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Protein

Platelet-derived growth factor subunit B

Gene

PDGFB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (PubMed:26599395). Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei108 – 1081Involved in receptor binding
Sitei111 – 1111Involved in receptor binding

GO - Molecular functioni

  • chemoattractant activity Source: BHF-UCL
  • collagen binding Source: MGI
  • growth factor activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
  • platelet-derived growth factor binding Source: BHF-UCL
  • platelet-derived growth factor receptor binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • superoxide-generating NADPH oxidase activator activity Source: UniProtKB

GO - Biological processi

  • activation of protein kinase activity Source: UniProtKB
  • activation of protein kinase B activity Source: UniProtKB
  • cell chemotaxis Source: UniProtKB
  • cell growth Source: Ensembl
  • cellular response to growth factor stimulus Source: BHF-UCL
  • cellular response to mycophenolic acid Source: UniProtKB
  • DNA replication Source: Ensembl
  • embryonic placenta development Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • heart development Source: UniProtKB
  • MAPK cascade Source: Reactome
  • metanephric glomerular mesangial cell development Source: UniProtKB
  • monocyte chemotaxis Source: BHF-UCL
  • negative regulation of gene expression Source: BHF-UCL
  • negative regulation of phosphatidylinositol biosynthetic process Source: BHF-UCL
  • negative regulation of platelet activation Source: BHF-UCL
  • negative regulation of protein binding Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of vascular smooth muscle cell differentiation Source: BHF-UCL
  • paracrine signaling Source: UniProtKB
  • peptidyl-serine phosphorylation Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: Reactome
  • platelet degranulation Source: Reactome
  • platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of calcium ion import Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of chemotaxis Source: UniProtKB
  • positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of DNA biosynthetic process Source: UniProtKB
  • positive regulation of DNA replication Source: BHF-UCL
  • positive regulation of endothelial cell proliferation Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of glomerular filtration Source: UniProtKB
  • positive regulation of glomerular mesangial cell proliferation Source: UniProtKB
  • positive regulation of hyaluronan biosynthetic process Source: UniProtKB
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of metanephric mesenchymal cell migration Source: UniProtKB
  • positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of pri-miRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of protein autophosphorylation Source: UniProtKB
  • positive regulation of protein tyrosine kinase activity Source: UniProtKB
  • positive regulation of reactive oxygen species metabolic process Source: UniProtKB
  • positive regulation of smooth muscle cell migration Source: UniProtKB
  • positive regulation of smooth muscle cell proliferation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of vascular associated smooth muscle cell migration Source: BHF-UCL
  • positive regulation of vascular smooth muscle cell dedifferentiation Source: BHF-UCL
  • positive regulation of vascular smooth muscle cell proliferation Source: BHF-UCL
  • protein kinase C signaling Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • reactive oxygen species metabolic process Source: UniProtKB
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • response to drug Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to insulin Source: Ensembl
  • response to wounding Source: UniProtKB
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-186763. Downstream signal transduction.
R-HSA-186797. Signaling by PDGF.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLinkiP01127.
SIGNORiP01127.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-derived growth factor subunit B
Short name:
PDGF subunit B
Alternative name(s):
PDGF-2
Platelet-derived growth factor B chain
Platelet-derived growth factor beta polypeptide
Proto-oncogene c-Sis
INN: Becaplermin
Gene namesi
Name:PDGFB
Synonyms:PDGF2, SIS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:8800. PDGFB.

Subcellular locationi

  • Secreted

  • Note: Released by platelets upon wounding.

GO - Cellular componenti

  • basolateral plasma membrane Source: UniProtKB
  • cell surface Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular matrix Source: BHF-UCL
  • extracellular region Source: UniProtKB
  • extracellular space Source: GO_Central
  • Golgi membrane Source: Reactome
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Basal ganglia calcification, idiopathic, 5 (IBGC5)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas.
See also OMIM:615483
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91L → R in IBGC5; loss of protein expression. 2 Publications
VAR_070870
Natural varianti119 – 1191L → P in IBGC5; loss of protein expression. 2 Publications
Corresponds to variant rs397515632 [ dbSNP | Ensembl ].
VAR_070871

A chromosomal aberration involving PDGFB is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGFB.

Pharmaceutical usei

Available under the name Regranex (Ortho-McNeil). Used to promote healing in diabetic neuropathic foot ulcers.

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

MalaCardsiPDGFB.
MIMi607907. phenotype.
615483. phenotype.
Orphaneti1980. Bilateral striopallidodentate calcinosis.
31112. Dermatofibrosarcoma protuberans.
263662. Familial multiple meningioma.
PharmGKBiPA33145.

Chemistry

ChEMBLiCHEMBL3108633.

Polymorphism and mutation databases

BioMutaiPDGFB.
DMDMi129724.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Propeptidei21 – 8161Removed in mature formPRO_0000023371Add
BLAST
Chaini82 – 190109Platelet-derived growth factor subunit BPRO_0000023372Add
BLAST
Propeptidei191 – 24151Removed in mature formPRO_0000023373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence analysis
Disulfide bondi97 ↔ 1411 Publication
Disulfide bondi124 – 124Interchain1 Publication
Disulfide bondi130 ↔ 1781 Publication
Disulfide bondi133 – 133Interchain1 Publication
Disulfide bondi134 ↔ 1801 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP01127.
PeptideAtlasiP01127.
PRIDEiP01127.
TopDownProteomicsiP01127-2. [P01127-2]

PTM databases

iPTMnetiP01127.
PhosphoSiteiP01127.
UniCarbKBiP01127.

Miscellaneous databases

PMAP-CutDBP01127.

Expressioni

Tissue specificityi

Expressed at high levels in the heart, brain (sustantia nigra), placenta and fetal kidney. Expressed at moderate levels in the brain (hippocampus), skeletal muscle, kidney and lung.1 Publication

Gene expression databases

BgeeiENSG00000100311.
CleanExiHS_PDGFB.
ExpressionAtlasiP01127. baseline and differential.
GenevisibleiP01127. HS.

Organism-specific databases

HPAiCAB011604.
CAB018341.
HPA011972.

Interactioni

Subunit structurei

Homodimer; antiparallel disulfide-linked dimer. Heterodimer with PDGFA; antiparallel disulfide-linked dimer. The PDGFB homodimer interacts with PDGFRA and PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB interacts with PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts with XLKD1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1554925,EBI-1554925
PDGFRAP1623411EBI-1554925,EBI-2861522
PDGFRBP0961913EBI-1554925,EBI-641237

GO - Molecular functioni

  • collagen binding Source: MGI
  • growth factor activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • platelet-derived growth factor binding Source: BHF-UCL
  • platelet-derived growth factor receptor binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi111181. 77 interactions.
DIPiDIP-5737N.
IntActiP01127. 6 interactions.
STRINGi9606.ENSP00000330382.

Chemistry

BindingDBiP01127.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi97 – 1059Combined sources
Helixi108 – 1114Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi123 – 1319Combined sources
Beta strandi140 – 15920Combined sources
Beta strandi162 – 18120Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDGX-ray3.00A/B/C82-190[»]
3MJGX-ray2.30A/B21-185[»]
4HQUX-ray2.20A82-190[»]
4HQXX-ray2.30A82-183[»]
4QCIX-ray2.30C/D82-190[»]
ProteinModelPortaliP01127.
SMRiP01127. Positions 25-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01127.

Family & Domainsi

Sequence similaritiesi

Belongs to the PDGF/VEGF growth factor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJ45. Eukaryota.
ENOG410XWTB. LUCA.
GeneTreeiENSGT00510000046755.
HOGENOMiHOG000286027.
HOVERGENiHBG053546.
InParanoidiP01127.
KOiK17386.
OMAiHGDSVDE.
OrthoDBiEOG091G0LNU.
PhylomeDBiP01127.
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 promoter usage. AlignAdd to basket

Isoform 1 (identifier: P01127-1) [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
MNRCWALFLS LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHG
60 70 80 90 100
DPGEEDGAEL DLNMTRSHSG GELESLARGR RSLGSLTIAE PAMIAECKTR
110 120 130 140 150
TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP
160 170 180 190 200
VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETVAAARPVT RSPGGSQEQR
210 220 230 240
AKTPQTRVTI RTVRVRRPPK GKHRKFKHTH DKTALKETLG A
Length:241
Mass (Da):27,283
Last modified:July 21, 1986 - v1
Checksum:i9F9A3474CE203C0B
GO
Isoform 2 (identifier: P01127-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MNRCWALFLSLCCYLRLVSAE → MFIMGL

Show »
Length:226
Mass (Da):25,502
Checksum:i523AC7394E29C0D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011T → E AA sequence (PubMed:6844921).Curated
Sequence conflicti105 – 1051E → C AA sequence (PubMed:6844921).Curated
Sequence conflicti107 – 1071S → C AA sequence (PubMed:6844921).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91L → R in IBGC5; loss of protein expression. 2 Publications
VAR_070870
Natural varianti88 – 881I → V.
Corresponds to variant rs17565 [ dbSNP | Ensembl ].
VAR_014578
Natural varianti119 – 1191L → P in IBGC5; loss of protein expression. 2 Publications
Corresponds to variant rs397515632 [ dbSNP | Ensembl ].
VAR_070871

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MNRCW…LVSAE → MFIMGL in isoform 2. 1 PublicationVSP_044913Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01401
, K01918, J00121, K01398, K01399, K01400 Genomic DNA. Translation: AAA60552.1.
X02811 mRNA. Translation: CAA26579.1.
X02744 mRNA. Translation: CAA26524.1.
M12783 mRNA. Translation: AAA60553.1.
CR456538 mRNA. Translation: CAG30424.1.
Z81010 Genomic DNA. Translation: CAB02635.1.
Z81010 Genomic DNA. Translation: CAP58849.1.
CR541807 mRNA. Translation: CAG46606.1.
CH471095 Genomic DNA. Translation: EAW60306.1.
CH471095 Genomic DNA. Translation: EAW60307.1.
BC029822 mRNA. Translation: AAH29822.1.
BC077725 mRNA. Translation: AAH77725.1.
X83705 mRNA. Translation: CAA58679.1.
X98706 Genomic DNA. Translation: CAA67262.1.
K01917
, K01913, K01914, K01915, K01916 Genomic DNA. Translation: AAA98793.1.
X03702 mRNA. Translation: CAA27333.1.
X00561 Genomic DNA. Translation: CAA25228.1.
X00561 Genomic DNA. Translation: CAA25229.1.
CCDSiCCDS13987.1. [P01127-1]
CCDS33650.1. [P01127-2]
PIRiA94276. PFHUG2.
RefSeqiNP_002599.1. NM_002608.3. [P01127-1]
NP_148937.1. NM_033016.3. [P01127-2]
UniGeneiHs.1976.

Genome annotation databases

EnsembliENST00000331163; ENSP00000330382; ENSG00000100311. [P01127-1]
ENST00000381551; ENSP00000370963; ENSG00000100311. [P01127-2]
GeneIDi5155.
KEGGihsa:5155.
UCSCiuc003axe.4. human. [P01127-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01401
, K01918, J00121, K01398, K01399, K01400 Genomic DNA. Translation: AAA60552.1.
X02811 mRNA. Translation: CAA26579.1.
X02744 mRNA. Translation: CAA26524.1.
M12783 mRNA. Translation: AAA60553.1.
CR456538 mRNA. Translation: CAG30424.1.
Z81010 Genomic DNA. Translation: CAB02635.1.
Z81010 Genomic DNA. Translation: CAP58849.1.
CR541807 mRNA. Translation: CAG46606.1.
CH471095 Genomic DNA. Translation: EAW60306.1.
CH471095 Genomic DNA. Translation: EAW60307.1.
BC029822 mRNA. Translation: AAH29822.1.
BC077725 mRNA. Translation: AAH77725.1.
X83705 mRNA. Translation: CAA58679.1.
X98706 Genomic DNA. Translation: CAA67262.1.
K01917
, K01913, K01914, K01915, K01916 Genomic DNA. Translation: AAA98793.1.
X03702 mRNA. Translation: CAA27333.1.
X00561 Genomic DNA. Translation: CAA25228.1.
X00561 Genomic DNA. Translation: CAA25229.1.
CCDSiCCDS13987.1. [P01127-1]
CCDS33650.1. [P01127-2]
PIRiA94276. PFHUG2.
RefSeqiNP_002599.1. NM_002608.3. [P01127-1]
NP_148937.1. NM_033016.3. [P01127-2]
UniGeneiHs.1976.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDGX-ray3.00A/B/C82-190[»]
3MJGX-ray2.30A/B21-185[»]
4HQUX-ray2.20A82-190[»]
4HQXX-ray2.30A82-183[»]
4QCIX-ray2.30C/D82-190[»]
ProteinModelPortaliP01127.
SMRiP01127. Positions 25-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111181. 77 interactions.
DIPiDIP-5737N.
IntActiP01127. 6 interactions.
STRINGi9606.ENSP00000330382.

Chemistry

BindingDBiP01127.
ChEMBLiCHEMBL3108633.

PTM databases

iPTMnetiP01127.
PhosphoSiteiP01127.
UniCarbKBiP01127.

Polymorphism and mutation databases

BioMutaiPDGFB.
DMDMi129724.

Proteomic databases

PaxDbiP01127.
PeptideAtlasiP01127.
PRIDEiP01127.
TopDownProteomicsiP01127-2. [P01127-2]

Protocols and materials databases

DNASUi5155.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331163; ENSP00000330382; ENSG00000100311. [P01127-1]
ENST00000381551; ENSP00000370963; ENSG00000100311. [P01127-2]
GeneIDi5155.
KEGGihsa:5155.
UCSCiuc003axe.4. human. [P01127-1]

Organism-specific databases

CTDi5155.
GeneCardsiPDGFB.
HGNCiHGNC:8800. PDGFB.
HPAiCAB011604.
CAB018341.
HPA011972.
MalaCardsiPDGFB.
MIMi190040. gene.
607907. phenotype.
615483. phenotype.
neXtProtiNX_P01127.
Orphaneti1980. Bilateral striopallidodentate calcinosis.
31112. Dermatofibrosarcoma protuberans.
263662. Familial multiple meningioma.
PharmGKBiPA33145.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ45. Eukaryota.
ENOG410XWTB. LUCA.
GeneTreeiENSGT00510000046755.
HOGENOMiHOG000286027.
HOVERGENiHBG053546.
InParanoidiP01127.
KOiK17386.
OMAiHGDSVDE.
OrthoDBiEOG091G0LNU.
PhylomeDBiP01127.
TreeFamiTF319554.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-186763. Downstream signal transduction.
R-HSA-186797. Signaling by PDGF.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLinkiP01127.
SIGNORiP01127.

Miscellaneous databases

ChiTaRSiPDGFB. human.
EvolutionaryTraceiP01127.
GeneWikiiPDGFB.
GenomeRNAii5155.
PMAP-CutDBP01127.
PROiP01127.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100311.
CleanExiHS_PDGFB.
ExpressionAtlasiP01127. baseline and differential.
GenevisibleiP01127. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiPDGFB_HUMAN
AccessioniPrimary (citable) accession number: P01127
Secondary accession number(s): G3XAG8
, P78431, Q15354, Q6FHE7, Q9UF23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 7, 2016
This is version 199 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, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.