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P01583 (IL1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-1 alpha

Short name=IL-1 alpha
Alternative name(s):
Hematopoietin-1
Gene names
Name:IL1A
Synonyms:IL1F1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.

Subunit structure

Monomer.

Subcellular location

Secreted. 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.

Domain

The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function.

Sequence similarities

Belongs to the IL-1 family.

Ontologies

Keywords
   Biological processInflammatory response
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   Molecular functionCytokine
Mitogen
Pyrogen
   PTMGlycoprotein
Lipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement PubMed 1924307. Source: ProtInc

cell proliferation

Traceable author statement PubMed 6209582. Source: ProtInc

cellular response to heat

Inferred from direct assay PubMed 12746488. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

ectopic germ cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

fever generation

Inferred from electronic annotation. Source: UniProtKB-KW

immune response

Inferred from electronic annotation. Source: InterPro

inflammatory response

Traceable author statement PubMed 6209582. Source: ProtInc

negative regulation of cell proliferation

Inferred from direct assay Ref.6. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Traceable author statement PubMed 10748004. Source: BHF-UCL

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cytokine secretion

Inferred from direct assay PubMed 1739124. Source: BHF-UCL

positive regulation of interleukin-2 biosynthetic process

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

positive regulation of mitosis

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation vascular endothelial growth factor production

Inferred from sequence or structural similarity. Source: BHF-UCL

response to copper ion

Inferred from direct assay PubMed 12746488. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay PubMed 12746488. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 12746488. Source: UniProtKB

   Molecular_functioncopper ion binding

Inferred from direct assay PubMed 12746488. Source: UniProtKB

cytokine activity

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 12746488. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CASP1P294663EBI-1749782,EBI-516667

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 112112
PRO_0000015265
Chain113 – 271159Interleukin-1 alpha
PRO_0000015266

Amino acid modifications

Modified residue871Phosphoserine By similarity
Lipidation821N6-myristoyl lysine Ref.16
Lipidation831N6-myristoyl lysine Ref.16
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential

Natural variations

Natural variant851R → Q. Ref.10
Corresponds to variant rs3783531 [ dbSNP | Ensembl ].
VAR_014304
Natural variant1141A → S. Ref.3 Ref.4 Ref.10
Corresponds to variant rs17561 [ dbSNP | Ensembl ].
VAR_014305
Natural variant1251N → D.
Corresponds to variant rs17562 [ dbSNP | Ensembl ].
VAR_014600
Natural variant1381D → N. Ref.10
Corresponds to variant rs3783581 [ dbSNP | Ensembl ].
VAR_014306
Natural variant1761D → H.
Corresponds to variant rs1801715 [ dbSNP | Ensembl ].
VAR_014601

Secondary structure

..................................... 271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01583 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: CBCCC49569D9ED40

FASTA27130,607
        10         20         30         40         50         60 
MAKVPDMFED LKNCYSENEE DSSSIDHLSL NQKSFYHVSY GPLHEGCMDQ SVSLSISETS 

        70         80         90        100        110        120 
KTSKLTFKES MVVVATNGKV LKKRRLSLSQ SITDDDLEAI ANDSEEEIIK PRSAPFSFLS 

       130        140        150        160        170        180 
NVKYNFMRII KYEFILNDAL NQSIIRANDQ YLTAAALHNL DEAVKFDMGA YKSSKDDAKI 

       190        200        210        220        230        240 
TVILRISKTQ LYVTAQDEDQ PVLLKEMPEI PKTITGSETN LLFFWETHGT KNYFTSVAHP 

       250        260        270 
NLFIATKQDY WVCLAGGPPS ITDFQILENQ A 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs."
March C.J., Mosley B., Larsen A., Cerretti D.P., Braedt G., Price V., Gillis S., Henney C.S., Kronheim S.R., Grabstein K., Conlon P.J., Hopp T.P., Cosman D.
Nature 315:641-647(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete nucleotide sequence of the gene for human interleukin 1 alpha."
Furutani Y., Notake M., Fukui T., Ohue M., Nomura H., Yamada M., Nakamura S.
Nucleic Acids Res. 14:3167-3179(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning and characterization of the cDNAs for human and rabbit interleukin-1 precursor."
Furutani Y., Notake M., Yamayoshi M., Yamagishi J., Nomura H., Ohue M., Furuta R., Fukui T., Yamada M., Nakamura S.
Nucleic Acids Res. 13:5869-5882(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-114.
[4]"Cloning of the cDNA coding for human prointerleukin-1 alpha and prointerleukin-1 beta."
Kotenko S.V., Bulenkov M.T., Veiko V.P., Epishin S.M., Lomakin I.B., Emel'Yanov A.V., Kozlov A.P., Konusova V.G., Kotov A.Y., Kurbatova T.V., Reshetnikov V.L., Simbirtsev A.S., Ketlinskii S.A., Vinetskii Y.P.
Dokl. Akad. Nauk SSSR 309:1005-1008(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-114.
[5]"Recombinant human interleukin 1 alpha: purification and biological characterization."
Gubler U., Chua A.O., Stern A.S., Hellmann C.P., Vitek M.P., Dechiara T.M., Benjamin W.R., Collier K.J., Dukovich M., Familletti P.C., Fiedler-Nagy C., Jenson J., Kaffka K., Kilian P.L., Stremlo D., Wittreich B.H., Woehle D., Mizel S.B., Lomedico P.T.
J. Immunol. 136:2492-2497(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"cDNA cloning of IL-1 alpha and IL-1 beta from mRNA of U937 cell line."
Nishida T., Nishino N., Takano M., Kawai K., Bando K., Masui Y., Nakai S., Hirai Y.
Biochem. Biophys. Res. Commun. 143:345-352(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"A sequence-based map of the nine genes of the human interleukin-1 cluster."
Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G., Kornman K.
Genomics 79:718-725(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]SeattleSNPs variation discovery resource
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-85; SER-114 AND ASN-138.
[11]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[12]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[15]"Effects of hematopoietin-1 and interleukin 1 activities on early hematopoietic cells of the bone marrow."
Zsebo K.M., Wypych J., Yuschenkoff V.N., Lu H., Hunt P., Dukes P.P., Langley K.E.
Blood 71:962-968(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 113-132.
[16]"The 31-kDa precursor of interleukin 1 alpha is myristoylated on specific lysines within the 16-kDa N-terminal propiece."
Stevenson F.T., Bursten S.L., Fanton C., Locksley R.M., Lovett D.H.
Proc. Natl. Acad. Sci. U.S.A. 90:7245-7249(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT LYS-82 AND LYS-83.
[17]"Structure of interleukin 1 alpha at 2.7-A resolution."
Graves B.J., Hatada M.H., Hendrickson W.A., Miller J.K., Madison V.S., Satow Y.
Biochemistry 29:2679-2684(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Wikipedia

Interleukin-1 entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02531 mRNA. Translation: CAA26371.1.
X03833 Genomic DNA. Translation: CAA27448.1.
X02851 mRNA. Translation: CAA26604.1.
X56086 mRNA. Translation: CAA39566.1.
M28983 mRNA. Translation: AAA59134.1.
M15329 mRNA. Translation: AAA59133.1.
BN000002 Genomic DNA. Translation: CAD29871.1.
BT007014 mRNA. Translation: AAP35660.1.
CR457414 mRNA. Translation: CAG33695.1.
AF536338 Genomic DNA. Translation: AAM96189.1.
AK314850 mRNA. Translation: BAG37367.1.
AC112235 Genomic DNA. Translation: AAX93054.1.
CH471217 Genomic DNA. Translation: EAW73604.1.
BC013142 mRNA. Translation: AAH13142.1.
CCDSCCDS2101.1.
PIRICHU1A. A23385.
RefSeqNP_000566.3. NM_000575.3.
UniGeneHs.1722.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITAmodel-A121-271[»]
2ILAX-ray2.30A117-271[»]
2KKINMR-A121-271[»]
2L5XNMR-A/D121-271[»]
ProteinModelPortalP01583.
SMRP01583. Positions 121-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109768. 11 interactions.
IntActP01583. 2 interactions.
MINTMINT-1534764.
STRING9606.ENSP00000263339.

PTM databases

PhosphoSiteP01583.

Polymorphism databases

DMDM124297.

Proteomic databases

MaxQBP01583.
PaxDbP01583.
PRIDEP01583.

Protocols and materials databases

DNASU3552.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263339; ENSP00000263339; ENSG00000115008.
GeneID3552.
KEGGhsa:3552.
UCSCuc002tig.3. human.

Organism-specific databases

CTD3552.
GeneCardsGC02M113531.
HGNCHGNC:5991. IL1A.
HPAHPA048546.
MIM147760. gene.
neXtProtNX_P01583.
PharmGKBPA29807.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39906.
HOGENOMHOG000113034.
HOVERGENHBG002432.
InParanoidP01583.
KOK04383.
OMANQKSFYD.
OrthoDBEOG76473H.
PhylomeDBP01583.
TreeFamTF300203.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_6900. Immune System.
SignaLinkP01583.

Gene expression databases

BgeeP01583.
CleanExHS_IL1A.
GenevestigatorP01583.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR003295. IL-1_alpha.
IPR003294. IL-1_alpha/beta.
IPR020877. IL-1_CS.
IPR000975. IL-1_fam.
IPR003502. IL-1_propep.
[Graphical view]
PANTHERPTHR11420. PTHR11420. 1 hit.
PfamPF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]
PRINTSPR00264. INTERLEUKIN1.
PR01358. INTRLEUKIN1A.
PR01357. INTRLEUKN1AB.
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01583.
GeneWikiIL1A.
GenomeRNAi3552.
NextBio13868.
PMAP-CutDBP01583.
PROP01583.
SOURCESearch...

Entry information

Entry nameIL1A_HUMAN
AccessionPrimary (citable) accession number: P01583
Secondary accession number(s): Q53QF9, Q7RU02
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM