| Type |
Details |
Score |
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline and WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline and WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Murakami M |
| Year: |
2003 |
| Journal: |
J Mol Neurosci |
| Title: |
Structures of the murine genes for the beta1- and beta4-subunits of the voltage-dependent calcium channel. |
| Volume: |
21 |
| Issue: |
1 |
| Pages: |
13-21 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Suzumori N |
| Year: |
2003 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway. |
| Volume: |
100 |
| Issue: |
2 |
| Pages: |
550-5 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
745
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
752
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
489
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
826
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
265
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
585
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
414
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
680
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
443
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
500
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
249
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
414
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Borniego MB |
| Year: |
2016 |
| Journal: |
Virology |
| Title: |
Bioinformatic and mutational analysis of ophiovirus movement proteins, belonging to the 30K superfamily. |
| Volume: |
498 |
|
| Pages: |
172-180 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Smith SM |
| Year: |
1999 |
| Journal: |
Ann N Y Acad Sci |
| Title: |
Neuronal voltage-activated calcium channels: on the roles of the alpha 1E and beta 3 subunits. |
| Volume: |
868 |
|
| Pages: |
175-98 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chen YH |
| Year: |
2004 |
| Journal: |
Nature |
| Title: |
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels. |
| Volume: |
429 |
| Issue: |
6992 |
| Pages: |
675-80 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mangoni ME |
| Year: |
1997 |
| Journal: |
Receptors Channels |
| Title: |
Characterisation of alpha 1A Ba2+, Sr2+ and Ca2+ currents recorded with the ancillary beta 1-4 subunits. |
| Volume: |
5 |
| Issue: |
1 |
| Pages: |
1-14 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bonnefont J |
| Year: |
2011 |
| Journal: |
Cell Death Differ |
| Title: |
Primate-specific RFPL1 gene controls cell-cycle progression through cyclin B1/Cdc2 degradation. |
| Volume: |
18 |
| Issue: |
2 |
| Pages: |
293-303 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Heim KP |
| Year: |
2014 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
An intramolecular lock facilitates folding and stabilizes the tertiary structure of Streptococcus mutans adhesin P1. |
| Volume: |
111 |
| Issue: |
44 |
| Pages: |
15746-51 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Liang SL |
| Year: |
2006 |
| Journal: |
IUBMB Life |
| Title: |
RNase L: its biological roles and regulation. |
| Volume: |
58 |
| Issue: |
9 |
| Pages: |
508-14 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dong B |
| Year: |
2001 |
| Journal: |
RNA |
| Title: |
Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p. |
| Volume: |
7 |
| Issue: |
3 |
| Pages: |
361-73 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rökman A |
| Year: |
2002 |
| Journal: |
Am J Hum Genet |
| Title: |
Germline alterations of the RNASEL gene, a candidate HPC1 gene at 1q25, in patients and families with prostate cancer. |
| Volume: |
70 |
| Issue: |
5 |
| Pages: |
1299-304 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Casey G |
| Year: |
2002 |
| Journal: |
Nat Genet |
| Title: |
RNASEL Arg462Gln variant is implicated in up to 13% of prostate cancer cases. |
| Volume: |
32 |
| Issue: |
4 |
| Pages: |
581-3 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kieffer N |
| Year: |
2006 |
| Journal: |
Bull Soc Sci Med Grand Duche Luxemb |
| Title: |
Involvement of the RNAse L gene in prostate cancer. |
|
| Issue: |
1 |
| Pages: |
21-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dai S |
| Year: |
2004 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
RF2b, a rice bZIP transcription activator, interacts with RF2a and is involved in symptom development of rice tungro disease. |
| Volume: |
101 |
| Issue: |
2 |
| Pages: |
687-92 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ordiz MI |
| Year: |
2010 |
| Journal: |
Plant Biotechnol J |
| Title: |
Functional analysis of the activation domain of RF2a, a rice transcription factor. |
| Volume: |
8 |
| Issue: |
7 |
| Pages: |
835-44 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tsugama D |
| Year: |
2018 |
| Journal: |
Ann Bot |
| Title: |
Calcium signalling regulates the functions of the bZIP protein VIP1 in touch responses in Arabidopsis thaliana. |
| Volume: |
122 |
| Issue: |
7 |
| Pages: |
1219-1229 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tsugama D |
| Year: |
2016 |
| Journal: |
Plant Physiol |
| Title: |
The bZIP Protein VIP1 Is Involved in Touch Responses in Arabidopsis Roots. |
| Volume: |
171 |
| Issue: |
2 |
| Pages: |
1355-65 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tsugama D |
| Year: |
2014 |
| Journal: |
PLoS One |
| Title: |
Analysis of functions of VIP1 and its close homologs in osmosensory responses of Arabidopsis thaliana. |
| Volume: |
9 |
| Issue: |
8 |
| Pages: |
e103930 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fryer CJ |
| Year: |
2002 |
| Journal: |
Genes Dev |
| Title: |
Mastermind mediates chromatin-specific transcription and turnover of the Notch enhancer complex. |
| Volume: |
16 |
| Issue: |
11 |
| Pages: |
1397-411 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Decroly E |
| Year: |
2011 |
| Journal: |
PLoS Pathog |
| Title: |
Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2'-O-methyltransferase nsp10/nsp16 complex. |
| Volume: |
7 |
| Issue: |
5 |
| Pages: |
e1002059 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zeng C |
| Year: |
2016 |
| Journal: |
J Virol |
| Title: |
Identification and Characterization of a Ribose 2'-O-Methyltransferase Encoded by the Ronivirus Branch of Nidovirales. |
| Volume: |
90 |
| Issue: |
15 |
| Pages: |
6675-6685 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nga PT |
| Year: |
2011 |
| Journal: |
PLoS Pathog |
| Title: |
Discovery of the first insect nidovirus, a missing evolutionary link in the emergence of the largest RNA virus genomes. |
| Volume: |
7 |
| Issue: |
9 |
| Pages: |
e1002215 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lehmann KC |
| Year: |
2015 |
| Journal: |
J Gen Virol |
| Title: |
Arterivirus nsp12 versus the coronavirus nsp16 2'-O-methyltransferase: comparison of the C-terminal cleavage products of two nidovirus pp1ab polyproteins. |
| Volume: |
96 |
| Issue: |
9 |
| Pages: |
2643-2655 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Viswanathan T |
| Year: |
2020 |
| Journal: |
Nat Commun |
| Title: |
Structural basis of RNA cap modification by SARS-CoV-2. |
| Volume: |
11 |
| Issue: |
1 |
| Pages: |
3718 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Katz E |
| Year: |
1991 |
| Journal: |
Fertil Steril |
| Title: |
Increased circulating levels of bromocriptine after vaginal compared with oral administration. |
| Volume: |
55 |
| Issue: |
5 |
| Pages: |
882-4 |
|
•
•
•
•
•
|
| Protein Domain |
| 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. The replicase gene encodes two polyproteins, pp1a and pp1ab, which are proteolytically processed to nonstructural proteins (NSPs). Among the NSPs found in Nidovirales, nonstructural protein 15 (NSP15) from coronaviruses (CoV) and NSP11 from arteriviruses (AV) participate in the viral replication process and in the evasion of the host immune system. They contain in their C-terminal region a conserved endoribonuclease domain called nidoviral uridylate-specific endoribonuclease (NendoU) with cleavage specificity for single- and double-stranded RNA 5' of uridine nucleotides to produce a 2'-3'-cyclic phosphate end product. Arterivirus Nsp11 contains two conserved compact domains: the N-terminal domain (NTD) and C-terminal domain (NendoU), whereas CoV NSP15 folds into three domains: N-terminal, middle domain, and C-terminal catalytic NendoU domain. No counterpart corresponding to the NTD of CoV NSP15 exists in AV NSP11. The NTD of AV NSP11 is small and related to NSP15 middle domain, which may serve as an interaction hub with other proteins and RNA [, , , , , ].This domain contains a central β-sheet flanked by two small α-helices on either side [, , ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This is the bZIP domain found in plant transcription factors with similarity to Oryza sativa RF2a and RF2b, which are important for plant development. RF2a and b interact, as homodimers or heterodimers, with each other, and activate transcription from the RTBV (rice tungro bacilliform virus) promoter, which is regulated by sequence-specific DNA-binding proteins that bind to the essential cis element BoxII. They show differences in binding affinities to BoxII, expression patterns in different rice organs, and subcellular localisation. Transgenic rice with increased RF2a and RF2b display increased resistance to rice tungro disease (RTD) with no impact on plant development [, ].bZIP domains from Arabidopsis have been classified into 11 groups (groups A-I and S), the ones included in this entry belong to group I such as VIP1 or PosF21 (also known as bZIP transcription factor 59) [, , , ].bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
This entry represents the N-terminal domain found in a family of neurogenic mastermind-like proteins (MAMLs), which act as critical transcriptional co-activators for Notch signaling [, , ]. Notch receptors are cleaved upon ligand engagement and the intracellular domain of Notch shuttles to the nucleus. MAMLs form a functional DNA-binding complex with the cleaved Notch receptor and the transcription factor CSL, thereby regulating transcriptional events that are specific to the Notch pathway. MAML proteins may also play roles as key transcriptional co-activators in other signal transduction pathways as well, including: muscle differentiation and myopathies (MEF2C) [], tumour suppressor pathway (p53) []and colon carcinoma survival (beta-catenin) []. MAML proteins could mediate cross-talk among the various signaling pathways and the diverse activities of the MAML proteins converge to impact normal biological processes and human diseases, including cancers.The N-terminal domain of MAML proteins adopt an elongated kinked helix that wraps around ANK and CSL forming one of the complexes in the build-up of the Notch transcriptional complex for recruiting general transcription factors []. This N-terminal domain is responsible for its interaction with the ankyrin repeat region of the Notch proteins NOTCH1 [], NOTCH2 [], NOTCH3 []and NOTCH4. It forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1, and also binds CREBBP/CBP []and CDK8 []. The C-terminal region is required for transcriptional activation. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This family includes the neurogenic mastermind-like proteins 1-3 (MAML1-3) from chordates, which act as critical transcriptional co-activators for Notch signaling [, ]. Notch receptors are cleaved upon ligand engagement and the intracellular domain of Notch shuttles to the nucleus. MAMLs form a functional DNA-binding complex with the cleaved Notch receptor and the transcription factor CSL, thereby regulating transcriptional events that are specific to the Notch pathway. MAML proteins may also play roles as key transcriptional co-activators in other signal transduction pathways as well, including: muscle differentiation and myopathies (MEF2C) [], tumour suppressor pathway (p53) []and colon carcinoma survival (beta-catenin) []. MAML proteins could mediate cross-talk among the various signaling pathways and the diverse activities of the MAML proteins converge to impact normal biological processes and human diseases, including cancers.They consist of an N-terminal domain which adopt an elongated kinked helix that wraps around ANK and CSL forming one of the complexes in the build-up of the Notch transcriptional complex for recruiting general transcription factors [, ]]. This N-terminal domain is responsible for its interaction with the ankyrin repeat region of the Notch proteins NOTCH1 [], NOTCH2 [], NOTCH3 []and NOTCH4. It forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1, and also binds CREBBP/CBP []and CDK8 []. The C-terminal region is required for transcriptional activation. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Ribonuclease L (RNase L) is a highly regulated, latent endoribonuclease (thus the 'L' in RNase L) and is widely expressed in most mammalian tissues. It is involved in the mediation of the antiviral and pro-apoptotic activities of the interferon-inducible 2-5A system, which blocks infections by certain types of viruses through cleavage of viral and cellular single-stranded RNA [, ]. RNase L is unique in that it is composed of threemajor domains; N terminus regulatory ankyrin repeat domain (ARD), followed by a linker, a protein kinase (PK)-like domain and a C-terminal ribonuclease (RNase) domain. The RNase domain has homology with IRE1, also containing both a kinase and an endoribonuclease, that functions in the unfolded protein response (UPR) []. RNase L has been shown to have an impact on the pathogenesis of prostate cancer; the RNase L gene, RNASEL, has been identified as a strong candidate for the hereditary prostate cancer 1 (HPC1) allele [, , ]. The broad range of biological functions of RNase offers a possibility for RNase L as a therapeutic target.This entry represents the RNase domain of RNase L. |
|
•
•
•
•
•
|
| Protein Domain |
| 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.The 3'-terminal region of the most conserved ORF1b in three of the four families of the order Nidovirales (except for the family Arteriviridae) encodes a 2'-O-methyltransferase (2'-O-MTase), known as non structural protein (NSP) 16 in CoV and implicated in methylation of the 5' cap structure of nidoviral mRNAs. Assembly of a cap1 structure at the 5' end of viral mRNA assists in translation and evading host defense. The cap structure consists of a 7-methylguanosine (m7G) linked to the first nucleotide of the RNA transcript through a 5'-5' triphosphate bridge. The CoV NSP16 methyltransferase forms an obligatory complex with NSP10 to efficiently convert client mRNA species from the cap-0 ((me7)G(0)pppA(1)) to the cap-1 form ((me7)G(0)pppA(1m)) by methylating the ribose 2'-O of the first nucleotide of the nascent mRNA using S-adenosyl methionine (SAM) as the methyl donor [, , , ].The nidovirus 2'-O-MTase domain exhibits the characteristic fold of the class I MTase family, comprising a β-sheet flanked by α-helices and loops. The nidovirus 2'-O-MTase domain harbors a catalytic K-D-K-E tetrad that is conserved among 2'-O-MTases [, , ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the N-terminal domain found in a family of neurogenic mastermind-like proteins (MAMLs), which act as critical transcriptional co-activators for Notch signaling [, , ]. Notch receptors are cleaved upon ligand engagement and the intracellular domain of Notch shuttles to the nucleus. MAMLs form a functional DNA-binding complex with the cleaved Notch receptor and the transcription factor CSL, thereby regulating transcriptional events that are specific to the Notch pathway. MAML proteins may also play roles as key transcriptional co-activators in other signal transduction pathways as well, including: muscle differentiation and myopathies (MEF2C) [], tumour suppressor pathway (p53) []and colon carcinoma survival (beta-catenin) []. MAML proteins could mediate cross-talk among the various signaling pathways and the diverse activities of the MAML proteins converge to impact normal biological processes and human diseases, including cancers.The N-terminal domain of MAML proteins adopt an elongated kinked helix that wraps around ANK and CSL forming one of the complexes in the build-up of the Notch transcriptional complex for recruiting general transcription factors []. This N-terminal domain is responsible for its interaction with the ankyrin repeat region of the Notch proteins NOTCH1 [], NOTCH2 [], NOTCH3 []and NOTCH4. It forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1, and also binds CREBBP/CBP []and CDK8 []. The C-terminal region is required for transcriptional activation. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The beta4 subunit of voltage-dependent calcium channels (Ca(V)s) is one of four beta subunits present in vertebrates. It is highly expressed in the brain, predominantly in the cerebellum []. Ca(V)s are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane []. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants []. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain [].This entry represents the SH3 domain of the subunit beta-3. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| 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. |
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| Publication |
| First Author: |
Lane PW |
| Year: |
1972 |
| Journal: |
J Hered |
| Title: |
Two new mutations in linkage group XVI of the house mouse. Flaky tail and varitint-waddler-J. |
| Volume: |
63 |
| Issue: |
3 |
| Pages: |
135-40 |
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| Publication |
| First Author: |
Wu K |
| Year: |
2020 |
| Journal: |
J Immunol |
| Title: |
Group 2 Innate Lymphoid Cells Must Partner with the Myeloid-Macrophage Lineage for Long-Term Postviral Lung Disease. |
| Volume: |
205 |
| Issue: |
4 |
| Pages: |
1084-1101 |
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| Publication |
| First Author: |
Zuberbuehler MK |
| Year: |
2019 |
| Journal: |
Nat Immunol |
| Title: |
The transcription factor c-Maf is essential for the commitment of IL-17-producing γδ T cells. |
| Volume: |
20 |
| Issue: |
1 |
| Pages: |
73-85 |
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| Publication |
| First Author: |
Parker ME |
| Year: |
2020 |
| Journal: |
J Exp Med |
| Title: |
c-Maf regulates the plasticity of group 3 innate lymphoid cells by restraining the type 1 program. |
| Volume: |
217 |
| Issue: |
1 |
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| Publication |
| First Author: |
Berthault C |
| Year: |
2017 |
| Journal: |
Nat Immunol |
| Title: |
Asynchronous lineage priming determines commitment to T cell and B cell lineages in fetal liver. |
| Volume: |
18 |
| Issue: |
10 |
| Pages: |
1139-1149 |
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| Publication |
| First Author: |
Flamar AL |
| Year: |
2020 |
| Journal: |
Immunity |
| Title: |
Interleukin-33 Induces the Enzyme Tryptophan Hydroxylase 1 to Promote Inflammatory Group 2 Innate Lymphoid Cell-Mediated Immunity. |
| Volume: |
52 |
| Issue: |
4 |
| Pages: |
606-619.e6 |
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| Publication |
| First Author: |
Cho HS |
| Year: |
2019 |
| Journal: |
Nat Commun |
| Title: |
The Tec kinase ITK is essential for ILC2 survival and epithelial integrity in the intestine. |
| Volume: |
10 |
| Issue: |
1 |
| Pages: |
784 |
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| Publication |
| First Author: |
Chea S |
| Year: |
2016 |
| Journal: |
Sci Signal |
| Title: |
Notch signaling in group 3 innate lymphoid cells modulates their plasticity. |
| Volume: |
9 |
| Issue: |
426 |
| Pages: |
ra45 |
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| Publication |
| First Author: |
Leung GA |
| Year: |
2019 |
| Journal: |
Development |
| Title: |
The lymphoid-associated interleukin 7 receptor (IL7R) regulates tissue-resident macrophage development. |
| Volume: |
146 |
| Issue: |
14 |
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| Publication |
| First Author: |
Obeng EA |
| Year: |
2015 |
| Journal: |
Cancer Cell |
| Title: |
Charting the "Splice" Routes to MDS. |
| Volume: |
27 |
| Issue: |
5 |
| Pages: |
607-9 |
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| Publication |
| First Author: |
Cairns RA |
| Year: |
2016 |
| Journal: |
Cell Metab |
| Title: |
Lung Cancer Resets the Liver's Metabolic Clock. |
| Volume: |
23 |
| Issue: |
5 |
| Pages: |
767-9 |
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| Publication |
| First Author: |
Davies DM |
| Year: |
2021 |
| Journal: |
Cancer Cell |
| Title: |
Crosstown Traffic: Lymphodepleting Chemotherapy Drives CAR T Cells. |
| Volume: |
39 |
| Issue: |
2 |
| Pages: |
138-140 |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
| Series Id: |
GSE6238 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
Baseline |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE25017 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
Baseline |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE11035 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE9743 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE30651 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE73131 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE81959 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
Baseline |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE70179 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE65506 |
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
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| HT Experiment |
| Series Id: |
GSE43620 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
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| HT Experiment |
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| Experiment Type: |
transcription profiling by array |
| Study Type: |
Baseline |
| Source: |
ArrayExpress |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
| Series Id: |
GSE48811 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
Baseline |
| Source: |
ArrayExpress |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
| Series Id: |
GSE35293 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
Baseline |
| Source: |
GEO |
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