| Type |
Details |
Score |
| Publication |
| First Author: |
Mashiguchi K |
| Year: |
2009 |
| Journal: |
Biosci Biotechnol Biochem |
| Title: |
Genome-wide identification, structure and expression studies, and mutant collection of 22 early nodulin-like protein genes in Arabidopsis. |
| Volume: |
73 |
| Issue: |
11 |
| Pages: |
2452-9 |
|
•
•
•
•
•
|
| HT Experiment |
| Series Id: |
GSE39621 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
|
•
•
•
•
•
|
| 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 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
189
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
189
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
189
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
192
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
593
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
502
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
359
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
309
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
530
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
377
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
500
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
363
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
479
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
528
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
299
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
486
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
322
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
373
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
83
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
291
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
404
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
502
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
233
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
502
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Min T |
| Year: |
2003 |
| Journal: |
J Biol Chem |
| Title: |
Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases. |
| Volume: |
278 |
| Issue: |
50 |
| Pages: |
50714-23 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chillappagari S |
| Year: |
2009 |
| Journal: |
J Bacteriol |
| Title: |
Copper acquisition is mediated by YcnJ and regulated by YcnK and CsoR in Bacillus subtilis. |
| Volume: |
191 |
| Issue: |
7 |
| Pages: |
2362-70 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Peñalver-Mellado M |
| Year: |
2006 |
| Journal: |
Mol Microbiol |
| Title: |
Recruitment of a novel zinc-bound transcriptional factor by a bacterial HMGA-type protein is required for regulating multiple processes in Myxococcus xanthus. |
| Volume: |
61 |
| Issue: |
4 |
| Pages: |
910-26 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Waltersperger S |
| Year: |
2010 |
| Journal: |
Proteins |
| Title: |
Crystal structure of archaemetzincin AmzA from Methanopyrus kandleri at 1.5 A resolution. |
| Volume: |
78 |
| Issue: |
12 |
| Pages: |
2720-3 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
ElÃas-Arnanz M |
| Year: |
2010 |
| Journal: |
FEMS Microbiol Rev |
| Title: |
The regulatory action of the myxobacterial CarD/CarG complex: a bacterial enhanceosome? |
| Volume: |
34 |
| Issue: |
5 |
| Pages: |
764-78 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Flühe L |
| Year: |
2013 |
| Journal: |
J Am Chem Soc |
| Title: |
Two [4Fe-4S] clusters containing radical SAM enzyme SkfB catalyze thioether bond formation during the maturation of the sporulation killing factor. |
| Volume: |
135 |
| Issue: |
3 |
| Pages: |
959-62 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sivaraman J |
| Year: |
2000 |
| Journal: |
J Mol Biol |
| Title: |
Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine. |
| Volume: |
295 |
| Issue: |
4 |
| Pages: |
939-51 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Guncar G |
| Year: |
2000 |
| Journal: |
Structure |
| Title: |
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease. |
| Volume: |
8 |
| Issue: |
3 |
| Pages: |
305-13 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nägler DK |
| Year: |
1999 |
| Journal: |
Biochemistry |
| Title: |
Human cathepsin X: A cysteine protease with unique carboxypeptidase activity. |
| Volume: |
38 |
| Issue: |
39 |
| Pages: |
12648-54 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Klemencic I |
| Year: |
2000 |
| Journal: |
Eur J Biochem |
| Title: |
Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase. |
| Volume: |
267 |
| Issue: |
17 |
| Pages: |
5404-12 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Devanathan G |
| Year: |
2005 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Carboxy-monopeptidase substrate specificity of human cathepsin X. |
| Volume: |
329 |
| Issue: |
2 |
| Pages: |
445-52 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Puzer L |
| Year: |
2005 |
| Journal: |
Biol Chem |
| Title: |
Recombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L. |
| Volume: |
386 |
| Issue: |
11 |
| Pages: |
1191-5 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Obermajer N |
| Year: |
2006 |
| Journal: |
Exp Cell Res |
| Title: |
Carboxypeptidase cathepsin X mediates beta2-integrin-dependent adhesion of differentiated U-937 cells. |
| Volume: |
312 |
| Issue: |
13 |
| Pages: |
2515-27 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kraus S |
| Year: |
2011 |
| Journal: |
Eur J Cell Biol |
| Title: |
Cellular senescence induced by cathepsin X downregulation. |
| Volume: |
90 |
| Issue: |
8 |
| Pages: |
678-86 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Krueger S |
| Year: |
2005 |
| Journal: |
J Pathol |
| Title: |
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer. |
| Volume: |
207 |
| Issue: |
1 |
| Pages: |
32-42 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Obermajer N |
| Year: |
2009 |
| Journal: |
Eur J Cell Biol |
| Title: |
Cathepsin X prevents an effective immune response against Helicobacter pylori infection. |
| Volume: |
88 |
| Issue: |
8 |
| Pages: |
461-71 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hattori A |
| Year: |
1999 |
| Journal: |
J Biochem |
| Title: |
Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase. |
| Volume: |
125 |
| Issue: |
5 |
| Pages: |
931-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Schomburg L |
| Year: |
2000 |
| Journal: |
Eur J Biochem |
| Title: |
Molecular characterization of a puromycin-insensitive leucyl-specific aminopeptidase, PILS-AP. |
| Volume: |
267 |
| Issue: |
11 |
| Pages: |
3198-207 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Georgiadou D |
| Year: |
2010 |
| Journal: |
J Immunol |
| Title: |
Placental leucine aminopeptidase efficiently generates mature antigenic peptides in vitro but in patterns distinct from endoplasmic reticulum aminopeptidase 1. |
| Volume: |
185 |
| Issue: |
3 |
| Pages: |
1584-92 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chang SC |
| Year: |
2005 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism. |
| Volume: |
102 |
| Issue: |
47 |
| Pages: |
17107-12 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hattori A |
| Year: |
2000 |
| Journal: |
J Biochem |
| Title: |
Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells. |
| Volume: |
128 |
| Issue: |
5 |
| Pages: |
755-62 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chen R |
| Year: |
2012 |
| Journal: |
Rheumatol Int |
| Title: |
The association between seven ERAP1 polymorphisms and ankylosing spondylitis susceptibility: a meta-analysis involving 8,530 cases and 12,449 controls. |
| Volume: |
32 |
| Issue: |
4 |
| Pages: |
909-14 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Genetic Analysis of Psoriasis Consortium & the Wellcome Trust Case Control Consortium 2. |
| Year: |
2010 |
| Journal: |
Nat Genet |
| Title: |
A genome-wide association study identifies new psoriasis susceptibility loci and an interaction between HLA-C and ERAP1. |
| Volume: |
42 |
| Issue: |
11 |
| Pages: |
985-90 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fung EY |
| Year: |
2009 |
| Journal: |
Genes Immun |
| Title: |
Analysis of 17 autoimmune disease-associated variants in type 1 diabetes identifies 6q23/TNFAIP3 as a susceptibility locus. |
| Volume: |
10 |
| Issue: |
2 |
| Pages: |
188-91 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Li GH |
| Year: |
2011 |
| Journal: |
Hum Genet |
| Title: |
Identification of QTL genes for BMD variation using both linkage and gene-based association approaches. |
| Volume: |
130 |
| Issue: |
4 |
| Pages: |
539-46 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Binding of a specific DNA fragment and S-adenosyl methionine (SAM) co-repressor molecules to the Escherichia coli methionine repressor (MetJ) leads to a significant reduction in dynamic flexibility of the ternary complex, with considerable entropy-enthalpy compensation, not necessarily involving any overall conformational change []. MetJ is a regulatory protein which when combined with S-adenosylmethionine (SAM) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis. It is also autoregulated.MetJ binds arrays of two to five adjacent copies of an eight base-pair 'metbox' sequence. MetJ forms sufficiently strong interactions with the sugar-phosphate backbone to accomodate sequence variation in natural operators. However, it is very sensitive to particular base changes in the operator. MetJ exists as a homodimer [, , ].The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein β-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognises sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Peptidase family M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to be aminopeptidases, degrading synthetic substrates and peptides. The peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events [, ].Archaemetzincin (from Mycococcus xanthus) seem to have evolved into a zinc-binding transcription factor fulfilling only a structuralrole [, ]. The structure of archaemetzincin from Methanopyrus kandleri has been resolved []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Endoplasmic reticulum aminopeptidase 1 (ERAP1 or PILS; MEROPS identifier M01.018) is an aminopeptidase with a preference to release Leu or Met from the N terminus of a peptide, but can hydrolyze Phe, Tyr, Ile or Cys bonds but poorly [, ]. The aminopeptidase is insensitive to inhibition by puromycin (which inhibits cytosol alanyl aminopeptidase and dipeptidyl-peptidases II and IV) and is also known as puromycin-insensitive leucyl-specific aminopeptidase or PILS-AP [, ]. In humans, ERAP1 associates with another aminopeptidase, ERAP2, in the endoplasmic reticulum and both participate in the processing of MHC-presented peptides []. Peptides generated by degradation of proteins by the proteasome bind to a transporter associated with antigen presentation (TAP) and are exported across the plasma membrane from the cytoplasm to the endoplasmic reticulum where they are trimmed by the ERAP aminopeptidases and cystinyl aminopeptidase to be 8-11 amino acids in length which then associate with the MHC complex and beta2-microglobulin []. ERAP1 is most active with peptides 9-16 residues long, but activity drops once a peptide optimal for antigen presentation is achieved. This molecular ruler effect is achieved by binding the C terminus of the substrate peptide close to the active site []. ERAP1 may also function in blood pressure regulation because it cleaves angiotensin II to the tripeptide His-Pro-Phe via angiotensin II and IV intermediates, and converts kallidin to bradykinin []. ERAP1 has been associated with several human diseases, including ankylosing spondylitis [], psoriasis [], type 1 diabetes []and osteoporsis []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Spore formation by the bacterium Bacillus subtilis is a stress response triggered by nutrient limitation. Two operons are strongly induced at the start of sporulation; one of them is skf (for sporulation killing factor). skf produces a killing factor which, together with a signaling protein, act cooperatively to block sister cells from sporulating and cause them to lyse, providing a source of nutrients to support the sporulation process [].The first gene of the skf operon, skfA, encodes a small peptide. SkfA induces the lysis of sibling cells that have not entered the sporulation pathway []. The product of the second gene, skfB, encodes a radical SAM enzyme. SkfB creates a sactipeptide (sulfur-to-α-carbon) crosslink of Cys-4 to Met-12 of the mature form of SkfA. In Paenibacillus larvae subsp larvae B-3650, the Met is replaced by Leu, so the modification must be different. SkfB has 2 4Fe-4S clusters, one in its radical SAM domain () and one in a region that somewhat resembles the SPASM domain () []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Binding of a specific DNA fragment and S-adenosyl methionine (SAM) co-repressor molecules to the Escherichia coli methionine repressor (MetJ) leads to a significant reduction in dynamic flexibility of the ternary complex, with considerable entropy-enthalpy compensation, not necessarily involving any overall conformational change []. MetJ is a regulatory protein which when combined with S-adenosylmethionine (SAM) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis. It is also autoregulated.MetJ binds arrays of two to five adjacent copies of an eight base-pair 'metbox' sequence. MetJ forms sufficiently strong interactions with the sugar-phosphate backbone to accomodate sequence variation in natural operators. However, it is very sensitive to particular base changes in the operator. MetJ exists as a homodimer [, , ].The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein β-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognises sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Cathepsin Z (also known as Cathepsin X , and MEROPS identifier C01.013) is predominantly a cysteine-type carboxypeptidase with limited endopeptidase or dipeptidyl-peptidase activity, mainly against synthetic substrates [, ]. The substrate specificity has been examined by peptide scanning and shows that proline is not tolerated in the P1 or P1' positions and poorly accepted in P2, and Tyr, Met and Cys are marginally prefered in P2, P1 and P1' [, ].Cathepsin X is synthesized as an inactive zymogen, but the propeptide lacks the ERFNIN motif characteristic of lysosomal cysteine peptidases. A disulfide bridge can be formed between the proregion and the enzyme which leads to inactivation of the zymogen by the formation of a reversible covalent bond with the active site residue []. From the crystal structure of the mature enzyme, a short, five-residue 'mini-loop' which includes the motif His-Xaa-Xaa-Xaa-Tyr restricts access to the S2' binding pocket, and it is the histidine that confers carboxypeptidase activity []. Rotation of the histidine ring permits dipeptidyl-peptidase substrates to bind. The presence of an exposed RGD motif allows binding to beta3-integrin []and the enzyme may have a role in cell signalling. Cathepsin X deficiency leads to accelerated cell senescence []. Cathepsin X also regulates the immune response to Helicobacter pylori infection [, ]. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dickson R |
| Year: |
1994 |
| Journal: |
J Biol Chem |
| Title: |
Cloning, expression, and purification of a functional nonacetylated mammalian mitochondrial chaperonin 10. |
| Volume: |
269 |
| Issue: |
43 |
| Pages: |
26858-64 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tucker KL |
| Year: |
1996 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Complementation of methylation deficiency in embryonic stem cells by a DNA methyltransferase minigene. |
| Volume: |
93 |
| Issue: |
23 |
| Pages: |
12920-5 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rorick NK |
| Year: |
2011 |
| Journal: |
Am J Med Genet A |
| Title: |
Genomic strategy identifies a missense mutation in WD-repeat domain 65 (WDR65) in an individual with Van der Woude syndrome. |
| Volume: |
155A |
| Issue: |
6 |
| Pages: |
1314-21 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yousaf R |
| Year: |
2018 |
| Journal: |
J Clin Invest |
| Title: |
Modifier variant of METTL13 suppresses human GAB1-associated profound deafness. |
| Volume: |
128 |
| Issue: |
4 |
| Pages: |
1509-1522 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tooley CE |
| Year: |
2010 |
| Journal: |
Nature |
| Title: |
NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein. |
| Volume: |
466 |
| Issue: |
7310 |
| Pages: |
1125-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jakubczak JL |
| Year: |
1998 |
| Journal: |
Mol Cell Biol |
| Title: |
NK1, a natural splice variant of hepatocyte growth factor/scatter factor, is a partial agonist in vivo. |
| Volume: |
18 |
| Issue: |
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