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P02775

- CXCL7_HUMAN

UniProt

P02775 - CXCL7_HUMAN

Protein

Platelet basic protein

Gene

PPBP

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

    LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation.4 Publications

    GO - Molecular functioni

    1. glucose transmembrane transporter activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell chemotaxis Source: GOC
    3. defense response to bacterium Source: UniProtKB-KW
    4. glucose transport Source: ProtInc
    5. immune response Source: InterPro
    6. platelet activation Source: Reactome
    7. platelet degranulation Source: Reactome
    8. positive regulation of cell division Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Cytokine, Growth factor, Mitogen

    Keywords - Biological processi

    Chemotaxis

    Enzyme and pathway databases

    ReactomeiREACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet basic protein
    Short name:
    PBP
    Alternative name(s):
    C-X-C motif chemokine 7
    Leukocyte-derived growth factor
    Short name:
    LDGF
    Macrophage-derived growth factor
    Short name:
    MDGF
    Small-inducible cytokine B7
    Cleaved into the following 10 chains:
    Alternative name(s):
    LA-PF4
    Low-affinity platelet factor IV
    Beta-thromboglobulin
    Short name:
    Beta-TG
    Gene namesi
    Name:PPBP
    Synonyms:CTAP3, CXCL7, SCYB7, TGB1, THBGB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:9240. PPBP.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB-KW
    3. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33561.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 34342 PublicationsAdd
    BLAST
    Chaini35 – 12894Platelet basic proteinPRO_0000005088Add
    BLAST
    Chaini44 – 12885Connective tissue-activating peptide IIIPRO_0000005089Add
    BLAST
    Chaini44 – 12683TC-2PRO_0000005090Add
    BLAST
    Chaini44 – 12481Connective tissue-activating peptide III(1-81)PRO_0000041949Add
    BLAST
    Chaini48 – 12881Beta-thromboglobulinPRO_0000005091Add
    BLAST
    Chaini55 – 12874Neutrophil-activating peptide 2(74)PRO_0000005092Add
    BLAST
    Chaini56 – 12873Neutrophil-activating peptide 2(73)PRO_0000005093Add
    BLAST
    Chaini59 – 12870Neutrophil-activating peptide 2PRO_0000005094Add
    BLAST
    Chaini59 – 12668TC-1PRO_0000005095Add
    BLAST
    Chaini59 – 12466Neutrophil-activating peptide 2(1-66)PRO_0000005096Add
    BLAST
    Chaini59 – 12163Neutrophil-activating peptide 2(1-63)PRO_0000041950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi63 ↔ 89
    Disulfide bondi65 ↔ 105

    Post-translational modificationi

    Proteolytic removal of residues 1-9 produces the active peptide connective tissue-activating peptide III (CTAP-III) (low-affinity platelet factor IV (LA-PF4)).
    Proteolytic removal of residues 1-13 produces the active peptide beta-thromboglobulin, which is released from platelets along with platelet factor 4 and platelet-derived growth factor.
    NAP-2(1-66) is produced by proteolytical processing, probably after secretion by leukocytes other than neutrophils.1 Publication
    NAP-2(73) and NAP-2(74) seem not be produced by proteolytical processing of secreted precursors but are released in an active form from platelets.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond

    Proteomic databases

    PaxDbiP02775.
    PeptideAtlasiP02775.
    PRIDEiP02775.

    2D gel databases

    SWISS-2DPAGEP02775.

    PTM databases

    PhosphoSiteiP02775.

    Miscellaneous databases

    PMAP-CutDBP02775.

    Expressioni

    Gene expression databases

    ArrayExpressiP02775.
    BgeeiP02775.
    CleanExiHS_PPBP.
    GenevestigatoriP02775.

    Organism-specific databases

    HPAiCAB017624.
    HPA008354.

    Interactioni

    Subunit structurei

    Beta-thromboglobulin is a homotetramer.

    Protein-protein interaction databases

    BioGridi111469. 16 interactions.
    DIPiDIP-5913N.
    IntActiP02775. 20 interactions.
    MINTiMINT-1393871.
    STRINGi9606.ENSP00000296028.

    Structurei

    Secondary structure

    1
    128
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 545
    Helixi58 – 603
    Helixi74 – 763
    Beta strandi77 – 837
    Beta strandi89 – 913
    Beta strandi93 – 986
    Beta strandi103 – 1064
    Helixi111 – 12212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F9PX-ray1.93A44-128[»]
    1NAPX-ray1.90A/B/C/D59-128[»]
    1TVXX-ray1.75A/B/C/D54-128[»]
    ProteinModelPortaliP02775.
    SMRiP02775. Positions 44-124.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02775.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG39945.
    HOGENOMiHOG000220915.
    HOVERGENiHBG107789.
    InParanoidiP02775.
    KOiK10029.
    OMAiLYAELRC.
    OrthoDBiEOG7W156N.
    PhylomeDBiP02775.
    TreeFamiTF333433.

    Family and domain databases

    InterProiIPR001089. Chemokine_CXC.
    IPR018048. Chemokine_CXC_CS.
    IPR001811. Chemokine_IL8-like_dom.
    [Graphical view]
    PANTHERiPTHR10179. PTHR10179. 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.

    P02775-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLRLDTTPS CNSARPLHAL QVLLLLSLLL TALASSTKGQ TKRNLAKGKE    50
    ESLDSDLYAE LRCMCIKTTS GIHPKNIQSL EVIGKGTHCN QVEVIATLKD 100
    GRKICLDPDA PRIKKIVQKK LAGDESAD 128
    Length:128
    Mass (Da):13,894
    Last modified:November 1, 1991 - v3
    Checksum:iBEAB7B75916723D9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M54995 mRNA. Translation: AAA62836.1.
    AF349466 Genomic DNA. Translation: AAK29642.1.
    CR456805 mRNA. Translation: CAG33086.1.
    AC097709 Genomic DNA. Translation: AAY41004.1.
    AK312166 mRNA. Translation: BAG35100.1.
    CH471057 Genomic DNA. Translation: EAX05695.1.
    BC028217 mRNA. Translation: AAH28217.1.
    CCDSiCCDS3563.1.
    PIRiA39546. TGHU.
    RefSeqiNP_002695.1. NM_002704.3.
    UniGeneiHs.2164.

    Genome annotation databases

    EnsembliENST00000296028; ENSP00000296028; ENSG00000163736.
    GeneIDi5473.
    KEGGihsa:5473.
    UCSCiuc003hhj.3. human.

    Polymorphism databases

    DMDMi129874.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    CXCL7 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M54995 mRNA. Translation: AAA62836.1 .
    AF349466 Genomic DNA. Translation: AAK29642.1 .
    CR456805 mRNA. Translation: CAG33086.1 .
    AC097709 Genomic DNA. Translation: AAY41004.1 .
    AK312166 mRNA. Translation: BAG35100.1 .
    CH471057 Genomic DNA. Translation: EAX05695.1 .
    BC028217 mRNA. Translation: AAH28217.1 .
    CCDSi CCDS3563.1.
    PIRi A39546. TGHU.
    RefSeqi NP_002695.1. NM_002704.3.
    UniGenei Hs.2164.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F9P X-ray 1.93 A 44-128 [» ]
    1NAP X-ray 1.90 A/B/C/D 59-128 [» ]
    1TVX X-ray 1.75 A/B/C/D 54-128 [» ]
    ProteinModelPortali P02775.
    SMRi P02775. Positions 44-124.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111469. 16 interactions.
    DIPi DIP-5913N.
    IntActi P02775. 20 interactions.
    MINTi MINT-1393871.
    STRINGi 9606.ENSP00000296028.

    PTM databases

    PhosphoSitei P02775.

    Polymorphism databases

    DMDMi 129874.

    2D gel databases

    SWISS-2DPAGE P02775.

    Proteomic databases

    PaxDbi P02775.
    PeptideAtlasi P02775.
    PRIDEi P02775.

    Protocols and materials databases

    DNASUi 5473.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296028 ; ENSP00000296028 ; ENSG00000163736 .
    GeneIDi 5473.
    KEGGi hsa:5473.
    UCSCi uc003hhj.3. human.

    Organism-specific databases

    CTDi 5473.
    GeneCardsi GC04M074841.
    H-InvDB HIX0031528.
    HGNCi HGNC:9240. PPBP.
    HPAi CAB017624.
    HPA008354.
    MIMi 121010. gene.
    neXtProti NX_P02775.
    PharmGKBi PA33561.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39945.
    HOGENOMi HOG000220915.
    HOVERGENi HBG107789.
    InParanoidi P02775.
    KOi K10029.
    OMAi LYAELRC.
    OrthoDBi EOG7W156N.
    PhylomeDBi P02775.
    TreeFami TF333433.

    Enzyme and pathway databases

    Reactomei REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P02775.
    GeneWikii CXCL7.
    GenomeRNAii 5473.
    NextBioi 21188.
    PMAP-CutDB P02775.
    PROi P02775.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02775.
    Bgeei P02775.
    CleanExi HS_PPBP.
    Genevestigatori P02775.

    Family and domain databases

    InterProi IPR001089. Chemokine_CXC.
    IPR018048. Chemokine_CXC_CS.
    IPR001811. Chemokine_IL8-like_dom.
    [Graphical view ]
    PANTHERi PTHR10179. PTHR10179. 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. "Cloning of cDNA coding for connective tissue activating peptide III from a human platelet-derived lambda gt11 expression library."
      Wenger R.H., Wicki A.N., Walz A., Kieffer N., Clemetson K.J.
      Blood 73:1498-1503(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Platelet.
    2. "Characterization of the human beta-thromboglobulin gene. Comparison with the gene for platelet factor 4."
      Majumdar S., Gonder D., Koutsis B., Poncz M.
      J. Biol. Chem. 266:5785-5789(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Localization of distal regulatory domains in the megakaryocyte-specific platelet basic protein/platelet factor 4 gene locus."
      Zhang C., Thornton M.A., Kowalska M.A., Sachis B.S., Feldman M., Poncz M., McKenzie S.E., Reilly M.P.
      Blood 98:610-617(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
      Tissue: Umbilical cord blood.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Leukocyte.
    9. "Characterization of human platelet basic protein, a precursor form of low-affinity platelet factor 4 and beta-thromboglobulin."
      Holt J.C., Harris M.E., Holt A.M., Lange E., Henschen A., Niewiarowski S.
      Biochemistry 25:1988-1996(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 35-53.
    10. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 35-49.
    11. "Thrombocidins, microbicidal proteins from human blood platelets, are C-terminal deletion products of CXC chemokines."
      Krijgsveld J., Zaat S.A., Meeldijk J., van Veelen P.A., Fang G., Poolman B., Brandt E., Ehlert J.E., Kuijpers A.J., Engbers G.H., Feijen J., Dankert J.
      J. Biol. Chem. 275:20374-20381(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-126, IDENTIFICATION OF TC-1 AND TC-2, FUNCTION.
    12. "Structural and biological characteristics of connective tissue activating peptide (CTAP-III), a major human platelet-derived growth factor."
      Castor C.W., Miller J.W., Walz D.A.
      Proc. Natl. Acad. Sci. U.S.A. 80:765-769(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-66 AND 125-128.
    13. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-62.
      Tissue: Platelet.
    14. "Complete covalent structure of human beta-thromboglobulin."
      Begg G.S., Pepper D.S., Chesterman C.N., Morgan F.J.
      Biochemistry 17:1739-1744(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 48-126.
    15. "Thrombin-activated human platelets release two NAP-2 variants that stimulate polymorphonuclear leukocytes."
      Piccardoni P., Evangelista V., Piccoli A., de Gaetano G., Walz A., Cerletti C.
      Thromb. Haemost. 76:780-785(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 55-128, IDENTIFICATION OF NAP-2(73) AND NAP-2(74), FUNCTION.
      Tissue: Platelet.
    16. "Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets."
      Castor C.W., Walz D.A., Ragsdale C.G., Hossler P.A., Smith E.M., Bignall M.C., Aaron B.P., Mountjoy K.
      Biochem. Biophys. Res. Commun. 163:1071-1078(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 57-68.
    17. "A novel cleavage product of beta-thromboglobulin formed in cultures of stimulated mononuclear cells activates human neutrophils."
      Walz A., Baggiolini M.
      Biochem. Biophys. Res. Commun. 159:969-975(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 59-126.
    18. "Limited and defined truncation at the C-terminus enhances receptor binding and degranulation activity of the neutrophil-activating peptide 2 (NAP-2). Comparison of native and recombinant NAP-2 variants."
      Ehlert J.E., Petersen F., Kubbutat M.H., Gerdes J., Flad H.D., Brandt E.
      J. Biol. Chem. 270:6338-6344(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 59-124, IDENTIFICATION OF NAP-2(1-66), FUNCTION.
      Tissue: Peripheral blood monocyte.
    19. "Generation of the neutrophil-activating peptide NAP-2 from platelet basic protein or connective tissue-activating peptide III through monocyte proteases."
      Walz A., Baggiolini M.
      J. Exp. Med. 171:449-454(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 59-67.
    20. "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 59-126.
    21. "Novel C-terminally truncated isoforms of the CXC chemokine beta-thromboglobulin and their impact on neutrophil functions."
      Ehlert J.E., Gerdes J., Flad H.-D., Brandt E.
      J. Immunol. 161:4975-4982(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF CTAP-III(1-81) AND NAP-2(1-63), FUNCTION, PROTEOLYTIC PROCESSING OF C-TERMINAL.
    22. "Purification, crystallization and preliminary X-ray diffraction analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-2)."
      Kungl A.J., Machius M., Huber R., Schwer C., Lam C., Aschauer H., Ehn G., Lindley I.J.D., Auer M.
      FEBS Lett. 347:300-303(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 59-128.
    23. "The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution."
      Malkowski M.G., Wu J.Y., Lazar J.B., Johnson P.H., Edwards B.F.P.
      J. Biol. Chem. 270:7077-7087(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 59-128.

    Entry informationi

    Entry nameiCXCL7_HUMAN
    AccessioniPrimary (citable) accession number: P02775
    Secondary accession number(s): B2R5F3, Q6IBJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 163 of the entry and version 3 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