PDGFB_HUMAN
ID PDGFB_HUMAN Reviewed; 241 AA.
AC P01127; G3XAG8; P78431; Q15354; Q6FHE7; Q9UF23;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 245.
DE RecName: Full=Platelet-derived growth factor subunit B;
DE Short=PDGF subunit B;
DE AltName: Full=PDGF-2;
DE AltName: Full=Platelet-derived growth factor B chain;
DE AltName: Full=Platelet-derived growth factor beta polypeptide;
DE AltName: Full=Proto-oncogene c-Sis;
DE AltName: INN=Becaplermin;
DE Flags: Precursor;
GN Name=PDGFB; Synonyms=PDGF2, SIS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6740330; DOI=10.1126/science.6740330;
RA Josephs S.F., Ratner L., Clarke M.F., Westin E.H., Reitz M.S.,
RA Wong-Staal F.;
RT "Transforming potential of human c-sis nucleotide sequences encoding
RT platelet-derived growth factor.";
RL Science 225:636-639(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=4033772; DOI=10.1038/316748a0;
RA Collins T., Ginsburg D., Boss J.M., Orkin S.H., Pober J.S.;
RT "Cultured human endothelial cells express platelet-derived growth factor B
RT chain: cDNA cloning and structural analysis.";
RL Nature 316:748-750(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2991848; DOI=10.1093/nar/13.14.5007;
RA Ratner L., Josephs S.F., Jarrett R., Reitz M.S., Wong-Staal F.;
RT "Nucleotide sequence of transforming human c-sis cDNA clones with homology
RT to platelet-derived growth factor.";
RL Nucleic Acids Res. 13:5007-5018(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3472769; DOI=10.1101/sqb.1986.051.01.109;
RA Rao C.D., Igarashi H., Pech M.W., Robbins K.C., Aaronson S.A.;
RT "Oncogenic potential of the human platelet-derived growth factor
RT transcriptional unit.";
RL Cold Spring Harb. Symp. Quant. Biol. 51:959-966(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3517869; DOI=10.1073/pnas.83.8.2392;
RA Rao C.D., Igarashi H., Chiu I.-M., Robbins K.C., Aaronson S.A.;
RT "Structure and sequence of the human c-sis/platelet-derived growth factor 2
RT (SIS/PDGF2) transcriptional unit.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2392-2396(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, Pancreas, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-185 (ISOFORM 2).
RC TISSUE=Choriocarcinoma;
RX PubMed=7659502; DOI=10.1093/nar/23.15.2815;
RA Dirks R.P.H., Onnekink C., Jansen H.J., de Jong A., Bloemers H.P.J.;
RT "A novel human c-sis mRNA species is transcribed from a promoter in c-sis
RT intron 1 and contains the code for an alternative PDGF B-like protein.";
RL Nucleic Acids Res. 23:2815-2822(1995).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53, AND CHROMOSOMAL TRANSLOCATION
RP WITH COL1A1.
RX PubMed=8988177; DOI=10.1038/ng0197-95;
RA Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F.,
RA Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D., Blin N.,
RA Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I., Guilbaud C.,
RA Dumanski J.P.;
RT "Deregulation of the platelet-derived growth factor B-chain gene via fusion
RT with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell
RT fibroblastoma.";
RL Nat. Genet. 15:95-98(1997).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-241.
RX PubMed=6327048; DOI=10.1016/0092-8674(84)90307-6;
RA Chiu I.-M., Reddy E.P., Givol D., Robbins K.C., Tronick S.R.,
RA Aaronson S.A.;
RT "Nucleotide sequence analysis identifies the human c-sis proto-oncogene as
RT a structural gene for platelet-derived growth factor.";
RL Cell 37:123-129(1984).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-241 (ISOFORM 1).
RX PubMed=3456904; DOI=10.1016/0014-5793(86)80433-1;
RA Weich H.A., Sebald W., Schairer H.U., Hoppe J.;
RT "The human osteosarcoma cell line U-2 OS expresses a 3.8 kilobase mRNA
RT which codes for the sequence of the PDGF-B chain.";
RL FEBS Lett. 198:344-348(1986).
RN [15]
RP PROTEIN SEQUENCE OF 82-112.
RX PubMed=6306471; DOI=10.1038/304035a0;
RA Waterfield M.D., Scrace G.T., Whittle N., Stroobant P., Johnsson A.,
RA Wasteson A., Westermark B., Heldin C.H., Huang J.S., Deuel T.F.;
RT "Platelet-derived growth factor is structurally related to the putative
RT transforming protein p28sis of simian sarcoma virus.";
RL Nature 304:35-39(1983).
RN [16]
RP PROTEIN SEQUENCE OF 82-110.
RX PubMed=6844921; DOI=10.1126/science.6844921;
RA Antoniades H.N., Hunkapiller M.W.;
RT "Human platelet-derived growth factor (PDGF): amino-terminal amino acid
RT sequence.";
RL Science 220:963-965(1983).
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-200, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=6329745; DOI=10.1002/j.1460-2075.1984.tb01908.x;
RA Johnsson A., Heldin C.H., Wasteson A., Westermark B., Deuel T.F.,
RA Huang J.S., Seeburg P.H., Gray A., Ullrich A., Scrace G., Stroobant P.,
RA Waterfield M.D.;
RT "The c-sis gene encodes a precursor of the B chain of platelet-derived
RT growth factor.";
RL EMBO J. 3:921-928(1984).
RN [18]
RP MUTAGENESIS, AND IMPORTANCE OF ARG-108 AND ILE-111 FOR RECEPTOR BINDING.
RX PubMed=1661670; DOI=10.1002/j.1460-2075.1991.tb04988.x;
RA Clements J.M., Bawden L.J., Bloxidge R.E., Catlin G., Cook A.L., Craig S.,
RA Drummond A.H., Edwards R.M., Fallon A., Green D.R., Hellewell P.G.,
RA Kirwin P.M., Nayee P.D., Richardson S.J., Brown D., Chahwala S.B.,
RA Snarey M., Winslow D.;
RT "Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor
RT binding and activation.";
RL EMBO J. 10:4113-4120(1991).
RN [19]
RP INTERCHAIN DISULFIDE BONDS.
RX PubMed=1317862; DOI=10.1016/s0021-9258(19)49905-5;
RA Andersson M., Oestman A., Baeckstroem G., Hellman U., George-Nascimento C.,
RA Westermark B., Heldin C.-H.;
RT "Assignment of interchain disulfide bonds in platelet-derived growth factor
RT (PDGF) and evidence for agonist activity of monomeric PDGF.";
RL J. Biol. Chem. 267:11260-11266(1992).
RN [20]
RP TISSUE SPECIFICITY.
RX PubMed=11331882; DOI=10.1038/35074593;
RA LaRochelle W.J., Jeffers M., McDonald W.F., Chillakuru R.A., Giese N.A.,
RA Lokker N.A., Sullivan C., Boldog F.L., Yang M., Vernet C., Burgess C.E.,
RA Fernandez E., Deegler L.L., Rittman B., Shimkets J., Shimkets R.A.,
RA Rothberg J.M., Lichenstein H.S.;
RT "PDGF D, a novel protease-activated growth factor.";
RL Nat. Cell Biol. 3:517-521(2001).
RN [21]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH COL1A1.
RX PubMed=12660034; DOI=10.1016/s0165-4608(02)00844-0;
RA Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.;
RT "Dermatofibrosarcoma protuberans of breast.";
RL Cancer Genet. Cytogenet. 142:56-59(2003).
RN [22]
RP INTERACTION WITH LRP1 AND SORL1.
RX PubMed=15053742; DOI=10.1042/bj20040149;
RA Gliemann J., Hermey G., Nykjaer A., Petersen C.M., Jacobsen C.,
RA Andreasen P.A.;
RT "The mosaic receptor sorLA/LR11 binds components of the plasminogen-
RT activating system and platelet-derived growth factor-BB similarly to LRP1
RT (low-density lipoprotein receptor-related protein), but mediates slow
RT internalization of bound ligand.";
RL Biochem. J. 381:203-212(2004).
RN [23]
RP INTERACTION WITH SORL1.
RX PubMed=16393139; DOI=10.1042/bj20051364;
RA Hermey G., Sjoegaard S.S., Petersen C.M., Nykjaer A., Gliemann J.;
RT "Tumour necrosis factor alpha-converting enzyme mediates ectodomain
RT shedding of Vps10p-domain receptor family members.";
RL Biochem. J. 395:285-293(2006).
RN [24]
RP CHARACTERIZATION OF VARIANTS IBGC5 ARG-9 AND PRO-119, AND FUNCTION.
RX PubMed=26599395; DOI=10.1371/journal.pone.0143407;
RA Vanlandewijck M., Lebouvier T., Andaloussi Maee M., Nahar K., Hornemann S.,
RA Kenkel D., Cunha S.I., Lennartsson J., Boss A., Heldin C.H., Keller A.,
RA Betsholtz C.;
RT "Functional characterization of germline mutations in PDGFB and PDGFRB in
RT primary familial brain calcification.";
RL PLoS ONE 10:E0143407-E0143407(2015).
RN [25]
RP REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE.
RX PubMed=18483217; DOI=10.1101/gad.1653708;
RA Andrae J., Gallini R., Betsholtz C.;
RT "Role of platelet-derived growth factors in physiology and medicine.";
RL Genes Dev. 22:1276-1312(2008).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=1396586; DOI=10.1002/j.1460-2075.1992.tb05485.x;
RA Oefner C., D'Arcy A., Winkler F.K., Eggimann B., Hosang M.;
RT "Crystal structure of human platelet-derived growth factor BB.";
RL EMBO J. 11:3921-3926(1992).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-185 IN COMPLEX WITH PDGFRB,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=20534510; DOI=10.1073/pnas.1000806107;
RA Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.;
RT "Structures of a platelet-derived growth factor/propeptide complex and a
RT platelet-derived growth factor/receptor complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010).
RN [28]
RP VARIANTS IBGC5 ARG-9 AND PRO-119.
RX PubMed=23913003; DOI=10.1038/ng.2723;
RA Keller A., Westenberger A., Sobrido M.J., Garcia-Murias M., Domingo A.,
RA Sears R.L., Lemos R.R., Ordonez-Ugalde A., Nicolas G., da Cunha J.E.,
RA Rushing E.J., Hugelshofer M., Wurnig M.C., Kaech A., Reimann R.,
RA Lohmann K., Dobricic V., Carracedo A., Petrovic I., Miyasaki J.M.,
RA Abakumova I., Mae M.A., Raschperger E., Zatz M., Zschiedrich K.,
RA Klepper J., Spiteri E., Prieto J.M., Navas I., Preuss M., Dering C.,
RA Jankovic M., Paucar M., Svenningsson P., Saliminejad K., Khorshid H.R.,
RA Novakovic I., Aguzzi A., Boss A., Le Ber I., Defer G., Hannequin D.,
RA Kostic V.S., Campion D., Geschwind D.H., Coppola G., Betsholtz C.,
RA Klein C., Oliveira J.R.;
RT "Mutations in the gene encoding PDGF-B cause brain calcifications in humans
RT and mice.";
RL Nat. Genet. 45:1077-1082(2013).
CC -!- FUNCTION: Growth factor that plays an essential role in the regulation
CC of embryonic development, cell proliferation, cell migration, survival
CC and chemotaxis. Potent mitogen for cells of mesenchymal origin
CC (PubMed:26599395). Required for normal proliferation and recruitment of
CC pericytes and vascular smooth muscle cells in the central nervous
CC system, skin, lung, heart and placenta. Required for normal blood
CC vessel development, and for normal development of kidney glomeruli.
CC Plays an important role in wound healing. Signaling is modulated by the
CC formation of heterodimers with PDGFA (By similarity).
CC {ECO:0000250|UniProtKB:P31240, ECO:0000269|PubMed:26599395}.
CC -!- SUBUNIT: Antiparallel homodimer; disulfide-linked. Antiparallel
CC heterodimer with PDGFA; disulfide-linked. The PDGFB homodimer interacts
CC with PDGFRA and PDGFRB homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB
CC interacts with PDGFRB homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. Interacts with XLKD1 (By similarity). Interacts with
CC LRP1 (PubMed:15053742). Interacts with SORL1 (via the N-terminal
CC ectodomain) (PubMed:15053742, PubMed:16393139). {ECO:0000250,
CC ECO:0000269|PubMed:15053742, ECO:0000269|PubMed:16393139}.
CC -!- INTERACTION:
CC P01127; Q9P287: BCCIP; NbExp=3; IntAct=EBI-1554925, EBI-711154;
CC P01127; P01127: PDGFB; NbExp=3; IntAct=EBI-1554925, EBI-1554925;
CC P01127; P16234: PDGFRA; NbExp=11; IntAct=EBI-1554925, EBI-2861522;
CC P01127; P09619: PDGFRB; NbExp=16; IntAct=EBI-1554925, EBI-641237;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon
CC wounding.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=P01127-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P01127-2; Sequence=VSP_044913;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the heart, brain
CC (sustantia nigra), placenta and fetal kidney. Expressed at moderate
CC levels in the brain (hippocampus), skeletal muscle, kidney and lung.
CC {ECO:0000269|PubMed:11331882}.
CC -!- DISEASE: Basal ganglia calcification, idiopathic, 5 (IBGC5)
CC [MIM:615483]: A form of basal ganglia calcification, an autosomal
CC dominant condition characterized by symmetric calcification in the
CC basal ganglia and other brain regions. Affected individuals can either
CC be asymptomatic or show a wide spectrum of neuropsychiatric symptoms,
CC including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis,
CC seizures, and chronic headache. Serum levels of calcium, phosphate,
CC alkaline phosphatase and parathyroid hormone are normal. The
CC neuropathological hallmark of the disease is vascular and pericapillary
CC calcification, mainly of calcium phosphate, in the affected brain
CC areas. {ECO:0000269|PubMed:23913003, ECO:0000269|PubMed:26599395}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving PDGFB is found in
CC dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with
CC PDGFB. {ECO:0000269|PubMed:12660034}.
CC -!- PHARMACEUTICAL: Available under the name Regranex (Ortho-McNeil). Used
CC to promote healing in diabetic neuropathic foot ulcers.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PDGFBID155.html";
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DR EMBL; K01401; AAA60552.1; -; Genomic_DNA.
DR EMBL; K01918; AAA60552.1; JOINED; Genomic_DNA.
DR EMBL; J00121; AAA60552.1; JOINED; Genomic_DNA.
DR EMBL; K01398; AAA60552.1; JOINED; Genomic_DNA.
DR EMBL; K01399; AAA60552.1; JOINED; Genomic_DNA.
DR EMBL; K01400; AAA60552.1; JOINED; Genomic_DNA.
DR EMBL; X02811; CAA26579.1; -; mRNA.
DR EMBL; X02744; CAA26524.1; -; mRNA.
DR EMBL; M12783; AAA60553.1; -; mRNA.
DR EMBL; CR456538; CAG30424.1; -; mRNA.
DR EMBL; Z81010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR541807; CAG46606.1; -; mRNA.
DR EMBL; CH471095; EAW60306.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60307.1; -; Genomic_DNA.
DR EMBL; BC029822; AAH29822.1; -; mRNA.
DR EMBL; BC077725; AAH77725.1; -; mRNA.
DR EMBL; X83705; CAA58679.1; -; mRNA.
DR EMBL; X98706; CAA67262.1; -; Genomic_DNA.
DR EMBL; K01917; AAA98793.1; -; Genomic_DNA.
DR EMBL; K01913; AAA98793.1; JOINED; Genomic_DNA.
DR EMBL; K01914; AAA98793.1; JOINED; Genomic_DNA.
DR EMBL; K01915; AAA98793.1; JOINED; Genomic_DNA.
DR EMBL; K01916; AAA98793.1; JOINED; Genomic_DNA.
DR EMBL; X03702; CAA27333.1; -; mRNA.
DR EMBL; X00561; CAA25228.1; -; Genomic_DNA.
DR EMBL; X00561; CAA25229.1; -; Genomic_DNA.
DR CCDS; CCDS13987.1; -. [P01127-1]
DR CCDS; CCDS33650.1; -. [P01127-2]
DR PIR; A94276; PFHUG2.
DR RefSeq; NP_002599.1; NM_002608.3. [P01127-1]
DR RefSeq; NP_148937.1; NM_033016.3. [P01127-2]
DR PDB; 1PDG; X-ray; 3.00 A; A/B/C=82-190.
DR PDB; 3MJG; X-ray; 2.30 A; A/B=21-185.
DR PDB; 4HQU; X-ray; 2.20 A; A=82-190.
DR PDB; 4HQX; X-ray; 2.30 A; A=82-183.
DR PDB; 4QCI; X-ray; 2.30 A; C/D=82-190.
DR PDB; 6T9E; X-ray; 2.99 A; CCC/DDD=82-190.
DR PDBsum; 1PDG; -.
DR PDBsum; 3MJG; -.
DR PDBsum; 4HQU; -.
DR PDBsum; 4HQX; -.
DR PDBsum; 4QCI; -.
DR PDBsum; 6T9E; -.
DR AlphaFoldDB; P01127; -.
DR SMR; P01127; -.
DR BioGRID; 111181; 93.
DR ComplexPortal; CPX-1875; Platelet-derived growth factor AB complex.
DR ComplexPortal; CPX-1876; Platelet-derived growth factor BB complex.
DR ComplexPortal; CPX-2882; PDGF receptor beta - PDGF-BB complex.
DR ComplexPortal; CPX-2883; PDGF receptor alpha-beta - PDGF-BB complex.
DR ComplexPortal; CPX-2884; PDGF receptor alpha - PDGF-BB complex.
DR ComplexPortal; CPX-2885; PDGF receptor alpha - PDGF-AB complex.
DR ComplexPortal; CPX-2886; PDGF receptor beta - PDGF-AB complex.
DR ComplexPortal; CPX-2892; PDGF receptor alpha-beta - PDGF-AB complex.
DR CORUM; P01127; -.
DR DIP; DIP-5737N; -.
DR IntAct; P01127; 64.
DR STRING; 9606.ENSP00000330382; -.
DR BindingDB; P01127; -.
DR ChEMBL; CHEMBL3108633; -.
DR DrugBank; DB06325; Pegpleranib.
DR GlyConnect; 754; 4 N-Linked glycans (1 site).
DR GlyGen; P01127; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; P01127; -.
DR PhosphoSitePlus; P01127; -.
DR BioMuta; PDGFB; -.
DR DMDM; 129724; -.
DR MassIVE; P01127; -.
DR PaxDb; P01127; -.
DR PeptideAtlas; P01127; -.
DR PRIDE; P01127; -.
DR ProteomicsDB; 33745; -.
DR ProteomicsDB; 51325; -. [P01127-1]
DR TopDownProteomics; P01127-2; -. [P01127-2]
DR ABCD; P01127; 9 sequenced antibodies.
DR Antibodypedia; 293; 728 antibodies from 41 providers.
DR DNASU; 5155; -.
DR Ensembl; ENST00000331163.11; ENSP00000330382.6; ENSG00000100311.17. [P01127-1]
DR Ensembl; ENST00000381551.8; ENSP00000370963.4; ENSG00000100311.17. [P01127-2]
DR GeneID; 5155; -.
DR KEGG; hsa:5155; -.
DR MANE-Select; ENST00000331163.11; ENSP00000330382.6; NM_002608.4; NP_002599.1.
DR UCSC; uc003axe.4; human. [P01127-1]
DR CTD; 5155; -.
DR DisGeNET; 5155; -.
DR GeneCards; PDGFB; -.
DR GeneReviews; PDGFB; -.
DR HGNC; HGNC:8800; PDGFB.
DR HPA; ENSG00000100311; Low tissue specificity.
DR MalaCards; PDGFB; -.
DR MIM; 190040; gene.
DR MIM; 607907; phenotype.
DR MIM; 615483; phenotype.
DR neXtProt; NX_P01127; -.
DR OpenTargets; ENSG00000100311; -.
DR Orphanet; 1980; Bilateral striopallidodentate calcinosis.
DR Orphanet; 31112; Dermatofibrosarcoma protuberans.
DR Orphanet; 263662; Familial multiple meningioma.
DR Orphanet; 2495; Meningioma.
DR PharmGKB; PA33145; -.
DR VEuPathDB; HostDB:ENSG00000100311; -.
DR eggNOG; ENOG502S2VW; Eukaryota.
DR GeneTree; ENSGT00940000157367; -.
DR HOGENOM; CLU_094438_0_0_1; -.
DR InParanoid; P01127; -.
DR OMA; ACKCETI; -.
DR OrthoDB; 1439735at2759; -.
DR PhylomeDB; P01127; -.
DR TreeFam; TF319554; -.
DR PathwayCommons; P01127; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; P01127; -.
DR SIGNOR; P01127; -.
DR BioGRID-ORCS; 5155; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; PDGFB; human.
DR EvolutionaryTrace; P01127; -.
DR GeneWiki; PDGFB; -.
DR GenomeRNAi; 5155; -.
DR Pharos; P01127; Tbio.
DR PRO; PR:P01127; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P01127; protein.
DR Bgee; ENSG00000100311; Expressed in olfactory bulb and 187 other tissues.
DR ExpressionAtlas; P01127; baseline and differential.
DR Genevisible; P01127; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:1990265; C:platelet-derived growth factor complex; IPI:ComplexPortal.
DR GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IPI:BHF-UCL.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; IDA:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISS:BHF-UCL.
DR GO; GO:0001892; P:embryonic placenta development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0072255; P:metanephric glomerular mesangial cell development; ISS:UniProtKB.
DR GO; GO:0002548; P:monocyte chemotaxis; IDA:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0010544; P:negative regulation of platelet activation; IDA:BHF-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1905064; P:negative regulation of vascular associated smooth muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0038001; P:paracrine signaling; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:BHF-UCL.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0003104; P:positive regulation of glomerular filtration; ISS:UniProtKB.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IDA:UniProtKB.
DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:2000591; P:positive regulation of metanephric mesenchymal cell migration; IDA:UniProtKB.
DR GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; IDA:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:BHF-UCL.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1905176; P:positive regulation of vascular associated smooth muscle cell dedifferentiation; IDA:BHF-UCL.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IDA:UniProtKB.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IDA:UniProtKB.
DR GO; GO:0070528; P:protein kinase C signaling; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IDA:BHF-UCL.
DR CDD; cd00135; PDGF; 1.
DR DisProt; DP02770; -.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR006782; PDGF_N.
DR InterPro; IPR015583; PDGF_suB.
DR PANTHER; PTHR11633:SF2; PTHR11633:SF2; 1.
DR Pfam; PF00341; PDGF; 1.
DR Pfam; PF04692; PDGF_N; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00249; PDGF_1; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Chromosomal rearrangement;
KW Cleavage on pair of basic residues; Developmental protein;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Growth factor; Mitogen; Pharmaceutical; Proto-oncogene; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT PROPEP 21..81
FT /note="Removed in mature form"
FT /id="PRO_0000023371"
FT CHAIN 82..190
FT /note="Platelet-derived growth factor subunit B"
FT /id="PRO_0000023372"
FT PROPEP 191..241
FT /note="Removed in mature form"
FT /id="PRO_0000023373"
FT REGION 216..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 108
FT /note="Involved in receptor binding"
FT SITE 111
FT /note="Involved in receptor binding"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..141
FT /evidence="ECO:0000269|PubMed:20534510"
FT DISULFID 124
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:20534510"
FT DISULFID 130..178
FT /evidence="ECO:0000269|PubMed:20534510"
FT DISULFID 133
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:20534510"
FT DISULFID 134..180
FT /evidence="ECO:0000269|PubMed:20534510"
FT VAR_SEQ 1..21
FT /note="MNRCWALFLSLCCYLRLVSAE -> MFIMGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7659502"
FT /id="VSP_044913"
FT VARIANT 9
FT /note="L -> R (in IBGC5; loss of protein expression)"
FT /evidence="ECO:0000269|PubMed:23913003,
FT ECO:0000269|PubMed:26599395"
FT /id="VAR_070870"
FT VARIANT 88
FT /note="I -> V (in dbSNP:rs17565)"
FT /id="VAR_014578"
FT VARIANT 119
FT /note="L -> P (in IBGC5; loss of protein expression;
FT dbSNP:rs397515632)"
FT /evidence="ECO:0000269|PubMed:23913003,
FT ECO:0000269|PubMed:26599395"
FT /id="VAR_070871"
FT CONFLICT 101
FT /note="T -> E (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="E -> C (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> C (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:4HQU"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:4HQU"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:4HQU"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:4HQU"
FT STRAND 140..159
FT /evidence="ECO:0007829|PDB:4HQU"
FT STRAND 162..181
FT /evidence="ECO:0007829|PDB:4HQU"
SQ 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
