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Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Proto-oncogene c-Sis) (Becaplermin)

 PDGFB_HUMAN             Reviewed;         241 AA.
P01127; G3XAG8; P78431; Q15354; Q6FHE7; Q9UF23;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 209.
RecName: Full=Platelet-derived growth factor subunit B;
Short=PDGF subunit B;
AltName: Full=PDGF-2;
AltName: Full=Platelet-derived growth factor B chain;
AltName: Full=Platelet-derived growth factor beta polypeptide;
AltName: Full=Proto-oncogene c-Sis;
AltName: INN=Becaplermin;
Flags: Precursor;
Name=PDGFB; Synonyms=PDGF2, SIS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6740330; DOI=10.1126/science.6740330;
Josephs S.F., Ratner L., Clarke M.F., Westin E.H., Reitz M.S.,
Wong-Staal F.;
"Transforming potential of human c-sis nucleotide sequences encoding
platelet-derived growth factor.";
Science 225:636-639(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=4033772; DOI=10.1038/316748a0;
Collins T., Ginsburg D., Boss J.M., Orkin S.H., Pober J.S.;
"Cultured human endothelial cells express platelet-derived growth
factor B chain: cDNA cloning and structural analysis.";
Nature 316:748-750(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2991848; DOI=10.1093/nar/13.14.5007;
Ratner L., Josephs S.F., Jarrett R., Reitz M.S., Wong-Staal F.;
"Nucleotide sequence of transforming human c-sis cDNA clones with
homology to platelet-derived growth factor.";
Nucleic Acids Res. 13:5007-5018(1985).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3472769;
Rao C.D., Igarashi H., Pech M.W., Robbins K.C., Aaronson S.A.;
"Oncogenic potential of the human platelet-derived growth factor
transcriptional unit.";
Cold Spring Harb. Symp. Quant. Biol. 51:959-966(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3517869; DOI=10.1073/pnas.83.8.2392;
Rao C.D., Igarashi H., Chiu I.-M., Robbins K.C., Aaronson S.A.;
"Structure and sequence of the human c-sis/platelet-derived growth
factor 2 (SIS/PDGF2) transcriptional unit.";
Proc. Natl. Acad. Sci. U.S.A. 83:2392-2396(1986).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Lung, Pancreas, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-185 (ISOFORM 2).
TISSUE=Choriocarcinoma;
PubMed=7659502; DOI=10.1093/nar/23.15.2815;
Dirks R.P.H., Onnekink C., Jansen H.J., de Jong A., Bloemers H.P.J.;
"A novel human c-sis mRNA species is transcribed from a promoter in c-
sis intron 1 and contains the code for an alternative PDGF B-like
protein.";
Nucleic Acids Res. 23:2815-2822(1995).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53, AND CHROMOSOMAL
TRANSLOCATION WITH COL1A1.
PubMed=8988177; DOI=10.1038/ng0197-95;
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.;
"Deregulation of the platelet-derived growth factor B-chain gene via
fusion with collagen gene COL1A1 in dermatofibrosarcoma protuberans
and giant-cell fibroblastoma.";
Nat. Genet. 15:95-98(1997).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-241.
PubMed=6327048; DOI=10.1016/0092-8674(84)90307-6;
Chiu I.-M., Reddy E.P., Givol D., Robbins K.C., Tronick S.R.,
Aaronson S.A.;
"Nucleotide sequence analysis identifies the human c-sis proto-
oncogene as a structural gene for platelet-derived growth factor.";
Cell 37:123-129(1984).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 26-241 (ISOFORM 1).
PubMed=3456904; DOI=10.1016/0014-5793(86)80433-1;
Weich H.A., Sebald W., Schairer H.U., Hoppe J.;
"The human osteosarcoma cell line U-2 OS expresses a 3.8 kilobase mRNA
which codes for the sequence of the PDGF-B chain.";
FEBS Lett. 198:344-348(1986).
[15]
PROTEIN SEQUENCE OF 82-112.
PubMed=6306471; DOI=10.1038/304035a0;
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.;
"Platelet-derived growth factor is structurally related to the
putative transforming protein p28sis of simian sarcoma virus.";
Nature 304:35-39(1983).
[16]
PROTEIN SEQUENCE OF 82-110.
PubMed=6844921; DOI=10.1126/science.6844921;
Antoniades H.N., Hunkapiller M.W.;
"Human platelet-derived growth factor (PDGF): amino-terminal amino
acid sequence.";
Science 220:963-965(1983).
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-200, AND PARTIAL PROTEIN
SEQUENCE.
PubMed=6329745;
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.;
"The c-sis gene encodes a precursor of the B chain of platelet-derived
growth factor.";
EMBO J. 3:921-928(1984).
[18]
MUTAGENESIS, AND IMPORTANCE OF ARG-108 AND ILE-111 FOR RECEPTOR
BINDING.
PubMed=1661670;
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.;
"Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate
receptor binding and activation.";
EMBO J. 10:4113-4120(1991).
[19]
INTERCHAIN DISULFIDE BONDS.
PubMed=1317862;
Andersson M., Oestman A., Baeckstroem G., Hellman U.,
George-Nascimento C., Westermark B., Heldin C.-H.;
"Assignment of interchain disulfide bonds in platelet-derived growth
factor (PDGF) and evidence for agonist activity of monomeric PDGF.";
J. Biol. Chem. 267:11260-11266(1992).
[20]
TISSUE SPECIFICITY.
PubMed=11331882; DOI=10.1038/35074593;
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.;
"PDGF D, a novel protease-activated growth factor.";
Nat. Cell Biol. 3:517-521(2001).
[21]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH COL1A1.
PubMed=12660034; DOI=10.1016/S0165-4608(02)00844-0;
Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.;
"Dermatofibrosarcoma protuberans of breast.";
Cancer Genet. Cytogenet. 142:56-59(2003).
[22]
CHARACTERIZATION OF VARIANTS IBGC5 ARG-9 AND PRO-119, AND FUNCTION.
PubMed=26599395; DOI=10.1371/journal.pone.0143407;
Vanlandewijck M., Lebouvier T., Andaloussi Maee M., Nahar K.,
Hornemann S., Kenkel D., Cunha S.I., Lennartsson J., Boss A.,
Heldin C.H., Keller A., Betsholtz C.;
"Functional characterization of germline mutations in PDGFB and PDGFRB
in primary familial brain calcification.";
PLoS ONE 10:E0143407-E0143407(2015).
[23]
REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE.
PubMed=18483217; DOI=10.1101/gad.1653708;
Andrae J., Gallini R., Betsholtz C.;
"Role of platelet-derived growth factors in physiology and medicine.";
Genes Dev. 22:1276-1312(2008).
[24]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=1396586;
Oefner C., D'Arcy A., Winkler F.K., Eggimann B., Hosang M.;
"Crystal structure of human platelet-derived growth factor BB.";
EMBO J. 11:3921-3926(1992).
[25]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-185 IN COMPLEX WITH
PDGFRB, SUBUNIT, AND DISULFIDE BONDS.
PubMed=20534510; DOI=10.1073/pnas.1000806107;
Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.;
"Structures of a platelet-derived growth factor/propeptide complex and
a platelet-derived growth factor/receptor complex.";
Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010).
[26]
VARIANTS IBGC5 ARG-9 AND PRO-119.
PubMed=23913003; DOI=10.1038/ng.2723;
Keller A., Westenberger A., Sobrido M.J., Garcia-Murias M.,
Domingo A., Sears R.L., Lemos R.R., Ordonez-Ugalde A., Nicolas G.,
da Cunha J.E., Rushing E.J., Hugelshofer M., Wurnig M.C., Kaech A.,
Reimann R., Lohmann K., Dobricic V., Carracedo A., Petrovic I.,
Miyasaki J.M., Abakumova I., Mae M.A., Raschperger E., Zatz M.,
Zschiedrich K., Klepper J., Spiteri E., Prieto J.M., Navas I.,
Preuss M., Dering C., Jankovic M., Paucar M., Svenningsson P.,
Saliminejad K., Khorshid H.R., Novakovic I., Aguzzi A., Boss A.,
Le Ber I., Defer G., Hannequin D., Kostic V.S., Campion D.,
Geschwind D.H., Coppola G., Betsholtz C., Klein C., Oliveira J.R.;
"Mutations in the gene encoding PDGF-B cause brain calcifications in
humans and mice.";
Nat. Genet. 45:1077-1082(2013).
-!- 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 (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).
{ECO:0000250|UniProtKB:P31240, ECO:0000269|PubMed:26599395}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1554925, EBI-1554925;
P16234:PDGFRA; NbExp=11; IntAct=EBI-1554925, EBI-2861522;
P09619:PDGFRB; NbExp=13; IntAct=EBI-1554925, EBI-641237;
-!- SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon
wounding.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1;
IsoId=P01127-1; Sequence=Displayed;
Name=2;
IsoId=P01127-2; Sequence=VSP_044913;
-!- 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. {ECO:0000269|PubMed:11331882}.
-!- DISEASE: Basal ganglia calcification, idiopathic, 5 (IBGC5)
[MIM:615483]: A 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.
{ECO:0000269|PubMed:23913003, ECO:0000269|PubMed:26599395}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving PDGFB is found in
dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13)
with PDGFB. {ECO:0000269|PubMed:12660034}.
-!- PHARMACEUTICAL: Available under the name Regranex (Ortho-McNeil).
Used to promote healing in diabetic neuropathic foot ulcers.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PDGFBID155.html";
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EMBL; K01401; AAA60552.1; -; Genomic_DNA.
EMBL; K01918; AAA60552.1; JOINED; Genomic_DNA.
EMBL; J00121; AAA60552.1; JOINED; Genomic_DNA.
EMBL; K01398; AAA60552.1; JOINED; Genomic_DNA.
EMBL; K01399; AAA60552.1; JOINED; Genomic_DNA.
EMBL; K01400; AAA60552.1; JOINED; Genomic_DNA.
EMBL; X02811; CAA26579.1; -; mRNA.
EMBL; X02744; CAA26524.1; -; mRNA.
EMBL; M12783; AAA60553.1; -; mRNA.
EMBL; CR456538; CAG30424.1; -; mRNA.
EMBL; Z81010; CAB02635.1; -; Genomic_DNA.
EMBL; Z81010; CAP58849.1; -; Genomic_DNA.
EMBL; CR541807; CAG46606.1; -; mRNA.
EMBL; CH471095; EAW60306.1; -; Genomic_DNA.
EMBL; CH471095; EAW60307.1; -; Genomic_DNA.
EMBL; BC029822; AAH29822.1; -; mRNA.
EMBL; BC077725; AAH77725.1; -; mRNA.
EMBL; X83705; CAA58679.1; -; mRNA.
EMBL; X98706; CAA67262.1; -; Genomic_DNA.
EMBL; K01917; AAA98793.1; -; Genomic_DNA.
EMBL; K01913; AAA98793.1; JOINED; Genomic_DNA.
EMBL; K01914; AAA98793.1; JOINED; Genomic_DNA.
EMBL; K01915; AAA98793.1; JOINED; Genomic_DNA.
EMBL; K01916; AAA98793.1; JOINED; Genomic_DNA.
EMBL; X03702; CAA27333.1; -; mRNA.
EMBL; X00561; CAA25228.1; -; Genomic_DNA.
EMBL; X00561; CAA25229.1; -; Genomic_DNA.
CCDS; CCDS13987.1; -. [P01127-1]
CCDS; CCDS33650.1; -. [P01127-2]
PIR; A94276; PFHUG2.
RefSeq; NP_002599.1; NM_002608.3. [P01127-1]
RefSeq; NP_148937.1; NM_033016.3. [P01127-2]
UniGene; Hs.1976; -.
PDB; 1PDG; X-ray; 3.00 A; A/B/C=82-190.
PDB; 3MJG; X-ray; 2.30 A; A/B=21-185.
PDB; 4HQU; X-ray; 2.20 A; A=82-190.
PDB; 4HQX; X-ray; 2.30 A; A=82-183.
PDB; 4QCI; X-ray; 2.30 A; C/D=82-190.
PDBsum; 1PDG; -.
PDBsum; 3MJG; -.
PDBsum; 4HQU; -.
PDBsum; 4HQX; -.
PDBsum; 4QCI; -.
ProteinModelPortal; P01127; -.
SMR; P01127; -.
BioGrid; 111181; 91.
DIP; DIP-5737N; -.
IntAct; P01127; 6.
STRING; 9606.ENSP00000330382; -.
BindingDB; P01127; -.
ChEMBL; CHEMBL3108633; -.
iPTMnet; P01127; -.
PhosphoSitePlus; P01127; -.
UniCarbKB; P01127; -.
BioMuta; PDGFB; -.
DMDM; 129724; -.
PaxDb; P01127; -.
PeptideAtlas; P01127; -.
PRIDE; P01127; -.
TopDownProteomics; P01127-2; -. [P01127-2]
DNASU; 5155; -.
Ensembl; ENST00000331163; ENSP00000330382; ENSG00000100311. [P01127-1]
Ensembl; ENST00000381551; ENSP00000370963; ENSG00000100311. [P01127-2]
GeneID; 5155; -.
KEGG; hsa:5155; -.
UCSC; uc003axe.4; human. [P01127-1]
CTD; 5155; -.
DisGeNET; 5155; -.
GeneCards; PDGFB; -.
HGNC; HGNC:8800; PDGFB.
HPA; CAB011604; -.
HPA; CAB018341; -.
HPA; HPA011972; -.
MalaCards; PDGFB; -.
MIM; 190040; gene.
MIM; 607907; phenotype.
MIM; 615483; phenotype.
neXtProt; NX_P01127; -.
OpenTargets; ENSG00000100311; -.
Orphanet; 1980; Bilateral striopallidodentate calcinosis.
Orphanet; 31112; Dermatofibrosarcoma protuberans.
Orphanet; 263662; Familial multiple meningioma.
PharmGKB; PA33145; -.
eggNOG; ENOG410IJ45; Eukaryota.
eggNOG; ENOG410XWTB; LUCA.
GeneTree; ENSGT00510000046755; -.
HOGENOM; HOG000286027; -.
HOVERGEN; HBG053546; -.
InParanoid; P01127; -.
KO; K17386; -.
OMA; QGDPIPE; -.
OrthoDB; EOG091G0LNU; -.
PhylomeDB; P01127; -.
TreeFam; TF319554; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLink; P01127; -.
SIGNOR; P01127; -.
ChiTaRS; PDGFB; human.
EvolutionaryTrace; P01127; -.
GeneWiki; PDGFB; -.
GenomeRNAi; 5155; -.
PMAP-CutDB; P01127; -.
PRO; PR:P01127; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100311; -.
CleanEx; HS_PDGFB; -.
ExpressionAtlas; P01127; baseline and differential.
Genevisible; P01127; HS.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL.
GO; GO:0005518; F:collagen binding; IDA:MGI.
GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0048407; F:platelet-derived growth factor binding; IPI:BHF-UCL.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; IDA:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:BHF-UCL.
GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; ISS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0072255; P:metanephric glomerular mesangial cell development; ISS:UniProtKB.
GO; GO:0002548; P:monocyte chemotaxis; IDA:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; IDA:BHF-UCL.
GO; GO:0010544; P:negative regulation of platelet activation; IDA:BHF-UCL.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; TAS:Reactome.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1905064; P:negative regulation of vascular smooth muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0038001; P:paracrine signaling; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0090280; P:positive regulation of calcium ion import; IDA:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0003104; P:positive regulation of glomerular filtration; ISS:UniProtKB.
GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IDA:UniProtKB.
GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:2000591; P:positive regulation of metanephric mesenchymal cell migration; IDA:UniProtKB.
GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; IDA:UniProtKB.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:1905176; P:positive regulation of vascular smooth muscle cell dedifferentiation; IDA:BHF-UCL.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0070528; P:protein kinase C signaling; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0009611; P:response to wounding; IDA:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR023581; PD_growth_factor_CS.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR006782; PDGF_N.
InterPro; IPR015583; PDGF_suB.
PANTHER; PTHR11633:SF9; PTHR11633:SF9; 1.
Pfam; PF00341; PDGF; 1.
Pfam; PF04692; PDGF_N; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00249; PDGF_1; 1.
PROSITE; PS50278; PDGF_2; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Chromosomal rearrangement;
Cleavage on pair of basic residues; Complete proteome;
Developmental protein; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Growth factor; Mitogen; Pharmaceutical;
Polymorphism; Proto-oncogene; Reference proteome; Secreted; Signal.
SIGNAL 1 20
PROPEP 21 81 Removed in mature form.
/FTId=PRO_0000023371.
CHAIN 82 190 Platelet-derived growth factor subunit B.
/FTId=PRO_0000023372.
PROPEP 191 241 Removed in mature form.
/FTId=PRO_0000023373.
SITE 108 108 Involved in receptor binding.
SITE 111 111 Involved in receptor binding.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 97 141 {ECO:0000269|PubMed:20534510}.
DISULFID 124 124 Interchain.
{ECO:0000269|PubMed:20534510}.
DISULFID 130 178 {ECO:0000269|PubMed:20534510}.
DISULFID 133 133 Interchain.
{ECO:0000269|PubMed:20534510}.
DISULFID 134 180 {ECO:0000269|PubMed:20534510}.
VAR_SEQ 1 21 MNRCWALFLSLCCYLRLVSAE -> MFIMGL (in
isoform 2). {ECO:0000303|PubMed:7659502}.
/FTId=VSP_044913.
VARIANT 9 9 L -> R (in IBGC5; loss of protein
expression).
{ECO:0000269|PubMed:23913003,
ECO:0000269|PubMed:26599395}.
/FTId=VAR_070870.
VARIANT 88 88 I -> V (in dbSNP:rs17565).
/FTId=VAR_014578.
VARIANT 119 119 L -> P (in IBGC5; loss of protein
expression; dbSNP:rs397515632).
{ECO:0000269|PubMed:23913003,
ECO:0000269|PubMed:26599395}.
/FTId=VAR_070871.
CONFLICT 101 101 T -> E (in Ref. 16; AA sequence).
{ECO:0000305}.
CONFLICT 105 105 E -> C (in Ref. 16; AA sequence).
{ECO:0000305}.
CONFLICT 107 107 S -> C (in Ref. 16; AA sequence).
{ECO:0000305}.
STRAND 97 105 {ECO:0000244|PDB:4HQU}.
HELIX 108 111 {ECO:0000244|PDB:4HQU}.
STRAND 118 121 {ECO:0000244|PDB:4HQU}.
STRAND 123 131 {ECO:0000244|PDB:4HQU}.
STRAND 140 159 {ECO:0000244|PDB:4HQU}.
STRAND 162 181 {ECO:0000244|PDB:4HQU}.
SEQUENCE 241 AA; 27283 MW; 9F9A3474CE203C0B CRC64;
MNRCWALFLS LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHG DPGEEDGAEL
DLNMTRSHSG GELESLARGR RSLGSLTIAE PAMIAECKTR TEVFEISRRL IDRTNANFLV
WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC
ETVAAARPVT RSPGGSQEQR AKTPQTRVTI RTVRVRRPPK GKHRKFKHTH DKTALKETLG
A


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