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P10145

- IL8_HUMAN

UniProt

P10145 - IL8_HUMAN

Protein

Interleukin-8

Gene

CXCL8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei27 – 282Cleavage; by thrombinCurated
    Sitei28 – 292Cleavage; by MMP9

    GO - Molecular functioni

    1. chemokine activity Source: UniProtKB
    2. interleukin-8 receptor binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. angiogenesis Source: UniProtKB
    3. calcium-mediated signaling Source: UniProtKB
    4. cell cycle arrest Source: UniProtKB
    5. cellular component movement Source: ProtInc
    6. cellular protein metabolic process Source: Reactome
    7. cellular response to fibroblast growth factor stimulus Source: UniProtKB
    8. cellular response to interleukin-1 Source: UniProtKB
    9. cellular response to lipopolysaccharide Source: BHF-UCL
    10. cellular response to tumor necrosis factor Source: UniProtKB
    11. chemotaxis Source: UniProtKB
    12. embryonic digestive tract development Source: DFLAT
    13. endoplasmic reticulum unfolded protein response Source: Reactome
    14. G-protein coupled receptor signaling pathway Source: ProtInc
    15. immune response Source: InterPro
    16. induction of positive chemotaxis Source: UniProtKB
    17. inflammatory response Source: UniProtKB
    18. intracellular signal transduction Source: UniProtKB
    19. negative regulation of cell proliferation Source: ProtInc
    20. negative regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    21. neutrophil activation Source: UniProtKB
    22. neutrophil chemotaxis Source: UniProtKB
    23. positive regulation of neutrophil chemotaxis Source: BHF-UCL
    24. receptor internalization Source: UniProtKB
    25. regulation of cell adhesion Source: UniProtKB
    26. regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
    27. response to endoplasmic reticulum stress Source: UniProtKB
    28. response to molecule of bacterial origin Source: BHF-UCL
    29. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Cytokine

    Keywords - Biological processi

    Chemotaxis, Inflammatory response

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_15344. Chemokine receptors bind chemokines.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_18355. ATF4 activates genes.
    REACT_19231. G alpha (i) signalling events.

    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
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:6025. CXCL8.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29841.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20203 PublicationsAdd
    BLAST
    Chaini21 – 9979MDNCF-aPRO_0000005126Add
    BLAST
    Chaini23 – 9977Interleukin-8PRO_0000005127Add
    BLAST
    Chaini27 – 9973IL-8(5-77)PRO_0000041948Add
    BLAST
    Chaini28 – 9972IL-8(6-77)PRO_0000005128Add
    BLAST
    Chaini29 – 9971IL-8(7-77)PRO_0000005129Add
    BLAST
    Chaini30 – 9970IL-8(8-77)PRO_0000005130Add
    BLAST
    Chaini31 – 9969IL-8(9-77)PRO_0000005131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Citrulline2 Publications
    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

    Keywords - PTMi

    Citrullination, Disulfide bond

    Proteomic databases

    PaxDbiP10145.
    PRIDEiP10145.

    Miscellaneous databases

    PMAP-CutDBP10145.

    Expressioni

    Inductioni

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

    Gene expression databases

    ArrayExpressiP10145.
    BgeeiP10145.
    CleanExiHS_IL8.
    GenevestigatoriP10145.

    Organism-specific databases

    HPAiHPA057179.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CXCR2P250252EBI-3917999,EBI-2835281

    Protein-protein interaction databases

    BioGridi109790. 14 interactions.
    DIPiDIP-3778N.
    IntActiP10145. 5 interactions.
    MINTiMINT-1516890.

    Structurei

    Secondary structure

    1
    99
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 426
    Helixi46 – 483
    Beta strandi49 – 557
    Beta strandi58 – 603
    Beta strandi61 – 633
    Beta strandi65 – 706
    Turni71 – 733
    Beta strandi75 – 784
    Helixi83 – 9715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP10145.
    SMRiP10145. Positions 32-99.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10145.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG73311.
    HOVERGENiHBG107789.
    InParanoidiP10145.
    KOiK10030.
    OMAiPFHPKYI.
    OrthoDBiEOG7GTT6P.
    PhylomeDBiP10145.
    TreeFamiTF333433.

    Family and domain databases

    InterProiIPR001089. Chemokine_CXC.
    IPR018048. Chemokine_CXC_CS.
    IPR001811. Chemokine_IL8-like_dom.
    IPR028469. Interleukin-8.
    [Graphical view]
    PANTHERiPTHR10179. PTHR10179. 1 hit.
    PTHR10179:SF35. PTHR10179:SF35. 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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P10145-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTSKLAVALL AAFLISAALC EGAVLPRSAK ELRCQCIKTY SKPFHPKFIK   50
    ELRVIESGPH CANTEIIVKL SDGRELCLDP KENWVQRVVE KFLKRAENS 99
    Length:99
    Mass (Da):11,098
    Last modified:July 1, 1989 - v1
    Checksum:i15C649996E89319F
    GO
    Isoform 2 (identifier: P10145-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:102
    Mass (Da):11,338
    Checksum:iE184B7B31606CFAD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531R → L AA sequence (PubMed:2659722)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei92 – 998FLKRAENS → AEVPENRGMDS in isoform 2. 1 PublicationVSP_001058

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    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.
    CCDSiCCDS34005.1. [P10145-1]
    PIRiA37034.
    RefSeqiNP_000575.1. NM_000584.3. [P10145-1]
    UniGeneiHs.624.

    Genome annotation databases

    EnsembliENST00000307407; ENSP00000306512; ENSG00000169429. [P10145-1]
    GeneIDi3576.
    KEGGihsa:3576.
    UCSCiuc003hhe.3. human. [P10145-1]

    Polymorphism databases

    DMDMi124359.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Interleukin-8 entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    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 .
    CCDSi CCDS34005.1. [P10145-1 ]
    PIRi A37034.
    RefSeqi NP_000575.1. NM_000584.3. [P10145-1 ]
    UniGenei Hs.624.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 28-80 [» ]
    2IL8 NMR - A/B 28-99 [» ]
    3IL8 X-ray 2.00 A 28-99 [» ]
    ProteinModelPortali P10145.
    SMRi P10145. Positions 32-99.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109790. 14 interactions.
    DIPi DIP-3778N.
    IntActi P10145. 5 interactions.
    MINTi MINT-1516890.

    Chemistry

    BindingDBi P10145.
    ChEMBLi CHEMBL2157.
    DrugBanki DB01009. Ketoprofen.
    DB01001. Salbutamol.
    DB00641. Simvastatin.
    DB00744. Zileuton.

    Polymorphism databases

    DMDMi 124359.

    Proteomic databases

    PaxDbi P10145.
    PRIDEi P10145.

    Protocols and materials databases

    DNASUi 3576.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307407 ; ENSP00000306512 ; ENSG00000169429 . [P10145-1 ]
    GeneIDi 3576.
    KEGGi hsa:3576.
    UCSCi uc003hhe.3. human. [P10145-1 ]

    Organism-specific databases

    CTDi 3576.
    GeneCardsi GC04P074595.
    HGNCi HGNC:6025. CXCL8.
    HPAi HPA057179.
    MIMi 146930. gene.
    neXtProti NX_P10145.
    PharmGKBi PA29841.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG73311.
    HOVERGENi HBG107789.
    InParanoidi P10145.
    KOi K10030.
    OMAi PFHPKYI.
    OrthoDBi EOG7GTT6P.
    PhylomeDBi P10145.
    TreeFami TF333433.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_15344. Chemokine receptors bind chemokines.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_18355. ATF4 activates genes.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    ChiTaRSi IL8. human.
    EvolutionaryTracei P10145.
    GeneWikii Interleukin_8.
    GenomeRNAii 3576.
    NextBioi 13978.
    PMAP-CutDB P10145.
    PROi P10145.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10145.
    Bgeei P10145.
    CleanExi HS_IL8.
    Genevestigatori P10145.

    Family and domain databases

    InterProi IPR001089. Chemokine_CXC.
    IPR018048. Chemokine_CXC_CS.
    IPR001811. Chemokine_IL8-like_dom.
    IPR028469. Interleukin-8.
    [Graphical view ]
    PANTHERi PTHR10179. PTHR10179. 1 hit.
    PTHR10179:SF35. PTHR10179:SF35. 1 hit.
    Pfami PF00048. IL8. 1 hit.
    [Graphical view ]
    PRINTSi PR00437. SMALLCYTKCXC.
    SMARTi SM00199. SCY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54117. SSF54117. 1 hit.
    PROSITEi PS00471. SMALL_CYTOKINES_CXC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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 AT ARG-27.
    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. 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.

    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: October 1, 2014
    This is version 175 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

    External Data

    Dasty 3