IL1A
entrez
3552
canonical
uniprot
P01583
canonical
ensembl
ENSG00000115008
resolver
ensp
ENSP00000263339
resolver
ensp
ENSP00000629482
resolver
enst
ENST00000263339
resolver
enst
ENST00000959423
resolver
genesymbol
IL1A
resolver
genesymbol_syn
IL1F1
resolver
hgnc
HGNC:5991
resolver
uniprot
Q53QF9
resolver
uniprot
Q7RU02
resolver
uniprot_entry
IL1A_HUMAN
resolver
uniprot_sec
Q53QF9
resolver
uniprot_sec
Q7RU02
resolver
amino_acid_sequence
MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA
uniprot
proteins
function
FUNCTION: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems (PubMed:26439902). After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex (PubMed:17507369, PubMed:2950091). Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4 (PubMed:17507369). In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways (PubMed:14687581). Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage (PubMed:15679580). In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as a signal for genotoxic stress without loss of cell integrity (PubMed:26439902). {ECO:0000269|PubMed:14687581, ECO:0000269|PubMed:15679580, ECO:0000269|PubMed:17507369, ECO:0000269|PubMed:26439902, ECO:0000269|PubMed:2950091, ECO:0000269|PubMed:3258335}.
uniprot
proteins
mass_dalton
30607
uniprot
proteins
mutagenesis
MUTAGEN 82; /note="K->Q: About 50% loss of cytokine secretion after DNA damage."; /evidence="ECO:0000269|PubMed:26439902
uniprot
proteins
post_translational_modification
PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization. {ECO:0000269|PubMed:26439902}.; PTM: Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules. {ECO:0000269|PubMed:2115174}.; PTM: Phosphorylated. Phosphorylation greatly enhances susceptibility to digestion and promotes the conversion of pre-IL1A alpha to the biologically active IL1A. {ECO:0000269|PubMed:3258335}.
uniprot
proteins
protein_family
IL-1 family
uniprot
proteins
pubmed
11991722
uniprot
proteins
pubmed
14687581
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15679580
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17507369
uniprot
proteins
pubmed
2115174
uniprot
proteins
pubmed
21270123
uniprot
proteins
pubmed
2346741
uniprot
proteins
pubmed
2635664
uniprot
proteins
pubmed
26439902
uniprot
proteins
pubmed
2950091
uniprot
proteins
pubmed
2989698
uniprot
proteins
pubmed
2994016
uniprot
proteins
pubmed
32272059
uniprot
proteins
pubmed
3258335
uniprot
proteins
pubmed
3281727
uniprot
proteins
pubmed
3485152
uniprot
proteins
pubmed
3486405
uniprot
proteins
pubmed
3493774
uniprot
proteins
pubmed
8346241
uniprot
proteins
sequence_length
271
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26439902}. Cytoplasm {ECO:0000269|PubMed:32272059}. Secreted {ECO:0000269|PubMed:26439902}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). Recruited to DNA damage sites and secreted after genotoxic stress. {ECO:0000269|PubMed:32272059}.
uniprot
proteins