| Type |
Details |
Score |
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the RNA-binding domains RBS1 and RBS2 found at the C-terminal of Gem-associated protein 5 (GEMI5) from vertebrates. The RBS1 domain is involved in the recognition of viral IRES elements and cellular RNAs. This domain is intrinsically unstructured and interacts with RNA through conserved Arg and aromatic residues [].GEMI5 is a component of the survival of motor neurons (SMN) complex, that binds small nuclear RNAs (snRNAs). The SMN complex assembles the heptameric Sm protein core on snRNAs playing a critical role in the biogenesis of small nuclear ribonucleoproteins (snRNPs) [, ]. GEMI5 is also implicated in translation control, and gene expression reprogramming []. GEMI5 from animals share a domain architecture consisting of two N-terminal ��-propellers followed by a TPR domain and a C-terminal RNA-binding domain. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the first ��-propeller found at the N-terminal of Protein rigor mortis (RIG) from Drosophila melanogaster, also known as Gem-associated protein 5 (GEMI5), the orthologue of GEMI5 from vertebrates []. RIG, apart from being a component of the survival motor neuron (SMN) complex, it is a nuclear receptor-interacting protein required for the response to steroid hormone ecdysone during larval development [].GEMI5 is a component of the survival of motor neurons (SMN) complex, that binds small nuclear RNAs (snRNAs). The SMN complex assembles the heptameric Sm protein core on snRNAs playing a critical role in the biogenesis of small nuclear ribonucleoproteins (snRNPs) [, ]. GEMI5 is also implicated in translation control, and gene expression reprogramming []. GEMI5 from animals share a domain architecture consisting of two N-terminal ��-propellers followed by a TPR domain and a C-terminal RNA-binding domain. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This region of HEAT repeats is found in human Serine/threonine-protein kinase ATR andsimilar eukaryotic proteins. This entry represents the M-HEAT region.This region is also found in Serine/threonine-protein kinase MEC1 from Saccharomyces cerevisiae, which activates checkpoint signalling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor [, , , ].ATR acts as a DNA damage sensor and is associated with severe disorders such as Seckel syndrome 1. This protein is organised into a large N-terminal ��-solenoid containing HEAT repeats, a FAT (FRAP, ATM, TRRAP) domain (), a kinase domain (), and a C-terminal short segment referred to as FATC (). N-terminal part has two continuous HEAT repeat regions, the N-HEAT and the M-HEAT. The FAT domain contains TPR (tetratricopeptide) repeats followed by a HEAT repeat domain []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This is a GreAB-C-like domain found mostly in the N-terminal of uncharacterised bacterial proteins. This domain has been found in antiviral immunity systems, where it forms a circular permuted domain embedded in TPR repeats. In these proteins, the GreAB-C domain is located at the C-terminal followed, usually, by a PIN domain with a variable N-terminal domain often harbouring effector domains [, ].GreA and GreB are prokaryotic transcript cleavage factors that play a crucial role in regulating RNA polymerase (RNAP) transcript elongation. They have several key functions in preventing elongation arrest, improving transcription accuracy, and facilitating the transition from transcription initiation to elongation. They have a similar structural organisation and consist of two domains: a C-terminal globular and an extended N-terminal coiled-coil domain. Their structural features, particularly the coiled-coil domain, are essential for modifying the RNAP active site to perform these cleavage reactions []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
BEND3 is a transcriptional repressor that associates with the nucleolar-remodeling complex (NoRC) and is involved in ribosomal DNA (rDNA) silencing []. SUMOylated BEND3 stabilizes the NoRC component Tip5 via USP21 deubiquitinase []. NorC serves as a molecular platform that recruits chromatin modifiers, such as histone deacetylases and histone methyltransferases, leading to deacetylation of histone H4 and trimethylation of H3K9 and H4K20 []. NoRC also targets histone deacetylases and histone methyltransferases to rDNA to establish a heterochromatic state that inhibits transcription activation. Hence, BEND3 and NoRC seem to play a concerted role in the maintenance of heterochromatin architecture [, ].BEND3 has also been shown to mediate Polycomb recruitment in the absence of H3K9Me3 or DNA methylation at the pericentromeric regions []. BEND3 interacts with PICH (ERCC6L), a DNA translocase required for the maintenance of chromosome stability, and stimulates its translocase and ATPase activities. This interaction occurs via an interface betweena TPR domain in PICH and a BEN domain in BEND3 []. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
724
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
416
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
458
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
313
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
790
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
363
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
389
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
832
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
724
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
724
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
724
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
313
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
434
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
983
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
614
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
229
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
773
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
218
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
773
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
258
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Groves MR |
| Year: |
1999 |
| Journal: |
Curr Opin Struct Biol |
| Title: |
Topological characteristics of helical repeat proteins. |
| Volume: |
9 |
| Issue: |
3 |
| Pages: |
383-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Liu N |
| Year: |
1997 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
The human XRCC9 gene corrects chromosomal instability and mutagen sensitivities in CHO UV40 cells. |
| Volume: |
94 |
| Issue: |
17 |
| Pages: |
9232-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
de Winter JP |
| Year: |
1998 |
| Journal: |
Nat Genet |
| Title: |
The Fanconi anaemia group G gene FANCG is identical with XRCC9. |
| Volume: |
20 |
| Issue: |
3 |
| Pages: |
281-3 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sjogren CA |
| Year: |
2017 |
| Journal: |
Plant Cell Environ |
| Title: |
SUV2, which encodes an ATR-related cell cycle checkpoint and putative plant ATRIP, is required for aluminium-dependent root growth inhibition in Arabidopsis. |
| Volume: |
40 |
| Issue: |
9 |
| Pages: |
1849-1860 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sakamoto AN |
| Year: |
2009 |
| Journal: |
Plant J |
| Title: |
A UVB-hypersensitive mutant in Arabidopsis thaliana is defective in the DNA damage response. |
| Volume: |
60 |
| Issue: |
3 |
| Pages: |
509-17 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sweeney PR |
| Year: |
2009 |
| Journal: |
Plant J |
| Title: |
The Arabidopsis ATRIP ortholog is required for a programmed response to replication inhibitors. |
| Volume: |
60 |
| Issue: |
3 |
| Pages: |
518-26 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
3053
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
762
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
753
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
754
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1624
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
970
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
970
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
970
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
837
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Burikhanov R |
| Year: |
2017 |
| Journal: |
Cell Rep |
| Title: |
Chloroquine-Inducible Par-4 Secretion Is Essential for Tumor Cell Apoptosis and Inhibition of Metastasis. |
| Volume: |
18 |
| Issue: |
2 |
| Pages: |
508-519 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
179
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
856
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
777
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
890
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
490
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
799
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
433
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
428
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
962
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1207
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
890
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
890
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1207
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
890
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
814
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1069
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
830
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
815
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
813
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
903
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1133
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
814
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
456
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
428
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
428
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
477
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
200
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ma C |
| Year: |
2013 |
| Journal: |
J Biol Chem |
| Title: |
Redox-regulated cargo binding and release by the peroxisomal targeting signal receptor, Pex5. |
| Volume: |
288 |
| Issue: |
38 |
| Pages: |
27220-27231 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Liu H |
| Year: |
1995 |
| Journal: |
J Biol Chem |
| Title: |
PER3, a gene required for peroxisome biogenesis in Pichia pastoris, encodes a peroxisomal membrane protein involved in protein import. |
| Volume: |
270 |
| Issue: |
18 |
| Pages: |
10940-51 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dujon B |
| Year: |
2004 |
| Journal: |
Nature |
| Title: |
Genome evolution in yeasts. |
| Volume: |
430 |
| Issue: |
6995 |
| Pages: |
35-44 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sala V |
| Year: |
2012 |
| Journal: |
Mol Med |
| Title: |
Signaling to cardiac hypertrophy: insights from human and mouse RASopathies. |
| Volume: |
18 |
| Issue: |
1 |
| Pages: |
938-47 |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bankston JR |
| Year: |
2012 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Structure and stoichiometry of an accessory subunit TRIP8b interaction with hyperpolarization-activated cyclic nucleotide-gated channels. |
| Volume: |
109 |
| Issue: |
20 |
| Pages: |
7899-904 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Perini ED |
| Year: |
2014 |
| Journal: |
Traffic |
| Title: |
Mammalian CORVET is required for fusion and conversion of distinct early endosome subpopulations. |
| Volume: |
15 |
| Issue: |
12 |
| Pages: |
1366-89 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
164
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
166
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
79
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
99
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
397
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
517
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
430
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
297
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
205
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chan C |
| Year: |
2004 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Structural basis of activity and allosteric control of diguanylate cyclase. |
| Volume: |
101 |
| Issue: |
49 |
| Pages: |
17084-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Aggarwal AK |
| Year: |
1988 |
| Journal: |
Science |
| Title: |
Recognition of a DNA operator by the repressor of phage 434: a view at high resolution. |
| Volume: |
242 |
| Issue: |
4880 |
| Pages: |
899-907 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Steinmetzer K |
| Year: |
2002 |
| Journal: |
Nucleic Acids Res |
| Title: |
CopR binds and bends its target DNA: a footprinting and fluorescence resonance energy transfer study. |
| Volume: |
30 |
| Issue: |
9 |
| Pages: |
2052-60 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yang H |
| Year: |
2016 |
| Journal: |
Protein Cell |
| Title: |
4.4 ? Resolution Cryo-EM structure of human mTOR Complex 1. |
| Volume: |
7 |
| Issue: |
12 |
| Pages: |
878-887 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Christianson JC |
| Year: |
2011 |
| Journal: |
Nat Cell Biol |
| Title: |
Defining human ERAD networks through an integrative mapping strategy. |
| Volume: |
14 |
| Issue: |
1 |
| Pages: |
93-105 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hao HX |
| Year: |
2009 |
| Journal: |
Science |
| Title: |
SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma. |
| Volume: |
325 |
| Issue: |
5944 |
| Pages: |
1139-42 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
McNeil MB |
| Year: |
2012 |
| Journal: |
J Biol Chem |
| Title: |
SdhE is a conserved protein required for flavinylation of succinate dehydrogenase in bacteria. |
| Volume: |
287 |
| Issue: |
22 |
| Pages: |
18418-28 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fairall L |
| Year: |
2001 |
| Journal: |
Mol Cell |
| Title: |
Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. |
| Volume: |
8 |
| Issue: |
2 |
| Pages: |
351-61 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cooper JP |
| Year: |
1997 |
| Journal: |
Nature |
| Title: |
Regulation of telomere length and function by a Myb-domain protein in fission yeast. |
| Volume: |
385 |
| Issue: |
6618 |
| Pages: |
744-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ito R |
| Year: |
2001 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Temperature-sensitive phenotype of Chinese hamster ovary cells defective in PEX5 gene. |
| Volume: |
288 |
| Issue: |
2 |
| Pages: |
321-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ito R |
| Year: |
2005 |
| Journal: |
J Biochem |
| Title: |
Identification of Pex5pM, and retarded maturation of 3-ketoacyl-CoA thiolase and acyl-CoA oxidase in CHO cells expressing mutant Pex5p isoforms. |
| Volume: |
138 |
| Issue: |
6 |
| Pages: |
781-90 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Otera H |
| Year: |
2002 |
| Journal: |
Mol Cell Biol |
| Title: |
Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import. |
| Volume: |
22 |
| Issue: |
6 |
| Pages: |
1639-55 |
|
•
•
•
•
•
|