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Identification
HMDB Protein ID HMDBP02768
Secondary Accession Numbers
  • 8274
Name Platelet basic protein
Synonyms
  1. Beta-TG
  2. Beta-thromboglobulin
  3. C-X-C motif chemokine 7
  4. CTAP-III
  5. CTAP-III(1-81)
  6. Connective tissue-activating peptide III
  7. Connective tissue-activating peptide III(1-81)
  8. LA-PF4
  9. LDGF
  10. Leukocyte-derived growth factor
  11. Low-affinity platelet factor IV
  12. MDGF
  13. Macrophage-derived growth factor
  14. NAP-2
  15. NAP-2(1-63)
  16. NAP-2(1-66)
  17. NAP-2(73)
  18. NAP-2(74)
  19. Neutrophil-activating peptide 2
  20. Neutrophil-activating peptide 2(1-63)
  21. Neutrophil-activating peptide 2(1-66)
  22. Neutrophil-activating peptide 2(73)
  23. Neutrophil-activating peptide 2(74)
  24. PBP
  25. Small-inducible cytokine B7
  26. TC-1
  27. TC-2
Gene Name PPBP
Protein Type Unknown
Biological Properties
General Function Involved in cytokine activity
Specific Function 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
Pathways Not Available
Reactions Not Available
GO Classification
Component
extracellular region
Function
cytokine activity
chemokine activity
binding
protein binding
receptor binding
Process
immune system process
immune response
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Chromosome:4
Locus 4q12-q13
SNPs PPBP
Gene Sequence
>387 bp
ATGAGCCTCAGACTTGATACCACCCCTTCCTGTAACAGTGCGAGACCACTTCATGCCTTG
CAGGTGCTGCTGCTTCTGTCATTGCTGCTGACTGCTCTGGCTTCCTCCACCAAAGGACAA
ACTAAGAGAAACTTGGCGAAAGGCAAAGAGGAAAGTCTAGACAGTGACTTGTATGCTGAA
CTCCGCTGCATGTGTATAAAGACAACCTCTGGAATTCATCCCAAAAACATCCAAAGTTTG
GAAGTGATCGGGAAAGGAACCCATTGCAACCAAGTCGAAGTGATAGCCACACTGAAGGAT
GGGAGGAAAATCTGCCTGGACCCAGATGCTCCCAGAATCAAGAAAATTGTACAGAAAAAA
TTGGCAGGTGATGAATCTGCTGATTAA
Protein Properties
Number of Residues 128
Molecular Weight 13894.0
Theoretical pI 9.07
Pfam Domain Function
Signals
  • 1-34
Transmembrane Regions
  • None
Protein Sequence
>Platelet basic protein
MSLRLDTTPSCNSARPLHALQVLLLLSLLLTALASSTKGQTKRNLAKGKEESLDSDLYAE
LRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKK
LAGDESAD
GenBank ID Protein 181176
UniProtKB/Swiss-Prot ID P02775
UniProtKB/Swiss-Prot Entry Name CXCL7_HUMAN
PDB IDs
GenBank Gene ID M54995
GeneCard ID PPBP
GenAtlas ID PPBP
HGNC ID HGNC:9240
References
General References
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  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
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  8. Wenger RH, Wicki AN, Walz A, Kieffer N, Clemetson KJ: Cloning of cDNA coding for connective tissue activating peptide III from a human platelet-derived lambda gt11 expression library. Blood. 1989 May 1;73(6):1498-503. [PubMed:2713489 ]
  9. Majumdar S, Gonder D, Koutsis B, Poncz M: Characterization of the human beta-thromboglobulin gene. Comparison with the gene for platelet factor 4. J Biol Chem. 1991 Mar 25;266(9):5785-9. [PubMed:1826003 ]
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  12. Castor CW, Miller JW, Walz DA: Structural and biological characteristics of connective tissue activating peptide (CTAP-III), a major human platelet-derived growth factor. Proc Natl Acad Sci U S A. 1983 Feb;80(3):765-9. [PubMed:6572368 ]
  13. Begg GS, Pepper DS, Chesterman CN, Morgan FJ: Complete covalent structure of human beta-thromboglobulin. Biochemistry. 1978 May 2;17(9):1739-44. [PubMed:77677 ]
  14. Piccardoni P, Evangelista V, Piccoli A, de Gaetano G, Walz A, Cerletti C: Thrombin-activated human platelets release two NAP-2 variants that stimulate polymorphonuclear leukocytes. Thromb Haemost. 1996 Nov;76(5):780-5. [PubMed:8950790 ]
  15. Castor CW, Walz DA, Ragsdale CG, Hossler PA, Smith EM, Bignall MC, Aaron BP, Mountjoy K: Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets. Biochem Biophys Res Commun. 1989 Sep 15;163(2):1071-8. [PubMed:2783111 ]
  16. Walz A, Baggiolini M: A novel cleavage product of beta-thromboglobulin formed in cultures of stimulated mononuclear cells activates human neutrophils. Biochem Biophys Res Commun. 1989 Mar 31;159(3):969-75. [PubMed:2522778 ]
  17. Ehlert JE, Petersen F, Kubbutat MH, Gerdes J, Flad HD, Brandt E: 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. J Biol Chem. 1995 Mar 17;270(11):6338-44. [PubMed:7890771 ]
  18. Walz A, Baggiolini M: Generation of the neutrophil-activating peptide NAP-2 from platelet basic protein or connective tissue-activating peptide III through monocyte proteases. J Exp Med. 1990 Feb 1;171(2):449-54. [PubMed:2406364 ]
  19. Ehlert JE, Gerdes J, Flad HD, Brandt E: Novel C-terminally truncated isoforms of the CXC chemokine beta-thromboglobulin and their impact on neutrophil functions. J Immunol. 1998 Nov 1;161(9):4975-82. [PubMed:9794434 ]
  20. Kungl AJ, Machius M, Huber R, Schwer C, Lam C, Aschauer H, Ehn G, Lindley IJ, Auer M: Purification, crystallization and preliminary X-ray diffraction analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-2). FEBS Lett. 1994 Jun 27;347(2-3):300-3. [PubMed:8034022 ]
  21. Malkowski MG, Wu JY, Lazar JB, Johnson PH, Edwards BF: The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution. J Biol Chem. 1995 Mar 31;270(13):7077-87. [PubMed:7706245 ]