Reviewed, UniProtKB/Swiss-Prot P16234 (PGFRA_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-type platelet-derived growth factor receptor
    EC=2.7.10.1
Alternative name(s):
    PDGF-R-alpha
    CD140 antigen-like family member A
    CD140a antigen
    CD_antigen=CD140a

Gene names

Name:

PDGFRA

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	1089 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	Receptor that binds both PDGFA and PDGFB and has a tyrosine-protein kinase activity.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Homodimer, and heterodimer with PDGFRB. Interacts with the SH2 domain of SHB via phosphorylated Tyr-720 By similarity. Interacts with the SH2 domain of SHF via phosphorylated Tyr-720.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in primary and metastatic colon tumors and in normal colon tissue. Tumors may express a different isoform to that found in normal tissue.
Involvement in disease	A fusion of PDGFRA and FIP1L1 (FIP1L1-PDGFRA), due to an interstitial chromosomal deletion, is the cause of some cases of hypereosinophilic syndrome (HES) [MIM:607685]. HES is a rare hematologic disorder characterized by sustained overproduction of eosinophils in the bone marrow, eosinophilia, tissue infiltration and organ damage. Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. Contains 5 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell activation Traceable author statement. Source: UniProtKB peptidyl-tyrosine phosphorylation Ref.2 Inferred from direct assay. Source: UniProtKB platelet-derived growth factor receptor signaling pathway Ref.2 Inferred from direct assay. Source: UniProtKB positive regulation of DNA replication Inferred from direct assay. Source: UniProtKB positive regulation of cell migration Inferred from direct assay. Source: UniProtKB positive regulation of fibroblast proliferation Inferred from direct assay. Source: UniProtKB protein amino acid autophosphorylation Ref.2 Inferred from direct assay. Source: UniProtKB
Cellular component	integral to plasma membrane Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Ref.2 Inferred by curator. Source: UniProtKB platelet-derived growth factor alpha-receptor activity Ref.2 Inferred from direct assay. Source: UniProtKB platelet-derived growth factor binding Ref.2 Inferred from physical interaction. Source: UniProtKB platelet-derived growth factor receptor binding Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB vascular endothelial growth factor receptor activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P16234-1)

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.

Isoform 2 (identifier: P16234-2)

The sequence of this isoform differs from the canonical sequence as follows:
     210-218: ATSELDLEM → GTCIISFLL
     219-1089: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23
	Chain	24 – 1089	1066	Alpha-type platelet-derived growth factor receptor		PRO_0000016760
Regions
	Topological domain	24 – 524	501	Extracellular Potential
	Transmembrane	525 – 549	25	Potential
	Topological domain	550 – 1089	540	Cytoplasmic Potential
	Domain	24 – 113	90	Ig-like C2-type 1
	Domain	117 – 201	85	Ig-like C2-type 2
	Domain	202 – 306	105	Ig-like C2-type 3
	Domain	319 – 410	92	Ig-like C2-type 4
	Domain	414 – 517	104	Ig-like C2-type 5
	Domain	593 – 954	362	Protein kinase
	Nucleotide binding	599 – 607	9	ATP By similarity
	Compositional bias	1041 – 1087	47	Ser-rich
Sites
	Active site	818	1	Proton acceptor By similarity
	Binding site	627	1	ATP By similarity
	Site	578 – 579	2	Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein
Amino acid modifications
	Modified residue	720	1	Phosphotyrosine Probable
	Modified residue	762	1	Phosphotyrosine Ref.10
	Modified residue	768	1	Phosphotyrosine Ref.10
	Modified residue	849	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1018	1	Phosphotyrosine Ref.10
	Glycosylation	42	1	N-linked (GlcNAc...) Potential
	Glycosylation	76	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
	Glycosylation	353	1	N-linked (GlcNAc...) Potential
	Glycosylation	359	1	N-linked (GlcNAc...) Potential
	Glycosylation	458	1	N-linked (GlcNAc...) Potential
	Glycosylation	468	1	N-linked (GlcNAc...) Potential
	Disulfide bond	49 ↔ 100		By similarity
	Disulfide bond	150 ↔ 189		By similarity
	Disulfide bond	235 ↔ 290		By similarity
	Disulfide bond	435 ↔ 501		By similarity
Natural variations
	Alternative sequence	210 – 218	9	ATSELDLEM → GTCIISFLL in isoform 2.		VSP_007833
	Alternative sequence	219 – 1089	871	Missing in isoform 2.		VSP_007834
	Natural variant	79	1	G → D: dbSNP rs36035373. Ref.12		VAR_042032
	Natural variant	426	1	G → D Ref.12		VAR_042033
	Natural variant	478	1	S → P: dbSNP rs35597368. Ref.12 Ref.4		VAR_034378
	Natural variant	764	1	R → C Ref.12		VAR_042034
	Natural variant	829	1	G → R in a glioblastoma multiforme sample; somatic mutation. Ref.12		VAR_042035
	Natural variant	996	1	E → K in a metastatic melanoma sample; somatic mutation. Ref.12		VAR_042036
	Natural variant	1071	1	D → N in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.12		VAR_042037

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 5E3FB9940ACD1BE8	FASTA	1,089	122,670
	10 20 30 40 50 60 MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP 70 80 90 100 110 120 MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY 130 140 150 160 170 180 VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG 190 200 210 220 230 240 TFTVGPYICE ATVKGKKFQT IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN 250 260 270 280 290 300 EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK 310 320 330 340 350 360 EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL KNNLTLIENL 370 380 390 400 410 420 TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED AVKSYTFELL TQVPSSILDL 430 440 450 460 470 480 VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC KDIKKCNNET SWTILANNVS NIITEIHSRD 490 500 510 520 530 540 RSTVEGRVTF AKVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII 550 560 570 580 590 600 SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG 610 620 630 640 650 660 SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL 670 680 690 700 710 720 LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK PKKELDIFGL NPADESTRSY 730 740 750 760 770 780 VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN 790 800 810 820 830 840 LLSDDNSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA 850 860 870 880 890 900 RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM 910 920 930 940 950 960 VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV ENLLPGQYKK 970 980 990 1000 1010 1020 SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII 1030 1040 1050 1060 1070 1080 PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL
	Isoform 2. Checksum: E8144A73DFD069BF	FASTA	218	24,023
	10 20 30 40 50 60 MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP 70 80 90 100 110 120 MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY 130 140 150 160 170 180 VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG 190 200 210 TFTVGPYICE ATVKGKKFQT IPFNVYALKG TCIISFLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity to the B-type PDGF receptor." Claesson-Welsh L., Eriksson A., Westermark B., Heldin C.H. Proc. Natl. Acad. Sci. U.S.A. 86:4917-4921(1989) [PubMed: 2544881] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Foreskin.
[2]	"Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes." Matsui T., Heidaran M., Miki T., Popescu N., la Rochelle W., Kraus M., Pierce J., Aaronson S. Science 243:800-804(1989) [PubMed: 2536956] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Structure, organization, and transcription units of the human alpha-platelet-derived growth factor receptor gene, PDGFRA." Kawagishi J., Ku T. Genomics 30:224-232(1995) [PubMed: 8586421] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-478. Tissue: Trachea.
[5]	"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] (ISOFORM 2). Tissue: Placenta.
[6]	"Discovery of a fusion kinase in EOL-1 cells and idiopathic hypereosinophilic syndrome." Griffin J.H., Leung J., Bruner R.J., Caligiuri M.A., Briesewitz R. Proc. Natl. Acad. Sci. U.S.A. 100:7830-7835(2003) [PubMed: 12808148] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 579-1089, DISEASE, IDENTIFICATION BY MASS SPECTROMETRY OF FIP1L1-PDGFRA FUSION PROTEIN. Tissue: Eosinophil.
[7]	"Receptor tyrosine kinases expressed in metastatic colon cancer." Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., Srivastava S., Varnum B., Liu E.T., Cance W.G. Int. J. Cancer 60:791-797(1995) [PubMed: 7896447] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 823-876, TISSUE SPECIFICITY. Tissue: Colon tumor.
[8]	"Shf, a Shb-like adapter protein, is involved in PDGF-alpha-receptor regulation of apoptosis." Lindholm C.K., Frantz J.D., Shoelson S.E., Welsh M. Biochem. Biophys. Res. Commun. 278:537-543(2000) [PubMed: 11095946] [Abstract] Cited for: INTERACTION WITH SHF, PROBABLE PHOSPHORYLATION AT TYR-720.
[9]	"A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a therapeutic target of imatinib in idiopathic hypereosinophilic syndrome." Cools J., DeAngelo D.J., Gotlib J., Stover E.H., Legare R.D., Cortes J., Kutok J., Clark J., Galinsky I., Griffin J.D., Cross N.C., Tefferi A., Malone J., Alam R., Schrier S.L., Schmid J., Rose M., Vandenberghe P. , Verhoef G., Boogaerts M., Wlodarska I., Kantarjian H., Marynen P., Coutre S.E., Stone R., Gilliland D.G. N. Engl. J. Med. 348:1201-1214(2003) [PubMed: 12660384] [Abstract] Cited for: INVOLVEMENT IN HES.
[10]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-762; TYR-768; TYR-849 AND TYR-1018, MASS SPECTROMETRY.
[11]	"Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors." Karthikeyan S., Leung T., Ladias J.A.A. J. Biol. Chem. 277:18973-18978(2002) [PubMed: 11882663] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1185-1189 IN COMPLEX WITH SLC9A3R1 AND PDGFRB.
[12]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-79; ASP-426; PRO-478; CYS-764; ARG-829; LYS-996 AND ASN-1071.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M22734 mRNA. Translation: AAA60048.1.
M21574 mRNA. Translation: AAA96715.1.
D50017 Genomic DNA. Translation: BAA08742.1.
AK316578 mRNA. Translation: BAG38166.1.
BC015186 mRNA. Translation: AAH15186.1.
AY229892 mRNA. Translation: AAP69563.1. Different initiation.

IPI

IPI00027721.
IPI00336178.

PIR

PFHUGA. A40162.

RefSeq

NP_006197.1.

UniGene

Hs.74615

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQ5	X-ray	2.20

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5736N.

PTM databases

PhosphoSite

P16234.

Proteomic databases

PRIDE

P16234.

Genome annotation databases

Ensembl

ENSG00000134853. Homo sapiens. [Contig view]

GeneID

5156.

KEGG

hsa:5156.

Organism-specific databases

GeneCards

GC04P054806.

H-InvDB

HIX0004218.

HGNC

HGNC:8803. PDGFRA.

HPA

CAB018143.

MIM

173490. gene.
607685. phenotype.

Orphanet

44890. Gastrointestinal stromal tumor.
3260. Idiopathic hypereosinophilic syndrome.
513. Leukemia, lymphoblastic, acute.

PharmGKB

PA33147.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P16234.

HOVERGEN

P16234.

OMA

P16234. VARMRVD.

Enzyme and pathway databases

BRENDA

2.7.10.1. 247.

Pathway_Interaction_DB

pdgfrapathway. PDGFR-alpha signaling pathway.

Gene expression databases

ArrayExpress

P16234.

Bgee

P16234.

CleanEx

HS_PDGFRA.

GermOnline

ENSG00000134853. Homo sapiens.

Family and domain databases

InterPro

IPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR015776. Platelet-der_grow_fac_rcpt_a.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001824. Recept_tyr_kinase-III_CS.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR016243. TyrPK_CSF1-R.
IPR009134. VEGFR_N.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 2 hits.

PANTHER

PTHR23256:SF207. PDGFR_alpha. 1 hit.

Pfam

PF07679. I-set. 1 hit.
PF00047. ig. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000615. TyrPK_CSF1-R. 1 hit.

PRINTS

PR01832. VEGFRECEPTOR.

ProDom

PD000001. Prot_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00102. Becaplermin.
DB00619. Imatinib.
DB01268. Sunitinib.

NextBio

19946.

SOURCE

Search...

Entry information

Entry name

PGFRA_HUMAN

Accession

Primary (citable) accession number: P16234
Secondary accession number(s): B2RE69, Q96KZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)