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P02775

- CXCL7_HUMAN

UniProt

P02775 - CXCL7_HUMAN

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Protein
Platelet basic protein
Gene
PPBP, CTAP3, CXCL7, SCYB7, TGB1, THBGB1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33561.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 34342 Publications
Add
BLAST
Chaini35 – 12894Platelet basic protein
PRO_0000005088Add
BLAST
Chaini44 – 12885Connective tissue-activating peptide III
PRO_0000005089Add
BLAST
Chaini44 – 12683TC-2
PRO_0000005090Add
BLAST
Chaini44 – 12481Connective tissue-activating peptide III(1-81)
PRO_0000041949Add
BLAST
Chaini48 – 12881Beta-thromboglobulin
PRO_0000005091Add
BLAST
Chaini55 – 12874Neutrophil-activating peptide 2(74)
PRO_0000005092Add
BLAST
Chaini56 – 12873Neutrophil-activating peptide 2(73)
PRO_0000005093Add
BLAST
Chaini59 – 12870Neutrophil-activating peptide 2
PRO_0000005094Add
BLAST
Chaini59 – 12668TC-1
PRO_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.
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.

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

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.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 162 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

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