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P04085

- PDGFA_HUMAN

UniProt

P04085 - PDGFA_HUMAN

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
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Nov 1986)
      Previous versions | rss
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    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 binding Source: IntAct
    6. protein heterodimerization activity Source: BHF-UCL
    7. 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

    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

    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

    ArrayExpressiP04085.
    BgeeiP04085.
    CleanExiHS_PDGFA.
    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 – 348
    Helixi41 – 477
    Beta strandi96 – 1049
    Helixi107 – 1093
    Beta strandi118 – 13013
    Beta strandi134 – 18047

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MRTLACLLLL GCGYLAHVLA EEAEIPREVI ERLARSQIHS IRDLQRLLEI    50
    DSVGSEDSLD TSLRAHGVHA TKHVPEKRPL PIRRKRSIEE AVPAVCKTRT 100
    VIYEIPRSQV DPTSANFLIW PPCVEVKRCT GCCNTSSVKC QPSRVHHRSV 150
    KVAKVEYVRK KPKLKEVQVR LEEHLECACA TTSLNPDYRE EDTGRPRESG 200
    KKRKRKRLKP T 211
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.

    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.
    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

    ArrayExpressi P04085.
    Bgeei P04085.
    CleanExi HS_PDGFA.
    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

    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: October 1, 2014
    This is version 157 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