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0PDGFB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePDGFB
DescriptionPlatelet-derived growth factor b chain precursor (pdgf b-chain) (platelet-derived growth factor beta polypeptide) (pdgf-2) (c-sis) (becaplermin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (NAS)
0005161 platelet-derived growth factor receptor bin... (NAS)
0009611 response to wounding (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Platelet-derived growth factor (PDGF) .s a potent mitogen for cells ofmesenchymal origin.ncluding smooth muscle cells and glial cells. In both mouse and human.he PDGF signalling network consists of four ligands.DGFA-D.nd two receptors.DGFRalpha and PDGFRbeta. All PDGFs function as secreted.isulfide-linkedhomodimers.ut only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic PDGF domains.hich include eight conserved cysteines that are involved in inter- and intramolecular bonds.Alternate splicing of the A chain transcript can give rise to two differentforms that differ only in their C-terminal extremity. The transforming proteinof simian sarcoma virus (SSV).ncoded by the v-sis oncogene.s derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages.riving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages.DGF signalling has been implicated in tissue remodelling and cellular differentiation.nd in inductive events involved in patterning and morphogenesis. In addition to drivingmesenchymal proliferation.DGFs have been shown to direct the migration.ifferentiation and function of a variety of specialised mesenchymal and migratory cell types.oth during development and in theadult animal .PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers.This domain consists of the N-terminal regions of PGDF A and B.
  IPR006782:Platelet-derived growth factor, N-terminal
Platelet-derived growth factor (PDGF) .s a potent mitogen for cells ofmesenchymal origin.ncluding smooth muscle cells and glial cells. In both mouse and human.he PDGF signalling network consists of four ligands.DGFA-D.nd two receptors.DGFRalpha and PDGFRbeta. All PDGFs function as secreted.isulfide-linkedhomodimers.ut only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic PDGF domains.hich include eight conserved cysteines that are involved in inter- and intramolecular bonds.Alternate splicing of the A chain transcript can give rise to two differentforms that differ only in their C-terminal extremity. The transforming proteinof simian sarcoma virus (SSV).ncoded by the v-sis oncogene.s derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages.riving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages.DGF signalling has been implicated in tissue remodelling and cellular differentiation.nd in inductive events involved in patterning and morphogenesis. In addition to drivingmesenchymal proliferation.DGFs have been shown to direct the migration.ifferentiation and function of a variety of specialised mesenchymal and migratory cell types.oth during development and in theadult animal . Other growth factors in this family include vascular endothelial growth factors B and C (VEGF-B.EGF-C) .hich are active in angiogenesis and endothelial cell growth.nd placenta growth factor (PlGF) which is also active in angiogenesis . PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers.
  IPR000072:Platelet-derived growth factor (PDGF)
The crystal structures of several proteins have been reported as having unusual folds.nvolving intramolecular disulphide bridges. In transforming growth factor-beta 2 (TGF-beta2) .latelet-derived growth factor (PDGF).erve growth factor (NGF) and human chorionic gonadotropin (hCG) .ix conserved cysteines (I to VI in sequence order) form three disulphide links arranged in a knot-like topology. Cystines [II-V] and [III-VI] form a ring of eight amino acids through which the remaining disulphide bond (Cys[I-IV]) penetrates.A similar knotted arrangement of disulphide bonds has been noted in the structures of some enzyme inhibitors and neurotoxins that bind to voltage- gated Ca2+ channels . In those sequences.owever.he cystine topology differs. Cys[III-VI] penetrates a macrocyclic ring formed by Cys[I-IV] and Cys[II-V]. Thus.ystine knots fall into two structural classes: growth factor type and inhibitor-like cystine knots .All growth factor cystine knots structures have similar topology.ith two distorted beta-hairpin loops "above" the knot and a single loop "below". The sizes of the hairpin loop vary significantly.
  IPR002400:Growth factor, cystine knot
IPR000072:PDGF 
Evalue:-61.6020584106445 
Location:97-180IPR006782:PDGF_N 
Evalue:-42.4685211181641 
Location:21-96
SequencesProtein: PDGFB_HUMAN (241 aa)
mRNA: NM_002608
Local Annotation
Synapse Ontology
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:keywords)
KO assignmentK04359
  Level 3 annotation:
    platelet derived growth factor A/B
  Level 2 annotation:
    MAPK signaling pathway
    Cytokines
    Cytokine-cytokine receptor interaction
    CAM ligands
    Regulation of actin cytoskeleton
    Focal adhesion
    Gap junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 534 residues, 37949664-37951264Exon2: 53 residues, 37951645-37951798Exon3: 50 residues, 37956034-37956179Exon4: 70 residues, 37957572-37957778Exon5: 32 residues, 37959385-37959475Exon6: 34 residues, 37961728-37961825Exon7: 363 residues, 37969851-37970936Exon8: 2 residues, -Jump to PDGFB_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3318 38075899-38111525 ~-36K 24775(SYNGR1)(+)Loci: 3319 38296703-38415684 ~-119K 24788(CACNA1I)(+)Loci: 4573 38468995-38619740 ~-151K 24792(-)Loci: 4572 37949664-37970936 ~-21K 24769(PDGFB)(-)Link out to UCSC