CSPG4_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CSPG4_RAT
• UniProt AC: Q00657
• Protein Name: Chondroitin sulfate proteoglycan 4
• Gene Name: Cspg4
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 2326
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein ; Extracellular side . Apical cell membrane ; Single-pass type I membrane protein ; Extracellular side . Cell projection, lamellipodium membrane ; Single-pass type I membrane protein ; Extracellular side
• Protein Description: Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades..
• Protein Sequence: MLLSPGHPLSAPALALILTLALLVRSTAPASFFGENHLEVPVPSALTRVDLLLQFSTSQPEALLLLAAGQTDHLLLQLQSGHLQVRLALGQNELSLQTPADTVLSDSTTHTVVLTVSNSWAVLSVDGVLNTSAPIPKASHLKVPYGLFVGSSGSLDLPYLKGISRPLRGCLHSAILNGRNLLRPLTPDVHEGCAEEFSAGDEVGLGFSGPHSLAAFPAWSTREEGTLEFTLTTRSQQAPLAFQAGDKRGNFIYVDIFEGHLRAVVEKGQGTMLLRNSVPVADGQPHEVSVHIDVHRLEISVDQYPTRTFNRGVLSYLEPRGSLLLGGLDTEASRHLQEHRLGLTPGAANISLVGCIEDFSVNGRRLGLRDAWLTRDMAAGCRPEEDEYEEEVYGPFEAFSTLAPEAWPVMDLPEPCVPEPGLPAVFANFTQLLTISPLVVAEGGTAWLEWRHVQPTLDLTEAELRKSQVLFSVSQGARHGELELDIPGAQTRKMFTLLDVVNRKARFVHDGSEDTSDQLMLEVSVTSRAPVPSCLRRGQIYILPIQVNPVNDPPRIVFPHGSLMVILEHTQKPLGPEIFQAYDPDSACEGLTIQLLGVSASVPVEHRDQPGEPVTEFSCRDLEAGNIVYVHRGGPAQDLTFRVSDGMQASGPATLKVVAVRPAIQILHNTGLRLAQGSAAAILPANLSVETNAVGQDVSVLFRVTGTLQFGELQKQGAGGVEGTEWWDTLAFHQRDVEQGRVRYLSTDPQHHTQDTVEDLTLEVQVGQETLSNLSFPVTIQRATVWMLQLEPLHTQNPHQETLTSAHLEASLEEEGEGGPYPHIFHYELVQAPRRGNLLLQGTRLSDGQSFSQSDLQAGRVTYRATTRTSEAAEDSFRFRVTSPPHFSPLYTFPIHIGGDPNAPVLTNVLLMVPEGGEGVLSADHLFVKSLNSASYLYEVMEQPHHGSLAWRDPKGRATPVTSFTNEDLLHGRLVYQHDDSETIEDDIPFVATRQGEGSGDMAWEEVRGVFRVAIQPVNDHAPVQTISRVFHVARGGQRLLTTDDVAFSDADSGFSDAQLVLTRKDLLFGSIVAMEEPTRPIYRFTQEDLRKKQVLFVHSGADHGWLQLQVSDGQHQATAMLEVQASEPYLHVANSSSLVVPQGGQGTIDTAVLHLDTNLDIRSGNEVHYHVTAGPHWGQLLRDGQSVTSFSQRDLLDGAILYSHNGSLSPQDTLALSVAAGPVHTSTVLQVTIALEGPLAPLQLVQHKRIYVFQGEAAEIRRDQLEVVQEAVLPADIMFSLRSPPNAGYLVMVSHGASADGPPSLDPVQRFSQEAINSGRVLYLHSRPGAWSDSFSLDVASGLGDPLEGISVELEVLPTVIPLDVQNFSVPEGGTRTLAPPLIQITGPYLGTLPGLVLQVLEPPQHGALQKEDRPQDGTLSTFSWREVEEQLIRYVHDGSETQTDGFILLANASEMDRQSQPMAFTITILPVNDQPPVITTNTGLQIWEGAIVPIPPEALRGIDSDSGPEDLVYTIEQPSNGRIALRVAPDAEAHRFTQAQLDSGLVLFSHRGALEGGFHFDLSDGVHTSPGHFFRVVAQKQVLLSLEGSRKLTVCPESVQPLSSQSLSASSSTGSDPRHLLYQVVRGPQLGRLLHAQQGSAEEALVNFTQAEVNAGNILYEHEISSEPFWEAHDTIGLLLSSSPARDLAATLAVTVSFDAACPQRPSRLWRNKGLWVPEGQRAKITVAALDAANLLASVPASQRGRHDVLFQITQFPTRGQLLVSEEPLHARRPHFLQSELTAGQLVYAHGGGGTQQDGFRFRAHLQGPTGASVAGPQTSEAFVITVRDVNERPPQPQASIPLRITRGSRAPVSRAQLSVVDPDSAPGEIEYEVQRAPHNGFLSLAGDNTGPVTHFTQADVDAGRLAFVANGSSVAGVFQLSMSDGASPPIPMSLAVDVLPSTIEVQLRAPLEVPQALGRSSLSRQQLQVISDREEPDVAYRLTQGPLYGQVLVGGQPASAFSQLQVDQGDVVFAFTNFSSSQDHFKVLALARGVNASATVNVTVQALLHVWAGGPWPQGTTLRLDPTVLDASELANRTGSMPRFRLLEGPRYGRVVRVSQGRAESRTNQLVEDFTQQDLEEGRLGLEVGRPEGRSTGPTGDRLTLELQATGVPPAVALLDFATEPYHAAKFYKVTLLSVPEAARTETEKTGKSTPTGQPGQAASSPMPTVAKSGFLGFLEANMFSVIIPVCLVLLLLALILPLLFYLRKRNKTGKHDVQVLTAKPRNGLAGDTETFRKVEPGQAIPLTTVPGQGPPPGGQPDPELLQFCRTPNPALRNGQYWV

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
130	N-linked_Glycosylation	LSVDGVLNTSAPIPK EEECCEECCCCCCCC	29.58	-
349	N-linked_Glycosylation	GLTPGAANISLVGCI CCCCCCCCEEEEEEE	24.69	-
428	N-linked_Glycosylation	GLPAVFANFTQLLTI CCCCCCCCCCCCEEC	29.09	-
686	N-linked_Glycosylation	AAAILPANLSVETNA EEEEEECCEEEECCC	30.80	-
773	N-linked_Glycosylation	VGQETLSNLSFPVTI ECCCHHHCCCCCEEE	42.70	-
999	O-linked_Glycosylation	ATRQGEGSGDMAWEE EEECCCCCCCCHHHH	27.58	11493670
1086	Phosphorylation	TRPIYRFTQEDLRKK CCCCEECCHHHHHHC	23.27	24259510
1135	N-linked_Glycosylation	EPYLHVANSSSLVVP CCEEEECCCCCEEEC	41.14	-
1189	Phosphorylation	LRDGQSVTSFSQRDL CCCCCCCCCCHHHHC	29.33	27097102
1190	Phosphorylation	RDGQSVTSFSQRDLL CCCCCCCCCHHHHCC	22.27	27097102
1192	Phosphorylation	GQSVTSFSQRDLLDG CCCCCCCHHHHCCCC	24.87	27097102
1206	N-linked_Glycosylation	GAILYSHNGSLSPQD CCEEEEECCCCCHHH	35.49	-
1368	N-linked_Glycosylation	VIPLDVQNFSVPEGG EEECCCCCCCCCCCC	30.89	-
1453	N-linked_Glycosylation	DGFILLANASEMDRQ CCEEEEEEHHHCCCC	43.92	-
1649	N-linked_Glycosylation	SAEEALVNFTQAEVN CHHHHHHHHHHHHHH	34.79	-
1913	N-linked_Glycosylation	GRLAFVANGSSVAGV CCEEEEECCCCEEEE	45.65	-
2020	N-linked_Glycosylation	DVVFAFTNFSSSQDH CEEEEEECCCCCCCH	28.48	-
2038	N-linked_Glycosylation	LALARGVNASATVNV HHHHCCCCCCCEECH	30.88	-
2044	N-linked_Glycosylation	VNASATVNVTVQALL CCCCCEECHHHHHHH	21.27	-
2079	N-linked_Glycosylation	LDASELANRTGSMPR ECHHHHHHHCCCCCC	55.46	-
2190	Phosphorylation	PEAARTETEKTGKST CHHHCCCCCCCCCCC	42.01	16641100
2207	Phosphorylation	GQPGQAASSPMPTVA CCCCCCCCCCCCCCH	37.68	16641100
2208	Phosphorylation	QPGQAASSPMPTVAK CCCCCCCCCCCCCHH	22.08	16641100
2256	Phosphorylation	YLRKRNKTGKHDVQV HHHHHCCCCCCCEEE	55.82	17591920
2265	Phosphorylation	KHDVQVLTAKPRNGL CCCEEEEEECCCCCC	33.50	17591920
2314	Phosphorylation	ELLQFCRTPNPALRN HHHHHHCCCCHHHCC	28.71	17591920

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
2256	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
2256	T	Phosphorylation	Kinase	PRKCA	P05696	Uniprot
2265	T	Phosphorylation	Kinase	MAPK1	P63085	GPS
2314	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
2314	T	Phosphorylation	Kinase	ERK2	P63085	PSP
2314	T	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CSPG4_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CSPG4_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MPDZ_RAT	Mpdz	physical	10967549

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

O-linked Glycosylation

"Chondroitin sulfate and cytoplasmic domain-dependent membranetargeting of the NG2 proteoglycan promotes retraction fiber formationand cell polarization.";
Stallcup W.B., Dahlin-Huppe K.;
J. Cell Sci. 114:2315-2325(2001).
Cited for: MUTAGENESIS OF SER-999 AND SER-1342, SUBCELLULAR LOCATION,GLYCOSYLATION AT SER-999, AND FUNCTION.
PubMed: 11493670

Phosphorylation

"Phosphorylation of NG2 proteoglycan by protein kinase C-alpharegulates polarized membrane distribution and cell motility.";
Makagiansar I.T., Williams S., Dahlin-Huppe K., Fukushi J.,Mustelin T., Stallcup W.B.;
J. Biol. Chem. 279:55262-55270(2004).
Cited for: PHOSPHORYLATION AT THR-2256, INTERACTION WITH PRKCA, SUBCELLULARLOCATION, MUTAGENESIS OF THR-2256; THR-2265 AND THR-2278, ANDFUNCTION.
PubMed: 15504744