CSPG4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CSPG4_MOUSE
• UniProt AC: Q8VHY0
• Protein Name: Chondroitin sulfate proteoglycan 4
• Gene Name: Cspg4
• Organism: Mus musculus (Mouse).
• Sequence Length: 2327
• 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: MLLGPGHPLSAPALALALTLALLVRSTAPASFFGENHLEVPVPSALTRVDLLLQFSTSQPEALLLLAAGQDDHLLLQLHSGCLQVRLALGQKELKLQTPADTVLSDSAPHTVVLTVSDSWAVLSVDGVLNTSAPIPRASHLKATYGLFVGSSGSLDLPYLKGISRPLRGCLHSAILNGRNLLRPLTSDVHEGCAEEFSAGDEVGLGFSGPHSLAAFPAWSTREEGTLEFTLTTRSQQAPLAFQAGDKRGNFIYVDIFEGHLRAVVEKGQGTMLLRNSVPVADGQPHEVSVHIDVHRLEISVDQYPTRTFNRGVLSYLEPRGSLLLGGLDTEASRHLQEHRLGLAPGAANISLVGCIEDFSVNGRRQGLRDAWLTRDMSAGCRPEEDEYEEEVYGPYETFSTLAPEAWPAMELPEPCIPEPGLPAVFANFTQLLTISPLVVAEGGTAWLEWRHVQPTLDLTEAELRKSQVLFSVSQSARHGDLELDILGAQTRKMFTLLDVVNRKARFVHDGSEDTSDQLMLEVSVTARAPVPSCLRRGQIYILPIQVNPVNDPPRIIFPHGSLMVILEHTQKPLGPEIFQAYDPDSACEGLTFQLLGVSSGVPVEHRDQPGEPATEFSCRELEVGDIVYVHRGGPAQDLTFRVSDGMQASAPATLKVVAVRPAIQILHNTGLHLAQGSAAAILPANLSVETNAVGQDVSVLFRVTGTLQFGELQKQGAGGVEGTEWWDTLAFHQRDVEQGRVRYLSTDPQHHTQDTVEDLILEVQVGQETLSNLSFPVTIQRATVWMLRLEPLHTQNPHQETLTPAHLEASLEEEEEEGSPQPHTFHYELVQAPRRGNLLLQGTRLSDGESFSQSDLQAGRVTYRATMRTSEAADDSFRFRVTSPPHFSPLYTFPIHIGGDPNAPVLTNVLLMVPEGGEGVLSADHLFVKSLNSASYLYEVMEQPHHGKLAWRDPKGKSTPVTSFTNEDLLHGRLVYQHDDSETIEDDIPFVATRQGEGSGDMAWEEVRGVFRVAIQPVNDHAPVQTISRVFHVARGGQRLLTTDDVAFSDADSGFSDAQLVLTRKDLLFGSIVAMEEPTRPIYRFTQEDLRKKQVLFVHSGADHGWLQLQVSDGQHQATAMLEVQASEPYLHVANSSSLVVPQGGQGTIDTAVLQLDTNLDIRSGNEVHYHVTAGPQWGQLLRDGQSVTSFSQRDLLDGAILYSHNGSLSPQDTLAFSVAAGPVHTNTFLQVTIALEGPLAPLQLVQHKKIYVFQGEAAEIRRDQLEVVQEAVLPADIMFSLRSPPNAGYLVMVSHGASAEEPPSLDPVQSFSQEAVNSGRVLYLHSRPGAWSDSFSLDVASGLGDPLEGISVELEVLPTVIPLDVQNFSVPEGGTRTLAPPLVQITGPYFPTLPGLVLQVLEPPQHGALQKEDHSQDGSLSTFSWREVEEQLIRYVHDGSETQTDAFVLLANASEMDRQSQPVAFTITILPVNDQPPVLTTNTGLQIWEGAIVPIPPEALRGTDNDSGPEDLVYTIEQPSNGRIALRVAPDTEVHRFTQAQLDSGLVLFSHRGALEGGFHFDLSDGAHTSPGHFFRVVAQKQALLSLEGTRKLTVCPESVQPLSSQSLSASSSTGADPRHLLYRVVRGPQLGRLLHAQQGSAEEVLVNFTQAEVNAGNILYEHEMSSEPFWEAHDTIGLLLSSPPARDLAATLAVMVSFDAACPQRPSRLWKNKGLWVPEGQRAKITVAALDAANLLASVPASQRSRHDVLFQVTQFPTRGQLLVSEEPLHARRPYFLQSELAAGQLVYAHGGGGTQQDGFRFRAHLQGPTGTSVAGPQTSEAFVITVRDVNERPPQPQASIPLRVTRGSRAPVSRAQLSVVDPDSAPGEIEYEVQRAPHNGFLSLAGDNTGPVTHFTQADVDAGRLAFVANGSSVAGVFQLSMSDGASPPIPMSLAVDVLPSTIEVQLRAPLEVPQALGRTSLSRQQLQVISDREEPDVAYRLTQGPLYGQLLVGGQPASAFSQLQVDQGDVVFVFTNFSSSQDHFKVVALARGVNASATVNVTVQALLHVWAGGPWPQGTTLRLDPTVLDASELANRTGSMPHFRLLAGPRYGRVVRVSQGRTESRSNQLVEHFTQRDLEEGQLGLEVGKPEGRSTGPAGDRLTLELWAKGVPPAVALLDFATEPYHAAKSYSVALLSVPEAVRTETEKPGRSVPTGQPGQAASSPVPTAAKGGFLGFLEANMFSIIIPVCLILLLLALILPLLFYLRKRNKTGKHDVQVLTAKPRNGLAGDTETFRKVEPGQAIPLITVPGQGPPPGGQPDPELLQFCRTPNPALRNGQYWV

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	LSVDGVLNTSAPIPR EEECCEECCCCCCCC	29.58	19656770
349	N-linked_Glycosylation	GLAPGAANISLVGCI CCCCCCCEEEEEEEE	24.69	-
428	N-linked_Glycosylation	GLPAVFANFTQLLTI CCCCHHCCCCCCEEC	29.09	-
686	N-linked_Glycosylation	AAAILPANLSVETNA EEEEEECCEEEECCC	30.80	-
773	N-linked_Glycosylation	VGQETLSNLSFPVTI CCCHHHHCCCCCEEE	42.70	-
1000	O-linked_Glycosylation	ATRQGEGSGDMAWEE EEECCCCCCCCHHHH	27.58	-
1136	N-linked_Glycosylation	EPYLHVANSSSLVVP CCEEEECCCCCEEEC	41.14	-
1207	N-linked_Glycosylation	GAILYSHNGSLSPQD CCEEEEECCCCCHHH	35.49	-
1285	Phosphorylation	DIMFSLRSPPNAGYL HEEEEECCCCCCCEE	50.42	23649490
1291	Phosphorylation	RSPPNAGYLVMVSHG CCCCCCCEEEEEECC	8.16	26160508
1296	Phosphorylation	AGYLVMVSHGASAEE CCEEEEEECCCCCCC	9.71	28638064
1300	Phosphorylation	VMVSHGASAEEPPSL EEEECCCCCCCCCCC	40.58	24453211
1306	Phosphorylation	ASAEEPPSLDPVQSF CCCCCCCCCCCCCCC	57.00	23649490
1312	Phosphorylation	PSLDPVQSFSQEAVN CCCCCCCCCCHHHHH	27.40	23649490
1369	N-linked_Glycosylation	VIPLDVQNFSVPEGG EEECCCCCCCCCCCC	30.89	19656770
1454	N-linked_Glycosylation	DAFVLLANASEMDRQ HEEEEEECHHHCCCC	43.92	19656770
1505	Phosphorylation	PPEALRGTDNDSGPE CHHHHCCCCCCCCCC	25.79	26525534
1509	Phosphorylation	LRGTDNDSGPEDLVY HCCCCCCCCCCCEEE	63.60	26525534
1592	Phosphorylation	ALLSLEGTRKLTVCP HHHHCCCCCCEEECC	18.43	28059163
1650	N-linked_Glycosylation	SAEEVLVNFTQAEVN CHHHHEEEEEHHEEH	30.04	-
1829	Phosphorylation	TSEAFVITVRDVNER CCCEEEEEEEECCCC	12.27	-
1914	N-linked_Glycosylation	GRLAFVANGSSVAGV CCEEEEECCCCEEEE	45.65	-
2021	N-linked_Glycosylation	DVVFVFTNFSSSQDH CEEEEEECCCCCCCC	24.28	19656770
2039	N-linked_Glycosylation	VALARGVNASATVNV EEEECCCCCCCEECH	30.88	-
2045	N-linked_Glycosylation	VNASATVNVTVQALL CCCCCEECHHHHHHH	21.27	-
2080	N-linked_Glycosylation	LDASELANRTGSMPH ECHHHHHHHHCCCCC	55.46	19656770
2257	Phosphorylation	YLRKRNKTGKHDVQV HHHHHCCCCCCCEEE	55.82	-
2315	Phosphorylation	ELLQFCRTPNPALRN HHHHHHCCCCHHHCC	28.71	26824392
2325	Phosphorylation	PALRNGQYWV----- HHHCCCCCCC-----	14.99	29514104

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
2257	T	Phosphorylation	Kinase	PRKCA	P20444	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CSPG4_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 CSPG4_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CSPG4_MOUSE !!

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-130; ASN-1369; ASN-1454;ASN-2021 AND ASN-2080, AND MASS SPECTROMETRY.
PubMed: 19656770