P01127 (PDGFB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PDGFB
Synonyms:	PDGF2, SIS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 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.
Subunit structure	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. Ref.18 Ref.23
Subcellular location	Secreted. Note: Released by platelets upon wounding.
Tissue specificity	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. Ref.19
Involvement in disease	Note=A chromosomal aberration involving PDGFB is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGFB. Ref.20
Pharmaceutical use	Available under the name Regranex (Ortho-McNeil). Used to promote healing in diabetic neuropathic foot ulcers.
Sequence similarities	Belongs to the PDGF/VEGF growth factor family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Signal
Molecular function	Developmental protein Growth factor Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological process	activation of protein kinase B activity Inferred from direct assay. Source: UniProtKB cellular response to mycophenolic acid Inferred from sequence or structural similarity. Source: UniProtKB embryonic placenta development Inferred from sequence or structural similarity. Source: UniProtKB heart development Inferred from sequence or structural similarity. Source: UniProtKB metanephric glomerular mesangial cell development Inferred from sequence or structural similarity. Source: UniProtKB monocyte chemotaxis Inferred from direct assay. Source: BHF-UCL negative regulation of phosphatidylinositol biosynthetic process Inferred from direct assay. Source: BHF-UCL negative regulation of platelet activation Inferred from direct assay. Source: BHF-UCL negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: UniProtKB paracrine signaling Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of DNA biosynthetic process Inferred from direct assay. Source: UniProtKB positive regulation of DNA replication Inferred from direct assay. Source: BHF-UCL positive regulation of ERK1 and ERK2 cascade Inferred from direct assay. Source: UniProtKB positive regulation of MAP kinase activity Inferred from direct assay. Source: UniProtKB positive regulation of blood vessel endothelial cell migration Inferred from direct assay. Source: BHF-UCL positive regulation of calcium ion import Inferred from direct assay. Source: UniProtKB positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of chemotaxis Inferred from direct assay. Source: UniProtKB positive regulation of cyclin-dependent protein kinase activity Inferred from direct assay. Source: UniProtKB positive regulation of endothelial cell proliferation Inferred from direct assay. Source: BHF-UCL positive regulation of fibroblast proliferation Inferred from direct assay. Source: UniProtKB positive regulation of glomerular filtration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of glomerular mesangial cell proliferation Inferred from direct assay. Source: UniProtKB positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of mitosis Inferred from direct assay. Source: UniProtKB positive regulation of peptidyl-tyrosine phosphorylation Inferred from direct assay. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase activity Inferred from direct assay. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase cascade Inferred from direct assay. Source: UniProtKB positive regulation of protein autophosphorylation Inferred from direct assay. Source: UniProtKB positive regulation of protein tyrosine kinase activity Inferred from direct assay. Source: UniProtKB positive regulation of reactive oxygen species metabolic process Inferred from direct assay. Source: UniProtKB positive regulation of smooth muscle cell migration Inferred from direct assay. Source: UniProtKB positive regulation of smooth muscle cell proliferation Inferred from direct assay. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: UniProtKB reactive oxygen species metabolic process Inferred from mutant phenotype. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi membrane Traceable author statement. Source: Reactome basolateral plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB cell surface Inferred from direct assay. Source: BHF-UCL endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular region Non-traceable author statement Ref.17. Source: UniProtKB platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular function	collagen binding Inferred from direct assay. Source: MGI eukaryotic cell surface binding Inferred from direct assay. Source: UniProtKB growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW platelet-derived growth factor binding Inferred from physical interaction. Source: BHF-UCL platelet-derived growth factor receptor binding Non-traceable author statement Ref.17. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction. Source: BHF-UCL protein homodimerization activity Inferred from direct assay. Source: BHF-UCL protein tyrosine kinase activity Traceable author statement. Source: Reactome superoxide-generating NADPH oxidase activator activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Propeptide

21 – 81

61

Removed in mature form

PRO_0000023371

Chain

82 – 190

109

Platelet-derived growth factor subunit B

PRO_0000023372

Propeptide

191 – 241

51

Removed in mature form

PRO_0000023373

Sites

Site

108

1

Involved in receptor binding

Site

111

1

Involved in receptor binding

Amino acid modifications

Disulfide bond

97 ↔ 141

Ref.18 Ref.23

Disulfide bond

124

Interchain Ref.18 Ref.23

Disulfide bond

130 ↔ 178

Ref.18 Ref.23

Disulfide bond

133

Interchain Ref.18 Ref.23

Disulfide bond

134 ↔ 180

Ref.18 Ref.23

Natural variations

Natural variant

88

1

I → V.
Corresponds to variant rs17565 [ dbSNP | Ensembl ].

VAR_014578

Experimental info

Sequence conflict

101

1

T → E AA sequence Ref.15

Sequence conflict

105

1

E → C AA sequence Ref.15

Sequence conflict

107

1

S → C AA sequence Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

241

Helix Strand Turn

Details...

Beta strand

97 – 105

9

Beta strand

120 – 131

12

Beta strand

139 – 144

6

Beta strand

146 – 159

14

Beta strand

162 – 175

14

Beta strand

178 – 182

5

Sequences

	Sequence		Length	Mass (Da)
	P01127 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 9F9A3474CE203C0B	FASTA	241	27,283
	10 20 30 40 50 60 MNRCWALFLS LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHG DPGEEDGAEL 70 80 90 100 110 120 DLNMTRSHSG GELESLARGR RSLGSLTIAE PAMIAECKTR TEVFEISRRL IDRTNANFLV 130 140 150 160 170 180 WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC 190 200 210 220 230 240 ETVAAARPVT RSPGGSQEQR AKTPQTRVTI RTVRVRRPPK GKHRKFKHTH DKTALKETLG A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transforming potential of human c-sis nucleotide sequences encoding platelet-derived growth factor." Josephs S.F., Ratner L., Clarke M.F., Westin E.H., Reitz M.S., Wong-Staal F. Science 225:636-639(1984) [PubMed: 6740330] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cultured human endothelial cells express platelet-derived growth factor B chain: cDNA cloning and structural analysis." Collins T., Ginsburg D., Boss J.M., Orkin S.H., Pober J.S. Nature 316:748-750(1985) [PubMed: 4033772] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Nucleotide sequence of transforming human c-sis cDNA clones with homology to platelet-derived growth factor." Ratner L., Josephs S.F., Jarrett R., Reitz M.S., Wong-Staal F. Nucleic Acids Res. 13:5007-5018(1985) [PubMed: 2991848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Oncogenic potential of the human platelet-derived growth factor transcriptional unit." Rao C.D., Igarashi H., Pech M.W., Robbins K.C., Aaronson S.A. Cold Spring Harb. Symp. Quant. Biol. 51:959-966(1986) [PubMed: 3472769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Structure and sequence of the human c-sis/platelet-derived growth factor 2 (SIS/PDGF2) transcriptional unit." Rao C.D., Igarashi H., Chiu I.-M., Robbins K.C., Aaronson S.A. Proc. Natl. Acad. Sci. U.S.A. 83:2392-2396(1986) [PubMed: 3517869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"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 (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Lung, Pancreas and Testis.
[11]	"Deregulation of the platelet-derived growth factor B-chain gene via fusion with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell fibroblastoma." Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F., Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D., Blin N., Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I., Guilbaud C., Dumanski J.P. Nat. Genet. 15:95-98(1997) [PubMed: 8988177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53, CHROMOSOMAL TRANSLOCATION WITH COL1A1.
[12]	"Nucleotide sequence analysis identifies the human c-sis proto-oncogene as a structural gene for platelet-derived growth factor." Chiu I.-M., Reddy E.P., Givol D., Robbins K.C., Tronick S.R., Aaronson S.A. Cell 37:123-129(1984) [PubMed: 6327048] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-241.
[13]	"The human osteosarcoma cell line U-2 OS expresses a 3.8 kilobase mRNA which codes for the sequence of the PDGF-B chain." Weich H.A., Sebald W., Schairer H.U., Hoppe J. FEBS Lett. 198:344-348(1986) [PubMed: 3456904] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-241.
[14]	"Platelet-derived growth factor is structurally related to the putative transforming protein p28sis of simian sarcoma virus." Waterfield M.D., Scrace G.T., Whittle N., Stroobant P., Johnsson A., Wasteson A., Westermark B., Heldin C.H., Huang J.S., Deuel T.F. Nature 304:35-39(1983) [PubMed: 6306471] [Abstract] Cited for: PROTEIN SEQUENCE OF 82-112.
[15]	"Human platelet-derived growth factor (PDGF): amino-terminal amino acid sequence." Antoniades H.N., Hunkapiller M.W. Science 220:963-965(1983) [PubMed: 6844921] [Abstract] Cited for: PROTEIN SEQUENCE OF 82-110.
[16]	"The c-sis gene encodes a precursor of the B chain of platelet-derived growth factor." Johnsson A., Heldin C.H., Wasteson A., Westermark B., Deuel T.F., Huang J.S., Seeburg P.H., Gray A., Ullrich A., Scrace G., Stroobant P., Waterfield M.D. EMBO J. 3:921-928(1984) [PubMed: 6329745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-200, PARTIAL PROTEIN SEQUENCE.
[17]	"Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation." Clements J.M., Bawden L.J., Bloxidge R.E., Catlin G., Cook A.L., Craig S., Drummond A.H., Edwards R.M., Fallon A., Green D.R., Hellewell P.G., Kirwin P.M., Nayee P.D., Richardson S.J., Brown D., Chahwala S.B., Snarey M., Winslow D. EMBO J. 10:4113-4120(1991) [PubMed: 1661670] [Abstract] Cited for: MUTAGENESIS, IMPORTANCE OF ARG-108 AND ILE-111 FOR RECEPTOR BINDING.
[18]	"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: 1317862] [Abstract] Cited for: INTERCHAIN DISULFIDE BONDS.
[19]	"PDGF D, a novel protease-activated growth factor." LaRochelle W.J., Jeffers M., McDonald W.F., Chillakuru R.A., Giese N.A., Lokker N.A., Sullivan C., Boldog F.L., Yang M., Vernet C., Burgess C.E., Fernandez E., Deegler L.L., Rittman B., Shimkets J., Shimkets R.A., Rothberg J.M., Lichenstein H.S. Nat. Cell Biol. 3:517-521(2001) [PubMed: 11331882] [Abstract] Cited for: TISSUE SPECIFICITY.
[20]	"Dermatofibrosarcoma protuberans of breast." Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H. Cancer Genet. Cytogenet. 142:56-59(2003) [PubMed: 12660034] [Abstract] Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH COL1A1.
[21]	"Role of platelet-derived growth factors in physiology and medicine." Andrae J., Gallini R., Betsholtz C. Genes Dev. 22:1276-1312(2008) [PubMed: 18483217] [Abstract] Cited for: REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE.
[22]	"Crystal structure of human platelet-derived growth factor BB." Oefner C., D'Arcy A., Winkler F.K., Eggimann B., Hosang M. EMBO J. 11:3921-3926(1992) [PubMed: 1396586] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[23]	"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: 20534510] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-185 IN COMPLEX WITH PDGFRB, SUBUNIT, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

R&D Systems' cytokine source book: PDGF

Regranex

Clinical information on Regranex

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
CR541807 mRNA. Translation: CAG46606.1.
CH471095 Genomic DNA. Translation: EAW60306.1.
BC029822 mRNA. Translation: AAH29822.1.
BC077725 mRNA. Translation: AAH77725.1.
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.

IPI

IPI00000044.

PIR

PFHUG2. A94276.

RefSeq

NP_002599.1. NM_002608.2.
NP_148937.1. NM_033016.2.

UniGene

Hs.1976.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PDG	X-ray	3.00	A/B/C	82-190	[»]
3MJG	X-ray	2.30	A/B	21-185	[»]

ProteinModelPortal

P01127.

SMR

P01127. Positions 23-183.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5737N.

IntAct

P01127. 5 interactions.

STRING

P01127.

PTM databases

PhosphoSite

P01127.

Polymorphism databases

DMDM

129724.

Proteomic databases

PRIDE

P01127.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331163; ENSP00000330382; ENSG00000100311.
ENST00000396740; ENSP00000379966; ENSG00000100311.

GeneID

5155.

KEGG

hsa:5155.

UCSC

uc003axf.1. human.

Organism-specific databases

CTD

5155.

GeneCards

GC22M039619.

H-InvDB

HIX0016487.

HGNC

HGNC:8800. PDGFB.

HPA

CAB011604.
CAB018341.
HPA011972.

MIM

190040. gene.
607907. phenotype.

neXtProt

NX_P01127.

Orphanet

31112. Dermatofibrosarcoma protuberans.
263662. Familial multiple meningioma.

PharmGKB

PA33145.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG717466.

HOVERGEN

HBG053546.

InParanoid

P01127.

OMA

CKCETVV.

OrthoDB

EOG4F4SCF.

PhylomeDB

P01127.

Enzyme and pathway databases

Pathway_Interaction_DB

pdgfrapathway. PDGFR-alpha signaling pathway.
pdgfrbpathway. PDGFR-beta signaling pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P01127.

Bgee

P01127.

CleanEx

HS_PDGFB.

Genevestigator

P01127.

GermOnline

ENSG00000100311. Homo sapiens.

Family and domain databases

InterPro

IPR000072. PD_growth_factor.
IPR023581. PD_growth_factor_CS.
IPR006782. PDGF_N.
[Graphical view]

KO

K04359.

Pfam

PF00341. PDGF. 1 hit.
PF04692. PDGF_N. 1 hit.
[Graphical view]

SMART

SM00141. PDGF. 1 hit.
[Graphical view]

PROSITE

PS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00102. Becaplermin.

NextBio

19940.

PMAP-CutDB

P01127.

SOURCE

Search...

Entry information

Entry name

PDGFB_HUMAN

Accession

Primary (citable) accession number: P01127
Secondary accession number(s): P78431, Q6FHE7, Q9UF23

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.