Reviewed, UniProtKB/Swiss-Prot P01583 (IL1A_HUMAN)

Names and origin

Protein names

Recommended name:
    Interleukin-1 alpha
      Short name=IL-1 alpha
Alternative name(s):
    Hematopoietin-1

Gene names

Name:	IL1A
Synonyms:	IL1F1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Inflammatory response
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Molecular function	Cytokine Mitogen Pyrogen
PTM	Glycoprotein Lipoprotein Myristate
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: ProtInc apoptosis Traceable author statement. Source: ProtInc cell proliferation Traceable author statement. Source: ProtInc cytokine-mediated signaling pathway Ref.1 Inferred from mutant phenotype. Source: UniProtKB fever Inferred from electronic annotation. Source: UniProtKB-KW immune response Inferred from electronic annotation. Source: InterPro negative regulation of cell proliferation Ref.6 Inferred from direct assay. Source: UniProtKB positive regulation of angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cytokine secretion Inferred from direct assay. Source: UniProtKB positive regulation of interleukin-2 biosynthetic process Ref.1 Inferred from mutant phenotype. Source: UniProtKB positive regulation of mitosis Ref.1 Inferred from mutant phenotype. Source: UniProtKB positive regulation vascular endothelial growth factor production Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular space Ref.6 Inferred from mutant phenotype. Source: UniProtKB
Molecular function	cytokine activity Ref.1 Inferred from mutant phenotype. Source: UniProtKB interleukin-1 receptor binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP1	P29466	3	EBI-1749782,EBI-516667

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 112

112

Ref.12

PRO_0000015265

Chain

113 – 271

159

Interleukin-1 alpha

PRO_0000015266

Amino acid modifications

Lipidation

82

1

N6-myristoyl lysine Ref.13

Lipidation

83

1

N6-myristoyl lysine Ref.13

Glycosylation

102

1

N-linked (GlcNAc...) Potential

Glycosylation

141

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

85

1

R → Q: dbSNP rs3783531. Ref.10

VAR_014304

Natural variant

114

1

A → S: dbSNP rs17561. Ref.10 Ref.3 Ref.4

VAR_014305

Natural variant

125

1

N → D: dbSNP rs17562.

VAR_014600

Natural variant

138

1

D → N: dbSNP rs3783581. Ref.10

VAR_014306

Natural variant

176

1

D → H: dbSNP rs1801715.

VAR_014601

Secondary structure

1

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271

Helix Strand Turn

Details...

Beta strand

124 – 138

15

Beta strand

143 – 146

4

Beta strand

152 – 155

4

Turn

161 – 162

2

Beta strand

166 – 172

7

Beta strand

181 – 186

6

Beta strand

191 – 194

4

Beta strand

203 – 206

4

Helix

216 – 221

6

Beta strand

222 – 228

7

Turn

229 – 230

2

Beta strand

231 – 236

6

Turn

240 – 241

2

Turn

258 – 259

2

Beta strand

264 – 267

4

Sequences

	Sequence		Length	Mass (Da)
	P01583-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: CBCCC49569D9ED40	FASTA	271	30,607
	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

References

	« Hide 'large scale' referencesShow '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: 2989698] [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: 3486405] [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: 2994016] [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: 2635664] [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: 3485152] [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: 3493774] [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: 11991722] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[12]	"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: 3281727] [Abstract] Cited for: PROTEIN SEQUENCE OF 113-132.
[13]	"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: 8346241] [Abstract] Cited for: MYRISTOYLATION AT LYS-82 AND LYS-83.
[14]	"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: 2346741] [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

EMBLGenBankDDBJ

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.
BC013142 mRNA. Translation: AAH13142.1.

IPI

IPI00003096.

PIR

ICHU1A. A23385.

RefSeq

NP_000566.3.

UniGene

Hs.1722

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ITA	model	-	A	121-271	[»]
2ILA	X-ray	2.30	A	117-271	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P01583. 2 interactions.

PTM databases

PhosphoSite

P01583.

Proteomic databases

PRIDE

P01583.

Genome annotation databases

Ensembl

ENSG00000115008. Homo sapiens. [Contig view]

GeneID

3552.

KEGG

hsa:3552.

UCSC

uc002tig.1. human.

Organism-specific databases

GeneCards

GC02M113247.

H-InvDB

HIX0002385.

HGNC

HGNC:5991. IL1A.

HPA

CAB004449.

MIM

147760. gene.

PharmGKB

PA29807.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P01583.

HOVERGEN

P01583.

OMA

P01583. NQKSFYD.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
il1pathway. IL1-mediated signaling events.

Gene expression databases

ArrayExpress

P01583.

Bgee

P01583.

CleanEx

HS_IL1A.

GermOnline

ENSG00000115008. Homo sapiens.

Family and domain databases

InterPro

IPR003502. IL1_propep.
IPR000975. Interleukin_1.
IPR003295. InterleukinIL1A.
IPR003294. InterleukinIL1AB.
[Graphical view]

PANTHER

PTHR11420. InterleukinIL1A. 1 hit.

Pfam

PF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]

PRINTS

PR00264. INTERLEUKIN1.
PR01358. INTRLEUKIN1A.
PR01357. INTRLEUKN1AB.

ProDom

PD002536. Interleukin_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00125. IL1. 1 hit.
[Graphical view]

PROSITE

PS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

13868.

PMAP-CutDB

P01583.

SOURCE

Search...

Entry information

Entry name

IL1A_HUMAN

Accession

Primary (citable) accession number: P01583
Secondary accession number(s): Q7RU02

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	July 7, 2009
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)