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Search results 401 to 500 out of 683 for Ina

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Type Details Score
Publication
10694879 | -
First Author: Aravind L
Year: 2000
Journal: Trends Biochem Sci
Title: SAP - a putative DNA-binding motif involved in chromosomal organization.
Volume: 25
Issue: 3
Pages: 112-4
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Publication
10212141 | -
 
First Author: Weighardt F
Year: 1999
Journal: J Cell Sci
Title: A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock.
Volume: 112 ( Pt 10)
Pages: 1465-76
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Publication
9671816 | -
First Author: Nayler O
Year: 1998
Journal: Nucleic Acids Res
Title: SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elements.
Volume: 26
Issue: 15
Pages: 3542-9
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Publication
10671544 | -
First Author: Kipp M
Year: 2000
Journal: J Biol Chem
Title: Apoptotic cleavage of scaffold attachment factor A (SAF-A) by caspase-3 occurs at a noncanonical cleavage site.
Volume: 275
Issue: 7
Pages: 5031-6
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Publication
10805787 | -
First Author: Liao J
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Distinct roles of the NH2- and COOH-terminal domains of the protein inhibitor of activated signal transducer and activator of transcription (STAT) 1 (PIAS1) in cytokine-induced PIAS1-Stat1 interaction.
Volume: 97
Issue: 10
Pages: 5267-72
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Publication
9862413 | -
First Author: Amor Y
Year: 1998
Journal: FEBS Lett
Title: The involvement of poly(ADP-ribose) polymerase in the oxidative stress responses in plants.
Volume: 440
Issue: 1-2
Pages: 1-7
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Publication
2515150 | -
First Author: Rorman EG
Year: 1989
Journal: Genomics
Title: Molecular cloning of a human co-beta-glucosidase cDNA: evidence that four sphingolipid hydrolase activator proteins are encoded by single genes in humans and rats.
Volume: 5
Issue: 3
Pages: 486-92
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Publication
2019586 | -
First Author: Holtschmidt H
Year: 1991
Journal: J Biol Chem
Title: Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease.
Volume: 266
Issue: 12
Pages: 7556-60
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Protein
Q9DBM1
Organism: Mus musculus/domesticus
Length: 930  
Fragment?: false
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Protein
Q7TQC7
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Protein
Q3TFK5
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
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Protein
Q9CZX5
Organism: Mus musculus/domesticus
Length: 332  
Fragment?: false
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Protein
Q3UFS4
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: false
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Protein
Q8CEZ8
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: false
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Protein
A0A0A6YWB3
Organism: Mus musculus/domesticus
Length: 239  
Fragment?: true
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Protein
Q9CS24
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: true
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Protein
A0A0R4J215
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
D6RET6
Organism: Mus musculus/domesticus
Length: 883  
Fragment?: false
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Protein
Q3U3V2
Organism: Mus musculus/domesticus
Length: 885  
Fragment?: false
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Protein
E0CZ29
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: false
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Protein
F6X398
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: true
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Protein
A0A494B9S9
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: true
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Protein Domain
IPR036361 | SAP_dom_sf
Type: Homologous_superfamily
Description: The SAP motif is a 35-residue motif, which has been named after SAF-A/B,Acinus and PIAS, three proteins known to contain it. The SAP motif is found ina variety of nuclear proteins involved in transcription, DNA repair, RNAprocessing or apoptotic chromatin degradation. As the sap motif of SAF-A hasbeen shown to be essential for specific DNA binding activity, it has beenproposed that it could be a DNA-binding motif [].A multiple alignment of the SAP motif reveals a bipartite distribution ofstrongly conserved hydrophobic, polar and bulky amino acids separated by aregion that contains a glycine. Secondary structure predictions suggest thatthe SAP motif could form two alpha helices separated by a turn [].Some proteins known to contain a SAP motif are listed below:Vertebrate scaffold attachment factors A and B (SAF-A/B). These twoproteins are heterogeneous nuclear ribonucleoproteins (hnRNPs) that bind toAT-rich chromosomal region. It has been proposed that they couple RNAmetabolism to nuclear organisation [, ]. The SAF-A protein is cleaved bycaspase-3 during apoptosis [].Mammalian Acinus, a protein which induces apoptotic chromatin condensationafter cleavage by caspase-3 []. Acinus also contains a RNA-recognitionmotif.Eukaryotic proteins of the PIAS (protein inhibitor of activated STAT)family. These proteins interact with phosphorylated STAT dimers and inhibitSTAT mediated gene activation. Deletion of the first 50 amino acid residuescontaining the SAP domain allows the interaction of PIAS1 with STAT1monomer [].Plant poly(ADP-ribose) polymerase (PARP). PARP is a nuclear protein thatcatalyzes the poly(ADP-ribosyl)ation of proteins. It is involved inresponses to mild and severe oxidative stresses, by mediating DNA repairand programmed cell death processes, respectively []. PARP is tightlybound to chromatin or nuclear matrix.Arabidopsis thaliana Arp, an apurinic endonuclease-redox protein.Yeast THO1 protein. It could be involved in the regulation oftranscriptional elongation by RNA polymerase II [].Animal Ku70. Together with Ku86, it forms a DNA ends binding complex thatis involved in repairing DNA double-strand breaks.Yeast RAD18, a protein involved in DNA repair.Neurospora crassa UVS-2, the homologue of RAD18.
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Protein Domain
IPR000467 | G_patch_dom
Type: Domain
Description: The G-patch domain is an approximately 48 amino acid domain, which is found ina single copy in several RNA-associated proteins and in type D retroviralpolyproteins. It is widespread among eukaryotes but is absent in archaea andbacteria. The G-patch domain has been called after its most notable feature,the presence of six highly conserved glycine residues. The position followingthe first conserved glycine is occupied almost invariably by an aromaticresidue, and several other positions are occupied predominantly by eitherhydrophobic or small residues. Several groups of G-patch containing proteinsare conserved in animals, plants and fungi. In some of these proteins the G-patch is the only recognisable domain but in most of them it is combined withother domains, which include well-defined RNA-binding domains, such as theRRM, dsRBD, SURP and R3H. It has been suggested that the G-patch domain has a specific function in RNA processing and, in particular, that it might be a previously undetected RNA-binding domain mediating a distinct type of RNA-protein interaction.Secondary structure prediction indicates that the G-patch domain probablycontains two α-helices, with four out of the six glycines located withinan intervening loop.Proteins known to contain a G-patch domain include:Eukaryotic 45kDa splicing factor (SPF-45).Mammmalian SON protein, a DNA-binding protein.Human LUCA15, a multidomain RNA-binding protein that is the product of a gene deleted in certain lung tumors.Human DAN26/EPROT, a multidomain protein, which, in addition to the G-patch domain, contains an RNA polymerase II C-terminal repeat-binding domain seen in many proteins of the polyA-addition machinery.Arabidopsis thaliana DRT111, a protein which has been shown to partially restore recombination proficiency and DNA-damage resistance to E. coli mutants.Type D retroviral polyprotein, where the G-patch domain is found directly downstream of the protease domain.
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Protein Domain
IPR003034 | SAP_dom
Type: Domain
Description: The SAP motif is a 35-residue motif, which has been named after SAF-A/B,Acinus and PIAS, three proteins known to contain it. The SAP motif is found ina variety of nuclear proteins involved in transcription, DNA repair, RNAprocessing or apoptotic chromatin degradation. As the sap motif of SAF-A hasbeen shown to be essential for specific DNA binding activity, it has beenproposed that it could be a DNA-binding motif [].A multiple alignment of the SAP motif reveals a bipartite distribution ofstrongly conserved hydrophobic, polar and bulky amino acids separated by aregion that contains a glycine. Secondary structure predictions suggest thatthe SAP motif could form two alpha helices separated by a turn [].Some proteins known to contain a SAP motif are listed below:Vertebrate scaffold attachment factors A and B (SAF-A/B). These twoproteins are heterogeneous nuclear ribonucleoproteins (hnRNPs) that bind toAT-rich chromosomal region. It has been proposed that they couple RNAmetabolism to nuclear organisation [, ]. The SAF-A protein is cleaved bycaspase-3 during apoptosis [].Mammalian Acinus, a protein which induces apoptotic chromatin condensationafter cleavage by caspase-3 []. Acinus also contains a RNA-recognitionmotif.Eukaryotic proteins of the PIAS (protein inhibitor of activated STAT)family. These proteins interact with phosphorylated STAT dimers and inhibitSTAT mediated gene activation. Deletion of the first 50 amino acid residuescontaining the SAP domain allows the interaction of PIAS1 with STAT1monomer [].Plant poly(ADP-ribose) polymerase (PARP). PARP is a nuclear protein thatcatalyzes the poly(ADP-ribosyl)ation of proteins. It is involved inresponses to mild and severe oxidative stresses, by mediating DNA repairand programmed cell death processes, respectively []. PARP is tightlybound to chromatin or nuclear matrix.Arabidopsis thaliana Arp, an apurinic endonuclease-redox protein.Yeast THO1 protein. It could be involved in the regulation oftranscriptional elongation by RNA polymerase II [].Animal Ku70. Together with Ku86, it forms a DNA ends binding complex thatis involved in repairing DNA double-strand breaks.Yeast RAD18, a protein involved in DNA repair.Neurospora crassa UVS-2, the homologue of RAD18.
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Protein
Q3UD82
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: false
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Protein
Q7TMM8
Organism: Mus musculus/domesticus
Length: 322  
Fragment?: false
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Protein
Q8BIY1
Organism: Mus musculus/domesticus
Length: 525  
Fragment?: false
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Protein
Q6P6P7
Organism: Mus musculus/domesticus
Length: 630  
Fragment?: false
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Publication
1709048 | J:22451
First Author: Brown J
Year: 1991
Journal: Int Immunol
Title: The gene encoding the stem cell antigen, CD34, is conserved in mouse and expressed in haemopoietic progenitor cell lines, brain, and embryonic fibroblasts.
Volume: 3
Issue: 2
Pages: 175-84
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Protein
Q8CH02
Organism: Mus musculus/domesticus
Length: 643  
Fragment?: false
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Protein
Q8CH09
Organism: Mus musculus/domesticus
Length: 1067  
Fragment?: false
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Protein
Q8BML7
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: true
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Protein
Q8K0V6
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Protein
Q0P4Z5
Organism: Mus musculus/domesticus
Length: 335  
Fragment?: false
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Protein
G5E856
Organism: Mus musculus/domesticus
Length: 630  
Fragment?: false
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Protein
Q91YU2
Organism: Mus musculus/domesticus
Length: 426  
Fragment?: true
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Protein
Q3UBH2
Organism: Mus musculus/domesticus
Length: 878  
Fragment?: false
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Protein
A0A0R4J0T1
Organism: Mus musculus/domesticus
Length: 610  
Fragment?: false
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Protein
A0A1L1SV38
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
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Protein
Q3UAI4
Organism: Mus musculus/domesticus
Length: 878  
Fragment?: false
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Protein
H9KV02
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
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Protein
Q78IW3
Organism: Mus musculus/domesticus
Length: 335  
Fragment?: false
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Protein
A0A5H1ZRM9
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
A0A1L1SQ23
Organism: Mus musculus/domesticus
Length: 498  
Fragment?: false
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Protein
F8WIK2
Organism: Mus musculus/domesticus
Length: 891  
Fragment?: false
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Protein
Q3TE26
Organism: Mus musculus/domesticus
Length: 303  
Fragment?: true
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Protein
Q99LW1
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
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Protein
A0A3Q4EH87
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: true
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Protein
Q80W39
Organism: Mus musculus/domesticus
Length: 878  
Fragment?: false
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Protein
Q3UQU5
Organism: Mus musculus/domesticus
Length: 681  
Fragment?: true
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Protein
Q9D505
Organism: Mus musculus/domesticus
Length: 106  
Fragment?: false
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Protein
B2X2E0
Organism: Mus musculus/domesticus
Length: 524  
Fragment?: false
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Protein
A0A0A6YVX0
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: true
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Protein
Q8BM30
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
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Protein
Q05BZ2
Organism: Mus musculus/domesticus
Length: 485  
Fragment?: false
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Protein
Q4VAB0
Organism: Mus musculus/domesticus
Length: 524  
Fragment?: false
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Protein
Q3UJB0
Organism: Mus musculus/domesticus
Length: 878  
Fragment?: false
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Publication
8755499 | -
First Author: Ruf A
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.
Volume: 93
Issue: 15
Pages: 7481-5
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Publication
15273990 | -
First Author: Amé JC
Year: 2004
Journal: Bioessays
Title: The PARP superfamily.
Volume: 26
Issue: 8
Pages: 882-93
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Publication
15561303 | -
First Author: Nguewa PA
Year: 2005
Journal: Prog Biophys Mol Biol
Title: Poly(ADP-ribose) polymerases: homology, structural domains and functions. Novel therapeutical applications.
Volume: 88
Issue: 1
Pages: 143-72
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Publication
14739238 | -
First Author: Oliver AW
Year: 2004
Journal: Nucleic Acids Res
Title: Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2.
Volume: 32
Issue: 2
Pages: 456-64
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Protein Domain
IPR012317 | Poly(ADP-ribose)pol_cat_dom
Type: Domain
Description: Poly(ADP-ribose) polymerases (PARP) are a family of enzymespresent in eukaryotes, which catalyze the poly(ADP-ribosyl)ation of a limitednumber of proteins involved in chromatin architecture, DNA repair, or in DNAmetabolism, including PARP itself. PARP, also known as poly(ADP-ribose)synthetase and poly(ADP-ribose) transferase, transfers the ADP-ribose moietyfrom its substrate, nicotinamide adenine dinucleotide (NAD), to carboxylategroups of aspartic and glutamic residues. Whereas some PARPs might function ingenome protection, others appear to play different roles in the cell,including telomere replication and cellular transport. PARP-1 is amultifunctional enzyme. The polypeptide has a highly conserved modularorganisation consisting of an N-terminal DNA-binding domain, a centralregulating segment, and a C-terminal or F region accommodating the catalyticcentre. The F region is composed of two parts: a purely α-helical N-terminal domain (alpha-hd), and the mixed alpha/beta C-terminal catalyticdomain bearing the putative NAD binding site. Although proteins of the PARPfamily are related through their PARP catalytic domain, they do not resembleeach other outside of that region, but rather, they contain unique domainsthat distinguish them from each other and hint at their discrete functions.Domains with which the PARP catalytic domain is found associated includezinc fingers, SAP, ankyrin, BRCT, Macro, SAM, WWE and UIM domains [, , ].The alpha-hd domain is about 130 amino acids in length and consists of an up-up-down-up-down-down motif of helices. It isthought to relay the activation signal issued on binding to damaged DNA [, ].The PARP catalytic domain is about 230 residues in length. Its core consists of a five-stranded antiparallel β-sheet andfour-stranded mixed β-sheet. The two sheets are consecutive and areconnected via a single pair of hydrogen bonds between two strands that run atan angle of 90 degrees. These central β-sheets are surrounded by five α-helices, three 3(10)-helices, and by a three- and a two-stranded β-sheet ina 37-residue excursion between two central β-strands [, ]. The activesite, known as the 'PARP signature' is formed by a block of 50 amino acids that is strictly conserved among the vertebrates andhighly conserved among all species. The 'PARP signature' is characteristic ofall PARP protein family members. It is formed by a segment of conserved aminoacid residues formed by a β-sheet, an α-helix, a 3(10)-helix, a β-sheet, and an α-helix [].
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Protein Domain
IPR008083 | CD34
Type: Family
Description: The CD34 group of monoclonal antibodies recognises CD34 (also termed CD34antigen), a 105-120kDa cell surface glycoprotein, which is selectively expressed by human myeloid and lymphoid progenitor cells, including the haemopoietic stem cell. The protein is also expressed on vascularendothelial cells. Here, it is concentrated on the surface of the inter-digitating processes, suggesting a possible involvement in cell interactionsor adhesion, by mediating the attachment of stem cells to the bone marrow extracellular matrix, or directly to stromal cells. The restricted patternof expression of CD34 in haemopoiesis suggests that it may have a significant function in the earliest stages of blood cell differentiation in the bone marrow [, ].CD34 is a phosphoprotein shown to be activated by protein kinase C (PKC) ina developmental stage-specific manner. Analysis of the human CD34 sequencereveals that the protein appears to be a type I transmembrane (TM) molecule.The predicted internal portion of the protein appears to retain basic amino acid residues adjacent to Ser residues, presenting at least two potentialtarget sites for PKC phosphorylation. In addition, there are two other consensus motifs that correspond to potential target sites for Ca+/calmodulin-dependent kinase and/or protease activated kinase I [].The protein is not strongly similar to other known proteins, but some weaksimilarities do exist: e.g., to the S+T region (a region rich in potentialO-linked carbohydrate attachment sites), the TM domain and cytoplasmic domain of cell surface proteins such as leukosialin, a major sialoglyco-protein of rat and human leukocytes; to the N-terminal glycosylated regionof CD45 (the leukocyte common antigen); and to groups of interrelatedproteins involved in cell adhesion or the regulation of complement.A homologue of human CD34 is expressed in mouse. The amino acid sequencesonly diverge significantly at their N-termini, which are predicted to be highly glycosylated and whose functions are probably modulated by carbohydrate. The observed pattern of expression of the murine CD34 geneis consistent with that of the human antigen. That CD34 is also highlyexpressed outside haematopoiesis, by vascular endothelial cells and by fibroblasts in differentiated tissue, suggests a role common to a varietyof cell types. Concentration of CD34 on the interdigitating membraneprojections of adjacent capillary endothelial cells has strengthened theidea that it functions in the control of events leading to cell-cell orcell-matrix adhesion, which role could be modulated by variation in itslevels of glycosylation. The conservation between the human and mousecysteine-rich domain in the extracellular part of the protein, and theexceptionally high conservation of the cytoplasmic domain, imply that theprotein is more than a carrier for either carbohydrate or negatively chargedterminal sialic acid residues (a role postulated for leukosialin/sialophorin).The highly conserved domain may serve to provide an internal signal of external contact with a ligand.
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Protein
Q7TMF2
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
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Publication
10490026 | J:64695
First Author: Sahara S
Year: 1999
Journal: Nature
Title: Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation.
Volume: 401
Issue: 6749
Pages: 168-73
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Protein
Q8VIM5
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: false
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Protein
Q8K4J6
Organism: Mus musculus/domesticus
Length: 964  
Fragment?: false
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Protein
P59759
Organism: Mus musculus/domesticus
Length: 1080  
Fragment?: false
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Protein
A0A5F8MQ33
Organism: Mus musculus/domesticus
Length: 1029  
Fragment?: false
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Protein
Q5DTZ3
Organism: Mus musculus/domesticus
Length: 1080  
Fragment?: true
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Protein
G3X8R8
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
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Protein
E9Q8Y1
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: true
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Protein
H3BJ41
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: false
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Protein
E0CZH5
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: true
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Protein
D6RHP9
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: false
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Protein
B9EJ16
Organism: Mus musculus/domesticus
Length: 948  
Fragment?: false
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Protein
A0A0R4J0C8
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
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Protein
A0A494B929
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: false
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Protein
A0A1L1SRL0
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: false
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Protein
Q3U1I6
Organism: Mus musculus/domesticus
Length: 964  
Fragment?: false
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Protein
A0A1B0GRC5
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: true
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Protein
Q3U4W4
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: true
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Protein
A0A1L1SRS2
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: true
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Protein
Q9CVL7
Organism: Mus musculus/domesticus
Length: 282  
Fragment?: true
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Protein
A0A8D4USI8
Organism: Mus musculus/domesticus
Length: 1112  
Fragment?: false
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Protein
D3YVJ6
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: true
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Protein
D3YUI2
Organism: Mus musculus/domesticus
Length: 979  
Fragment?: false
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Protein
D3YUG5
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: true
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Protein
Q3U3V7
Organism: Mus musculus/domesticus
Length: 574  
Fragment?: true
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Protein
A3KMF2
Organism: Mus musculus/domesticus
Length: 1079  
Fragment?: true
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Protein
D6RJ78
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Publication
9707445 | -
First Author: Piruat JI
Year: 1998
Journal: EMBO J
Title: A novel yeast gene, THO2, is involved in RNA pol II transcription and provides new evidence for transcriptional elongation-associated recombination.
Volume: 17
Issue: 16
Pages: 4859-72
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Protein
Q8CFF0
Organism: Mus musculus/domesticus
Length: 331  
Fragment?: false
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Protein
Q61858
Organism: Mus musculus/domesticus
Length: 372  
Fragment?: false
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Protein
Q8CIE4
Organism: Mus musculus/domesticus
Length: 960  
Fragment?: false
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Protein
Q64314
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
•
•
•
•
•
Protein
Q7TNV0
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
•
•
•
•
•
Protein
O88554
Organism: Mus musculus/domesticus
Length: 559  
Fragment?: false
•
•
•
•
•
Protein
Q9QX47
Organism: Mus musculus/domesticus
Length: 2444  
Fragment?: false
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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