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Protein

Interleukin-1 alpha

Gene

IL1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • copper ion binding Source: UniProtKB
  • cytokine activity Source: BHF-UCL

GO - Biological processi

  • apoptotic process Source: ProtInc
  • cell proliferation Source: ProtInc
  • cellular response to heat Source: UniProtKB
  • connective tissue replacement involved in inflammatory response wound healing Source: Ensembl
  • cytokine-mediated signaling pathway Source: BHF-UCL
  • ectopic germ cell programmed cell death Source: Ensembl
  • extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  • fever generation Source: UniProtKB-KW
  • immune response Source: InterPro
  • inflammatory response Source: ProtInc
  • negative regulation of cell proliferation Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of cytokine secretion Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: GO_Central
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: GO_Central
  • positive regulation of interleukin-2 biosynthetic process Source: BHF-UCL
  • positive regulation of JNK cascade Source: GO_Central
  • positive regulation of mitotic nuclear division Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of vascular endothelial growth factor production Source: BHF-UCL
  • response to copper ion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Mitogen, Pyrogen

Keywords - Biological processi

Inflammatory response

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_22442. Interleukin-1 signaling.
REACT_23950. Interleukin-1 processing.
SignaLinkiP01583.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-1 alpha
Short name:
IL-1 alpha
Alternative name(s):
Hematopoietin-1
Gene namesi
Name:IL1A
Synonyms:IL1F1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5991. IL1A.

Subcellular locationi

  • 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.

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29807.

Chemistry

DrugBankiDB06372. Rilonacept.

Polymorphism and mutation databases

BioMutaiIL1A.
DMDMi124297.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1121121 PublicationPRO_0000015265Add
BLAST
Chaini113 – 271159Interleukin-1 alphaPRO_0000015266Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi82 – 821N6-myristoyl lysine1 Publication
Lipidationi83 – 831N6-myristoyl lysine1 Publication
Modified residuei87 – 871PhosphoserineBy similarity
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP01583.
PaxDbiP01583.
PRIDEiP01583.

PTM databases

PhosphoSiteiP01583.

Miscellaneous databases

PMAP-CutDBP01583.

Expressioni

Gene expression databases

BgeeiP01583.
CleanExiHS_IL1A.
GenevisibleiP01583. HS.

Organism-specific databases

HPAiHPA048546.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP1P294663EBI-1749782,EBI-516667

Protein-protein interaction databases

BioGridi109768. 11 interactions.
DIPiDIP-40550N.
IntActiP01583. 4 interactions.
MINTiMINT-1534764.
STRINGi9606.ENSP00000263339.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi124 – 13714Combined sources
Beta strandi143 – 1508Combined sources
Beta strandi152 – 1554Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi165 – 1728Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi181 – 1899Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi212 – 2143Combined sources
Helixi216 – 2216Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi248 – 2514Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi264 – 2674Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITAmodel-A121-271[»]
2ILAX-ray2.30A117-271[»]
2KKINMR-A121-271[»]
2L5XNMR-A/D121-271[»]
ProteinModelPortaliP01583.
SMRiP01583. Positions 121-271.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01583.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the IL-1 family.Curated

Phylogenomic databases

eggNOGiNOG39906.
GeneTreeiENSGT00390000013353.
HOGENOMiHOG000113034.
HOVERGENiHBG002432.
InParanoidiP01583.
KOiK04383.
OMAiNQKSFYD.
OrthoDBiEOG76473H.
PhylomeDBiP01583.
TreeFamiTF300203.

Family and domain databases

InterProiIPR008996. 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]
PANTHERiPTHR11420. PTHR11420. 1 hit.
PfamiPF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]
PRINTSiPR00264. INTERLEUKIN1.
PR01358. INTRLEUKIN1A.
PR01357. INTRLEUKN1AB.
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01583-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVPDMFED LKNCYSENEE DSSSIDHLSL NQKSFYHVSY GPLHEGCMDQ
60 70 80 90 100
SVSLSISETS KTSKLTFKES MVVVATNGKV LKKRRLSLSQ SITDDDLEAI
110 120 130 140 150
ANDSEEEIIK PRSAPFSFLS NVKYNFMRII KYEFILNDAL NQSIIRANDQ
160 170 180 190 200
YLTAAALHNL DEAVKFDMGA YKSSKDDAKI TVILRISKTQ LYVTAQDEDQ
210 220 230 240 250
PVLLKEMPEI PKTITGSETN LLFFWETHGT KNYFTSVAHP NLFIATKQDY
260 270
WVCLAGGPPS ITDFQILENQ A
Length:271
Mass (Da):30,607
Last modified:July 21, 1986 - v1
Checksum:iCBCCC49569D9ED40
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851R → Q.1 Publication
Corresponds to variant rs3783531 [ dbSNP | Ensembl ].
VAR_014304
Natural varianti114 – 1141A → S.3 Publications
Corresponds to variant rs17561 [ dbSNP | Ensembl ].
VAR_014305
Natural varianti125 – 1251N → D.
Corresponds to variant rs17562 [ dbSNP | Ensembl ].
VAR_014600
Natural varianti138 – 1381D → N.1 Publication
Corresponds to variant rs3783581 [ dbSNP | Ensembl ].
VAR_014306
Natural varianti176 – 1761D → H.
Corresponds to variant rs1801715 [ dbSNP | Ensembl ].
VAR_014601

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2101.1.
PIRiA23385. ICHU1A.
RefSeqiNP_000566.3. NM_000575.3.
UniGeneiHs.1722.

Genome annotation databases

EnsembliENST00000263339; ENSP00000263339; ENSG00000115008.
GeneIDi3552.
KEGGihsa:3552.
UCSCiuc002tig.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Interleukin-1 entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2101.1.
PIRiA23385. ICHU1A.
RefSeqiNP_000566.3. NM_000575.3.
UniGeneiHs.1722.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITAmodel-A121-271[»]
2ILAX-ray2.30A117-271[»]
2KKINMR-A121-271[»]
2L5XNMR-A/D121-271[»]
ProteinModelPortaliP01583.
SMRiP01583. Positions 121-271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109768. 11 interactions.
DIPiDIP-40550N.
IntActiP01583. 4 interactions.
MINTiMINT-1534764.
STRINGi9606.ENSP00000263339.

Chemistry

DrugBankiDB06372. Rilonacept.

PTM databases

PhosphoSiteiP01583.

Polymorphism and mutation databases

BioMutaiIL1A.
DMDMi124297.

Proteomic databases

MaxQBiP01583.
PaxDbiP01583.
PRIDEiP01583.

Protocols and materials databases

DNASUi3552.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263339; ENSP00000263339; ENSG00000115008.
GeneIDi3552.
KEGGihsa:3552.
UCSCiuc002tig.3. human.

Organism-specific databases

CTDi3552.
GeneCardsiGC02M113531.
HGNCiHGNC:5991. IL1A.
HPAiHPA048546.
MIMi147760. gene.
neXtProtiNX_P01583.
PharmGKBiPA29807.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39906.
GeneTreeiENSGT00390000013353.
HOGENOMiHOG000113034.
HOVERGENiHBG002432.
InParanoidiP01583.
KOiK04383.
OMAiNQKSFYD.
OrthoDBiEOG76473H.
PhylomeDBiP01583.
TreeFamiTF300203.

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_22442. Interleukin-1 signaling.
REACT_23950. Interleukin-1 processing.
SignaLinkiP01583.

Miscellaneous databases

ChiTaRSiIL1A. human.
EvolutionaryTraceiP01583.
GeneWikiiIL1A.
GenomeRNAii3552.
NextBioi13868.
PMAP-CutDBP01583.
PROiP01583.
SOURCEiSearch...

Gene expression databases

BgeeiP01583.
CleanExiHS_IL1A.
GenevisibleiP01583. HS.

Family and domain databases

InterProiIPR008996. 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]
PANTHERiPTHR11420. PTHR11420. 1 hit.
PfamiPF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]
PRINTSiPR00264. INTERLEUKIN1.
PR01358. INTRLEUKIN1A.
PR01357. INTRLEUKN1AB.
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Entry informationi

Entry nameiIL1A_HUMAN
AccessioniPrimary (citable) accession number: P01583
Secondary accession number(s): Q53QF9, Q7RU02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.