acids Res
Title: Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses.
Volume: 43
Issue: 17
Pages: 8416-34
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Protein Domain
IPR044863 | NIRAN
Type: Domain
Description: Positive-stranded RNA (+RNA) viruses that belong to the order Nidovirales infect a wide range of vertebrates (families Arteriviridae and Coronaviridae) or invertebrates (Mesoniviridae and Roniviridae). Examples of nidoviruses with high economic and societal impact are the arterivirus porcine reproductive and respiratory syndrome virus (PRRSV) and the zoonotic coronaviruses (CoVs) causing severe acute respiratory syndrome (SARS), Middle East respiratory syndrome (MERS) and Covid-19 (SARS-CoV-2) in humans. In all nidoviruses, at least two-thirds of the capacity of the polycistronic genome is occupied by the two large open reading frames (ORFs; 1a and 1b) that together constitute the replicase gene. The two polyproteins produced, pp1a (ORF1a-encoded) and pp1ab (ORF1a/ORF1b-encoded), are processed to a dozen or more proteins by the virus main protease (3CLpro, encoded in ORF1a) with possible involvement of other protease(s). These and other proteins form a membrane-bound replication-transcription complex (RTC) that invariably includes two key ORF1b-encoded subunits: the RNA-dependent RNA polymerase (RdRp) and a superfamily 1 helicase domain (HEL1), which is fused with a multinuclear Zn-binding domain (ZBD). The RNA-dependent RNA polymerase (RdRp) domain of nidoviruses resides in a cleavage product of the replicase polyprotein named non- structural protein (nsp) 12 in coronaviruses and nsp9 in arteriviruses. In all nidoviruses, the C-terminal RdRp domain is linked to a conserved N-terminal domain, which has been coined NiRAN (nidovirus RdRp-associated nucleotidyl transferase). The NiRAN domain has an essential nucleotidylation activity and its potential functions in nidovirus replication may include RNA ligation, protein-primed RNA synthesis, and the guanylyl-transferase function that is necessary for mRNA capping [, , , , ].The NiRAN domain is characterised by an α+β fold composed of eight α-helices and a five stranded β-sheet. In addition, an N-terminal β-hairpin interacts with the palm subdomain of the RdRp domain [, ].
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Protein Domain
IPR013122 | PKD1_2_channel
Type: Domain
Description: Polycystic kidney diseases (PKD) are disorders characterised by large numbers of cysts distributed throughout grossly-enlarged kidneys. Cystdevelopment is associated with impairment of kidney function, and ultimately kidney failure and death [, ]. Most cases of autosomal dominant PKD result from mutations in the PKD1 gene that cause premature protein termination. A second gene for autosomal dominant polycystic kidney disease has been identified by positional cloning []. The predicted 968-amino acid sequence of the PKD2 gene product (polycystin-2) contains 6 transmembrane domains, with intracellular N- and C-termini. Polycystin-2 shares some similarity with the family of voltage-activated calcium (and sodium) channels, and contains a potential calcium-binding domain [].Polycystin-2 is strongly expressed in ovary, foetal and adult kidney, testis, and small intestine. Polycystin-1 requires the presence of this protein for stable expression and is believed to interact with it via its C terminus. All mutations between exons 1 and 11 result in a truncated polycystin-2 that lacks a calcium-binding EF-hand domain and the cytoplasmic domains required for the interaction of polycystin-2 with polycystin-1 []. PKD2, although clinically milder than PKD1, has a deleterious impact on life expectancy.This entry contains proteins belonging to the polycystin family including Mucolipin and Polycystin-1 and -2 (PKD1 and PKD2). The domain contains the cation channel region of PKD1 and PKD2 proteins. PKD1 and PKD2 may function through a common signalling pathway that is necessary for normal tubulogenesis. The PKD2 gene product has six transmembrane spans with intracellular amino- and carboxyl-termini [].Mucolipin is a cationic channel which probably plays a role in the endocytic pathway and in the control of membrane trafficking of proteins and lipids. It could play a major role in the calcium ion transport regulating lysosomal exocytosis [, , ].
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Publication
16113345 | J:100412
First Author: Morrison SG
Year: 2005
Journal: Infect Immun
Title: The protective effect of antibody in immunity to murine chlamydial genital tract reinfection is independent of immunoglobulin A.
Volume: 73
Issue: 9
Pages: 6183-6
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Publication
24574409 | J:214428
First Author: Douet JY
Year: 2014
Journal: J Virol
Title: PrP expression level and sensitivity to prion infection.
Volume: 88
Issue: 10
Pages: 5870-2
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Publication
29610476 | J:260935
First Author: Rogers ZN
Year: 2018
Journal: Nat Genet
Title: Mapping the in vivo fitness landscape of lung adenocarcinoma tumor suppression in mice.
Volume: 50
Issue: 4
Pages: 483-486
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Publication
8016642 | J:67942
First Author: Gu H
Year: 1994
Journal: Science
Title: Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting.
Volume: 265
Issue: 5168
Pages: 103-6
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Publication
26360644 | J:263899
First Author: Herbst EA
Year: 2015
Journal: Appl Physiol Nutr Metab
Title: Changes in nuclear receptor corepressor RIP140 do not influence mitochondrial content in the cortex.
Volume: 40
Issue: 10
Pages: 1086-8
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Publication
16158063 | J:101715
First Author: Gropp E
Year: 2005
Journal: Nat Neurosci
Title: Agouti-related peptide-expressing neurons are mandatory for feeding.
Volume: 8
Issue: 10
Pages: 1289-91
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Publication
38656660 | J:354183
First Author: Rother F
Year: 2024
Journal: FASEB J
Title: Karyopherin α2 is a maternal effect gene required for early embryonic development and female fertility in mice.
Volume: 38
Issue: 8
Pages: e23623
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Publication
3471390 | J:8665
First Author: Adolph S
Year: 1987
Journal: Cytogenet Cell Genet
Title: Mapping of the oncogenes Myc, Sis, and int-1 to the distal part of mouse chromosome 15.
Volume: 44
Issue: 2-3
Pages: 65-8
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Publication
16537100 | J:111920
First Author: Boengler K
Year: 2006
Journal: Exp Gerontol
Title: Connexin 43 and ischemic preconditioning: effects of age and disease.
Volume: 41
Issue: 5
Pages: 485-8
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Publication
19029958 | J:143065
First Author: Meyer N
Year: 2008
Journal: Nat Rev Cancer
Title: Reflecting on 25 years with MYC.
Volume: 8
Issue: 12
Pages: 976-90
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Publication
19154715 | J:144984
First Author: Skwarek LC
Year: 2009
Journal: Dev Cell
Title: Great expectations for PIP: phosphoinositides as regulators of signaling during development and disease.
Volume: 16
Issue: 1
Pages: 12-20
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Publication
22841718 | J:188707
First Author: Carneiro P
Year: 2012
Journal: FEBS Lett
Title: E-cadherin dysfunction in gastric cancer--cellular consequences, clinical applications and open questions.
Volume: 586
Issue: 18
Pages: 2981-9
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Publication
23475876 | J:198393
First Author: Schnepp RW
Year: 2013
Journal: Cancer Discov
Title: Targeting MYCN: a good BET for improving neuroblastoma therapy?
Volume: 3
Issue: 3
Pages: 255-7
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Publication
25017102 | J:220138
First Author: Cordeddu V
Year: 2014
Journal: Nat Genet
Title: Mutations in ZBTB20 cause Primrose syndrome.
Volume: 46
Issue: 8
Pages: 815-7
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Publication
26530157 | J:235911
First Author: Constantinou C
Year: 2016
Journal: Am J Physiol Endocrinol Metab
Title: Advances in high-density lipoprotein physiology: surprises, overturns, and promises.
Volume: 310
Issue: 1
Pages: E1-E14
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Publication
28758997 | J:258034
First Author: Oh Y
Year: 2017
Journal: Nat Neurosci
Title: Zika virus directly infects peripheral neurons and induces cell death.
Volume: 20
Issue: 9
Pages: 1209-1212
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Publication
32493814 | J:291448
First Author: Yap JKY
Year: 2020
Journal: J Immunol
Title: Inflammasomes and Pyroptosis as Therapeutic Targets for COVID-19.
Volume: 205
Issue: 2
Pages: 307-312
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Publication
35710627 | J:356153
First Author: Nefzger CM
Year: 2022
Journal: NPJ Regen Med
Title: Intestinal stem cell aging signature reveals a reprogramming strategy to enhance regenerative potential.
Volume: 7
Issue: 1
Pages: 31
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Strain
MGI:5650865 | ((C57BL/6J-Hps4<le> Pde6b<rd1> Unc5c<rcm> x MOLD/Rk)F2 x (B6C3Fe-a/a Mcoln3<Va-J>))F1-Mcoln<Va>
Attribute String: F1 hybrid, mutant stock
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Publication
28589929 | J:253152
 
First Author: Newland SA
Year: 2017
Journal: Nat Commun
Title: Type-2 innate lymphoid cells control the development of atherosclerosis in mice.
Volume: 8
Pages: 15781
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Publication
29526762 | J:266449
First Author: Rafei-Shamsabadi DA
Year: 2018
Journal: J Invest Dermatol
Title: Lack of Type 2 Innate Lymphoid Cells Promotes a Type I-Driven Enhanced Immune Response in Contact Hypersensitivity.
Volume: 138
Issue: 9
Pages: 1962-1972
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Publication
28228256 | J:252978
First Author: Saluzzo S
Year: 2017
Journal: Cell Rep
Title: First-Breath-Induced Type 2 Pathways Shape the Lung Immune Environment.
Volume: 18
Issue: 8
Pages: 1893-1905
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Publication
35072209 | J:323098
 
First Author: Worthington AK
Year: 2022
Journal: Development
Title: IL7Rα, but not Flk2, is required for hematopoietic stem cell reconstitution of tissue-resident lymphoid cells.
Volume: 149
Issue: 8
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Publication
29496881 | J:260759
First Author: Moriyama S
Year: 2018
Journal: Science
Title: β2-adrenergic receptor-mediated negative regulation of group 2 innate lymphoid cell responses.
Volume: 359
Issue: 6379
Pages: 1056-1061
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Publication
28747424 | J:244473
First Author: Schwartz C
Year: 2017
Journal: J Exp Med
Title: ILC2s regulate adaptive Th2 cell functions via PD-L1 checkpoint control.
Volume: 214
Issue: 9
Pages: 2507-2521
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Publication
31873294 | J:305769
First Author: Seillet C
Year: 2020
Journal: Nat Immunol
Title: The neuropeptide VIP confers anticipatory mucosal immunity by regulating ILC3 activity.
Volume: 21
Issue: 2
Pages: 168-177
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Publication
31358996 | J:306903
First Author: Harly C
Year: 2019
Journal: Nat Immunol
Title: The transcription factor TCF-1 enforces commitment to the innate lymphoid cell lineage.
Volume: 20
Issue: 9
Pages: 1150-1160
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Publication
25691468 | J:219556
First Author: Miyazaki M
Year: 2015
Journal: Genes Dev
Title: The E-Id protein axis modulates the activities of the PI3K-AKT-mTORC1-Hif1a and c-myc/p19Arf pathways to suppress innate variant TFH cell development, thymocyte expansion, and lymphomagenesis.
Volume: 29
Issue: 4
Pages: 409-25
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Publication
38653114 | J:349800
 
First Author: Reches G
Year: 2024
Journal: Biomed Pharmacother
Title: Controlling autoimmune diabetes onset by targeting Protease-Activated Receptor 2.
Volume: 175
Pages: 116622
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Publication
29038474 | J:253686
First Author: Mao AP
Year: 2017
Journal: Nat Commun
Title: A shared Runx1-bound Zbtb16 enhancer directs innate and innate-like lymphoid lineage development.
Volume: 8
Issue: 1
Pages: 863
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Publication
26675721 | J:228279
First Author: Huang W
Year: 2015
Journal: Nature
Title: DDX5 and its associated lncRNA Rmrp modulate TH17 cell effector functions.
Volume: 528
Issue: 7583
Pages: 517-22
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Publication
38677292 | J:360412
First Author: Das A
Year: 2024
Journal: Immunity
Title: Transcription factor Tox2 is required for metabolic adaptation and tissue residency of ILC3 in the gut.
Volume: 57
Issue: 5
Pages: 1019-1036.e9
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Publication
24799710 | J:211053
First Author: Miller ML
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: Basal NF-κB controls IL-7 responsiveness of quiescent naïve T cells.
Volume: 111
Issue: 20
Pages: 7397-402
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Publication
32627520 | J:297235
First Author: Sagar
Year: 2020
Journal: EMBO J
Title: Deciphering the regulatory landscape of fetal and adult γδ T-cell development at single-cell resolution.
Volume: 39
Issue: 13
Pages: e104159
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Publication
37289545 | J:338886
 
First Author: Hernandez-Gutierrez A
Year: 2023
Journal: J Clin Invest
Title: Phospholipid scramblase-1 regulates innate type 2 inflammation in mouse lungs via CRTH2-dependent mechanisms.
Volume: 133
Issue: 15
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Publication
33949947 | J:309963
   
First Author: Dinh TTH
Year: 2021
Journal: Elife
Title: Disruption of entire Cables2 locus leads to embryonic lethality by diminished Rps21 gene expression and enhanced p53 pathway.
Volume: 10
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HT Experiment
GSE234679 | Differential susceptibility of male and female germ cells to glucocorticoid-mediated signaling [scRNAseq_Female]
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE248180 | Maternal SMARCA5 is required for major ZGA in mouse [RNA-seq]
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
E-GEOD-54917 | Mus musculus gene expression profiling for Wt, SKM-Tg, C and SKM-KO in Affymetrix 430PM strip arrays
Series Id: GSE54917
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
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HT Experiment
GSE164453 | Gene expression profiling of Hif1alpha defective hearts in E12.5 mice
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE158831 | Organ-, sex-, and age-dependent patterns of endogenous LINE-1 mRNA expression at a single locus resolution
 
Experiment Type: RNA-Seq
Study Type: Baseline
Source: GEO
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HT Experiment
GSE69227 | Combined heterozygous loss of Ebf1 and Pax5 allows for T-lineage conversion of B-cell progenitors
Series Id: E-GEOD-69227
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE232546 | Exploring the Stability of Genomic Imprinting and X-Chromosome Inactivation in the Aged Brain (RNA-Seq)
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE243469 | Loss of alkyladenine DNA glycosylase alters gene expression in developing mouse brain and leads to reduced anxiety and increased exploratory behavior
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Protein
Q8R4F0
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
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Protein
Q8K595
Organism: Mus musculus/domesticus
Length: 566  
Fragment?: false
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Protein
Q99J21
Organism: Mus musculus/domesticus
Length: 580  
Fragment?: false
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Protein
Q3U652
Organism: Mus musculus/domesticus
Length: 566  
Fragment?: false
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Protein
Q925J2
Organism: Mus musculus/domesticus
Length: 584  
Fragment?: true
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Protein
Q3KP77
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
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Protein
Q3KP78
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
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Protein
Q3TTV4
Organism: Mus musculus/domesticus
Length: 681  
Fragment?: true
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Publication
15313893 | -
First Author: Moore SD
Year: 2004
Journal: Cancer Res
Title: Uterine leiomyomata with t(10;17) disrupt the histone acetyltransferase MORF.
Volume: 64
Issue: 16
Pages: 5570-7
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Publication
1145128 | -
First Author: Elsayed S
Year: 1975
Journal: Scand J Immunol
Title: The primary structure of allergen M from cod.
Volume: 4
Issue: 2
Pages: 203-8
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Publication
2777802 | -
First Author: Swain AL
Year: 1989
Journal: J Biol Chem
Title: Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution.
Volume: 264
Issue: 28
Pages: 16620-8
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Publication
8845026 | -
First Author: Lindstrøm CD
Year: 1996
Journal: Scand J Immunol
Title: Cloning of two distinct cDNAs encoding parvalbumin, the major allergen of Atlantic salmon (Salmo salar).
Volume: 44
Issue: 4
Pages: 335-44
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Publication
19776169 | -
First Author: Bouley R
Year: 2009
Journal: Am J Physiol Renal Physiol
Title: Angiotensin II and hypertonicity modulate proximal tubular aquaporin 1 expression.
Volume: 297
Issue: 6
Pages: F1575-86
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Publication
19731985 | -
First Author: Tran ND
Year: 2010
Journal: J Neurosurg
Title: Aquaporin-1-mediated cerebral edema following traumatic brain injury: effects of acidosis and corticosteroid administration.
Volume: 112
Issue: 5
Pages: 1095-104
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Publication
10831612 | -
First Author: Bhamidipati A
Year: 2000
Journal: J Cell Biol
Title: ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin.
Volume: 149
Issue: 5
Pages: 1087-96
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Publication
30356097 | -
First Author: Kirchdoerfer RN
Year: 2018
Journal: Sci Rep
Title: Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis.
Volume: 8
Issue: 1
Pages: 15701
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Publication
11017199 | -
First Author: Fujii Y
Year: 2000
Journal: Nat Struct Biol
Title: Structural basis for the diversity of DNA recognition by bZIP transcription factors.
Volume: 7
Issue: 10
Pages: 889-93
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Protein Domain
IPR043473 | S2_sf_CoV
Type: Homologous_superfamily
Description: The type I glycoprotein S of Coronavirus, trimers of which constitute the typical viral spikes, is assembled into virions through noncovalent interactions with the M protein. The spike glycoprotein is translated as a large polypeptide that is subsequently cleaved to S1 and S2 []. The cleavage of S can occur at two distinct sites: S2 or S2' []. The S1 subunit is responsible for host-receptor binding while the S2 subunit contains the membrane-fusion machinery [].Both chimeric S proteins appeared to cause cell fusion when expressed individually, suggesting that they were biologically fully active []. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail [].The S2 subunit normally contains multiple key components, including one or more fusion peptides (FP), a second proteolytic site (S2') and two conserved heptad repeats (HRs), driving membrane penetration and virus-cell fusion. The HRs can trimerize into a coiled-coil structure built of three HR1-HR2 helical hairpins presenting as a canonical six-helix bundle and drag the virus envelope and the host cell bilayer into close proximity, preparing for fusion to occur []. The fusion core is composed of HR1 and HR2 and at least three membranotropic regions that are denoted as the fusion peptide (FP), internal fusion peptide (IFP), and pretransmembrane domain (PTM). The HR regions are further flanked by the three membranotropic components. Both FP and IFP are located upstream of HR1, while PTM is distally downstream of HR2 and directly precedes the transmembrane domain of SARS-CoV S. All of these three components are able to partition into the phospholipid bilayer to disturb membrane integrity. []. During the pandemic, many conservative amino acid changes in FP segment of SARS-CoV-2 have been reported (i.e., L821I, L822F, K825R, V826L, T827I, L828P, A829T, D830G/A, A831V/S/T, G832C/S, F833S, I834T), although their impact is not known as the active conformation and mode of insertion of SARS-CoV-2 fusion peptide have not been experimentally characterised. Differences in HR1 sequences between SARS-CoV and SARS-CoV-2 suggest that SARS-CoV-2 HR2 makes stronger interactions with HR1. However, the substitutions observed in the solvent accessible surface of the HR1 domain (e.g., D936Y, S943P, S939F) of SARS-CoV-2 do not seem to be involved in stabilizing interactions with HR2. Substitutions in HR2 (e.g., K1073N, V1176F) or the TM or cytoplasmic tail domains have also been observed, but further experimental work is required to determine the effects of these changes [].
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Protein Domain
IPR023274 | Aquaporin_1
Type: Family
Description: Aquaporins are water channels, present in both higher and lower organisms, that belong to the major intrinsic protein family. Most aquaporins are highly selective for water, though some also facilitate the movement of small uncharged molecules such as glycerol []. In higher eukaryotes these proteins play diverse roles in the maintenance of water homeostasis, indicating that membrane water permeability can be regulated independently of solute permeability. In microorganisms however, many of which do not contain aquaporins, they do not appear to play such a broad role. Instead, they assist specific microbial lifestyles within the environment, e.g. they confer protection against freeze-thaw stress and may help maintain water permeability at low temperatures []. The regulation of aquaporins is complex, including transcriptional, post-translational, protein-trafficking and channel-gating mechanisms that are frequently distinct for each family member.Structural studies show that aquaporins are present in the membrane as tetramers, though each monomer contains its own channel [, , ]. The monomer has an overall "hourglass"structure made up of three structural elements: an external vestibule, an internal vestibule, and an extended pore which connects the two vestibules. Substrate selectivity is conferred by two mechanisms. Firstly, the diameter of the pore physically limits the size of molecules that can pass through the channel. Secondly, specific amino acids within the molecule regulate the preference for hydrophobic or hydrophilic substrates.Aquaporins are classified into two subgroups: the aquaporins (also known as orthodox aquaporins), which transport only water, and the aquaglyceroporins, which transport glycerol, urea, and other small solutes in addition to water [, ].Aquaporin-1 is the major water channel present in the kidney proximal renal tubule. Members of the family contain approximately 275 amino acids. Aquaporin-1 is under complex regulation, including hormones and homeostatic factors like hypertonicity []. It is also expressed in red blood cells, the gastrointestinal tract, lungs and in the brain, where it may have a role in cerebral oedema after surgery or trauma []. Apart from controlling the water balance of the organism [, ], aquaporin-1 is thought to have an impact onvarious cellular processes, such as angiogenesis, and cell migration and metastasis observed in some human malignancies. Its expression has also been proposed as a characteristic feature of an aggressive sub-group of breast carcinomas.
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Protein Domain
IPR005819 | H1/H5
Type: Family
Description: Histone proteins have central roles in both chromatin organisation (asstructural units of the nucleosome) and gene regulation (as dynamic componentsthat have a direct impact on DNA transcription and replication). EukaryoticDNA wraps around a histone octamer to form a nucleosome, the first order ofcompaction of eukaryotic chromatin. The core histone octamer is composed of acentral H3-H4 tetramer and two flanking H2A-H2B dimers. Each of the corehistone contains a common structural motif, called the histone fold, whichfacilitates the interactions between the individual core histones.In addition to the core histones, there is a "linker histone"called H1 (or H5 in avian species). The linker histones present in all multicellular eukaryotes are the most divergent group of histones, with numerous cell type- and stage-specific variant. Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures.Histone H5 performs the same function as histone H1, and replaces H1 in certain cells. The structure of GH5, the globular domain of the linker histone H5 is known [, ]. The fold is similar to the DNA-binding domain of the catabolite gene activator protein, CAP, thus providing a possible model for the binding of GH5 to DNA.The linker histones, which do not contain the histone fold motif, are critical to the higher-order compaction of chromatin, because they bind to internucleosomal DNA and facilitate interactions between individual nucleosomes. In addition, H1 variants have been shown to be involved in the regulation of developmental genes. A common feature of this protein family is a tripartite structure in which a globular (H15) domain of about 80 amino acids is flanked by two less structured N- and C-terminal tails. The H15domain is also characterised by high sequence homology among the family oflinker histones. The highly conserved H15 domain is essential for the bindingof H1 or H5 to the nucleosome. It consists of a three helix bundle (I-III),with a β-hairpin at the C terminus. There is also a short three-residuestretch between helices I and II that is in the β-strand conformation.Together with the C-terminal β-hairpin, this strand forms the third strandof an antiparallel β-sheet [, , , ].Histone H5 is a nuclear protein involved in the condensation of nucleosome chains into higher order structures. In this respect, it performs the same function as histone H1, and replaces H1 in certain cells. The structure of GH5, the globular domain (residues 22-100) of the linker histone H5, has been solved. The fold is similar to the DNA-binding domain of the catabolite gene activator protein, CAP, thus providing a possible model for the binding of GH5 to DNA. The structure comprises 3 α-helices and 2 short β-strands [, ].
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Protein Domain
IPR005818 | Histone_H1/H5_H15
Type: Domain
Description: Histone proteins have central roles in both chromatin organisation (asstructural units of the nucleosome) and gene regulation (as dynamic componentsthat have a direct impact on DNA transcription and replication). EukaryoticDNA wraps around a histone octamer to form a nucleosome, the first order ofcompaction of eukaryotic chromatin. The core histone octamer is composed of acentral H3-H4 tetramer and two flanking H2A-H2B dimers. Each of the corehistone contains a common structural motif, called the histone fold, whichfacilitates the interactions between the individual core histones.In addition to the core histones, there is a "linker histone"called H1 (or H5 in avian species). The linker histones present in all multicellular eukaryotes are the most divergent group of histones, with numerous cell type- and stage-specific variant. Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures.Histone H5 performs the same function as histone H1, and replaces H1 in certain cells. The structure of GH5, the globular domain of the linker histone H5 is known [, ]. The fold is similar to the DNA-binding domain of the catabolite gene activator protein, CAP, thus providing a possible model for the binding of GH5 to DNA.The linker histones, which do not contain the histone fold motif, are critical to the higher-order compaction of chromatin, because they bind to internucleosomal DNA and facilitate interactions between individual nucleosomes. In addition, H1 variants have been shown to be involved in the regulation of developmental genes. A common feature of this protein family is a tripartite structure in which a globular (H15) domain of about 80 amino acids is flanked by two less structured N- and C-terminal tails. The H15domain is also characterised by high sequence homology among the family oflinker histones. The highly conserved H15 domain is essential for the bindingof H1 or H5 to the nucleosome. It consists of a three helix bundle (I-III),with a β-hairpin at the C terminus. There is also a short three-residuestretch between helices I and II that is in the β-strand conformation.Together with the C-terminal β-hairpin, this strand forms the third strandof an antiparallel β-sheet [, , , ].Proteins known to contain a H15 domain are:- Eukaryotic histone H1. The histones H1 constitute a family with many variants, differing in their affinity for chromatin. Several variants aresimultaneously present in a single cell. For example, the nucleatederythrocytes of birds contain both H1 and H5, the latter being an extremevariant of H1.- Eukaryotic MHYST family of histone acetyltransferase. Histoneacetyltransferases transfer an acetyl group from acetyl-CoA to the epsylon-amino group of lysine within the basic NH2-termini of histones, which bindthe acidic phosphates of DNA [].This entry represents the H15 domain.
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Protein Domain
IPR008080 | Parvalbumin
Type: Family
Description: Fish allergies are common in Europe, particularly among male children and young adults. Children allergic to fish react variably todifferent species.Cod is among the most common offenders, while salmon is the one besttolerated. The allergy-eliciting protein has been isolated from the whitemuscle albumin. It is a parvalbumin, designated Allergen M. Parvalbumins arecalcium (Ca)-binding proteins of low molecular weight. Like many other Ca-binding proteins, they belong to the EF-hand family characterised byhelix-loop-helix (HLH) binding motifs (two helices pack together at an angleof ~90 degrees, separated by a loop region where calcium binds). In the parvalbumin HLH structural motif, calcium is coordinated through one carbonyl oxygen atom and the oxygen-containing side-chains of 5 amino acidresidues, or 4 residues and a water molecule[, , ].Initially, parvalbumins were detected in relatively high amounts in lowervertebrate white muscle, where they were thought to be important for fibrerelaxation. They were subsequently found, although in lesser amounts, in thefast twitch skeletal muscles of higher vertebrates, as well as in a varietyof non-muscle tissues, including testis, endocrine glands, skin and specificneurons. There are two distinct phylogenetic lineages: alpha and beta. Mostmuscles contain parvalbumin of only alpha or beta origin. Cod parvalbumin belongs to the beta-lineage and shares significant similarity with parvalbumin of other fish species [, ].Allergen M contains 113 residues, is a homogenous acidic protein and belongsto a group of muscle sarcoplasmic proteins. It carries the major allergenicdeterminants associated with cod sensitivity, which is dependent directly onthe linear structure rather than on the molecular conformation. The allergenic activity of allergen M resides in particular epitopes found inthree loops: AB (~13-33), CD (~48-64) and EF (~80-103). It has an N-acetylterminal amino acid residue and includes 1 residue of glucose attached to the conserved N-terminal cysteine, and 1 residue each of tyrosine, tryptophan and arginine - the arginine is believed to play a key role in maintaining the tertiary structure. Mutation of the last conservedcoordinating residue of the Ca-binding loop (E101D-motif 4) has also beenshown to have a significant impact on the ability of the mutant to obtainthe sevenfold coordination preferred by Ca2+.
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Protein
O35245
Organism: Mus musculus/domesticus
Length: 966  
Fragment?: false
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Protein
A2A259
Organism: Mus musculus/domesticus
Length: 760  
Fragment?: false
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Publication
8384699 | -
First Author: Ramakrishnan V
Year: 1993
Journal: Nature
Title: Crystal structure of globular domain of histone H5 and its implications for nucleosome binding.
Volume: 362
Issue: 6417
Pages: 219-23
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Publication
3463990 | -
First Author: Zarbock J
Year: 1986
Journal: Proc Natl Acad Sci U S A
Title: Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure.
Volume: 83
Issue: 20
Pages: 7628-32
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Publication
14654695 | -
First Author: Ono K
Year: 2003
Journal: Nucleic Acids Res
Title: The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy.
Volume: 31
Issue: 24
Pages: 7199-207
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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.

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