PGFRB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PGFRB_MOUSE
• UniProt AC: P05622
• Protein Name: Platelet-derived growth factor receptor beta
• Gene Name: Pdgfrb
• Organism: Mus musculus (Mouse).
• Sequence Length: 1098
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
• Protein Description: Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM (By similarity). Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor..
• Protein Sequence: MGLPGVIPALVLRGQLLLSVLWLLGPQTSRGLVITPPGPEFVLNISSTFVLTCSGSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFTGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINISVIENGYVRLLETLGDVEIAELHRSRTLRVVFEAYPMPSVLWLKDNRTLGDSGAGELVLSTRNMSETRYVSELILVRVKVSEAGYYTMRAFHEDDEVQLSFKLQVNVPVRVLELSESHPANGEQTIRCRGRGMPQPNVTWSTCRDLKRCPRKLSPTPLGNSSKEESQLETNVTFWEEDQEYEVVSTLRLRHVDQPLSVRCMLQNSMGGDSQEVTVVPHSLPFKVVVISAILALVVLTVISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPVQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQRHSNKHCPPSAELYSNALPVGFSLPSHLNLTGESDGGYMDMSKDESIDYVPMLDMKGDIKYADIESPSYMAPYDNYVPSAPERTYRATLINDSPVLSYTDLVGFSYQVANGMDFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTYLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNDQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFETRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARFPGIHSLRSPLDTSSVLYTAVQPNESDNDYIIPLPDPKPDVADEGLPEGSPSLASSTLNEVNTSSTISCDSPLELQEEPQQAEPEAQLEQPQDSGCPGPLAEAEDSFL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	N-linked_Glycosylation	PGPEFVLNISSTFVL CCCCEEEEECCEEEE	27.13	-
88	N-linked_Glycosylation	SSVLTLTNVTGGDTG EEEEEEEECCCCCCC	32.25	-
102	N-linked_Glycosylation	GEYFCVYNNSLGPEL CCEEEEEECCCCCCH	15.95	-
214	N-linked_Glycosylation	SLQVSSINVSVNAVQ EEEEEEEEEEEEEEH	23.20	-
291	N-linked_Glycosylation	DSGTYTCNVSVSVND CCCEEEEEEEEEECC	22.69	-
306	N-linked_Glycosylation	HGDEKAINISVIENG CCCCEEEEEEEEECC	25.91	19656770
312	N-linked_Glycosylation	INISVIENGYVRLLE EEEEEEECCEEEHHH	35.65	19656770
353	N-linked_Glycosylation	SVLWLKDNRTLGDSG CEEEEECCCCCCCCC	36.93	-
370	N-linked_Glycosylation	ELVLSTRNMSETRYV EEEEEECCCCCCEEE	38.12	-
407	Phosphorylation	EDDEVQLSFKLQVNV CCCEEEEEEEEEECC	11.84	23140645
444	N-linked_Glycosylation	GRGMPQPNVTWSTCR CCCCCCCCCCHHHHH	38.31	-
467	N-linked_Glycosylation	LSPTPLGNSSKEESQ CCCCCCCCCCHHHHH	51.28	19656770
478	N-linked_Glycosylation	EESQLETNVTFWEED HHHHCEECEEEECCC	22.81	19656770
561	Phosphorylation	LWQKKPRYEIRWKVI HHHCCCCCEEEEEEE	25.00	-
570	Phosphorylation	IRWKVIESVSSDGHE EEEEEEEEECCCCCE	19.04	18515860
572	Phosphorylation	WKVIESVSSDGHEYI EEEEEEECCCCCEEE	31.80	18515860
573	Phosphorylation	KVIESVSSDGHEYIY EEEEEECCCCCEEEE	45.52	18515860
578	Phosphorylation	VSSDGHEYIYVDPVQ ECCCCCEEEEECCCC	7.59	11281646
580	Phosphorylation	SDGHEYIYVDPVQLP CCCCEEEEECCCCCC	9.63	11281646
588	Phosphorylation	VDPVQLPYDSTWELP ECCCCCCCCCCCCCC	30.99	18515860
644	Ubiquitination	STARSSEKQALMSEL HHCCCHHHHHHHHHH	42.70	-
677	Phosphorylation	CTKGGPIYIITEYCR HCCCCCEEEEECCCC	6.87	29514104
682	Phosphorylation	PIYIITEYCRYGDLV CEEEEECCCCCHHHH	3.58	29514104
685	Phosphorylation	IITEYCRYGDLVDYL EEECCCCCHHHHHHH	16.07	14993293
691	Phosphorylation	RYGDLVDYLHRNKHT CCHHHHHHHHHCCCC	9.27	18515860
704	Phosphorylation	HTFLQRHSNKHCPPS CCHHHHCCCCCCCCC	50.16	29514104
715	Phosphorylation	CPPSAELYSNALPVG CCCCHHHHCCCCCCC	7.44	-
739	Phosphorylation	TGESDGGYMDMSKDE CCCCCCCCCCCCCCC	8.75	17018529
747	Phosphorylation	MDMSKDESIDYVPML CCCCCCCCCCEEEEC	30.78	18515860
750	Phosphorylation	SKDESIDYVPMLDMK CCCCCCCEEEECCCC	12.56	18515860
761	Ubiquitination	LDMKGDIKYADIESP CCCCCCCCCCCCCCC	38.84	-
762	Phosphorylation	DMKGDIKYADIESPS CCCCCCCCCCCCCCC	15.16	18515860
767	Phosphorylation	IKYADIESPSYMAPY CCCCCCCCCCCCCCC	21.34	29514104
769	Phosphorylation	YADIESPSYMAPYDN CCCCCCCCCCCCCCC	36.50	18515860
770	Phosphorylation	ADIESPSYMAPYDNY CCCCCCCCCCCCCCC	10.73	18515860
774	Phosphorylation	SPSYMAPYDNYVPSA CCCCCCCCCCCCCCC	13.79	18515860
777	Phosphorylation	YMAPYDNYVPSAPER CCCCCCCCCCCCCCC	15.73	18515860
785	Phosphorylation	VPSAPERTYRATLIN CCCCCCCEEEEEEEC	18.72	29514104
840	Ubiquitination	ICEGKLVKICDFGLA EECCEEEEECCHHCH	48.32	-
854	Phosphorylation	ARDIMRDSNYISKGS HHHHHHCCCCCCCCC	22.59	25338131
855	Phosphorylation	RDIMRDSNYISKGST HHHHHCCCCCCCCCC	42.31	29514104
856	Phosphorylation	DIMRDSNYISKGSTY HHHHCCCCCCCCCCC	15.55	11281646
857	Phosphorylation	IMRDSNYISKGSTYL HHHCCCCCCCCCCCC	3.92	29514104
859	Ubiquitination	RDSNYISKGSTYLPL HCCCCCCCCCCCCCC	47.53	-
933	Phosphorylation	AHASDEIYEIMQKCW CCCCHHHHHHHHHHH	9.43	14993293
965	Phosphorylation	ERLLGEGYKKKYQQV HHHHCCHHHHHHHHH	18.48	29514104
969	Phosphorylation	GEGYKKKYQQVDEEF CCHHHHHHHHHCHHH	17.04	18515860
996	Phosphorylation	ARFPGIHSLRSPLDT CCCCCCCCCCCCCCC	24.45	26824392
1004	Phosphorylation	LRSPLDTSSVLYTAV CCCCCCCCCCEEEEE	20.37	25338131
1008	Phosphorylation	LDTSSVLYTAVQPNE CCCCCCEEEEECCCC	7.18	11940581
1016	Phosphorylation	TAVQPNESDNDYIIP EEECCCCCCCCEEEE	48.64	25338131
1020	Phosphorylation	PNESDNDYIIPLPDP CCCCCCCEEEECCCC	13.65	11940581

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
685	Y	Phosphorylation	Kinase	ABL1	P00520	Uniprot
685	Y	Phosphorylation	Kinase	ABL2	Q4JIM5	Uniprot
856	Y	Phosphorylation	Kinase	PDGFRB	P05622	PSP
856	Y	Phosphorylation	Kinase	PDGFRB	P05622	GPS
933	Y	Phosphorylation	Kinase	ABL1	P00520	Uniprot
933	Y	Phosphorylation	Kinase	ABL2	Q4JIM5	Uniprot
969	Y	Phosphorylation	Kinase	ABL1	P00520	Uniprot
969	Y	Phosphorylation	Kinase	ABL2	Q4JIM5	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Cbl	P22682	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PGFRB_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PGFRB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBL_MOUSE	Cbl	physical	15753096
CBL_MOUSE	Cbl	physical	18814181
PGFRB_MOUSE	Pdgfrb	physical	18505839
PLCG1_MOUSE	Plcg1	physical	9843497

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation.";
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.;
Mol. Cell. Proteomics 8:2555-2569(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-306; ASN-312; ASN-467 ANDASN-478, AND MASS SPECTROMETRY.
PubMed: 19656770

Phosphorylation

"Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor.";
Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.;
Mol. Cell. Biol. 24:2573-2583(2004).
Cited for: FUNCTION, AND PHOSPHORYLATION AT TYR-685; TYR-933 AND TYR-969.
PubMed: 14993293