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Protein

Interleukin-8

Gene

CXCL8

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

Functioni

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.3 Publications

GO - Molecular functioni

  • chemokine activity Source: UniProtKB
  • interleukin-8 receptor binding Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • calcium-mediated signaling Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • cellular response to fibroblast growth factor stimulus Source: UniProtKB
  • cellular response to interleukin-1 Source: UniProtKB
  • cellular response to lipopolysaccharide Source: BHF-UCL
  • cellular response to tumor necrosis factor Source: UniProtKB
  • chemokine-mediated signaling pathway Source: GO_Central
  • chemotaxis Source: UniProtKB
  • embryonic digestive tract development Source: DFLAT
  • G-protein coupled receptor signaling pathway Source: ProtInc
  • immune response Source: GO_Central
  • induction of positive chemotaxis Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • movement of cell or subcellular component Source: ProtInc
  • negative regulation of cell proliferation Source: ProtInc
  • negative regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  • neutrophil activation Source: UniProtKB
  • neutrophil chemotaxis Source: UniProtKB
  • PERK-mediated unfolded protein response Source: Reactome
  • positive regulation of angiogenesis Source: CACAO
  • positive regulation of neutrophil chemotaxis Source: BHF-UCL
  • receptor internalization Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • regulation of entry of bacterium into host cell Source: AgBase
  • regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
  • response to molecule of bacterial origin Source: BHF-UCL
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Chemotaxis, Inflammatory response

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169429-MONOMER.
ReactomeiR-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-380108. Chemokine receptors bind chemokines.
R-HSA-380994. ATF4 activates genes.
R-HSA-418594. G alpha (i) signalling events.
SIGNORiP10145.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-8
Short name:
IL-8
Alternative name(s):
C-X-C motif chemokine 8
Chemokine (C-X-C motif) ligand 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:
Alternative name(s):
GCP/IL-8 protein IV
IL8/NAP1 form I
Alternative name(s):
(Ala-IL-8)77
GCP/IL-8 protein II
IL-8(1-77)
IL8/NAP1 form II
MDNCF-b
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
Alternative name(s):
GCP/IL-8 protein V
IL8/NAP1 form IV
Alternative name(s):
GCP/IL-8 protein VI
IL8/NAP1 form V
Alternative name(s):
GCP/IL-8 protein III
IL8/NAP1 form VI
Gene namesi
Name:CXCL8
Synonyms:IL8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:6025. CXCL8.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi3576.
OpenTargetsiENSG00000169429.
PharmGKBiPA29841.

Chemistry databases

ChEMBLiCHEMBL2157.

Polymorphism and mutation databases

BioMutaiIL8.
DMDMi124359.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 203 PublicationsAdd BLAST20
ChainiPRO_000000512621 – 99MDNCF-aAdd BLAST79
ChainiPRO_000000512723 – 99Interleukin-8Add BLAST77
ChainiPRO_000004194827 – 99IL-8(5-77)Add BLAST73
ChainiPRO_000000512828 – 99IL-8(6-77)Add BLAST72
ChainiPRO_000000512929 – 99IL-8(7-77)Add BLAST71
ChainiPRO_000000513030 – 99IL-8(8-77)Add BLAST70
ChainiPRO_000000513131 – 99IL-8(9-77)Add BLAST69

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27Citrulline2 Publications1
Disulfide bondi34 ↔ 61
Disulfide bondi36 ↔ 77

Post-translational modificationi

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.6 Publications
Citrullination at Arg-27 prevents proteolysis, and dampens tissue inflammation, it also enhances leukocytosis, possibly through impaired chemokine clearance from the blood circulation.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei27 – 28Cleavage; by thrombinCurated2
Sitei28 – 29Cleavage; by MMP92

Keywords - PTMi

Citrullination, Disulfide bond

Proteomic databases

PaxDbiP10145.
PeptideAtlasiP10145.
PRIDEiP10145.

Miscellaneous databases

PMAP-CutDBP10145.

Expressioni

Inductioni

By ER stress in a DDIT3/CHOP-dependent manner.1 Publication

Gene expression databases

BgeeiENSG00000169429.
CleanExiHS_IL8.
ExpressionAtlasiP10145. baseline and differential.
GenevisibleiP10145. HS.

Organism-specific databases

HPAiHPA057179.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
ahcYP9WGV33EBI-3917999,EBI-11740468From a different organism.
CXCR2P250252EBI-3917999,EBI-2835281
glmUP9WMN33EBI-3917999,EBI-11740532From a different organism.
Rv0296cQ6MX513EBI-3917999,EBI-11740572From a different organism.
TNFAIP6P9806615EBI-3917999,EBI-11700693

GO - Molecular functioni

  • chemokine activity Source: UniProtKB
  • interleukin-8 receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109790. 11 interactors.
DIPiDIP-3778N.
IntActiP10145. 10 interactors.
MINTiMINT-1516890.
STRINGi9606.ENSP00000306512.

Chemistry databases

BindingDBiP10145.

Structurei

Secondary structure

199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 42Combined sources6
Helixi46 – 48Combined sources3
Beta strandi49 – 55Combined sources7
Beta strandi58 – 60Combined sources3
Beta strandi61 – 63Combined sources3
Beta strandi65 – 70Combined sources6
Turni71 – 73Combined sources3
Beta strandi75 – 78Combined sources4
Helixi83 – 97Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/B28-80[»]
2IL8NMR-A/B28-99[»]
3IL8X-ray2.00A28-99[»]
4XDXX-ray0.95A30-99[»]
5D14X-ray1.00A30-99[»]
ProteinModelPortaliP10145.
SMRiP10145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10145.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J24U. Eukaryota.
ENOG410Z1BP. LUCA.
GeneTreeiENSGT00530000062901.
HOVERGENiHBG107789.
InParanoidiP10145.
KOiK10030.
OMAiWVQKVVE.
OrthoDBiEOG091G13J8.
PhylomeDBiP10145.
TreeFamiTF333433.

Family and domain databases

CDDicd00273. Chemokine_CXC. 1 hit.
InterProiIPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR001811. Chemokine_IL8-like_dom.
IPR033899. CXC_Chemokine_domain.
IPR028469. Interleukin-8.
[Graphical view]
PANTHERiPTHR10179. PTHR10179. 1 hit.
PTHR10179:SF15. PTHR10179:SF15. 1 hit.
PfamiPF00048. IL8. 1 hit.
[Graphical view]
PRINTSiPR00437. SMALLCYTKCXC.
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSKLAVALL AAFLISAALC EGAVLPRSAK ELRCQCIKTY SKPFHPKFIK
60 70 80 90
ELRVIESGPH CANTEIIVKL SDGRELCLDP KENWVQRVVE KFLKRAENS
Length:99
Mass (Da):11,098
Last modified:July 1, 1989 - v1
Checksum:i15C649996E89319F
GO

Sequence cautioni

The sequence AAK00048 differs from that shown. Chimeric cDNA.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53R → L AA sequence (PubMed:2659722).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BT007067 mRNA. Translation: AAP35730.1.
AK311874 mRNA. Translation: BAG34815.1.
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.
AF043337 mRNA. Translation: AAK00048.1. Sequence problems.
CCDSiCCDS34005.1.
PIRiA37034.
RefSeqiNP_000575.1. NM_000584.3.
UniGeneiHs.624.

Genome annotation databases

EnsembliENST00000307407; ENSP00000306512; ENSG00000169429.
GeneIDi3576.
KEGGihsa:3576.
UCSCiuc003hhe.3. human.

Cross-referencesi

Web resourcesi

Wikipedia

Interleukin-8 entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BT007067 mRNA. Translation: AAP35730.1.
AK311874 mRNA. Translation: BAG34815.1.
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.
AF043337 mRNA. Translation: AAK00048.1. Sequence problems.
CCDSiCCDS34005.1.
PIRiA37034.
RefSeqiNP_000575.1. NM_000584.3.
UniGeneiHs.624.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/B28-80[»]
2IL8NMR-A/B28-99[»]
3IL8X-ray2.00A28-99[»]
4XDXX-ray0.95A30-99[»]
5D14X-ray1.00A30-99[»]
ProteinModelPortaliP10145.
SMRiP10145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109790. 11 interactors.
DIPiDIP-3778N.
IntActiP10145. 10 interactors.
MINTiMINT-1516890.
STRINGi9606.ENSP00000306512.

Chemistry databases

BindingDBiP10145.
ChEMBLiCHEMBL2157.

Polymorphism and mutation databases

BioMutaiIL8.
DMDMi124359.

Proteomic databases

PaxDbiP10145.
PeptideAtlasiP10145.
PRIDEiP10145.

Protocols and materials databases

DNASUi3576.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307407; ENSP00000306512; ENSG00000169429.
GeneIDi3576.
KEGGihsa:3576.
UCSCiuc003hhe.3. human.

Organism-specific databases

CTDi3576.
DisGeNETi3576.
GeneCardsiCXCL8.
HGNCiHGNC:6025. CXCL8.
HPAiHPA057179.
MIMi146930. gene.
neXtProtiNX_P10145.
OpenTargetsiENSG00000169429.
PharmGKBiPA29841.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J24U. Eukaryota.
ENOG410Z1BP. LUCA.
GeneTreeiENSGT00530000062901.
HOVERGENiHBG107789.
InParanoidiP10145.
KOiK10030.
OMAiWVQKVVE.
OrthoDBiEOG091G13J8.
PhylomeDBiP10145.
TreeFamiTF333433.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169429-MONOMER.
ReactomeiR-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-380108. Chemokine receptors bind chemokines.
R-HSA-380994. ATF4 activates genes.
R-HSA-418594. G alpha (i) signalling events.
SIGNORiP10145.

Miscellaneous databases

EvolutionaryTraceiP10145.
GeneWikiiInterleukin_8.
GenomeRNAii3576.
PMAP-CutDBP10145.
PROiP10145.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169429.
CleanExiHS_IL8.
ExpressionAtlasiP10145. baseline and differential.
GenevisibleiP10145. HS.

Family and domain databases

CDDicd00273. Chemokine_CXC. 1 hit.
InterProiIPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR001811. Chemokine_IL8-like_dom.
IPR033899. CXC_Chemokine_domain.
IPR028469. Interleukin-8.
[Graphical view]
PANTHERiPTHR10179. PTHR10179. 1 hit.
PTHR10179:SF15. PTHR10179:SF15. 1 hit.
PfamiPF00048. IL8. 1 hit.
[Graphical view]
PRINTSiPR00437. SMALLCYTKCXC.
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIL8_HUMAN
AccessioniPrimary (citable) accession number: P10145
Secondary accession number(s): B2R4L8
, Q6FGF6, Q6LAE6, Q96RG6, Q9C077, Q9UCE1, Q9UCR8, Q9UCR9, Q9UCS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 199 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.