Type |
Details |
Score |
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
295
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
454
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
832
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
416
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
402
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
724
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
225
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
614
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
363
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
422
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
422
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
614
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
295
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
454
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
504
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
434
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
450
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
388
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
313
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
542
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
157
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
241
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
724
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
230
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
229
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
353
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
422
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
446
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
323
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
746
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
530
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
218
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
216
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
115
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
133
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
530
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
174
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1242
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1421
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
983
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
427
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
724
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
443
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
638
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
312
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
289
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1302
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
422
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1232
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
427
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
530
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
422
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
105
 |
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: |
Andrade MA |
Year: |
2001 |
Journal: |
J Struct Biol |
Title: |
Protein repeats: structures, functions, and evolution. |
Volume: |
134 |
Issue: |
2-3 |
Pages: |
117-31 |
|
•
•
•
•
•
|
Publication |
First Author: |
Han Y |
Year: |
2020 |
Journal: |
Channels (Austin) |
Title: |
The structure and function of TRIP8b, an auxiliary subunit of hyperpolarization-activated cyclic-nucleotide gated channels. |
Volume: |
14 |
Issue: |
1 |
Pages: |
110-122 |
|
•
•
•
•
•
|
Publication |
First Author: |
Stuart MK |
Year: |
2017 |
Journal: |
Monoclon Antib Immunodiagn Immunother |
Title: |
Fine Epitope Mapping of Monoclonal Antibodies to the DNA Repair Protein, RadA. |
Volume: |
36 |
Issue: |
3 |
Pages: |
83-94 |
|
•
•
•
•
•
|
Publication |
First Author: |
Swingle MR |
Year: |
2004 |
Journal: |
J Biol Chem |
Title: |
Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5. |
Volume: |
279 |
Issue: |
32 |
Pages: |
33992-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hinds TD Jr |
Year: |
2008 |
Journal: |
Int J Biochem Cell Biol |
Title: |
Protein phosphatase 5. |
Volume: |
40 |
Issue: |
11 |
Pages: |
2358-62 |
|
•
•
•
•
•
|
Publication |
First Author: |
Chinkers M |
Year: |
2001 |
Journal: |
Trends Endocrinol Metab |
Title: |
Protein phosphatase 5 in signal transduction. |
Volume: |
12 |
Issue: |
1 |
Pages: |
28-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Andreeva AV |
Year: |
1999 |
Journal: |
Cell Signal |
Title: |
RdgC/PP5-related phosphatases: novel components in signal transduction. |
Volume: |
11 |
Issue: |
8 |
Pages: |
555-62 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhang J |
Year: |
2005 |
Journal: |
Mol Cell Biol |
Title: |
Protein phosphatase 5 is required for ATR-mediated checkpoint activation. |
Volume: |
25 |
Issue: |
22 |
Pages: |
9910-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Vaughan CK |
Year: |
2008 |
Journal: |
Mol Cell |
Title: |
Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. |
Volume: |
31 |
Issue: |
6 |
Pages: |
886-95 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
LapB (lipopolysaccharide assembly protein B) contains three major structural motifs: the N-terminal transmembrane helix, several tetratricopeptide repeats (TPR), and a C-terminal rubredoxin metal binding domain. This entry represents the rubredoxin-like metal binding domain. Rubredoxin proteins form small non-heme iron binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. Rubredoxins are most commonly found in bacterial systems, but have also been found in eukaryotes. The key features of these rubredoxin-like domains are the extended loops or 'knuckles' and the tetracysteine mode of iron binding. Structural analysis of LapB from Escherichia coli show that the rubredoxin metal binding domain is intimately bound to the TPR motifs and that this association to the TPR motifs is essential to LPS regulation and growth in vivo []. Proteins containing this domain also include RadA. In E. coli, RadA (or Sms) participates in the recombinational repair of radiation-damaged DNA in a process that uses an undamaged DNA strand in one DNA duplex to fill a DNA strand gap in a homologous sister DNA duplex. RadA carries a zinc finger at the N-terminal domain []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs [, , , , ]. This entry represents the C-terminal phosphatase domain. Proteins containing this domain also include yeast Ppt1, which is a serine/threonine phosphatase that regulates Hsp90 chaperone by affecting its ATPase and cochaperone binding activitie []. The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of manycellular processes [, ]. PPPs belong to the metallophosphatase (MPP) superfamily. |
|
•
•
•
•
•
|
Publication |
First Author: |
Capetanaki Y |
Year: |
1990 |
Journal: |
Oncogene |
Title: |
Mouse vimentin: structural relationship to fos, jun, CREB and tpr. |
Volume: |
5 |
Issue: |
5 |
Pages: |
645-55 |
|
•
•
•
•
•
|
Publication |
First Author: |
Melo LG |
Year: |
1999 |
Journal: |
Regul Pept |
Title: |
Chronic hypertension in ANP knockout mice: contribution of peripheral resistance. |
Volume: |
79 |
Issue: |
2-3 |
Pages: |
109-15 |
|
•
•
•
•
•
|
Publication |
First Author: |
Chaudhuri M |
Year: |
2001 |
Journal: |
Gene |
Title: |
Cloning and characterization of a novel serine/threonine protein phosphatase type 5 from Trypanosoma brucei. |
Volume: |
266 |
Issue: |
1-2 |
Pages: |
1-13 |
|
•
•
•
•
•
|
Publication |
First Author: |
Odunuga OO |
Year: |
2003 |
Journal: |
J Biol Chem |
Title: |
Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity. |
Volume: |
278 |
Issue: |
9 |
Pages: |
6896-904 |
|
•
•
•
•
•
|
Publication |
First Author: |
Walsh EK |
Year: |
2004 |
Journal: |
Am J Physiol Heart Circ Physiol |
Title: |
Control of myocardial oxygen consumption in transgenic mice overexpressing vascular eNOS. |
Volume: |
287 |
Issue: |
5 |
Pages: |
H2115-21 |
|
•
•
•
•
•
|
Publication |
First Author: |
He J |
Year: |
2013 |
Journal: |
Arterioscler Thromb Vasc Biol |
Title: |
Liver kinase B1 is required for thromboxane receptor-dependent nuclear factor-κB activation and inflammatory responses. |
Volume: |
33 |
Issue: |
6 |
Pages: |
1297-305 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang Y |
Year: |
2003 |
Journal: |
Eur J Neurosci |
Title: |
A hot spot for hotfoot mutations in the gene encoding the delta2 glutamate receptor. |
Volume: |
17 |
Issue: |
8 |
Pages: |
1581-90 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
856
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
830
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
240
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
815
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
773
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Saksouk N |
Year: |
2014 |
Journal: |
Mol Cell |
Title: |
Redundant mechanisms to form silent chromatin at pericentromeric regions rely on BEND3 and DNA methylation. |
Volume: |
56 |
Issue: |
4 |
Pages: |
580-94 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
210
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
93
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
144
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
159
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Lee YT |
Year: |
2004 |
Journal: |
J Biol Chem |
Title: |
Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. |
Volume: |
279 |
Issue: |
16 |
Pages: |
16511-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Garcia-Ranea JA |
Year: |
2002 |
Journal: |
FEBS Lett |
Title: |
p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families. |
Volume: |
529 |
Issue: |
2-3 |
Pages: |
162-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Khan A |
Year: |
2015 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
BEND3 represses rDNA transcription by stabilizing a NoRC component via USP21 deubiquitinase. |
Volume: |
112 |
Issue: |
27 |
Pages: |
8338-43 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sathyan KM |
Year: |
2011 |
Journal: |
J Cell Sci |
Title: |
A BEN-domain-containing protein associates with heterochromatin and represses transcription. |
Volume: |
124 |
Issue: |
Pt 18 |
Pages: |
3149-63 |
|
•
•
•
•
•
|
Publication |
First Author: |
Khan A |
Year: |
2015 |
Journal: |
Transcription |
Title: |
BEND3 mediates transcriptional repression and heterochromatin organization. |
Volume: |
6 |
Issue: |
5 |
Pages: |
102-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pitchai GP |
Year: |
2017 |
Journal: |
Nucleic Acids Res |
Title: |
A novel TPR-BEN domain interaction mediates PICH-BEND3 association. |
Volume: |
45 |
Issue: |
19 |
Pages: |
11413-11424 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
The GGDEF domain, which has been named after the conserved central sequence pattern GG[DE][DE]F is widespread in prokaryotes. It is typically present in multidomain proteins containing regulatory domains of signaling pathways or protein-protein or protein-ligand interaction modules, such as the response regulatory domain, the PAS/PAC domain, the HAMP domain, the GAF domain, the FHA domain or the TPR repeat. However a few single-domain proteins are also known. The GGDEF domain is involved in signal transduction and is likely to catalyze synthesis or hydrolysis of cyclic diguanylate (c-diGMP, bis(3',5')-cyclic diguanylic acid), an effector molecule that consists of two cGMP moieties bound head-to-tail [, , ].Structural studies of PleD from Caulobacter crescentus show that this domain forms a five-stranded beta sheet surrounded by helices, similar to the catalytic core of adenylate cyclase []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
The bipartite CS domain, which was named after CHORD-containing proteins and SGT1 [], is a ~100-residue protein-protein interaction module. The CS domain can be found in stand-alone form, as well as fused with other domains, such as CHORD (), SGS (), TPR (), cytochrome b5 () or b5 reductase, in multidomain proteins []. The CS domain has a compact antiparallel β-sandwich fold consisting of seven β-strands [, ]. Some proteins known to contain a CS domain are listed below []: Eukaryotic proteins of the SGT1 family. Eukaryotic Rar1, related to pathogenic resistance in plants, and to development in animals. Eukaryotic nuclear movement protein nudC. Eukaryotic proteins of the p23/wos2 family, which act as co-chaperone. Animal b5+b5R flavo-hemo cytochrome NAD(P)H oxydoreductase type B. Mammalian integrin beta-1-binding protein 2 (melusin). |
|
•
•
•
•
•
|
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 between a TPR domain in PICH and a BEN domain in BEND3 []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
458
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
777
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1207
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
389
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
416
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1862
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1207
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
604
 |
Fragment?: |
false |
|
•
•
•
•
•
|