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Search results 501 to 600 out of 1525 for Il1a

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Type Details Score
Publication
27318131 | J:239041
 
First Author: Norden DM
Year: 2016
Journal: Neurobiol Aging
Title: Insensitivity of astrocytes to interleukin 10 signaling following peripheral immune challenge results in prolonged microglial activation in the aged brain.
Volume: 44
Pages: 22-41
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Publication
1970330 | J:10440
First Author: Dickinson ME
Year: 1990
Journal: Genomics
Title: Chromosomal localization of seven members of the murine TGF-beta superfamily suggests close linkage to several morphogenetic mutant loci.
Volume: 6
Issue: 3
Pages: 505-20
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Publication
30937919 | J:346788
First Author: Schwartz C
Year: 2019
Journal: Allergy
Title: Spontaneous atopic dermatitis in mice with a defective skin barrier is independent of ILC2 and mediated by IL-1β.
Volume: 74
Issue: 10
Pages: 1920-1933
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Publication
30146158 | J:311882
First Author: Xu D
Year: 2018
Journal: Cell
Title: TBK1 Suppresses RIPK1-Driven Apoptosis and Inflammation during Development and in Aging.
Volume: 174
Issue: 6
Pages: 1477-1491.e19
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Publication
31505254 | J:295435
 
First Author: Yli-Karjanmaa M
Year: 2019
Journal: Brain Behav Immun
Title: TNF deficiency causes alterations in the spatial organization of neurogenic zones and alters the number of microglia and neurons in the cerebral cortex.
Volume: 82
Pages: 279-297
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Publication
36414671 | J:331482
First Author: Yan L
Year: 2022
Journal: Nat Commun
Title: SENP1 prevents steatohepatitis by suppressing RIPK1-driven apoptosis and inflammation.
Volume: 13
Issue: 1
Pages: 7153
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Publication
19571816 | J:157054
First Author: Egawa G
Year: 2009
Journal: J Invest Dermatol
Title: Transient expression of ephrin b2 in perinatal skin is required for maintenance of keratinocyte homeostasis.
Volume: 129
Issue: 10
Pages: 2386-95
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Publication
11518254 | J:72151
First Author: Drake TA
Year: 2001
Journal: J Orthop Res
Title: Genetic loci influencing natural variations in femoral bone morphometry in mice.
Volume: 19
Issue: 4
Pages: 511-7
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Publication
11698278 | J:98123
First Author: Geiger H
Year: 2001
Journal: Blood
Title: Age- and stage-specific regulation patterns in the hematopoietic stem cell hierarchy.
Volume: 98
Issue: 10
Pages: 2966-72
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Publication
38395995 | J:345820
First Author: Cardarelli S
Year: 2024
Journal: Cell Death Dis
Title: Modulation of cAMP/cGMP signaling as prevention of congenital heart defects in Pde2A deficient embryos: a matter of oxidative stress.
Volume: 15
Issue: 2
Pages: 169
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Publication
31562139 | J:282576
 
First Author: Nakajima K
Year: 2019
Journal: Dis Model Mech
Title: Lack of whey acidic protein (WAP) four-disulfide core domain protease inhibitor 2 (WFDC2) causes neonatal death from respiratory failure in mice.
Volume: 12
Issue: 11
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Publication
34905516 | J:320249
 
First Author: Godsel LM
Year: 2022
Journal: J Clin Invest
Title: Translational implications of Th17-skewed inflammation due to genetic deficiency of a cadherin stress sensor.
Volume: 132
Issue: 3
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Publication
8138038 | J:17723
First Author: Kohchi C
Year: 1994
Journal: Int J Biochem
Title: Constitutive expression of TNF-alpha and -beta genes in mouse embryo: roles of cytokines as regulator and effector on development.
Volume: 26
Issue: 1
Pages: 111-9
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Publication
36314682 | J:331873
First Author: Rasile M
Year: 2022
Journal: EMBO J
Title: Maternal immune activation leads to defective brain-blood vessels and intracerebral hemorrhages in male offspring.
Volume: 41
Issue: 23
Pages: e111192
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Publication
29180744 | J:255932
First Author: Mario Gonzalez-Meljem J
Year: 2017
Journal: Nat Commun
Title: Stem cell senescence drives age-attenuated induction of pituitary tumours in mouse models of paediatric craniopharyngioma.
Volume: 8
Issue: 1
Pages: 1819
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Publication
8482578 | J:16092
First Author: Malek TR
Year: 1993
Journal: Immunogenetics
Title: The IL-2 receptor beta chain gene (Il-2rb) is closely linked to the Pdgfb locus on mouse chromosome 15.
Volume: 38
Issue: 2
Pages: 154-6
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Publication
8288218 | J:15563
First Author: Wilkie TM
Year: 1993
Journal: Genomics
Title: Identification, chromosomal location, and genome organization of mammalian G-protein-coupled receptors.
Volume: 18
Issue: 2
Pages: 175-84
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Publication
8288233 | J:15567
First Author: Warden CH
Year: 1993
Journal: Genomics
Title: Linkage mapping of 40 randomly isolated liver cDNA clones in the mouse.
Volume: 18
Issue: 2
Pages: 295-307
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Publication
22682244 | J:186161
First Author: Hu B
Year: 2012
Journal: Cell
Title: Multifocal epithelial tumors and field cancerization from loss of mesenchymal CSL signaling.
Volume: 149
Issue: 6
Pages: 1207-20
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Publication
- | J:238766
     
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
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Publication
- | J:165963
     
First Author: Centre for Modeling Human Disease
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the NorCOMM project by the Centre for Modeling Human Disease (Cmhd), Institute of Biomaterials & Biomedical Engineering, University of Toronto
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Publication
- | J:101977
     
First Author: The Jackson Laboratory
Year: 2005
Journal: Unpublished
Title: Information obtained from The Jackson Laboratory, Bar Harbor, ME
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Publication
- | J:15839
       
First Author: International Committee on Standardized Genetic Nomenclature for Mice
Year: 1993
Title: Nomenclature rule change to delete hyphens and parentheses from mouse locus symbols
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Publication
- | J:155845
     
First Author: Wellcome Trust Sanger Institute
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Wellcome Trust Sanger Institute
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Publication
- | J:188991
     
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
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Publication
24194600 | J:228563
First Author: Koscielny G
Year: 2014
Journal: Nucleic Acids Res
Title: The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data.
Volume: 42
Issue: Database issue
Pages: D802-9
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Publication
- | J:155856
       
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
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
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
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 Genome 430 2.0 Array Platform
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Publication
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Allele
Il1a<em2Smoc> | MGI:7290451
Name: interleukin 1 alpha; endonuclease-mediated mutation 2, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Allele
Il1a<tm1(IL1A)Smoc> | MGI:7786885
Name: interleukin 1 alpha; targeted mutation 1, Shanghai Model Organisms Center
Allele Type: Targeted
Attribute String: Humanized sequence, Inserted expressed sequence
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Strain
MGI:6428937 | C57BL/6JSmoc-Il1a<em2Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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Strain
MGI:7788722 | C57BL/6JSmoc-Il1a<tm1(IL1A)Smoc>/Smoc
Attribute String: coisogenic, mutant strain, targeted mutation
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MP Term
MP:0008654 | increased interleukin-1 alpha secretion
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MP Term
MP:0008653 | abnormal interleukin-1 alpha secretion
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MP Term
MP:0008638 | increased circulating interleukin-1 alpha level
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MP Term
MP:0008637 | abnormal circulating interleukin-1 alpha level
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MP Term
MP:0008655 | decreased interleukin-1 alpha secretion
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Allele
Il1a<em1Tdk> | MGI:7431279
Name: interleukin 1 alpha; endonuclease-mediated mutation 1, Thirumala-Devi Kanneganti
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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MP Term
MP:0008639 | decreased circulating interleukin-1 alpha level
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Strain
MGI:7431280 | C57BL/6J-Il1a<em1Tdk>/J
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Publication
12746488 | -
First Author: Mandinova A
Year: 2003
Journal: J Cell Sci
Title: S100A13 mediates the copper-dependent stress-induced release of IL-1alpha from both human U937 and murine NIH 3T3 cells.
Volume: 116
Issue: Pt 13
Pages: 2687-96
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Publication
20863990 | -
First Author: Cao R
Year: 2010
Journal: J Formos Med Assoc
Title: Effect of human S100A13 gene silencing on FGF-1 transportation in human endothelial cells.
Volume: 109
Issue: 9
Pages: 632-40
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Publication
16165218 | -
First Author: Hayrabedyan S
Year: 2005
Journal: J Reprod Immunol
Title: FGF-1 and S100A13 possibly contribute to angiogenesis in endometriosis.
Volume: 67
Issue: 1-2
Pages: 87-101
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Protein Domain
IPR028487 | S100A13
Type: Family
Description: S100A13 belongs to the S100 calcium-binding family. S100A13 is a requisite component of the fibroblast growth factor-1 (FGF-1) protein release complex and is involved in human tumorigenesis by interacting with FGF-1 and interleukin-1 []. It is required for the copper-dependent stress-induced export of IL1A and FGF1 []. It also plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway [].
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Publication
39577420 | J:360628
First Author: Hänggi K
Year: 2024
Journal: Cancer Cell
Title: Interleukin-1α release during necrotic-like cell death generates myeloid-driven immunosuppression that restricts anti-tumor immunity.
Volume: 42
Issue: 12
Pages: 2015-2031.e11
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Publication
8188271 | J:16772
First Author: Nicklin MJ
Year: 1994
Journal: Genomics
Title: A physical map of the region encompassing the human interleukin-1 alpha, interleukin-1 beta, and interleukin-1 receptor antagonist genes.
Volume: 19
Issue: 2
Pages: 382-4
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Publication
34037658 | J:307937
 
First Author: Leon KE
Year: 2021
Journal: J Cell Biol
Title: DOT1L modulates the senescence-associated secretory phenotype through epigenetic regulation of IL1A.
Volume: 220
Issue: 8
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Publication
17215490 | J:121947
First Author: Robertson SA
Year: 2007
Journal: Biol Reprod
Title: Interleukin 10 regulates inflammatory cytokine synthesis to protect against lipopolysaccharide-induced abortion and fetal growth restriction in mice.
Volume: 76
Issue: 5
Pages: 738-48
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Publication
30061415 | J:265082
First Author: Kayama H
Year: 2018
Journal: Proc Natl Acad Sci U S A
Title: Heme ameliorates dextran sodium sulfate-induced colitis through providing intestinal macrophages with noninflammatory profiles.
Volume: 115
Issue: 33
Pages: 8418-8423
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Publication
26061908 | J:318749
First Author: Lodder J
Year: 2015
Journal: Autophagy
Title: Macrophage autophagy protects against liver fibrosis in mice.
Volume: 11
Issue: 8
Pages: 1280-92
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Publication
35916061 | J:357615
 
First Author: Torres P
Year: 2022
Journal: Dis Model Mech
Title: A motor neuron disease mouse model reveals a non-canonical profile of senescence biomarkers.
Volume: 15
Issue: 8
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Publication
27417459 | J:251113
First Author: Polyák Á
Year: 2016
Journal: Biochim Biophys Acta
Title: Brown adipose tissue in obesity: Fractalkine-receptor dependent immune cell recruitment affects metabolic-related gene expression.
Volume: 1861
Issue: 11
Pages: 1614-1622
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Publication
18337516 | J:140809
First Author: Fouladi-Nashta AA
Year: 2008
Journal: Biol Reprod
Title: Interleukin 1 signaling is regulated by leukemia inhibitory factor (LIF) and is aberrant in Lif-/- mouse uterus.
Volume: 79
Issue: 1
Pages: 142-53
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Publication
24893973 | J:241976
 
First Author: Ulrich JD
Year: 2014
Journal: Mol Neurodegener
Title: Altered microglial response to Aβ plaques in APPPS1-21 mice heterozygous for TREM2.
Volume: 9
Pages: 20
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Publication
16113081 | J:101157
First Author: Ohmura K
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: Variation in IL-1beta gene expression is a major determinant of genetic differences in arthritis aggressivity in mice.
Volume: 102
Issue: 35
Pages: 12489-94
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Publication
33361796 | J:305578
First Author: Zeitelhofer M
Year: 2020
Journal: Sci Rep
Title: Blocking PDGF-CC signaling ameliorates multiple sclerosis-like neuroinflammation by inhibiting disruption of the blood-brain barrier.
Volume: 10
Issue: 1
Pages: 22383
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Publication
37015809 | J:355315
First Author: Dong G
Year: 2023
Journal: J Neurosci
Title: Interleukin (IL)-1 Receptor Signaling Is Required for Complete Taste Bud Regeneration and the Recovery of Neural Taste Responses following Axotomy.
Volume: 43
Issue: 19
Pages: 3439-3455
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Protein
P97352
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
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Protein
Q545H7
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
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Protein
A0A0A0MQ90
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein Domain
IPR004076 | IL-1_rcpt_I-typ
Type: Family
Description: Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis []. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors []. The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution, and map to thesame chromosomal location []. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and IL-1RA).The crystal structures of IL1A and IL1B []have been solved, showing them to share the same 12-stranded β-sheet structure as both the heparin binding growth factors and the Kunitz-type soybean trypsin inhibitors []. The β-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel β-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding.The Vaccinia virus genes B15R and B18R each encode proteins with N-terminal hydrophobic sequences, possible sites for attachment of N-linked carbohydrate and a short C-terminal hydrophobic domain []. These propertiesare consistent with the mature proteins being either virion, cell surface or secretory glycoproteins. Protein sequence comparisons reveal that the gene products are related to each other (20% identity) and to the Ig superfamily. The highest degree of similarity is to the human and murine interleukin-1 receptors, although both proteins are related to a wide range of Ig superfamily members, including the interleukin-6 receptor. A novel method for virus immune evasion has been proposed in which the product of one or both of these proteins may bind interleukin-1 and/or interleukin-6, preventing these cytokines reaching their natural receptors []. A similar gene product from Cowpox virus (CPV) has also been shown to specifically bind murine IL-1 beta [].This entry represents Interleukin-1 receptor type 1 (IL1R1), the crystal structure of the soluble extracellular part of type-I IL1R complexed with IL1RA has been determined to 2.7A resolution []. The receptor structure is characterised by three Ig-like domains, of which domains 1 and 2 are tightly linked, while domain 3 is completely separate and connected by a flexible linker.
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Protein Domain
IPR004074 | IL-1_rcpt_I/II-typ
Type: Family
Description: Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis []. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors []. The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution, and map to thesame chromosomal location []. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and IL-1RA).The crystal structures of IL1A and IL1B []have been solved, showing them to share the same 12-stranded β-sheet structure as both the heparin binding growth factors and the Kunitz-type soybean trypsin inhibitors []. The β-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel β-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding.The Vaccinia virus genes B15R and B18R each encode proteins with N-terminal hydrophobic sequences, possible sites for attachment of N-linked carbohydrate and a short C-terminal hydrophobic domain []. These propertiesare consistent with the mature proteins being either virion, cell surface or secretory glycoproteins. Protein sequence comparisons reveal that the gene products are related to each other (20% identity) and to the Ig superfamily. The highest degree of similarity is to the human and murine interleukin-1 receptors, although both proteins are related to a wide range of Ig superfamily members, including the interleukin-6 receptor. A novel method for virus immune evasion has been proposed in which the product of one or both of these proteins may bind interleukin-1 and/or interleukin-6, preventing these cytokines reaching their natural receptors []. A similar gene product from Cowpox virus (CPV) has also been shown to specifically bind murine IL-1 beta [].The crystal structure of the soluble extracellular part of type-I IL1Rcomplexed with IL1RA has been determined to 2.7A resolution []. The receptor structure is characterised by three Ig-like domains, of whichdomains 1 and 2 are tightly linked, while domain 3 is completely separate and connected by a flexible linker.
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Protein Domain
IPR004078 | IL-1-bd
Type: Family
Description: Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis []. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors []. The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution, and map to thesame chromosomal location []. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and IL-1RA).The crystal structures of IL1A and IL1B []have been solved, showing them to share the same 12-stranded β-sheet structure as both the heparin binding growth factors and the Kunitz-type soybean trypsin inhibitors []. The β-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel β-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding.The Vaccinia virus genes B15R and B18R each encode proteins with N-terminal hydrophobic sequences, possible sites for attachment of N-linked carbohydrate and a short C-terminal hydrophobic domain []. These propertiesare consistent with the mature proteins being either virion, cell surface or secretory glycoproteins. Protein sequence comparisons reveal that the gene products are related to each other (20% identity) and to the Ig superfamily. The highest degree of similarity is to the human and murine interleukin-1 receptors, although both proteins are related to a wide range of Ig superfamily members, including the interleukin-6 receptor. A novel method for virus immune evasion has been proposed in which the product of one or both of these proteins may bind interleukin-1 and/or interleukin-6, preventing these cytokines reaching their natural receptors []. A similar gene product from Cowpox virus (CPV) has also been shown to specifically bind murine IL-1 beta [].
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Protein Domain
IPR003296 | IL-1_beta
Type: Family
Description: Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis []. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors []. The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution, and map to thesame chromosomal location []. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and IL-1RA).The crystal structures of IL1A and IL1B []have been solved, showing them to share the same 12-stranded β-sheet structure as both the heparin binding growth factors and the Kunitz-type soybean trypsin inhibitors []. The β-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel β-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding.The Vaccinia virus genes B15R and B18R each encode proteins with N-terminal hydrophobic sequences, possible sites for attachment of N-linked carbohydrate and a short C-terminal hydrophobic domain []. These propertiesare consistent with the mature proteins being either virion, cell surface or secretory glycoproteins. Protein sequence comparisons reveal that the gene products are related to each other (20% identity) and to the Ig superfamily. The highest degree of similarity is to the human and murine interleukin-1 receptors, although both proteins are related to a wide range of Ig superfamily members, including the interleukin-6 receptor. A novel method for virus immune evasion has been proposed in which the product of one or both of these proteins may bind interleukin-1 and/or interleukin-6, preventing these cytokines reaching their natural receptors []. A similar gene product from Cowpox virus (CPV) has also been shown to specifically bind murine IL-1 beta [].This entry represents IL-1 beta (IL1B)
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Protein Domain
IPR020877 | IL-1_CS
Type: Conserved_site
Description: Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis []. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors []. The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution, and map to thesame chromosomal location []. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and IL-1RA).The crystal structures of IL1A and IL1B []have been solved, showing them to share the same 12-stranded β-sheet structure as both the heparin binding growth factors and the Kunitz-type soybean trypsin inhibitors []. The β-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel β-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding.The Vaccinia virus genes B15R and B18R each encode proteins with N-terminal hydrophobic sequences, possible sites for attachment of N-linked carbohydrate and a short C-terminal hydrophobic domain []. These propertiesare consistent with the mature proteins being either virion, cell surface or secretory glycoproteins. Protein sequence comparisons reveal that the gene products are related to each other (20% identity) and to the Ig superfamily. The highest degree of similarity is to the human and murine interleukin-1 receptors, although both proteins are related to a wide range of Ig superfamily members, including the interleukin-6 receptor. A novel method for virus immune evasion has been proposed in which the product of one or both of these proteins may bind interleukin-1 and/or interleukin-6, preventing these cytokines reaching their natural receptors []. A similar gene product from Cowpox virus (CPV) has also been shown to specifically bind murine IL-1 beta [].This entry represents the Interleukin-1 conserved region in the C-terminal section.
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Protein Domain
IPR003295 | IL-1_alpha
Type: Family
Description: Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis []. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors []. The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution, and map to thesame chromosomal location []. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and IL-1RA).The crystal structures of IL1A and IL1B []have been solved, showing them to share the same 12-stranded β-sheet structure as both the heparin binding growth factors and the Kunitz-type soybean trypsin inhibitors []. The β-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel β-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding.The Vaccinia virus genes B15R and B18R each encode proteins with N-terminal hydrophobic sequences, possible sites for attachment of N-linked carbohydrate and a short C-terminal hydrophobic domain []. These propertiesare consistent with the mature proteins being either virion, cell surface or secretory glycoproteins. Protein sequence comparisons reveal that the gene products are related to each other (20% identity) and to the Ig superfamily. The highest degree of similarity is to the human and murine interleukin-1 receptors, although both proteins are related to a wide range of Ig superfamily members, including the interleukin-6 receptor. A novel method for virus immune evasion has been proposed in which the product of one or both of these proteins may bind interleukin-1 and/or interleukin-6, preventing these cytokines reaching their natural receptors []. A similar gene product from Cowpox virus (CPV) has also been shown to specifically bind murine IL-1 beta [].This entry represents the IL-1 family alpha (IL1A).
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Protein Domain
IPR003502 | IL-1_propep
Type: Domain
Description: Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis []. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors []. The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution, and map to thesame chromosomal location []. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and IL-1RA).The crystal structures of IL1A and IL1B []have been solved, showing them to share the same 12-stranded β-sheet structure as both the heparin binding growth factors and the Kunitz-type soybean trypsin inhibitors []. The β-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel β-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding.The Vaccinia virus genes B15R and B18R each encode proteins with N-terminal hydrophobic sequences, possible sites for attachment of N-linked carbohydrate and a short C-terminal hydrophobic domain []. These propertiesare consistent with the mature proteins being either virion, cell surface or secretory glycoproteins. Protein sequence comparisons reveal that the gene products are related to each other (20% identity) and to the Ig superfamily. The highest degree of similarity is to the human and murine interleukin-1 receptors, although both proteins are related to a wide range of Ig superfamily members, including the interleukin-6 receptor. A novel method for virus immune evasion has been proposed in which the product of one or both of these proteins may bind interleukin-1 and/or interleukin-6, preventing these cytokines reaching their natural receptors []. A similar gene product from Cowpox virus (CPV) has also been shown to specifically bind murine IL-1 beta [].The N-terminal of Interleukin-1 is approximately 115 amino acids long, it forms a propeptide that is cleaved off to release the active interleukin-1. This signature is for the propeptide.
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Protein Coding Gene
MGI:96544 | Casp1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CAROLIEiJ_G0031743 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0034312 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0034289 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0034219 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0034283 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0033995 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_96544 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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