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P04085

- PDGFA_HUMAN

UniProt

P04085 - PDGFA_HUMAN

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Protein

Platelet-derived growth factor subunit A

Gene

PDGFA

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

Functioni

Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity).By similarity

GO - Molecular functioni

  1. collagen binding Source: MGI
  2. growth factor activity Source: UniProtKB
  3. platelet-derived growth factor binding Source: BHF-UCL
  4. platelet-derived growth factor receptor binding Source: BHF-UCL
  5. protein heterodimerization activity Source: BHF-UCL
  6. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. angiogenesis Source: UniProtKB
  3. blood coagulation Source: Reactome
  4. cell activation Source: BHF-UCL
  5. cell-cell signaling Source: ProtInc
  6. cell projection assembly Source: UniProtKB
  7. embryo development Source: BHF-UCL
  8. epidermal growth factor receptor signaling pathway Source: Reactome
  9. extracellular matrix organization Source: Reactome
  10. Fc-epsilon receptor signaling pathway Source: Reactome
  11. fibroblast growth factor receptor signaling pathway Source: Reactome
  12. hair follicle development Source: UniProtKB
  13. innate immune response Source: Reactome
  14. inner ear development Source: Ensembl
  15. lung alveolus development Source: UniProtKB
  16. negative chemotaxis Source: BHF-UCL
  17. negative regulation of phosphatidylinositol biosynthetic process Source: BHF-UCL
  18. negative regulation of platelet activation Source: BHF-UCL
  19. neurotrophin TRK receptor signaling pathway Source: Reactome
  20. organ morphogenesis Source: UniProtKB
  21. phosphatidylinositol-mediated signaling Source: Reactome
  22. platelet activation Source: Reactome
  23. platelet degranulation Source: Reactome
  24. platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
  25. positive regulation of cell division Source: UniProtKB-KW
  26. positive regulation of cell migration Source: UniProtKB
  27. positive regulation of cell proliferation Source: BHF-UCL
  28. positive regulation of DNA replication Source: BHF-UCL
  29. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  30. positive regulation of fibroblast proliferation Source: BHF-UCL
  31. positive regulation of MAPK cascade Source: UniProtKB
  32. positive regulation of MAP kinase activity Source: UniProtKB
  33. positive regulation of mesenchymal cell proliferation Source: UniProtKB
  34. positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  35. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  36. positive regulation of protein autophosphorylation Source: UniProtKB
  37. positive regulation of protein kinase B signaling Source: UniProtKB
  38. regulation of actin cytoskeleton organization Source: BHF-UCL
  39. regulation of branching involved in salivary gland morphogenesis by epithelial-mesenchymal signaling Source: UniProtKB
  40. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  41. regulation of smooth muscle cell migration Source: BHF-UCL
  42. response to drug Source: Ensembl
  43. response to estradiol Source: Ensembl
  44. response to hypoxia Source: Ensembl
  45. response to inorganic substance Source: Ensembl
  46. response to retinoic acid Source: Ensembl
  47. response to wounding Source: BHF-UCL
  48. skin development Source: UniProtKB
  49. transforming growth factor beta receptor signaling pathway Source: Ensembl
  50. wound healing Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Enzyme and pathway databases

ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_16888. Signaling by PDGF.
REACT_17025. Downstream signal transduction.
REACT_75829. PIP3 activates AKT signaling.
SignaLinkiP04085.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-derived growth factor subunit A
Short name:
PDGF subunit A
Alternative name(s):
PDGF-1
Platelet-derived growth factor A chain
Platelet-derived growth factor alpha polypeptide
Gene namesi
Name:PDGFA
Synonyms:PDGF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:8799. PDGFA.

Subcellular locationi

Secreted
Note: Released by platelets upon wounding.

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. extracellular space Source: BHF-UCL
  5. Golgi membrane Source: Reactome
  6. microvillus Source: UniProtKB
  7. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33144.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Propeptidei21 – 8666Removed in mature formPRO_0000023356Add
BLAST
Chaini87 – 211125Platelet-derived growth factor subunit APRO_0000023357Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi96 ↔ 1401 Publication
Disulfide bondi123 – 123Interchain1 Publication
Disulfide bondi129 ↔ 1771 Publication
Disulfide bondi132 – 132Interchain1 Publication
Disulfide bondi133 ↔ 1791 Publication
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP04085.
PRIDEiP04085.

PTM databases

PhosphoSiteiP04085.

Expressioni

Gene expression databases

BgeeiP04085.
CleanExiHS_PDGFA.
ExpressionAtlasiP04085. baseline and differential.
GenevestigatoriP04085.

Organism-specific databases

HPAiCAB005579.

Interactioni

Subunit structurei

Homodimer; antiparallel disulfide-linked dimer. Heterodimer with PDGFB; antiparallel disulfide-linked dimer. The PDGFA homodimer interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts with CSPG4.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDGFRAP162346EBI-2881386,EBI-2861522

Protein-protein interaction databases

BioGridi111180. 11 interactions.
DIPiDIP-5735N.
IntActiP04085. 3 interactions.
STRINGi9606.ENSP00000346508.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 348Combined sources
Helixi41 – 477Combined sources
Beta strandi96 – 1049Combined sources
Helixi107 – 1093Combined sources
Beta strandi118 – 13013Combined sources
Beta strandi134 – 18047Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MJKX-ray2.40A/B/E/F/X/Y21-181[»]
ProteinModelPortaliP04085.
SMRiP04085. Positions 23-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04085.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 1625Receptor binding siteSequence Analysis

Domaini

The long form contains a basic insert which acts as a cell retention signal.

Sequence similaritiesi

Belongs to the PDGF/VEGF growth factor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG75094.
GeneTreeiENSGT00510000046755.
HOGENOMiHOG000286027.
HOVERGENiHBG053546.
InParanoidiP04085.
KOiK04359.
OMAiSNSDYRE.
OrthoDBiEOG78H3VV.
PhylomeDBiP04085.
TreeFamiTF319554.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
IPR006782. PDGF_N.
[Graphical view]
PfamiPF00341. PDGF. 1 hit.
PF04692. PDGF_N. 1 hit.
[Graphical view]
SMARTiSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P04085-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRTLACLLLL GCGYLAHVLA EEAEIPREVI ERLARSQIHS IRDLQRLLEI
60 70 80 90 100
DSVGSEDSLD TSLRAHGVHA TKHVPEKRPL PIRRKRSIEE AVPAVCKTRT
110 120 130 140 150
VIYEIPRSQV DPTSANFLIW PPCVEVKRCT GCCNTSSVKC QPSRVHHRSV
160 170 180 190 200
KVAKVEYVRK KPKLKEVQVR LEEHLECACA TTSLNPDYRE EDTGRPRESG
210
KKRKRKRLKP T
Length:211
Mass (Da):24,043
Last modified:November 1, 1986 - v1
Checksum:i48633DDE558EFA43
GO
Isoform Short (identifier: P04085-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     194-196: GRP → DVR
     197-211: Missing.

Show »
Length:196
Mass (Da):22,253
Checksum:i5EDBDB62D565904B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 663RAH → TRD in AAA60045. (PubMed:2832727)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei194 – 1963GRP → DVR in isoform Short. 1 PublicationVSP_004602
Alternative sequencei197 – 21115Missing in isoform Short. 1 PublicationVSP_004603Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03795 mRNA. Translation: CAA27421.1.
X06374 mRNA. Translation: CAA29677.1.
M20494
, M20488, M20489, M20490, M20491, M20492, M20493 Genomic DNA. Translation: AAA60045.1.
M19988
, M21571, M19984, M19985, M19986, M19987 Genomic DNA. Translation: AAA60046.1.
M19989
, M21571, M19984, M19985, M19986, M19987 Genomic DNA. Translation: AAA60047.1.
AB451309 mRNA. Translation: BAG70123.1.
AB451439 mRNA. Translation: BAG70253.1.
AC147651 Genomic DNA. No translation available.
S62078 Genomic DNA. Translation: AAB26566.1.
CCDSiCCDS34578.1. [P04085-1]
CCDS47524.1. [P04085-2]
PIRiA28964. PFHUG1.
B28964.
RefSeqiNP_002598.4. NM_002607.5. [P04085-1]
NP_148983.1. NM_033023.4. [P04085-2]
XP_006715796.1. XM_006715733.1. [P04085-1]
UniGeneiHs.535898.

Genome annotation databases

EnsembliENST00000354513; ENSP00000346508; ENSG00000197461. [P04085-1]
ENST00000402802; ENSP00000383889; ENSG00000197461. [P04085-2]
GeneIDi5154.
KEGGihsa:5154.
UCSCiuc003sir.3. human. [P04085-1]
uc003sis.3. human. [P04085-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

R&D Systems' cytokine mini-reviews: PDGF

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03795 mRNA. Translation: CAA27421.1 .
X06374 mRNA. Translation: CAA29677.1 .
M20494
, M20488 , M20489 , M20490 , M20491 , M20492 , M20493 Genomic DNA. Translation: AAA60045.1 .
M19988
, M21571 , M19984 , M19985 , M19986 , M19987 Genomic DNA. Translation: AAA60046.1 .
M19989
, M21571 , M19984 , M19985 , M19986 , M19987 Genomic DNA. Translation: AAA60047.1 .
AB451309 mRNA. Translation: BAG70123.1 .
AB451439 mRNA. Translation: BAG70253.1 .
AC147651 Genomic DNA. No translation available.
S62078 Genomic DNA. Translation: AAB26566.1 .
CCDSi CCDS34578.1. [P04085-1 ]
CCDS47524.1. [P04085-2 ]
PIRi A28964. PFHUG1.
B28964.
RefSeqi NP_002598.4. NM_002607.5. [P04085-1 ]
NP_148983.1. NM_033023.4. [P04085-2 ]
XP_006715796.1. XM_006715733.1. [P04085-1 ]
UniGenei Hs.535898.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MJK X-ray 2.40 A/B/E/F/X/Y 21-181 [» ]
ProteinModelPortali P04085.
SMRi P04085. Positions 23-182.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111180. 11 interactions.
DIPi DIP-5735N.
IntActi P04085. 3 interactions.
STRINGi 9606.ENSP00000346508.

Chemistry

ChEMBLi CHEMBL3137294.

PTM databases

PhosphoSitei P04085.

Proteomic databases

PaxDbi P04085.
PRIDEi P04085.

Protocols and materials databases

DNASUi 5154.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354513 ; ENSP00000346508 ; ENSG00000197461 . [P04085-1 ]
ENST00000402802 ; ENSP00000383889 ; ENSG00000197461 . [P04085-2 ]
GeneIDi 5154.
KEGGi hsa:5154.
UCSCi uc003sir.3. human. [P04085-1 ]
uc003sis.3. human. [P04085-2 ]

Organism-specific databases

CTDi 5154.
GeneCardsi GC07M000536.
H-InvDB HIX0167622.
HGNCi HGNC:8799. PDGFA.
HPAi CAB005579.
MIMi 173430. gene.
neXtProti NX_P04085.
PharmGKBi PA33144.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG75094.
GeneTreei ENSGT00510000046755.
HOGENOMi HOG000286027.
HOVERGENi HBG053546.
InParanoidi P04085.
KOi K04359.
OMAi SNSDYRE.
OrthoDBi EOG78H3VV.
PhylomeDBi P04085.
TreeFami TF319554.

Enzyme and pathway databases

Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_16888. Signaling by PDGF.
REACT_17025. Downstream signal transduction.
REACT_75829. PIP3 activates AKT signaling.
SignaLinki P04085.

Miscellaneous databases

EvolutionaryTracei P04085.
GeneWikii PDGFA.
GenomeRNAii 5154.
NextBioi 19930.
PROi P04085.
SOURCEi Search...

Gene expression databases

Bgeei P04085.
CleanExi HS_PDGFA.
ExpressionAtlasi P04085. baseline and differential.
Genevestigatori P04085.

Family and domain databases

Gene3Di 2.10.90.10. 1 hit.
InterProi IPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
IPR006782. PDGF_N.
[Graphical view ]
Pfami PF00341. PDGF. 1 hit.
PF04692. PDGF_N. 1 hit.
[Graphical view ]
SMARTi SM00141. PDGF. 1 hit.
[Graphical view ]
SUPFAMi SSF57501. SSF57501. 1 hit.
PROSITEi PS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Platelet-derived growth factor A chain: gene structure, chromosomal location, and basis for alternative mRNA splicing."
    Bonthron D.T., Morton C.C., Orkin S.H., Collins T.
    Proc. Natl. Acad. Sci. U.S.A. 85:1492-1496(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structural characterization of the human platelet-derived growth factor A-chain cDNA and gene: alternative exon usage predicts two different precursor proteins."
    Rorsman F., Bywater M., Knott T.J., Scott J., Betsholtz C.
    Mol. Cell. Biol. 8:571-577(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "cDNA sequence and chromosomal localization of human platelet-derived growth factor A-chain and its expression in tumour cell lines."
    Betsholtz C., Johnsson A., Heldin C.H., Westermark B., Lind P., Urdea M.S., Eddy R., Shows T.B., Philpott K., Mellor A.L., Knott T.J., Scott J.
    Nature 320:695-699(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The long 3'-untranslated regions of the PDGF-A and -B mRNAs are only distantly related."
    Hoppe J., Schumacher L., Eichner W., Weich H.A.
    FEBS Lett. 223:243-246(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Nucleotide sequence of the 5' region of the human platelet-derived growth factor A-chain gene."
    Takimoto Y., Li W.Y., Wang Z.Y., Tong B.D., Deuel T.F.
    Hiroshima J. Med. Sci. 42:47-52(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
  8. "Platelet-derived growth factor A chain: confirmation of localization of PDGFA to chromosome 7p22 and description of an unusual minisatellite."
    Bonthron D., Collins T., Grzeschik K.H., van Roy N., Speleman F.
    Genomics 13:257-263(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-211.
  9. "cDNA clones reveal differences between human glial and endothelial cell platelet-derived growth factor A-chains."
    Tong B.D., Auer D.E., Jaye M., Kaplow J.M., Ricca G., McConathy E., Drohan W., Deuel T.F.
    Nature 328:619-621(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  10. "Alternative RNA splicing affects function of encoded platelet-derived growth factor A chain."
    Collins T., Bonthron D.T., Orkin S.H.
    Nature 328:621-624(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  11. "Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF."
    Andersson M., Oestman A., Baeckstroem G., Hellman U., George-Nascimento C., Westermark B., Heldin C.-H.
    J. Biol. Chem. 267:11260-11266(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERCHAIN DISULFIDE BONDS.
  12. "High-affinity binding of basic fibroblast growth factor and platelet-derived growth factor-AA to the core protein of the NG2 proteoglycan."
    Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.
    J. Biol. Chem. 274:16831-16837(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG4.
  13. "Role of platelet-derived growth factors in physiology and medicine."
    Andrae J., Gallini R., Betsholtz C.
    Genes Dev. 22:1276-1312(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE.
  14. "Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex."
    Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.
    Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-181, DISULFIDE BONDS.

Entry informationi

Entry nameiPDGFA_HUMAN
AccessioniPrimary (citable) accession number: P04085
Secondary accession number(s): B5BU73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: November 26, 2014
This is version 159 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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