Interleukin-8 precursor - Homo sapiens (Human)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Web resources

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Web resources

Cross-references

Entry information

Relevant documents

Cleaved into the following 7 chains:

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Preferred order of sections

Cleaved into the following 7 chains:

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Contribute

Send feedback

Read comments (?) or add your own

P10145 (IL8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 18, 2012. Version 149. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Protein names

Recommended name:
Interleukin-8
Short name=IL-8

Alternative name(s):
C-X-C motif chemokine 8
Emoctakin
Granulocyte chemotactic protein 1
Short name=GCP-1
Monocyte-derived neutrophil chemotactic factor
Short name=MDNCF
Monocyte-derived neutrophil-activating peptide
Short name=MONAP
Neutrophil-activating protein 1
Short name=NAP-1
Protein 3-10C
T-cell chemotactic factor

MDNCF-a
Alternative name(s):
GCP/IL-8 protein IV
IL8/NAP1 form I
Interleukin-8
Alternative name(s):
(Ala-IL-8)77
GCP/IL-8 protein II
IL-8(1-77)
IL8/NAP1 form II
MDNCF-b
IL-8(5-77)
IL-8(6-77)
Alternative name(s):
(Ser-IL-8)72
GCP/IL-8 protein I
IL8/NAP1 form III
Lymphocyte-derived neutrophil-activating factor
Short name=LYNAP
MDNCF-c
Neutrophil-activating factor
Short name=NAF
IL-8(7-77)
Alternative name(s):
GCP/IL-8 protein V
IL8/NAP1 form IV
IL-8(8-77)
Alternative name(s):
GCP/IL-8 protein VI
IL8/NAP1 form V
IL-8(9-77)
Alternative name(s):
GCP/IL-8 protein III
IL8/NAP1 form VI

Gene names

Name:	IL8
Synonyms:	CXCL8

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Sequence length	99 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Function	IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively. Ref.15 Ref.24 Ref.27
Subunit structure	Homodimer.
Subcellular location	Secreted.
Post-translational modification	Several N-terminal processed forms are produced by proteolytic cleavage after secretion from at least peripheral blood monocytes, leukcocytes and endothelial cells. In general, IL-8(1-77) is referred to as interleukin-8. IL-8(6-77) is the most promiment form.
Sequence similarities	Belongs to the intercrine alpha (chemokine CxC) family.

Keywords
Biological process	Chemotaxis Inflammatory response
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Cytokine
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	G-protein coupled receptor signaling pathway Traceable author statement PubMed 8381837. Source: ProtInc activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome angiogenesis Traceable author statement PubMed 11483765. Source: UniProtKB calcium-mediated signaling Traceable author statement PubMed 11877327. Source: UniProtKB cell cycle arrest Inferred from direct assay PubMed 11564821. Source: UniProtKB cellular response to fibroblast growth factor stimulus Inferred from expression pattern PubMed 9407497. Source: UniProtKB cellular response to interleukin-1 Inferred from expression pattern PubMed 9407497. Source: UniProtKB cellular response to lipopolysaccharide Inferred from direct assay PubMed 19912257. Source: BHF-UCL cellular response to tumor necrosis factor Inferred from expression pattern PubMed 9407497. Source: UniProtKB embryonic digestive tract development Inferred from expression pattern PubMed 20875417. Source: DFLAT immune response Inferred from electronic annotation. Source: InterPro induction of positive chemotaxis Inferred from genetic interaction PubMed 11564821. Source: UniProtKB inflammatory response Traceable author statement PubMed 11483765. Source: UniProtKB negative regulation of G-protein coupled receptor protein signaling pathway Inferred from direct assay PubMed 10734056. Source: UniProtKB negative regulation of cell proliferation Traceable author statement PubMed 9551928. Source: ProtInc neutrophil activation Traceable author statement PubMed 11483765. Source: UniProtKB neutrophil chemotaxis Inferred from genetic interaction PubMed 11564821. Source: UniProtKB positive regulation of neutrophil chemotaxis Traceable author statement PubMed 1699135. Source: BHF-UCL receptor internalization Inferred from direct assay PubMed 10734056. Source: UniProtKB regulation of cell adhesion Inferred from direct assay Ref.25. Source: UniProtKB regulation of retroviral genome replication Inferred from direct assay PubMed 11483765. Source: UniProtKB
Cellular component	extracellular space Traceable author statement PubMed 10823949. Source: ProtInc intracellular Inferred from direct assay PubMed 10734056. Source: GOC
Molecular function	chemokine activity Traceable author statement PubMed 10881932. Source: ProtInc interleukin-8 receptor binding Inferred from physical interaction PubMed 1840701. Source: UniProtKB
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Signal peptide

1 – 20

Ref.14 Ref.15 Ref.16

Chain

21 – 99

MDNCF-a

PRO_0000005126

Chain

23 – 99

Interleukin-8

PRO_0000005127

Chain

27 – 99

IL-8(5-77)

PRO_0000041948

Chain

28 – 99

IL-8(6-77)

PRO_0000005128

Chain

29 – 99

IL-8(7-77)

PRO_0000005129

Chain

30 – 99

IL-8(8-77)

PRO_0000005130

Chain

31 – 99

IL-8(9-77)

PRO_0000005131

Site

27 – 28

Cleavage; by thrombin Probable

Site

28 – 29

Cleavage; by MMP9

Disulfide bond

34 ↔ 61

Disulfide bond

36 ↔ 77

Alternative sequence

92 – 99

FLKRAENS → AEVPENRGMDS in isoform 2.

VSP_001058

Sequence conflict

R → L AA sequence Ref.17

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 15C649996E89319F Show »	FASTA	99	11,098
10 20 30 40 50 60 MTSKLAVALL AAFLISAALC EGAVLPRSAK ELRCQCIKTY SKPFHPKFIK ELRVIESGPH 70 80 90 CANTEIIVKL SDGRELCLDP KENWVQRVVE KFLKRAENS « Hide
Isoform 2 [UniParc]. Checksum: E184B7B31606CFAD Show »	FASTA	102	11,338
10 20 30 40 50 60 MTSKLAVALL AAFLISAALC EGAVLPRSAK ELRCQCIKTY SKPFHPKFIK ELRVIESGPH 70 80 90 100 CANTEIIVKL SDGRELCLDP KENWVQRVVE KAEVPENRGM DS « Hide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Induction of mRNA for a serine protease and a beta-thromboglobulin-like protein in mitogen-stimulated human leukocytes." Schmid J., Weissmann C. J. Immunol. 139:250-256(1987) [PubMed: 2953813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Molecular cloning of a human monocyte-derived neutrophil chemotactic factor (MDNCF) and the induction of MDNCF mRNA by interleukin 1 and tumor necrosis factor." Matsushima K., Morishita K., Yoshimura T., Lavu S., Kobayashi Y., Lew W., Appella E., Kung H., Leonard E.J., Oppenheim J.J. J. Exp. Med. 167:1883-1893(1988) [PubMed: 3260265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Genomic structure of the human monocyte-derived neutrophil chemotactic factor IL-8." Mukaida N., Shiroo M., Matsushima K. J. Immunol. 143:1366-1371(1989) [PubMed: 2663993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Regulation of the mRNA for monocyte-derived neutrophil-activating peptide in differentiating HL60 promyelocytes." Kowalski J., Denhardt D.T. Mol. Cell. Biol. 9:1946-1957(1989) [PubMed: 2664463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Coding region structure of interleukin-8 gene of human lung giant cell carcinoma LU65C cells that produce LUCT/interleukin-8: homogeneity in interleukin-8 genes." Hotta K., Hayashi K., Ishikawa J., Tagawa M., Hashimoto K., Mizuno S., Suzuki K. Immunol. Lett. 24:165-169(1990) [PubMed: 2200751] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lung carcinoma.
[6]	Jang J.S., Kim B.E. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Peripheral blood leukocyte.
[7]	"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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Neutrophil.
[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] (ISOFORM 1).
[9]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[10]	SeattleSNPs variation discovery resource Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]	Mural R.J., Istrail S., Sutton G.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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"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] (ISOFORM 1). Tissue: Lung.
[13]	"cDNA cloning of human mesangial cell interleukin 8 by polymerase chain reaction." King C.H., Gordon G.S., Konieczkowski M., Sedor J.R. Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-97 (ISOFORM 1). Tissue: Kidney.
[14]	"Purification of granulocyte chemotactic peptide/interleukin-8 reveals N-terminal sequence heterogeneity similar to that of beta-thromboglobulin." van Damme J., van Beeumen J., Conings R., Decock B., Billiau A. Eur. J. Biochem. 181:337-344(1989) [PubMed: 2523801] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-41, IDENTIFICATION OF MDNCF-A; IL-8(1-77); IL-8(6-77); IL-8(7-77); IL-8(8-77) AND IL-8(9-77), PROTEOLYTIC PROCESSING OF N-TERMINAL.
[15]	"The neutrophil-activating proteins interleukin 8 and beta-thromboglobulin: in vitro and in vivo comparison of NH2-terminally processed forms." van Damme J., Rampart M., Coning R., Decock B., van Osselaer N., Willems J., Billiau A. Eur. J. Immunol. 20:2113-2118(1990) [PubMed: 2145175] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-41, IDENTIFICATION OF MDNCF-A; IL-8(1-77); IL-8(6-77); IL-8(7-77); IL-8(8-77) AND IL-8(9-77), PROTEOLYTIC PROCESSING OF N-TERMINAL, FUNCTION.
[16]	"Three forms of monocyte-derived neutrophil chemotactic factor (MDNCF) distinguished by different lengths of the amino-terminal sequence." Yoshimura T., Robinson E.A., Appella E., Matsushima K., Showalter S.D., Skeel A., Leonard E.J. Mol. Immunol. 26:87-93(1989) [PubMed: 2648135] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-32, IDENTIFICATION OF MDNCF-A; IL-8(1-77) AND IL-8(6-77), PROTEOLYTIC PROCESSING OF N-TERMINAL.
[17]	"Purification and partial primary sequence of a chemotactic protein for polymorphonuclear leukocytes derived from human lung giant cell carcinoma LU65C cells." Suzuki K., Miyasaka H., Ota H., Yamakawa Y., Tagawa M., Kuramoto A., Mizuno S. J. Exp. Med. 169:1895-1901(1989) [PubMed: 2659722] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-54, IDENTIFICATION OF IL-8(1-77).
[18]	"Biochemical and biological characterization of NAP-1/IL-8-related cytokines in lesional psoriatic scale." Schroeder J.-M. Adv. Exp. Med. Biol. 305:97-107(1991) [PubMed: 1755384] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-47. Tissue: Skin.
[19]	"Inflammatory cytokines induce synthesis and secretion of gro protein and a neutrophil chemotactic factor but not beta 2-microglobulin in human synovial cells and fibroblasts." Golds E.E., Mason P., Nyirkos P. Biochem. J. 259:585-588(1989) [PubMed: 2655583] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-46, IDENTIFICATION OF IL-8(1-77).
[20]	"Isolation and amino acid sequence of a chemotactic protein, LECT/interleukin 8, from a human myeloid leukemia cell line, ML-1." Suzuki K., Yamakawa Y., Matsuo Y., Kamiya T., Minowada J., Mizuno S. Immunol. Lett. 36:71-81(1993) [PubMed: 8344717] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-42. Tissue: Chronic myeloid leukemia cell.
[21]	"Structure determination of a human lymphocyte derived neutrophil activating peptide (LYNAP)." Gregory H., Young J., Schroeder J.-M., Mrowietz U., Christophers E. Biochem. Biophys. Res. Commun. 151:883-890(1988) [PubMed: 3279957] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-99, IDENTIFICATION OF IL-8(6-77).
[22]	"Purification of a human monocyte-derived neutrophil chemotactic factor that has peptide sequence similarity to other host defense cytokines." Yoshimura T., Matsushima K., Tanaka S., Robinson E.A., Appella E., Oppenheim J.J., Leonard E.J. Proc. Natl. Acad. Sci. U.S.A. 84:9233-9237(1987) [PubMed: 3480540] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-69, IDENTIFICATION OF IL-8(6-77).
[23]	"Purification and amino acid sequencing of NAF, a novel neutrophil-activating factor produced by monocytes." Walz A., Peveri P., Aschauer H., Baggiolini M. Biochem. Biophys. Res. Commun. 149:755-761(1987) [PubMed: 3322281] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-59, IDENTIFICATION OF IL-8(6-77).
[24]	"Endothelial and leukocyte forms of IL-8. Conversion by thrombin and interactions with neutrophils." Hebert C.A., Luscinskas F.W., Kiely J.-M., Luis E.A., Darbonne W.C., Bennett G.L., Liu C.C., Obin M.S., Gimbrone M.A. Jr., Baker J.B. J. Immunol. 145:3033-3040(1990) [PubMed: 2212672] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF N-TERMINAL BY THROMBIN, FUNCTION.
[25]	"Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil activating peptide." Clark-Lewis I., Mose B., Walz A., Baggiolini M., Scott G.J., Aebersold R. Biochemistry 30:3128-3135(1991) [PubMed: 2007144] [Abstract] Cited for: SYNTHESIS OF 28-99.
[26]	"Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact." Van den Steen P.E., Proost P., Wuyts A., Van Damme J., Opdenakker G. Blood 96:2673-2681(2000) [PubMed: 11023497] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF N-TERMINAL BY MMP9.
[27]	"Identification of biologically active chemokine isoforms from ascitic fluid and elevated levels of CCL18/pulmonary and activation-regulated chemokine in ovarian carcinoma." Schutyser E., Struyf S., Proost P., Opdenakker G., Laureys G., Verhasselt B., Peperstraete L., Van de Putte I., Saccani A., Allavena P., Mantovani A., Van Damme J. J. Biol. Chem. 277:24584-24593(2002) [PubMed: 11978786] [Abstract] Cited for: IDENTIFICATION OF IL-8(5-77) AND IL-8(6-77), FUNCTION, PROTEOLYTIC PROCESSING OF N-TERMINAL.
[28]	"Interleukin-8, a chemotactic and inflammatory cytokine." Baggiolini M., Clark-Lewis I. FEBS Lett. 307:97-101(1992) [PubMed: 1639201] [Abstract] Cited for: REVIEW.
[29]	"Regulation of the immune response by the interaction of chemokines and proteases." Struyf S., Proost P., Van Damme J. Adv. Immunol. 81:1-44(2003) [PubMed: 14711052] [Abstract] Cited for: REVIEW.
[30]	"Determination of the secondary structure of interleukin-8 by nuclear magnetic resonance spectroscopy." Clore G.M., Appella E., Yamada M., Matsushima K., Gronenborn A.M. J. Biol. Chem. 264:18907-18911(1989) [PubMed: 2681204] [Abstract] Cited for: STRUCTURE BY NMR OF 28-99.
[31]	"Three-dimensional structure of interleukin 8 in solution." Clore G.M., Appella E., Yamada M., Matsushima K., Gronenborn A.M. Biochemistry 29:1689-1696(1990) [PubMed: 2184886] [Abstract] Cited for: STRUCTURE BY NMR.
[32]	"Structure and activity of a chimeric interleukin-8-melanoma-growth-stimulatory-activity protein." Sticht H., Auer M., Schmitt B., Besemer J., Horcher M., Kirsch T., Lindley I.J., Rosch P. Eur. J. Biochem. 235:26-35(1996) [PubMed: 8631339] [Abstract] Cited for: STRUCTURE BY NMR OF 28-80.
[33]	"Structure of a CXC chemokine-receptor fragment in complex with interleukin-8." Skelton N.J., Quan C., Reilly D., Lowman H. Structure 7:157-168(1999) [PubMed: 10368283] [Abstract] Cited for: STRUCTURE BY NMR OF COMPLEX TO RECEPTOR.
[34]	"Crystallization of human interleukin-8. A protein chemotactic for neutrophils and T-lymphocytes." Baldwin E.T., Franklin K.A., Appella E., Yamada M., Matsushima K., Wlodawer A., Weber I.T. J. Biol. Chem. 265:6851-6853(1990) [PubMed: 2182630] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[35]	"Comparison of the solution nuclear magnetic resonance and crystal structures of interleukin-8. Possible implications for the mechanism of receptor binding." Clore G.M., Gronenborn A.M. J. Mol. Biol. 217:611-620(1991) [PubMed: 2005614] [Abstract] Cited for: STRUCTURE BY NMR, COMPARISON WITH X-RAY STRUCTURE.
[36]	"Crystal structure of interleukin 8: symbiosis of NMR and crystallography." Baldwin E.T., Weber I.T., St Charles R., Xuan J.C., Appella E., Yamada M., Matsushima K., Edwards B.F., Clore G.M., Gronenborn A.M. Proc. Natl. Acad. Sci. U.S.A. 88:502-506(1991) [PubMed: 1988949] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), STRUCTURE BY NMR.
[37]	"Receptor-binding conformation of the 'ELR' motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution." Gerber N., Lowman H., Artis D.R., Eigenbrot C. Proteins 38:361-367(2000) [PubMed: 10707023] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF MUTANT.
+	Additional computationally mapped references.

Wikipedia

Interleukin-8 entry

SeattleSNPs

EMBL
GenBank
DDBJ

M17017 mRNA. Translation: AAA35611.1.
Y00787 mRNA. Translation: CAA68742.1.
M28130 Genomic DNA. Translation: AAA59158.1.
M26383 mRNA. Translation: AAA36323.1.
D14283 Genomic DNA. Translation: BAA03245.1.
AF043337 mRNA. Translation: AAK00048.1.
AK311874 mRNA. Translation: BAG34815.1.
BT007067 mRNA. Translation: AAP35730.1.
CR542151 mRNA. Translation: CAG46948.1.
AF385628 Genomic DNA. Translation: AAK60276.1. Sequence problems.
CH471057 Genomic DNA. Translation: EAX05688.1.
BC013615 mRNA. Translation: AAH13615.1.
Z11686 mRNA. Translation: CAA77745.1.

IPI

IPI00215621.
IPI00288914.

PIR

A37034.

RefSeq

NP_000575.1. NM_000584.3.

UniGene

Hs.624.

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ICW	X-ray	2.01	A/B	28-99	[»]
1IKL	NMR	-	A	28-99	[»]
1IKM	NMR	-	A	28-99	[»]
1IL8	NMR	-	A/B	28-99	[»]
1ILP	NMR	-	A/B	28-99	[»]
1ILQ	NMR	-	A/B	28-99	[»]
1QE6	X-ray	2.35	A/B/C/D	28-99	[»]
1ROD	NMR	-	A/B	28-57	[»]
2IL8	NMR	-	A/B	28-99	[»]
3IL8	X-ray	2.00	A	28-99	[»]

ProteinModelPortal

P10145.

SMR

P10145. Positions 32-99.

ModBase

Search...

DIP

DIP-3778N.

IntAct

P10145. 4 interactions.

STRING

P10145.

DMDM

124359.

PRIDE

P10145.

DNASU

3576.

StructuralBiologyKnowledgebase

Search...

Ensembl

ENST00000307407; ENSP00000306512; ENSG00000169429.

GeneID

3576.

KEGG

hsa:3576.

UCSC

uc003hhe.3. human.

CTD

3576.

GeneCards

GC04P074595.

H-InvDB

HIX0004281.

HGNC

HGNC:6025. IL8.

MIM

146930. gene.

neXtProt

NX_P10145.

PharmGKB

PA29841.

GenAtlas

Search...

eggNOG

NOG73311.

GeneTree

ENSGT00530000062901.

HOVERGEN

HBG107789.

InParanoid

P10145.

K10030.

OMA

VCLDPKE.

OrthoDB

EOG428239.

PhylomeDB

P10145.

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
lysophospholipid_pathway. LPA receptor mediated events.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
syndecan_3_pathway. Syndecan-3-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.

ArrayExpress

P10145.

Bgee

P10145.

CleanEx

HS_IL8.

Genevestigator

P10145.

GermOnline

ENSG00000169429. Homo sapiens.

InterPro

IPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR002473. Chemokine_CXCL8/IL8.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]

PANTHER

PTHR10179. PTHR10179. 1 hit.

Pfam

PF00048. IL8. 1 hit.
[Graphical view]

PRINTS

PR00436. INTERLEUKIN8.
PR00437. SMALLCYTKCXC.

SMART

SM00199. SCY. 1 hit.
[Graphical view]

SUPFAM

SSF54117. Chemokine_IL8. 1 hit.

PROSITE

PS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]

ProtoNet

Search...

DrugBank

DB01009. Ketoprofen.
DB01001. Salbutamol.
DB00641. Simvastatin.
DB00744. Zileuton.

EvolutionaryTrace

P10145.

NextBio

13978.

PMAP-CutDB

P10145.

SOURCE

Search...

Entry name

IL8_HUMAN

Accession

Primary (citable) accession number: P10145
Secondary accession number(s): B2R4L8

Q9UCS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 18, 2012
This is version 149 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P10145-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P10145-2)

The sequence of this isoform differs from the canonical sequence as follows:
92-99: FLKRAENS → AEVPENRGMDS