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Search results 201 to 297 out of 297 for Sis

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Type Details Score
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1752522
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1821522
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:3557722
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1702122
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1756322
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1668822
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1757722
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1757522
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1738322
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression      
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1802422
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression    
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1768022
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Note: Expression was not detected in the skull (base and vault).
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
GXD Expression    
Probe: MGI:4426781
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:2672022
Stage: TS22
Assay Id: MGI:5422357
Age: embryonic day 14.5
Note: Expression was not detected in whisker follicle.
Specimen Label: ES2615; Specimen S1018
Detected: false
Specimen Num: 1
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: Data Curation Using Mouse Genome Assembly
Protein Domain
Type: Domain
Description: The sugar isomerase (SIS) domain is a phosphosugar-binding module that is found in a variety of eubacterial, archaebacterial and eukaryotic proteinsthat have a role in phosphosugar isomerization or regulation []. In enzymes, the SIS domain can have a catalytic function as an isomerase and bind to phosphorylated sugars. In bacterial transcriptional regulators of the rpiR family, the domain seems to bind substrates implicated in the genes for sugar metabolism that are controlled by the regulator. The SIS domain is found in one or two copies and can be linked to additional domains, such as helix-turn-helix (HTH), CBS, glutamine amidotransferases type 2, or phosphopantetheine-attachment [, ].The SIS domain has an α-β structure and is dominated by a five-stranded parallel β-sheet flanked on either side by α-helices forming a three-layer α-β-α sandwich []. The fold shows similarities to that of glucose-6-phosphate isomerase.
Protein Domain
Type: Domain
Description: AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli [].
Publication
First Author: Tzeng YL
Year: 2002
Journal: J Biol Chem
Title: KpsF is the arabinose-5-phosphate isomerase required for 3-deoxy-D-manno-octulosonic acid biosynthesis and for both lipooligosaccharide assembly and capsular polysaccharide expression in Neisseria meningitidis.
Volume: 277
Issue: 27
Pages: 24103-13
Protein Domain
Type: Domain
Description: AgaS is a putative isomerase in Escherichia coli []. It is similar to glucosamine-6-phosphate synthases (GlmS), which catalyzes the first step in hexosamine metabolism. GlmS converts fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source [].GlmS contains a N-terminal glutaminase domain and two C-terminal SIS (Sugar ISomerase) domains. This domain is the first SIS domain found in GlmS and AgaS.
Protein Domain
Type: Domain
Description: KpsF is an arabinose-5-phosphate isomerase which contains a SIS (Sugar ISomerase) domain. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway [, ].
Protein Domain
Type: Homologous_superfamily
Description: The sugar isomerase (SIS) domain is a phosphosugar-binding module that is found in a variety of eubacterial, archaebacterial and eukaryotic proteinsthat have a role in phosphosugar isomerization or regulation []. In enzymes, the SIS domain can have a catalytic function as an isomerase and bind to phosphorylated sugars. In bacterial transcriptional regulators of the rpiR family, the domain seems to bind substrates implicated in the genes for sugar metabolism that are controlled by the regulator. The SIS domain is found in one or two copies and can be linked to additional domains, such as helix-turn-helix (HTH), CBS, glutamine amidotransferases type 2, or phosphopantetheine-attachment [, ].The SIS domain has an α-β structure and is dominated by a five-stranded parallel β-sheet flanked on either side by α-helices forming a three-layer α-β-α sandwich []. The fold shows similarities to that of glucose-6-phosphate isomerase.
Publication
First Author: Teplyakov A
Year: 2001
Journal: J Mol Biol
Title: Channeling of ammonia in glucosamine-6-phosphate synthase.
Volume: 313
Issue: 5
Pages: 1093-102
Publication
First Author: Teplyakov A
Year: 1999
Journal: Protein Sci
Title: The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase.
Volume: 8
Issue: 3
Pages: 596-602
Publication
First Author: Milewski S
Year: 2002
Journal: Biochim Biophys Acta
Title: Glucosamine-6-phosphate synthase--the multi-facets enzyme.
Volume: 1597
Issue: 2
Pages: 173-92
Protein Domain
Type: Domain
Description: This entry represents the SIS (Sugar ISomerase) domain 2 found in glucosamine 6-phosphate synthase (GlmS) and fructosamine deglycase FrlB.GlmS contains a N-terminal glutaminase domain and C-terminal isomerase domain (consisting of two SIS domains) []and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source []. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate [, , ].FrlB catalyses the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid [].
Protein Domain
Type: Domain
Description: RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, RpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate [].This domain is also found in other members of the RpiR family of transcriptional regulators, such as MurR []and in uncharacterised proteins of the UPF0309 family.
Protein Domain
Type: Domain
Description: FrlB catalyses the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid [].This entry represents the first SIS domain of FrlB. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars [].
Publication
First Author: Kogerman P
Year: 1996
Journal: J Cell Physiol
Title: CD44 protein levels and its biological activity are regulated in Balb/c 3T3 fibroblasts by serum factors and by transformation with the ras but not with the sis oncogene.
Volume: 169
Issue: 2
Pages: 341-9
Publication
First Author: Hansen T
Year: 2004
Journal: J Biol Chem
Title: Bifunctional phosphoglucose/phosphomannose isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily.
Volume: 279
Issue: 3
Pages: 2262-72
Publication
First Author: Hansen T
Year: 2004
Journal: Extremophiles
Title: Bifunctional phosphoglucose/phosphomannose isomerase from the hyperthermophilic archaeon Pyrobaculum aerophilum.
Volume: 8
Issue: 6
Pages: 507-12
Protein Domain
Type: Domain
Description: Bifunctional phosphoglucose/phosphomannose isomerase has both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively, at an equal rate [, ].This protein contains two SIS (Sugar ISomerase) domains. This entry represents the first SIS domain.
Publication
First Author: Meredith TC
Year: 2006
Journal: Biochem J
Title: Characterization of Escherichia coli D-arabinose 5-phosphate isomerase encoded by kpsF: implications for group 2 capsule biosynthesis.
Volume: 395
Issue: 2
Pages: 427-32
Protein Domain
Type: Domain
Description: Phosphoglucose isomerase (PGI) is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate []. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF) [, ]. Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells.PGI is comprised of two domains; each domain is an α-β-alpha sandwich [], which correspond to a SIS (Sugar ISomerase) domain fold.
Protein Domain
Type: Domain
Description: Phosphoglucose isomerase (PGI) is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate []. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF) [, ]. Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells.PGI is comprised of two domains; each domain is an α-β-alpha sandwich [], which correspond to a SIS (Sugar ISomerase) domain fold.
Regulatory Region
Type: CTCF_binding_site
Organism: Mus musculus
Publication
First Author: Sørensen KI
Year: 1996
Journal: J Bacteriol
Title: Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression.
Volume: 178
Issue: 4
Pages: 1003-11
Publication
First Author: Jaeger T
Year: 2008
Journal: J Bacteriol
Title: The transcriptional factors MurR and catabolite activator protein regulate N-acetylmuramic acid catabolism in Escherichia coli.
Volume: 190
Issue: 20
Pages: 6598-608
Protein
Organism: Mus musculus
Length: 83  
Fragment?: true
Protein
Organism: Mus musculus
Length: 152  
Fragment?: true
Protein
Organism: Mus musculus
Length: 130  
Fragment?: false
Publication
First Author: Teplyakov A
Year: 1998
Journal: Structure
Title: Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain.
Volume: 6
Issue: 8
Pages: 1047-55
Publication
First Author: Mouilleron S
Year: 2011
Journal: Arch Biochem Biophys
Title: Dynamics of glucosamine-6-phosphate synthase catalysis.
Volume: 505
Issue: 1
Pages: 1-12
Publication
First Author: Jaeger T
Year: 2008
Journal: Cell Mol Life Sci
Title: N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism.
Volume: 65
Issue: 6
Pages: 928-39
Publication
First Author: Read J
Year: 2001
Journal: J Mol Biol
Title: The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia.
Volume: 309
Issue: 2
Pages: 447-63
Publication
First Author: Wiame E
Year: 2004
Journal: FEBS Lett
Title: Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis.
Volume: 577
Issue: 3
Pages: 469-72
Protein
Organism: Mus musculus
Length: 587  
Fragment?: false
Protein
Organism: Mus musculus
Length: 623  
Fragment?: false
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Publication
First Author: Sugiyama T
Year: 2016
Journal: Mol Cell
Title: Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly.
Volume: 61
Issue: 5
Pages: 747-759
Protein
Organism: Mus musculus
Length: 344  
Fragment?: false
Protein
Organism: Mus musculus
Length: 344  
Fragment?: false
Protein
Organism: Mus musculus
Length: 241  
Fragment?: false
Publication
First Author: Einecke G
Year: 2006
Journal: Am J Transplant
Title: Tubulitis and epithelial cell alterations in mouse kidney transplant rejection are independent of CD103, perforin or granzymes A/B.
Volume: 6
Issue: 9
Pages: 2109-20
Protein
Organism: Mus musculus
Length: 191  
Fragment?: true
Protein
Organism: Mus musculus
Length: 682  
Fragment?: false
Protein
Organism: Mus musculus
Length: 697  
Fragment?: false
Protein
Organism: Mus musculus
Length: 607  
Fragment?: false
Publication
First Author: Achari A
Year: 1981
Journal: Philos Trans R Soc Lond B Biol Sci
Title: Glucose-6-phosphate isomerase.
Volume: 293
Issue: 1063
Pages: 145-57
Publication
First Author: Sun YJ
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.
Volume: 96
Issue: 10
Pages: 5412-7
Publication
First Author: Chou CC
Year: 2000
Journal: J Biol Chem
Title: The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition.
Volume: 275
Issue: 30
Pages: 23154-60
Publication
First Author: Brinkkötter A
Year: 2000
Journal: Mol Microbiol
Title: Pathways for the utilization of N-acetyl-galactosamine and galactosamine in Escherichia coli.
Volume: 37
Issue: 1
Pages: 125-35
Protein
Organism: Mus musculus
Length: 558  
Fragment?: false
Protein Domain
Type: Domain
Description: This domain is found in the N-terminal region of glucose-6-phosphate isomerase-like protein, just before the phospho-glucose isomerase C-terminal SIS domain.
Protein Domain
Type: Domain
Description: This domain contains a helix-turn-helix motif [].Every member of this family is N-terminal to a SIS domain . Members of this family are probably regulators of genesinvolved in phosphosugar metobolism.
Publication
First Author: Adolph S
Year: 1987
Journal: Cytogenet Cell Genet
Title: Mapping of the oncogenes Myc, Sis, and int-1 to the distal part of mouse chromosome 15.
Volume: 44
Issue: 2-3
Pages: 65-8
Publication
First Author: Baldini A
Year: 1993
Journal: Genomics
Title: Mapping on human and mouse chromosomes of the gene for the beta-galactoside-binding protein, an autocrine-negative growth factor.
Volume: 15
Issue: 1
Pages: 216-8
Publication
First Author: Meredith TC
Year: 2005
Journal: J Bacteriol
Title: Identification of GutQ from Escherichia coli as a D-arabinose 5-phosphate isomerase.
Volume: 187
Issue: 20
Pages: 6936-42
Publication
First Author: Yamada M
Year: 1990
Journal: DNA Seq
Title: Nucleotide sequence and expression of the gutQ gene within the glucitol operon of Escherichia coli.
Volume: 1
Issue: 2
Pages: 141-5
Protein Domain
Type: Family
Description: This is a family of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. The group includes GutQ, a protein of the glucitol operon [, ]and KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of Escherichia coli [].
Protein Domain
Type: Domain
Description: This domain is conserved in the Bacillales. The function is not known, but given this domains relationship to the SIS domain it may carry out a sugar isomerase reaction. Several members are annotated as being YWJG, a protein expressed downstream of pyrG, a gene encoding for cytidine triphosphate synthetase.
Publication
First Author: McAllister KA
Year: 1997
Journal: Cancer Res
Title: Characterization of the rat and mouse homologues of the BRCA2 breast cancer susceptibility gene.
Volume: 57
Issue: 15
Pages: 3121-5
Publication
First Author: Swan MK
Year: 2004
Journal: J Biol Chem
Title: A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolution.
Volume: 279
Issue: 38
Pages: 39838-45
Protein Domain
Type: Domain
Description: Phosphoglucose isomerase (PGI) catalyses the interconversion of phosphoglucose and phosphofructose, and is a component of many sugar metabolic pathways. In some archaea and bacteria PGI activity occurs via a bifunctional enzyme that also exhibits phosphomannose isomerase (PMI) activity. Though not closely related to eukaryotic PGIs, the bifunctional enzyme is similar enough that the sequence includes the cluster of threonines and serines that forms the sugar phosphate-binding site in conventional PGI.The bifunctional PGI/PMI enzyme contains two SIS (Sugar ISomerase) domains. This entry represents the C-terminal SIS domain, which contains many of the active catalytic site residues. The enzyme is thought to use the same catalytic mechanisms for both glucose ring-opening and isomerisation for the interconversion of glucose 6-phosphate to fructose 6-phosphate [].
Protein Domain
Type: Family
Description: This entry contains MurR, which represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid (MurNAc). It binds to two adjacent inverted repeats within the operator region. MurNAc 6-phosphate, the substrate of MurQ, and is the specific inducer that weakens binding of MurR to the operator.MurR is paralogous to RpiR and has both HTH and SIS phosphosugar binding domains. The divergent murR and murQP transcripts have complementary 5' ends []. It is required for swarming phenotype.
Publication
First Author: Zelikowsky M
Year: 2018
Journal: Cell
Title: The Neuropeptide Tac2 Controls a Distributed Brain State Induced by Chronic Social Isolation Stress.
Volume: 173
Issue: 5
Pages: 1265-1279.e19
Publication
First Author: Liu Z
Year: 2006
Journal: Immunity
Title: A recombination silencer that specifies heterochromatin positioning and ikaros association in the immunoglobulin kappa locus.
Volume: 24
Issue: 4
Pages: 405-15
Publication
First Author: Chiu IM
Year: 1984
Journal: Cell
Title: Nucleotide sequence analysis identifies the human c-sis proto-oncogene as a structural gene for platelet-derived growth factor.
Volume: 37
Issue: 1
Pages: 123-9
Publication
First Author: Mielnicki LM
Year: 1993
Journal: Genomics
Title: Localization of the murine activating transcription factor 4 gene to mouse chromosome 15.
Volume: 15
Issue: 1
Pages: 197-9
Publication
First Author: Crespo P
Year: 1995
Journal: Biochem Biophys Res Commun
Title: Overexpression of mammalian protein kinase C-zeta does not affect the growth characteristics of NIH 3T3 cells.
Volume: 213
Issue: 1
Pages: 266-72
Publication
First Author: Veiga-Da-Cunha M
Year: 1994
Journal: Eur J Biochem
Title: Cloning and expression of a Xenopus liver cDNA encoding a fructose-phosphate-insensitive regulatory protein of glucokinase.
Volume: 225
Issue: 1
Pages: 43-51
Protein Domain
Type: Conserved_site
Description: The glucokinase regulatory protein (GCKR) []is a vertebrate protein thatinhibits glucokinase by forming a complex with the enzyme, which plays a rolein the control of blood glucose homeostasis. GCKR is a protein of about 70 Kdwhich is evolutionary related to bacterial N-acetylmuramic acid 6-phosphateetherases (MurNAc-6-P etherase, murQ), which are about half the size of GCKRand form active homodimers. MurNAc-6-P etherases catalyse the cleavage of theD-lactyl ether substituent of the bacterial cell wall sugar MurNAc and play arole in recycling of the cell wall []. The 3D structure of the Haemophilusinfluenzae HI0754/murQ protein shows structural relationshipswith other sugar isomerase (SIS) domain proteins. Incontrast to mono-SIS bacterial MurNAc-6-P etherase, mammalian GCKR is composedof two SIS domains.
Publication
First Author: Xiang Y
Year: 2011
Journal: J Immunol
Title: A multifunctional element in the mouse Igκ locus that specifies repertoire and Ig loci subnuclear location.
Volume: 186
Issue: 9
Pages: 5356-66
Publication
First Author: Pewe L
Year: 1997
Journal: J Virol
Title: Cytotoxic T-cell-resistant variants arise at early times after infection in C57BL/6 but not in SCID mice infected with a neurotropic coronavirus.
Volume: 71
Issue: 10
Pages: 7640-7
Publication
First Author: Meruelo D
Year: 1987
Journal: Immunogenetics
Title: Assignment of the Ly-6--Ril-1--Sis--H-30--Pol-5/Xmmv-72--Ins-3--Krt-1--Int-1 --Gdc-1 region to mouse chromosome 15.
Volume: 25
Issue: 6
Pages: 361-72
Publication
First Author: Lavrovsky Y
Year: 1994
Journal: Gene
Title: Characterization of a 142-bp fragment of the murine c-fos oncogene promoter upstream of the SIF-binding element.
Volume: 142
Issue: 2
Pages: 285-90
Publication  
First Author: Adolph S
Year: 1987
Journal: Mouse News Lett
Title: Physical gene map of murine chromosome 15
Volume: 79
Pages: 56
Publication
First Author: Natrajan G
Year: 2007
Journal: Mol Microbiol
Title: Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli.
Volume: 65
Issue: 4
Pages: 995-1005
Publication
First Author: Zawilak-Pawlik A
Year: 2007
Journal: Mol Microbiol
Title: HobA--a novel protein involved in initiation of chromosomal replication in Helicobacter pylori.
Volume: 65
Issue: 4
Pages: 979-94
Protein Domain
Type: Homologous_superfamily
Description: Proteins in this superfamily are approximately 180 amino acids in length found exclusively in epsilon-proteobacteria. The crystal structure of HobA from Helicobacter pylori has been reported at 1.7A resolution; HobA represents a modified Rossmann fold consisting of a five-stranded parallel β-sheet (beta1-5) flanked on one side by alpha-2, alpha-3 and alpha-6 helices and alpha-4 and alpha-5 on the other. The alpha-1 helix is extended away from and has minimal interaction with the globular part of the protein. Four monomers interact to form a tetrameric molecule. Four calcium atoms bind to the tetramer and these binding sites may have functional relevance. The closest structural homologue of HobA is a sugar isomerase (SIS) domain containing protein, the phosphoheptose isomerase from Pseudomonas aeruginosa. The SIS proteins share strong sequence homology with DiaA from Escherichia coli; yet, HobA and DiaA share no sequence homology []. HobA is a novel protein essential for initiation of H. pylori chromosome replication. It interacts specifically via DnaA with the oriC-DnaA complex. It is possible that HobA is essential for the correct formation and stabilisation of the orisome by facilitating the spatial positioning of DnaA at oriC [].
Protein Domain
Type: Family
Description: This family of proteins is found exclusively in epsilon-proteobacteria. Proteins in this family are approximately 180 amino acids in length. The crystal structure of HobA from Helicobacter pylori has been reported at 1.7A resolution; HobA represents a modified Rossmann fold consisting of a five-stranded parallel β-sheet (beta1-5) flanked on one side by alpha-2, alpha-3 and alpha-6 helices and alpha-4 and alpha-5 on the other. The alpha-1 helix is extended away from and has minimal interaction with the globular part of the protein. Four monomers interact to form a tetrameric molecule. Four calcium atoms bind to the tetramer and these binding sites may have functional relevance. The closest structural homologue of HobA is a sugar isomerase (SIS) domain containing protein, the phosphoheptose isomerase from Pseudomonas aeruginosa. The SIS proteins share strong sequence homology with DiaA from Escherichia coli; yet, HobA and DiaA share no sequence homology []. HobA is a novel protein essential for initiation of H. pylori chromosome replication. It interacts specifically via DnaA with the oriC-DnaA complex. It is possible that HobA is essential for the correct formation and stabilisation of the orisome by facilitating the spatial positioning of DnaA at oriC [].