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P10145 (IL8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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

Cleaved into the following 7 chains:

  1. MDNCF-a
    Alternative name(s):
    GCP/IL-8 protein IV
    IL8/NAP1 form I
  2. Interleukin-8
    Alternative name(s):
    (Ala-IL-8)77
    GCP/IL-8 protein II
    IL-8(1-77)
    IL8/NAP1 form II
    MDNCF-b
  3. IL-8(5-77)
  4. 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
  5. IL-8(7-77)
    Alternative name(s):
    GCP/IL-8 protein V
    IL8/NAP1 form IV
  6. IL-8(8-77)
    Alternative name(s):
    GCP/IL-8 protein VI
    IL8/NAP1 form V
  7. IL-8(9-77)
    Alternative name(s):
    GCP/IL-8 protein III
    IL8/NAP1 form VI
Gene names
Name:IL8
Synonyms:CXCL8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length99 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Induction

By ER stress in a DDIT3/CHOP-dependent manner. Ref.32

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.

Citrullination at Arg-27 prevents proteolysis, and dampens tissue inflammation, it also enhances leukocytosis, possibly through impaired chemokine clearance from the blood circulation.

Sequence similarities

Belongs to the intercrine alpha (chemokine CxC) family.

Ontologies

Keywords
   Biological processChemotaxis
Inflammatory response
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionCytokine
   PTMCitrullination
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-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 component movement

Traceable author statement PubMed 10820279. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

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

chemotaxis

Traceable author statement PubMed 12782716. Source: UniProtKB

embryonic digestive tract development

Inferred from expression pattern PubMed 20875417. Source: DFLAT

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

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

intracellular signal transduction

Inferred from direct assay PubMed 10734056. 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 single stranded viral RNA replication via double stranded DNA intermediate

Inferred from direct assay PubMed 11483765. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from direct assay Ref.32. Source: UniProtKB

response to molecule of bacterial origin

Inferred from direct assay PubMed 19912257. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 10820279. Source: ProtInc

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement PubMed 10823949. Source: ProtInc

   Molecular_functionchemokine activity

Traceable author statement PubMed 12782716. Source: UniProtKB

interleukin-8 receptor binding

Inferred from physical interaction PubMed 1840701. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CXCR2P250252EBI-3917999,EBI-2835281

Alternative products

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.14 Ref.15 Ref.16
Chain21 – 9979MDNCF-a
PRO_0000005126
Chain23 – 9977Interleukin-8
PRO_0000005127
Chain27 – 9973IL-8(5-77)
PRO_0000041948
Chain28 – 9972IL-8(6-77)
PRO_0000005128
Chain29 – 9971IL-8(7-77)
PRO_0000005129
Chain30 – 9970IL-8(8-77)
PRO_0000005130
Chain31 – 9969IL-8(9-77)
PRO_0000005131

Sites

Site27 – 282Cleavage; by thrombin Probable
Site28 – 292Cleavage; by MMP9

Amino acid modifications

Modified residue271Citrulline
Disulfide bond34 ↔ 61
Disulfide bond36 ↔ 77

Natural variations

Alternative sequence92 – 998FLKRAENS → AEVPENRGMDS in isoform 2.
VSP_001058

Experimental info

Sequence conflict531R → L AA sequence Ref.17

Secondary structure

................ 99
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 15C649996E89319F

FASTA9911,098
        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 »

FASTA10211,338

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. 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] (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. 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].
[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] [Europe PMC] [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] [Europe PMC] [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-TERMINUS.
[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] [Europe PMC] [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-TERMINUS, 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] [Europe PMC] [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-TERMINUS.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF N-TERMINUS 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF N-TERMINUS 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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF IL-8(5-77) AND IL-8(6-77), FUNCTION, PROTEOLYTIC PROCESSING OF N-TERMINUS.
[28]"Interleukin-8, a chemotactic and inflammatory cytokine."
Baggiolini M., Clark-Lewis I.
FEBS Lett. 307:97-101(1992) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: REVIEW.
[30]"Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation."
Proost P., Loos T., Mortier A., Schutyser E., Gouwy M., Noppen S., Dillen C., Ronsse I., Conings R., Struyf S., Opdenakker G., Maudgal P.C., Van Damme J.
J. Exp. Med. 205:2085-2097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION.
[31]"Citrullination of CXCL8 increases this chemokine's ability to mobilize neutrophils into the blood circulation."
Loos T., Opdenakker G., Van Damme J., Proost P.
Haematologica 94:1346-1353(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-27.
[32]"Endoplasmic reticulum stress-activated C/EBP homologous protein enhances nuclear factor-kappaB signals via repression of peroxisome proliferator-activated receptor gamma."
Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.
J. Biol. Chem. 285:35330-35339(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[33]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-99.
[34]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[35]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-80.
[36]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF COMPLEX TO RECEPTOR.
[37]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[38]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, COMPARISON WITH X-RAY STRUCTURE.
[39]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), STRUCTURE BY NMR.
[40]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF MUTANT.
+Additional computationally mapped references.

Web resources

Wikipedia

Interleukin-8 entry

SeattleSNPs

Cross-references

Sequence databases

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.
PIRA37034.
RefSeqNP_000575.1. NM_000584.3.
UniGeneHs.624.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ICWX-ray2.01A/B28-99[»]
1IKLNMR-A28-99[»]
1IKMNMR-A28-99[»]
1IL8NMR-A/B28-99[»]
1ILPNMR-A/B28-99[»]
1ILQNMR-A/B28-99[»]
1QE6X-ray2.35A/B/C/D28-99[»]
1RODNMR-A/B28-57[»]
2IL8NMR-A/B28-99[»]
3IL8X-ray2.00A28-99[»]
ProteinModelPortalP10145.
SMRP10145. Positions 32-99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109790. 14 interactions.
DIPDIP-3778N.
IntActP10145. 5 interactions.
MINTMINT-1516890.

Chemistry

BindingDBP10145.
ChEMBLCHEMBL2157.
DrugBankDB01009. Ketoprofen.
DB01001. Salbutamol.
DB00641. Simvastatin.
DB00744. Zileuton.

Polymorphism databases

DMDM124359.

Proteomic databases

PaxDbP10145.
PRIDEP10145.

Protocols and materials databases

DNASU3576.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307407; ENSP00000306512; ENSG00000169429. [P10145-1]
GeneID3576.
KEGGhsa:3576.
UCSCuc003hhe.3. human. [P10145-1]

Organism-specific databases

CTD3576.
GeneCardsGC04P074595.
HGNCHGNC:6025. IL8.
HPAHPA057179.
MIM146930. gene.
neXtProtNX_P10145.
PharmGKBPA29841.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG73311.
HOVERGENHBG107789.
InParanoidP10145.
KOK10030.
OMAVCLDPKE.
OrthoDBEOG7GTT6P.
PhylomeDBP10145.
TreeFamTF333433.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP10145.
BgeeP10145.
CleanExHS_IL8.
GenevestigatorP10145.

Family and domain databases

InterProIPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR001811. Chemokine_IL8-like_dom.
IPR028469. Interleukin-8.
[Graphical view]
PANTHERPTHR10179. PTHR10179. 1 hit.
PTHR10179:SF15. PTHR10179:SF15. 1 hit.
PfamPF00048. IL8. 1 hit.
[Graphical view]
PRINTSPR00437. SMALLCYTKCXC.
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
PROSITEPS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIL8. human.
EvolutionaryTraceP10145.
GeneWikiInterleukin_8.
GenomeRNAi3576.
NextBio13978.
PMAP-CutDBP10145.
PROP10145.
SOURCESearch...

Entry information

Entry nameIL8_HUMAN
AccessionPrimary (citable) accession number: P10145
Secondary accession number(s): B2R4L8 expand/collapse secondary AC list , Q6FGF6, Q6LAE6, Q96RG6, Q9C077, Q9UCE1, Q9UCR8, Q9UCR9, Q9UCS0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 170 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 chromosome 4

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