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P02776

- PLF4_HUMAN

UniProt

P02776 - PLF4_HUMAN

Protein

Platelet factor 4

Gene

PF4

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

    Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.1 Publication

    GO - Molecular functioni

    1. chemokine activity Source: UniProtKB
    2. CXCR3 chemokine receptor binding Source: UniProtKB
    3. heparin binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cytokine-mediated signaling pathway Source: UniProtKB
    3. immune response Source: InterPro
    4. leukocyte chemotaxis Source: UniProtKB
    5. negative regulation of angiogenesis Source: UniProtKB
    6. negative regulation of cytolysis Source: BHF-UCL
    7. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
    8. negative regulation of megakaryocyte differentiation Source: UniProtKB
    9. negative regulation of MHC class II biosynthetic process Source: BHF-UCL
    10. platelet activation Source: UniProtKB
    11. platelet degranulation Source: Reactome
    12. positive regulation of cAMP-mediated signaling Source: UniProtKB
    13. positive regulation of cAMP metabolic process Source: UniProtKB
    14. positive regulation of gene expression Source: BHF-UCL
    15. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    16. positive regulation of macrophage differentiation Source: BHF-UCL
    17. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    18. positive regulation of tumor necrosis factor production Source: BHF-UCL
    19. regulation of cell proliferation Source: UniProtKB

    Keywords - Molecular functioni

    Cytokine

    Keywords - Biological processi

    Chemotaxis

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
    REACT_1439. Common Pathway.
    REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet factor 4
    Short name:
    PF-4
    Alternative name(s):
    C-X-C motif chemokine 4
    Iroplact
    Oncostatin-A
    Cleaved into the following chain:
    Gene namesi
    Name:PF4
    Synonyms:CXCL4, SCYB4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:8861. PF4.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33203.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 31315 PublicationsAdd
    BLAST
    Chaini32 – 10170Platelet factor 4PRO_0000005068Add
    BLAST
    Chaini48 – 10154Platelet factor 4, short formPRO_0000351217Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 671 Publication
    Disulfide bondi43 ↔ 831 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP02776.
    PeptideAtlasiP02776.
    PRIDEiP02776.

    2D gel databases

    OGPiP02776.

    Miscellaneous databases

    PMAP-CutDBP02776.

    Expressioni

    Gene expression databases

    BgeeiP02776.
    CleanExiHS_PF4.
    GenevestigatoriP02776.

    Organism-specific databases

    HPAiCAB026008.
    HPA052485.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi111219. 7 interactions.
    IntActiP02776. 2 interactions.
    STRINGi9606.ENSP00000296029.

    Structurei

    Secondary structure

    1
    101
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 443
    Helixi52 – 543
    Beta strandi55 – 617
    Beta strandi64 – 663
    Beta strandi67 – 693
    Beta strandi71 – 766
    Beta strandi77 – 793
    Beta strandi81 – 833
    Beta strandi86 – 883
    Helixi90 – 9910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DN3NMR-A59-73[»]
    1F9QX-ray2.00A/B/C/D32-101[»]
    1F9RX-ray2.00A/B/C/D32-101[»]
    1F9SX-ray2.38A/B/C/D32-101[»]
    1PFMNMR-A/B/C/D39-101[»]
    1PFNNMR-A/B/C/D39-101[»]
    1RHPX-ray2.40A/B/C/D32-101[»]
    ProteinModelPortaliP02776.
    SMRiP02776. Positions 36-101.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02776.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni92 – 987Heparin-binding

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40449.
    HOGENOMiHOG000220915.
    HOVERGENiHBG107789.
    InParanoidiP02776.
    KOiK05407.
    OMAiRKICLDR.
    OrthoDBiEOG7B5WZS.
    PhylomeDBiP02776.
    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.

    P02776-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSAAGFCAS RPGLLFLGLL LLPLVVAFAS AEAEEDGDLQ CLCVKTTSQV    50
    RPRHITSLEV IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE 100
    S 101
    Length:101
    Mass (Da):10,845
    Last modified:July 1, 1989 - v2
    Checksum:iE96C2EFE9B944D85
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 781N → D AA sequence (PubMed:267922)Curated
    Sequence conflicti78 – 781N → D AA sequence (PubMed:601757)Curated

    Mass spectrometryi

    Molecular mass is 7765 Da from positions 32 - 101. Determined by ESI. 1 Publication
    Molecular mass is 6033 Da from positions 48 - 101. Determined by ESI. Short form.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25897 mRNA. Translation: AAA60066.1.
    AF349466 Genomic DNA. Translation: AAK29643.1.
    CR407677 mRNA. Translation: CAG28605.1.
    AC097709 Genomic DNA. Translation: AAY41003.1.
    BC093965 mRNA. Translation: AAH93965.1.
    BC112093 mRNA. Translation: AAI12094.1.
    CCDSiCCDS3562.1.
    PIRiA60161. PFHU4.
    RefSeqiNP_002610.1. NM_002619.3.
    UniGeneiHs.81564.

    Genome annotation databases

    EnsembliENST00000296029; ENSP00000296029; ENSG00000163737.
    GeneIDi5196.
    KEGGihsa:5196.
    UCSCiuc003hhi.3. human.

    Polymorphism databases

    DMDMi130304.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    CXCL4 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25897 mRNA. Translation: AAA60066.1 .
    AF349466 Genomic DNA. Translation: AAK29643.1 .
    CR407677 mRNA. Translation: CAG28605.1 .
    AC097709 Genomic DNA. Translation: AAY41003.1 .
    BC093965 mRNA. Translation: AAH93965.1 .
    BC112093 mRNA. Translation: AAI12094.1 .
    CCDSi CCDS3562.1.
    PIRi A60161. PFHU4.
    RefSeqi NP_002610.1. NM_002619.3.
    UniGenei Hs.81564.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DN3 NMR - A 59-73 [» ]
    1F9Q X-ray 2.00 A/B/C/D 32-101 [» ]
    1F9R X-ray 2.00 A/B/C/D 32-101 [» ]
    1F9S X-ray 2.38 A/B/C/D 32-101 [» ]
    1PFM NMR - A/B/C/D 39-101 [» ]
    1PFN NMR - A/B/C/D 39-101 [» ]
    1RHP X-ray 2.40 A/B/C/D 32-101 [» ]
    ProteinModelPortali P02776.
    SMRi P02776. Positions 36-101.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111219. 7 interactions.
    IntActi P02776. 2 interactions.
    STRINGi 9606.ENSP00000296029.

    Chemistry

    DrugBanki DB00055. Drotrecogin alfa.

    Polymorphism databases

    DMDMi 130304.

    2D gel databases

    OGPi P02776.

    Proteomic databases

    PaxDbi P02776.
    PeptideAtlasi P02776.
    PRIDEi P02776.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296029 ; ENSP00000296029 ; ENSG00000163737 .
    GeneIDi 5196.
    KEGGi hsa:5196.
    UCSCi uc003hhi.3. human.

    Organism-specific databases

    CTDi 5196.
    GeneCardsi GC04M074836.
    HGNCi HGNC:8861. PF4.
    HPAi CAB026008.
    HPA052485.
    MIMi 173460. gene.
    neXtProti NX_P02776.
    PharmGKBi PA33203.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40449.
    HOGENOMi HOG000220915.
    HOVERGENi HBG107789.
    InParanoidi P02776.
    KOi K05407.
    OMAi RKICLDR.
    OrthoDBi EOG7B5WZS.
    PhylomeDBi P02776.
    TreeFami TF333433.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1439. Common Pathway.
    REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P02776.
    GeneWikii Platelet_factor_4.
    GenomeRNAii 5196.
    NextBioi 20098.
    PMAP-CutDB P02776.
    PROi P02776.
    SOURCEi Search...

    Gene expression databases

    Bgeei P02776.
    CleanExi HS_PF4.
    Genevestigatori P02776.

    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 and characterization of platelet factor 4 cDNA derived from a human erythroleukemic cell line."
      Poncz M., Surrey S., Larocco P., Weiss M.J., Rappaport E.F., Conway T.M., Schwartz E.
      Blood 69:219-223(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural and functional comparison of the genes for human platelet factor 4 and PF4alt."
      Eisman R., Surrey S., Ramachandran B., Schwartz E., Poncz M.
      Blood 76:336-344(1990) [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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
    6. "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].
    7. "Isolation, crystallization, and primary amino acid sequence of human platelet factor 4."
      Hermodson M., Schmer G., Kurachi K.
      J. Biol. Chem. 252:6276-6279(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-101.
    8. Cited for: PROTEIN SEQUENCE OF 32-101.
    9. "Primary structure of human platelet factor 4."
      Walz D.A., Wu V.Y., de Lamo R., Dene H., McCoy L.E.
      Thromb. Res. 11:893-898(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-101.
    10. "Complete covalent structure of human platelet factor 4."
      Morgan F.J., Begg G.S., Chesterman C.N.
      Thromb. Haemost. 42:1652-1660(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-101.
    11. "A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4."
      Gupta S.K., Hassel T., Singh J.P.
      Proc. Natl. Acad. Sci. U.S.A. 92:7799-7803(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-101, N-TERMINAL CLEAVAGE, FUNCTION, MASS SPECTROMETRY.
      Tissue: Leukocyte.
    12. "Alternative C-terminal helix orientation alters chemokine function: Structure of the Anti-angiogenic Chemokine, CXCL4L1."
      Kuo J.H., Chen Y.P., Liu J.S., Dubrac A., Quemener C., Prats H., Bikfalvi A., Wu W.G., Sue S.C.
      J. Biol. Chem. 288:13522-13533(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEPARIN-BINDING REGION.
    13. "Crystal structure of recombinant human platelet factor 4."
      Zhang X., Chen L., Bancroft D.P., Lai C.K., Maione T.E.
      Biochemistry 33:8361-8366(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT, DISULFIDE BONDS.
    14. "NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-terminal chimera: a symmetric tetramer."
      Mayo K.H., Roongta V., Ilyina E., Milius R., Barker S., Quinlan C., La Rosa G., Daly T.J.
      Biochemistry 34:11399-11409(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 43-101, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiPLF4_HUMAN
    AccessioniPrimary (citable) accession number: P02776
    Secondary accession number(s): Q53X61, Q9UC64, Q9UC65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 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