The domain within your query sequence starts at position 5 and ends at position 72; the E-value for the IL1 domain shown below is 1e-42.

SGALCFRMKDSALKVLYLHNNQLLAGGLHAEKVIKGEEISVVPNRALDASLSPVILGVQG
GSQCLSCG

The domain was found using the schnipsel database

IL1

Interleukin-1 homologues

• SMART accession number: SM00125
• Description: Cytokines with various biological functions. Interluekin 1 alpha and beta are also known as hematopoietin and catabolin.

There are 2006 IL1 domains in 2001 proteins in SMART's nrdb database.

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Dinarello CA
• Interleukin-1.
• Cytokine Growth Factor Rev. 1997; 8: 253-65

Interleukin-1 (IL-1) is the prototypic pro-inflammatory cytokine. There are two forms of IL-1, IL-1alpha and IL-1beta and in most studies, their biological activities are indistinguishable. IL-1 affects nearly every cell type, often in concert with another pro-inflammatory cytokine, tumor necrosis factor (TNF). Although IL-1 can upregulate host defenses and function as an immunoadjuvant, IL-1 is a highly inflammatory cytokine. The margin between clinical benefit and unacceptable toxicity in humans is exceedingly narrow. In contrast, agents that reduce the production and/or activity of IL-1 are likely to have an impact on clinical medicine. The synthesis, processing, secretion and activity of IL-1, particularly IL-1beta, are tightly regulated events. A unique aspect of cytokine biology is the naturally occurring IL-1 receptor antagonist (IL-1Ra). IL-1Ra is structurally similar to IL-1beta but lacking agonist activity is used in clinical trials to reduce disease severity. In addition, regulation of IL-1 activity extends to low numbers of surface receptors, circulating soluble receptors and a cell surface "decoy" receptor to down-regulate responses to IL-1beta. This review updates the current knowledge on IL-1.

• Patarca R, Fletcher MA
• Interleukin-1: basic science and clinical applications.
• Crit Rev Oncog. 1997; 8: 143-88

• Kurzrock R, Wetzler M, Estrov Z, Talpaz M
• Interleukin-1 and its inhibitors: a biologic and therapeutic model for the role of growth regulatory factors in leukemias.
• Cytokines Mol Ther. 1995; 1: 177-84

Production of growth factors may provide a mechanism for disease evolution in some leukemias. Interleukin-1 is a plelotropic cytokine with the ability to synergize with other growth factors as well as to stimulate their production and release. Autocrine and/or paracrine secretion of interleukin-1 has been implicated in the pathogenesis of both chronic and acute myelogenous leukemia. Recently, a series of both specific and nonspecific IL-1 inhibitory molecules have been identified. These include IL-1 receptor antagonist, soluble IL-1 receptors, IL-1-converting enzyme inhibitor, IL-4, IL-10 and IL-1-antisense. Early experiments demonstrating the ability of some of these molecules to inhibit acute and chronic myelogenous leukemia growth suggest that clinical trials of these compounds may provide a novel management approach in these malignancies. Here we review the potential biologic and therapeutic role of IL-1 and its inhibitors in the myeloid leukemias.

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
19.19	map04060	Cytokine-cytokine receptor interaction
15.15	map04640	Hematopoietic cell lineage
15.15	map04010	MAPK signaling pathway
15.15	map04210	Apoptosis
15.15	map04940	Type I diabetes mellitus
9.09	map04620	Toll-like receptor signaling pathway
9.09	map05010	Alzheimer's disease
1.01	map00970	Aminoacyl-tRNA biosynthesis
1.01	map00290	Valine, leucine and isoleucine biosynthesis

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with IL1 domain which could be assigned to a KEGG orthologous group, and not all proteins containing IL1 domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of IL1 domains in PDB

PDB code	Title
1hib	THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION
1i1b	CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-1BETA AT 2.0 ANGSTROMS RESOLUTION
1ilr	CRYSTAL STRUCTURE OF THE INTERLEUKIN-1 RECEPTOR ANTAGONIST
1ilt	X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION
1iob	INTERLEUKIN-1 BETA FROM JOINT X-RAY AND NMR REFINEMENT
1ira	COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)
1irp	SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN
1itb	TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA
1j0s	Solution structure of the human interleukin-18
1l2h	Crystal structure of Interleukin 1-beta F42W/W120F mutant
1md6	High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity
1s0l	Interleukin 1 beta mutant F42W
1t4q	Interleukin 1 beta F101W
1too	Interleukin 1B Mutant F146W
1tp0	Triple mutation in interleukin 1 beta cavity:replacement of phenylalanines with tryptophan.
1twe	INTERLEUKIN 1 BETA MUTANT F101Y
1twm	Interleukin-1 Beta Mutant F146Y
21bi	INTERLEUKIN-1 BETA (IL-1 BETA) (MUTANT WITH CYS 71 REPLACED BY ALA) (C71A)
2i1b	CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION
2ila	STRUCTURE OF INTERLEUKIN 1ALPHA AT 2.7-ANGSTROMS RESOLUTION
2irt	INITIAL CRYSTALLOGRAPHIC ANALYSES OF A RECOMBINANT INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN
2kh2	Solution structure of a scFv-IL-1B complex
2kki	Solution structure of human Interleukin 1a
2l5x	Solution structure of IL1A-S100A13 complex
2mib	THE STRUCTURE OF MURINE INTERLEUKIN-1 BETA AT 2.8 ANGSTROMS RESOLUTION
2nvh	Determination of Solvent Content in Cavities in Interleukin-1 Using Experimentally-Phased Electron Density
2vxt	Crystal structure of human IL-18 complexed to murine reference antibody 125-2H Fab
2wry	Crystal structure of chicken cytokine interleukin 1 beta
31bi	INTERLEUKIN-1 BETA (IL-1 BETA) (MUTANT WITH CYS 71 REPLACED BY SER) (C71S)
3f62	Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein
3ltq	Structure of Interleukin 1B solved by SAD using an inserted Lanthanide Binding Tag
3nj5	Crystal structure of chicken IL-1 hydrophobic cavity mutant 157
3o4o	Crystal structure of an Interleukin-1 receptor complex
3pok	Interleukin-1-beta LBT L3 Mutant
3wo2	3WO2
3wo3	3WO3
3wo4	3WO4
41bi	INTERLEUKIN-1 BETA (IL-1 BETA) (MUTANT WITH CYS 8 REPLACED BY ALA (C8A)
4dep	Structure of the IL-1b signaling complex
4g6j	Crystal structure of human IL-1beta in complex with the therapeutic antibody binding fragment of canakinumab
4g6m	Crystal strucure of human IL-1beta in complex with therapeutic antibody binding fragment of gevokizumab
4gaf	Crystal structure of EBI-005, a chimera of human IL-1beta and IL-1Ra, bound to human Interleukin-1 receptor type 1
4gai	Crystal structure of EBI-005, a chimera of human IL-1beta and IL-1Ra
4hjj	Structure Reveals Function of the Dual Variable Domain Immunoglobulin (DVD-Ig) Molecule
4i1b	FUNCTIONAL IMPLICATIONS OF INTERLEUKIN-1BETA BASED ON THE THREE-DIMENSIONAL STRUCTURE
4ize	4IZE
4p0j	4P0J
4p0k	4P0K
4p0l	4P0L
4r6u	4R6U
4x37	4X37
4x38	4X38
4x39	4X39
4x3a	4X3A
4xfs	4XFS
5bow	5BOW
5bvp	5BVP
5i1b	A COMPARISON OF THE HIGH RESOLUTION STRUCTURES OF HUMAN AND MURINE INTERLEUKIN-1B
6i1b	HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1 BETA IN SOLUTION BY THREE-AND FOUR-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
7i1b	HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1 BETA IN SOLUTION BY THREE-AND FOUR-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
8i1b	A COMPARISON OF THE HIGH RESOLUTION STRUCTURES OF HUMAN AND MURINE INTERLEUKIN-1B
9ilb	HUMAN INTERLEUKIN-1 BETA

Links (links to other resources describing this domain)

• PROSITE: IL1_DOMAIN