| Type |
Details |
Score |
| 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 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: |
303
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
184
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
775
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1572
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1838
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1497
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
709
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
352
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
523
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
548
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1739
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ohta K |
| Year: |
1995 |
| Journal: |
Neuron |
| Title: |
Plexin: a novel neuronal cell surface molecule that mediates cell adhesion via a homophilic binding mechanism in the presence of calcium ions. |
| Volume: |
14 |
| Issue: |
6 |
| Pages: |
1189-99 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Repeat |
| Description: |
This is a cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found in plexin () []. Two copies of the repeat are found in mahogany protein. A related Caenorhabditis elegans protein () contains four copies of the repeat, while the Met receptor contains a single copy of the repeat. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kennedy LJ |
| Year: |
2001 |
| Journal: |
Anim Genet |
| Title: |
Nomenclature for factors of the dog major histocompatibility system (DLA), 2000: second report of the ISAG DLA Nomenclature Committee. |
| Volume: |
32 |
| Issue: |
4 |
| Pages: |
193-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Waldhart AN |
| Year: |
2023 |
| Journal: |
iScience |
| Title: |
Optimal HSF1 activation in response to acute cold stress in BAT requires nuclear TXNIP. |
| Volume: |
26 |
| Issue: |
5 |
| Pages: |
106538 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cassol F |
| Year: |
2019 |
| Journal: |
iScience |
| Title: |
Tracking Dynamics of Spontaneous Tumors in Mice Using Photon-Counting Computed Tomography. |
| Volume: |
21 |
|
| Pages: |
68-83 |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
coisogenic, mutant strain, transgenic |
|
•
•
•
•
•
|
| Allele |
| Name: |
H3.3 histone A; targeted mutation 1, Hans Joerg Fehling |
| Allele Type: |
Targeted |
| Attribute String: |
Conditional ready, Epitope tag, Reporter |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Gt(ROSA)26Sor/? Tg(Nes-cre)1Kln/? |
| Background: |
involves: 129S1/Sv * 129X1/SvJ * C57BL/6 * SJL |
| Zygosity: |
cn |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
transcription profiling by array |
| Study Type: |
Baseline |
| Source: |
GEO |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry includes hepatocyte growth factor (HGF; also called scatter factor) and HGF-like proteins (also known as macrophage stimulatory protein, MST1). Hepatocyte growth factor (HGF) is an activating ligand of the Met receptor tyrosine kinase, whose activity is essential for normal tissue development and organ regeneration []. HGF is essential for placental, liver, and muscle development, whereas MST1 is not required for embryogenesis, fertility, or wound healing. Genes for HGF and its receptor, the Met tyrosine kinase, are close together on chromosome 7, so that polysomy of chromosome 7 may contribute to malignancy through overproduction of both molecules. MST1 and its receptor, the Ron tyrosine kinase, are close together on chromosome 3. HGF and MST1 are closely related to plasminogen, having similar domain architecture: signal sequence followed by a PAN (formerly apple) domain, four (rather than five) kringle domains, and a trypsin domain, which appears to lack any peptidase activity. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
53
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bork P |
| Year: |
1999 |
| Journal: |
Trends Biochem Sci |
| Title: |
Domains in plexins: links to integrins and transcription factors. |
| Volume: |
24 |
| Issue: |
7 |
| Pages: |
261-3 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Collesi C |
| Year: |
1996 |
| Journal: |
Mol Cell Biol |
| Title: |
A splicing variant of the RON transcript induces constitutive tyrosine kinase activity and an invasive phenotype. |
| Volume: |
16 |
| Issue: |
10 |
| Pages: |
5518-26 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Webb KJ |
| Year: |
2010 |
| Journal: |
Biochemistry |
| Title: |
Identification of protein N-terminal methyltransferases in yeast and humans. |
| Volume: |
49 |
| Issue: |
25 |
| Pages: |
5225-35 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Petkowski JJ |
| Year: |
2013 |
| Journal: |
Biochem J |
| Title: |
NRMT2 is an N-terminal monomethylase that primes for its homologue NRMT1. |
| Volume: |
456 |
| Issue: |
3 |
| Pages: |
453-62 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dong C |
| Year: |
2018 |
| Journal: |
Commun Biol |
| Title: |
An asparagine/glycine switch governs product specificity of human N-terminal methyltransferase NTMT2. |
| Volume: |
1 |
|
| Pages: |
183 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wu R |
| Year: |
2015 |
| Journal: |
Genes Dev |
| Title: |
Molecular basis for histone N-terminal methylation by NRMT1. |
| Volume: |
29 |
| Issue: |
22 |
| Pages: |
2337-42 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zimmer AL |
| Year: |
2014 |
| Journal: |
Protein Sci |
| Title: |
Three-dimensional structure of a sugar N-formyltransferase from Francisella tularensis. |
| Volume: |
23 |
| Issue: |
3 |
| Pages: |
273-83 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The IPT (Ig-like, plexins, transcription factors) domain has an immunoglobulin like fold []. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. The Ron tyrosine kinase receptor shares with the members of its subfamily (Met and Sea) a unique functional feature: the control of cell dissociation, motility, and invasion of extracellular matrices (scattering) []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Phytocyanins are blue copper proteins found in chloropasts of higher plants. They can be further subdivided into uclacyanins, stellacyanins, plantacyanins, and early nodulins. Stellacyanins have a blue copper coordinated by two His, one Cys and one Gln. In plantacyanins and uclacyanins, the ligands of the type-I Cu sites are two His, one Cys and one Met [, , , ]. Early nodulins lack amino acid residues that coordinate Cu, so they are believed to be involved in unknown processes without binding Cu []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry includes the CoxC protein from the CO-metabolizing bacterium Oligotropha carboxidovorans []. In the CoxC and CoxH proteins, the LytTR DNA-binding transcriptional regulator domain []is found in association with MHYT, a recently described sensor domain, which contains six transmembrane segments carrying conserved His and Met residues []. The coxCand coxHgenes flank the operon encoding the CO dehydrogenase and are involved in transcriptional regulaton of the autotrophic metabolism in Oligotropha carboxidovorans []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This is the C-terminal domain of N-formyltransferase from Francisella tularensis. N-formylated sugars are observed on O-antigens of pathogenic Gram-negative bacteria. This C-terminal domain is responsible for dimerization. In particular, the beta hairpin motif present in the domain helps create a subunit-subunit interface. The dimeric interface is characterized by a hydrophobic patch formed by Ile 195, Leu 197, Val 201, Met 203, Ile 207, Phe 223, Val 231, Val 233, Leu 235, and Leu 237 from both monomers []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents a region of about 41 amino acids found in a number of small proteins in a wide range of bacteria. The region usually begins with the initiator Met and contains two CxxC motifs separated by 17 amino acids. One protein in this entry has been noted as a putative regulatory protein, designated FmdB []. Most proteins in this entry have a C-terminal region containing highly degenerate sequence. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
All fungal and animal N-terminally methylated proteins contain a unique N-terminal motif, Met-(Ala/Pro/Ser)-Pro-Lys. Alpha-N-methyltransferase methylates the N terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. It catalyses mono-, di- or tri-methylation of the exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif [, , ]. Some of the substrates may be primed by NTMT2-mediated monomethylation []. |
|
•
•
•
•
•
|
| 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 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: |
1464
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1372
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
184
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
432
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1487
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1453
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
770
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1224
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| HT Experiment |
| Series Id: |
GSE6398 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
|
•
•
•
•
•
|
| HT Experiment |
| Series Id: |
GSE6397 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
WT vs. Mutant |
| Source: |
ArrayExpress |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
congenic, mutant strain, transgenic |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
congenic, mutant strain, targeted mutation |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Myh6-tTA)6Smbf/? Tg(tetO-TPR/MET,-EGFP)12Tcre/? |
| Background: |
FVB.Cg-Tg(Myh6-tTA)6Smbf Tg(tetO-TPR/MET,-EGFP)12Tcre |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Tg(Islr-cre/ERT2)#Tobe/? |
| Background: |
involves: 129S6/SvEvTac * C57BL/6J * C57BL/6NCrl |
| Zygosity: |
cn |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wyborn NR |
| Year: |
1996 |
| Journal: |
Eur J Biochem |
| Title: |
Molecular characterisation of formamidase from Methylophilus methylotrophus. |
| Volume: |
240 |
| Issue: |
2 |
| Pages: |
314-22 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Stammers DK |
| Year: |
2001 |
| Journal: |
EMBO J |
| Title: |
The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases. |
| Volume: |
20 |
| Issue: |
23 |
| Pages: |
6619-26 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kotaka M |
| Year: |
2008 |
| Journal: |
J Mol Biol |
| Title: |
Structural analysis of the recognition of the negative regulator NmrA and DNA by the zinc finger from the GATA-type transcription factor AreA. |
| Volume: |
381 |
| Issue: |
2 |
| Pages: |
373-82 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhao Y |
| Year: |
2008 |
| Journal: |
J Biol Chem |
| Title: |
An NADPH sensor protein (HSCARG) down-regulates nitric oxide synthesis by association with argininosuccinate synthetase and is essential for epithelial cell viability. |
| Volume: |
283 |
| Issue: |
16 |
| Pages: |
11004-13 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
McGuirl MA |
| Year: |
2001 |
| Journal: |
J Biol Inorg Chem |
| Title: |
Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster. |
| Volume: |
6 |
| Issue: |
2 |
| Pages: |
189-95 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Shabani M |
| Year: |
2015 |
| Journal: |
Expert Opin Ther Targets |
| Title: |
Receptor tyrosine kinase-like orphan receptor 1: a novel target for cancer immunotherapy. |
| Volume: |
19 |
| Issue: |
7 |
| Pages: |
941-55 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cerpa W |
| Year: |
2015 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
RoR2 functions as a noncanonical Wnt receptor that regulates NMDAR-mediated synaptic transmission. |
| Volume: |
112 |
| Issue: |
15 |
| Pages: |
4797-802 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nomi M |
| Year: |
2001 |
| Journal: |
Mol Cell Biol |
| Title: |
Loss of mRor1 enhances the heart and skeletal abnormalities in mRor2-deficient mice: redundant and pleiotropic functions of mRor1 and mRor2 receptor tyrosine kinases. |
| Volume: |
21 |
| Issue: |
24 |
| Pages: |
8329-35 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gentile A |
| Year: |
2011 |
| Journal: |
Cancer Res |
| Title: |
Ror1 is a pseudokinase that is crucial for Met-driven tumorigenesis. |
| Volume: |
71 |
| Issue: |
8 |
| Pages: |
3132-41 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nomachi A |
| Year: |
2008 |
| Journal: |
J Biol Chem |
| Title: |
Receptor tyrosine kinase Ror2 mediates Wnt5a-induced polarized cell migration by activating c-Jun N-terminal kinase via actin-binding protein filamin A. |
| Volume: |
283 |
| Issue: |
41 |
| Pages: |
27973-81 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hughes JA |
| Year: |
2006 |
| Journal: |
Can J Microbiol |
| Title: |
In vivo hydrolysis of S-adenosyl-L-methionine in Escherichia coli increases export of 5-methylthioribose. |
| Volume: |
52 |
| Issue: |
6 |
| Pages: |
599-602 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Schultz JM |
| Year: |
2009 |
| Journal: |
Am J Hum Genet |
| Title: |
Noncoding mutations of HGF are associated with nonsyndromic hearing loss, DFNB39. |
| Volume: |
85 |
| Issue: |
1 |
| Pages: |
25-39 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents S-adenosyl-L-methionine (SAM) hydrolases (), which catalyse the hydrolysis of S-adenosyl-L-methionine, cleaving it to form L-homoserine and methylthioadenosine. This enzyme is produced by Bacteriophage T3, which infects Escherichia coli cells. SAM hydrolase can remove S-adenosylmethionine from the E. coli cell, thereby inhibiting a variety of SAM-related activities, such as dam and dcm methylase-directed DNA modifications and the synthesis of spermidine from putrescine []. Expression of SAM hydrolase in T3-transformed E. coli induces the met regulon by cleaving the SAM co-repressor to form 5'-methylthioadenosine, which is then cleaved to produce 5-methylthioribose []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The Ror family of receptor tyrosine kinases consists of two structurally related proteins, Ror1 and Ror2. Ror1 is a pseudokinase that acts as a substrate for the oncogenic tyrosine kinase Met []. It is expressed during development []. It shows no significant expression in normal adult tissues, but it is selectively overexpressed in a number of malignancies []. Ror2 functions as a Wnt receptor required to maintain basal NMDAR-mediated synaptic transmission []. For a time its ligand remained elusive, hence the name receptor tyrosine kinase-like orphan receptor-2 (Ror2). It is now established that Wnt5A acts a ligand for Ror2 []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Hepatocyte growth factor (HGF) is an activating ligand of the tyrosine kinase receptor Met. It activates Met by binding and promoting its dimerisation. This activation has been linked to promoting the invasive growth of many tumour types []. HGF acts as growth factor for a broad spectrum of tissues and cell types and has no detectable protease activity [].Defects in HGF are the cause of deafness autosomal recessive type 39 (DFNB39). A form of profound prelingual sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
FIP-Fve (Fungal Immunomodulatory Protein Fve) is a major fruiting body protein from Flammulina velutipes, a mushroom possessing immunomodulatory activity []. It stimulates lymphocyte mitogenesis, suppresses systemic anaphylaxis reactions and oedema, enhances transcription of IL-2, IFN-gamma and TNF-alpha, and haemagglutinates red blood cells. It appears to be a lectin with specificity for complex cell-surface carbohydrates. Fve adopts a tertiary structure consisting of an immunoglobulin-like β-sandwich, with seven strands arranged in two beta sheets, in a Greek-key topology. It forms a non-covalently linked homodimer containing no Cys, His or Met residues; dimerisation occurs by 3-D domain swapping of the N-terminal helices and is stabilised predominantly by hydrophobic interactions []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
FIP-Fve (Fungal Immunomodulatory Protein Fve) is a major fruiting body protein from Flammulina velutipes, a mushroom possessing immunomodulatory activity []. It stimulates lymphocyte mitogenesis, suppresses systemic anaphylaxis reactions and oedema, enhances transcription of IL-2, IFN-gamma and TNF-alpha, and haemagglutinates red blood cells. It appears to be a lectin with specificity for complex cell-surface carbohydrates. Fve adopts a tertiary structure consisting of an immunoglobulin-like β-sandwich, with seven strands arranged in two beta sheets, in a Greek-key topology. It forms a non-covalently linked homodimer containing no Cys, His or Met residues; dimerisation occurs by 3-D domain swapping of the N-terminal helices and is stabilised predominantly by hydrophobic interactions []. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA []. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. It lacks most of the active site residues of the SDR (short-chain dehydrogenases/reductases) family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG [].This domain can also be found in other atypical SDRs, such as HSCARG (an NADPH sensor) []and PCBER (phenylcoumaran benzylic ether reductase) []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
NosL is one of the accessory proteins of the nos (nitrous oxide reductase) gene cluster. NosL is a monomeric protein of 18,540 MW that specifically and stoichiometrically binds Cu(I). The copper ion in NosL is ligated by a Cys residue, and one Met and one His are thought to serve as the other ligands. It is possible that NosL is a copper chaperone involved in metallocentre assembly [].This entry also contains HTH-type transcriptional repressors, including YcnK. YcnK may act as a negative transcriptional regulator of YcnJ inthe presence of copper and may use copper as a corepressor. The gene, ycnK, is significantly induced under copper-limiting conditions []. |
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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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| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
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| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
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| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
913
 |
| Fragment?: |
false |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
304
 |
| Fragment?: |
false |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
695
 |
| Fragment?: |
false |
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| Publication |
| First Author: |
Paaventhan P |
| Year: |
2003 |
| Journal: |
J Mol Biol |
| Title: |
A 1.7A structure of Fve, a member of the new fungal immunomodulatory protein family. |
| Volume: |
332 |
| Issue: |
2 |
| Pages: |
461-70 |
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| Publication |
| First Author: |
Ko JL |
| Year: |
1995 |
| Journal: |
Eur J Biochem |
| Title: |
A new fungal immunomodulatory protein, FIP-fve isolated from the edible mushroom, Flammulina velutipes and its complete amino acid sequence. |
| Volume: |
228 |
| Issue: |
2 |
| Pages: |
244-9 |
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| Publication |
| First Author: |
Bourgis F |
| Year: |
1999 |
| Journal: |
Plant Cell |
| Title: |
S-methylmethionine plays a major role in phloem sulfur transport and is synthesized by a novel type of methyltransferase. |
| Volume: |
11 |
| Issue: |
8 |
| Pages: |
1485-98 |
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| Publication |
| First Author: |
James F |
| Year: |
1995 |
| Journal: |
J Biol Chem |
| Title: |
Purification and properties of S-adenosyl-L-methionine:L-methionine S-methyltransferase from Wollastonia biflora leaves. |
| Volume: |
270 |
| Issue: |
38 |
| Pages: |
22344-50 |
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| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents the methionine S-methyltransferase () family, which catalyse the S-methylmethionine (SMM) biosynthesis from adenosyl-L-homocysteine (AdoMet) and methionine []. All flowering plants produce S-methylmethionine (SMM) from Met and have a separate mechanism to convert SMM back to Met. The functions of SMM and the reasons for its interconversion with Met are unknown []. Methyltransferases (EC [intenz:2.1.1.-]) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule [, , ]. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM []. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids [, , ]. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [, , ]. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor. |
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| Publication |
| First Author: |
Tuteja N |
| Year: |
1988 |
| Journal: |
FEBS Lett |
| Title: |
Gamma-subunit of mouse retinal cyclic-GMP phosphodiesterase: cDNA and corresponding amino acid sequence. |
| Volume: |
232 |
| Issue: |
1 |
| Pages: |
182-6 |
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| Publication |
| First Author: |
Naylor SL |
| Year: |
1986 |
| Journal: |
Am J Hum Genet |
| Title: |
Linkage of cystic fibrosis locus and polymorphic DNA markers in 14 families. |
| Volume: |
39 |
| Issue: |
6 |
| Pages: |
707-12 |
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| Publication |
| First Author: |
Sweet A |
| Year: |
1992 |
| Journal: |
Biochem Med Metab Biol |
| Title: |
A potential animal model for studying CF heterozygote advantage: genetic variation in theophylline-inducible colonic chloride currents among inbred strains of mice. |
| Volume: |
47 |
| Issue: |
1 |
| Pages: |
97-102 |
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