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P02776

- PLF4_HUMAN

UniProt

P02776 - PLF4_HUMAN

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Protein

Platelet factor 4

Gene

PF4

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 443Combined sources
Helixi52 – 543Combined sources
Beta strandi55 – 617Combined sources
Beta strandi64 – 663Combined sources
Beta strandi67 – 693Combined sources
Beta strandi71 – 766Combined sources
Beta strandi77 – 793Combined sources
Beta strandi81 – 833Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 9910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000062901.
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

        10         20         30         40         50
MSSAAGFCAS RPGLLFLGLL LLPLVVAFAS AEAEEDGDLQ CLCVKTTSQV
60 70 80 90 100
RPRHITSLEV IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE

S
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00530000062901.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 150 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