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P02775 (CXCL7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Connective tissue-activating peptide III
    Short name=CTAP-III
    Alternative name(s):
    LA-PF4
    Low-affinity platelet factor IV
  2. TC-2
  3. Connective tissue-activating peptide III(1-81)
    Short name=CTAP-III(1-81)
  4. Beta-thromboglobulin
    Short name=Beta-TG
  5. Neutrophil-activating peptide 2(74)
    Short name=NAP-2(74)
  6. Neutrophil-activating peptide 2(73)
    Short name=NAP-2(73)
  7. Neutrophil-activating peptide 2
    Short name=NAP-2
  8. TC-1
  9. Neutrophil-activating peptide 2(1-66)
    Short name=NAP-2(1-66)
  10. Neutrophil-activating peptide 2(1-63)
    Short name=NAP-2(1-63)
Gene names
Name:PPBP
Synonyms:CTAP3, CXCL7, SCYB7, TGB1, THBGB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.11 Ref.15 Ref.18 Ref.21

Subunit structure

Beta-thromboglobulin is a homotetramer.

Subcellular location

Secreted.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the intercrine alpha (chemokine CxC) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Ref.9 Ref.10
Chain35 – 12894Platelet basic protein
PRO_0000005088
Chain44 – 12885Connective tissue-activating peptide III
PRO_0000005089
Chain44 – 12683TC-2
PRO_0000005090
Chain44 – 12481Connective tissue-activating peptide III(1-81)
PRO_0000041949
Chain48 – 12881Beta-thromboglobulin
PRO_0000005091
Chain55 – 12874Neutrophil-activating peptide 2(74)
PRO_0000005092
Chain56 – 12873Neutrophil-activating peptide 2(73)
PRO_0000005093
Chain59 – 12870Neutrophil-activating peptide 2
PRO_0000005094
Chain59 – 12668TC-1
PRO_0000005095
Chain59 – 12466Neutrophil-activating peptide 2(1-66)
PRO_0000005096
Chain59 – 12163Neutrophil-activating peptide 2(1-63)
PRO_0000041950

Amino acid modifications

Disulfide bond63 ↔ 89
Disulfide bond65 ↔ 105

Secondary structure

................ 128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02775 [UniParc].

Last modified November 1, 1991. Version 3.
Checksum: BEAB7B75916723D9

FASTA12813,894
        10         20         30         40         50         60 
MSLRLDTTPS CNSARPLHAL QVLLLLSLLL TALASSTKGQ TKRNLAKGKE ESLDSDLYAE 

        70         80         90        100        110        120 
LRCMCIKTTS GIHPKNIQSL EVIGKGTHCN QVEVIATLKD GRKICLDPDA PRIKKIVQKK 


LAGDESAD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Wikipedia

CXCL7 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3563.1.
PIRTGHU. A39546.
RefSeqNP_002695.1. NM_002704.3.
UniGeneHs.2164.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F9PX-ray1.93A44-128[»]
1NAPX-ray1.90A/B/C/D59-128[»]
1TVXX-ray1.75A/B/C/D54-128[»]
ProteinModelPortalP02775.
SMRP02775. Positions 44-124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111469. 16 interactions.
DIPDIP-5913N.
IntActP02775. 20 interactions.
MINTMINT-1393871.
STRING9606.ENSP00000296028.

PTM databases

PhosphoSiteP02775.

Polymorphism databases

DMDM129874.

2D gel databases

SWISS-2DPAGEP02775.

Proteomic databases

PaxDbP02775.
PeptideAtlasP02775.
PRIDEP02775.

Protocols and materials databases

DNASU5473.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296028; ENSP00000296028; ENSG00000163736.
GeneID5473.
KEGGhsa:5473.
UCSCuc003hhj.3. human.

Organism-specific databases

CTD5473.
GeneCardsGC04M074841.
H-InvDBHIX0031528.
HGNCHGNC:9240. PPBP.
HPACAB017624.
HPA008354.
MIM121010. gene.
neXtProtNX_P02775.
PharmGKBPA33561.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39945.
HOGENOMHOG000220915.
HOVERGENHBG107789.
InParanoidP02775.
KOK10029.
OMALYAELRC.
OrthoDBEOG7W156N.
PhylomeDBP02775.
TreeFamTF333433.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP02775.
BgeeP02775.
CleanExHS_PPBP.
GenevestigatorP02775.

Family and domain databases

InterProIPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PANTHERPTHR10179. PTHR10179. 1 hit.
PfamPF00048. IL8. 1 hit.
[Graphical view]
PRINTSPR00437. SMALLCYTKCXC.
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
PROSITEPS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02775.
GeneWikiCXCL7.
GenomeRNAi5473.
NextBio21188.
PMAP-CutDBP02775.
PROP02775.
SOURCESearch...

Entry information

Entry nameCXCL7_HUMAN
AccessionPrimary (citable) accession number: P02775
Secondary accession number(s): B2R5F3, Q6IBJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: July 9, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM