CSPG4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CSPG4_HUMAN
• UniProt AC: Q6UVK1
• Protein Name: Chondroitin sulfate proteoglycan 4
• Gene Name: CSPG4
• Organism: Homo sapiens (Human).
• Sequence Length: 2322
• 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: MQSGPRPPLPAPGLALALTLTMLARLASAASFFGENHLEVPVATALTDIDLQLQFSTSQPEALLLLAAGPADHLLLQLYSGRLQVRLVLGQEELRLQTPAETLLSDSIPHTVVLTVVEGWATLSVDGFLNASSAVPGAPLEVPYGLFVGGTGTLGLPYLRGTSRPLRGCLHAATLNGRSLLRPLTPDVHEGCAEEFSASDDVALGFSGPHSLAAFPAWGTQDEGTLEFTLTTQSRQAPLAFQAGGRRGDFIYVDIFEGHLRAVVEKGQGTVLLHNSVPVADGQPHEVSVHINAHRLEISVDQYPTHTSNRGVLSYLEPRGSLLLGGLDAEASRHLQEHRLGLTPEATNASLLGCMEDLSVNGQRRGLREALLTRNMAAGCRLEEEEYEDDAYGHYEAFSTLAPEAWPAMELPEPCVPEPGLPPVFANFTQLLTISPLVVAEGGTAWLEWRHVQPTLDLMEAELRKSQVLFSVTRGARHGELELDIPGAQARKMFTLLDVVNRKARFIHDGSEDTSDQLVLEVSVTARVPMPSCLRRGQTYLLPIQVNPVNDPPHIIFPHGSLMVILEHTQKPLGPEVFQAYDPDSACEGLTFQVLGTSSGLPVERRDQPGEPATEFSCRELEAGSLVYVHRGGPAQDLTFRVSDGLQASPPATLKVVAIRPAIQIHRSTGLRLAQGSAMPILPANLSVETNAVGQDVSVLFRVTGALQFGELQKQGAGGVEGAEWWATQAFHQRDVEQGRVRYLSTDPQHHAYDTVENLALEVQVGQEILSNLSFPVTIQRATVWMLRLEPLHTQNTQQETLTTAHLEATLEEAGPSPPTFHYEVVQAPRKGNLQLQGTRLSDGQGFTQDDIQAGRVTYGATARASEAVEDTFRFRVTAPPYFSPLYTFPIHIGGDPDAPVLTNVLLVVPEGGEGVLSADHLFVKSLNSASYLYEVMERPRHGRLAWRGTQDKTTMVTSFTNEDLLRGRLVYQHDDSETTEDDIPFVATRQGESSGDMAWEEVRGVFRVAIQPVNDHAPVQTISRIFHVARGGRRLLTTDDVAFSDADSGFADAQLVLTRKDLLFGSIVAVDEPTRPIYRFTQEDLRKRRVLFVHSGADRGWIQLQVSDGQHQATALLEVQASEPYLRVANGSSLVVPQGGQGTIDTAVLHLDTNLDIRSGDEVHYHVTAGPRWGQLVRAGQPATAFSQQDLLDGAVLYSHNGSLSPRDTMAFSVEAGPVHTDATLQVTIALEGPLAPLKLVRHKKIYVFQGEAAEIRRDQLEAAQEAVPPADIVFSVKSPPSAGYLVMVSRGALADEPPSLDPVQSFSQEAVDTGRVLYLHSRPEAWSDAFSLDVASGLGAPLEGVLVELEVLPAAIPLEAQNFSVPEGGSLTLAPPLLRVSGPYFPTLLGLSLQVLEPPQHGALQKEDGPQARTLSAFSWRMVEEQLIRYVHDGSETLTDSFVLMANASEMDRQSHPVAFTVTVLPVNDQPPILTTNTGLQMWEGATAPIPAEALRSTDGDSGSEDLVYTIEQPSNGRVVLRGAPGTEVRSFTQAQLDGGLVLFSHRGTLDGGFRFRLSDGEHTSPGHFFRVTAQKQVLLSLKGSQTLTVCPGSVQPLSSQTLRASSSAGTDPQLLLYRVVRGPQLGRLFHAQQDSTGEALVNFTQAEVYAGNILYEHEMPPEPFWEAHDTLELQLSSPPARDVAATLAVAVSFEAACPQRPSHLWKNKGLWVPEGQRARITVAALDASNLLASVPSPQRSEHDVLFQVTQFPSRGQLLVSEEPLHAGQPHFLQSQLAAGQLVYAHGGGGTQQDGFHFRAHLQGPAGASVAGPQTSEAFAITVRDVNERPPQPQASVPLRLTRGSRAPISRAQLSVVDPDSAPGEIEYEVQRAPHNGFLSLVGGGLGPVTRFTQADVDSGRLAFVANGSSVAGIFQLSMSDGASPPLPMSLAVDILPSAIEVQLRAPLEVPQALGRSSLSQQQLRVVSDREEPEAAYRLIQGPQYGHLLVGGRPTSAFSQFQIDQGEVVFAFTNFSSSHDHFRVLALARGVNASAVVNVTVRALLHVWAGGPWPQGATLRLDPTVLDAGELANRTGSVPRFRLLEGPRHGRVVRVPRARTEPGGSQLVEQFTQQDLEDGRLGLEVGRPEGRAPGPAGDSLTLELWAQGVPPAVASLDFATEPYNAARPYSVALLSVPEAARTEAGKPESSTPTGEPGPMASSPEPAVAKGGFLSFLEANMFSVIIPMCLVLLLLALILPLLFYLRKRNKTGKHDVQVLTAKPRNGLAGDTETFRKVEPGQAIPLTAVPGQGPPPGGQPDPELLQFCRTPNPALKNGQYWV

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
21	Phosphorylation	LALALTLTMLARLAS HHHHHHHHHHHHHHH	12.61	22817900
130	N-linked_Glycosylation	LSVDGFLNASSAVPG EEECCCCCCCCCCCC	35.20	UniProtKB CARBOHYD
163	Phosphorylation	LPYLRGTSRPLRGCL CCCCCCCCCCCCCCC	34.42	-
348	N-linked_Glycosylation	GLTPEATNASLLGCM CCCHHHHCHHHCHHH	34.28	UniProtKB CARBOHYD
427	N-linked_Glycosylation	GLPPVFANFTQLLTI CCCCCCCCHHEEEEC	29.09	UniProtKB CARBOHYD
643	Phosphorylation	QDLTFRVSDGLQASP CCCEEEECCCCCCCC	23.00	-
685	N-linked_Glycosylation	AMPILPANLSVETNA CCCCCCCCCEEECCC	30.80	UniProtKB CARBOHYD
743	Phosphorylation	VEQGRVRYLSTDPQH HHCCCEEEEECCCCC	11.35	-
772	N-linked_Glycosylation	VGQEILSNLSFPVTI HHHHHHHCCCCCEEE	35.94	UniProtKB CARBOHYD
926	Phosphorylation	ADHLFVKSLNSASYL CCEEEEEECCCCHHH	27.73	22210691
929	Phosphorylation	LFVKSLNSASYLYEV EEEEECCCCHHHHHH	24.72	22210691
931	Phosphorylation	VKSLNSASYLYEVME EEECCCCHHHHHHHH	18.58	22210691
932	Phosphorylation	KSLNSASYLYEVMER EECCCCHHHHHHHHC	17.02	22210691
995	O-linked_Glycosylation	ATRQGESSGDMAWEE EEECCCCCCCCHHHH	34.21	-
1131	N-linked_Glycosylation	EPYLRVANGSSLVVP CCEEEECCCCEEEEC	48.28	UniProtKB CARBOHYD
1185	Phosphorylation	VRAGQPATAFSQQDL CCCCCCCCCCCHHHH	34.61	24719451
1202	N-linked_Glycosylation	GAVLYSHNGSLSPRD CCEEEEECCCCCCCC	35.49	UniProtKB CARBOHYD
1204	Phosphorylation	VLYSHNGSLSPRDTM EEEEECCCCCCCCCE	30.87	24719451
1206	Phosphorylation	YSHNGSLSPRDTMAF EEECCCCCCCCCEEE	21.42	24719451
1277	Phosphorylation	PPADIVFSVKSPPSA CCHHEEEEECCCCCC	20.10	23312004
1364	N-linked_Glycosylation	AIPLEAQNFSVPEGG CCCCCCCCCCCCCCC	37.90	UniProtKB CARBOHYD
1449	N-linked_Glycosylation	DSFVLMANASEMDRQ CEEEEEECHHHCCCC	29.99	UniProtKB CARBOHYD
1457	Phosphorylation	ASEMDRQSHPVAFTV HHHCCCCCCCEEEEE	30.56	30257219
1583	Phosphorylation	AQKQVLLSLKGSQTL ECCEEEEEECCCCEE	24.71	24719451
1587	Phosphorylation	VLLSLKGSQTLTVCP EEEEECCCCEEEECC	20.57	24043423
1589	Phosphorylation	LSLKGSQTLTVCPGS EEECCCCEEEECCCC	26.54	24043423
1591	Phosphorylation	LKGSQTLTVCPGSVQ ECCCCEEEECCCCCC	24.37	24043423
1596	Phosphorylation	TLTVCPGSVQPLSSQ EEEECCCCCCCCCCC	11.61	24043423
1601	Phosphorylation	PGSVQPLSSQTLRAS CCCCCCCCCCCHHHH	27.38	24043423
1602	Phosphorylation	GSVQPLSSQTLRASS CCCCCCCCCCHHHHC	34.56	24043423
1604	Phosphorylation	VQPLSSQTLRASSSA CCCCCCCCHHHHCCC	21.84	24043423
1645	N-linked_Glycosylation	STGEALVNFTQAEVY CCCCEEEECEEEEEE	34.79	UniProtKB CARBOHYD
1857	Phosphorylation	PISRAQLSVVDPDSA CCCCEEEEEECCCCC	14.17	29507054
1909	N-linked_Glycosylation	GRLAFVANGSSVAGI CCEEEEECCCCEEEE	45.65	UniProtKB CARBOHYD
2016	N-linked_Glycosylation	EVVFAFTNFSSSHDH EEEEEEECCCCCCCH	28.48	UniProtKB CARBOHYD
2034	N-linked_Glycosylation	LALARGVNASAVVNV HHHHCCCCHHHEEHH	30.88	UniProtKB CARBOHYD
2036	Phosphorylation	LARGVNASAVVNVTV HHCCCCHHHEEHHHH	19.18	-
2040	N-linked_Glycosylation	VNASAVVNVTVRALL CCHHHEEHHHHHHHH	19.69	UniProtKB CARBOHYD
2042	Phosphorylation	ASAVVNVTVRALLHV HHHEEHHHHHHHHHH	10.08	-
2075	N-linked_Glycosylation	LDAGELANRTGSVPR ECHHHHHHCCCCCCC	55.46	16335952
2077	Phosphorylation	AGELANRTGSVPRFR HHHHHHCCCCCCCEE	33.35	-
2079	Phosphorylation	ELANRTGSVPRFRLL HHHHCCCCCCCEEEC	28.47	-
2203	O-linked_Glycosylation	GEPGPMASSPEPAVA CCCCCCCCCCCCCHH	39.93	OGP
2204	O-linked_Glycosylation	EPGPMASSPEPAVAK CCCCCCCCCCCCHHC	24.60	OGP
2252	Phosphorylation	YLRKRNKTGKHDVQV HHHHHCCCCCCCEEE	55.82	-
2261	Phosphorylation	KHDVQVLTAKPRNGL CCCEEEEEECCCCCC	33.50	26699800
2263	Ubiquitination	DVQVLTAKPRNGLAG CEEEEEECCCCCCCC	39.00	23000965
2272	Phosphorylation	RNGLAGDTETFRKVE CCCCCCCCCCCCCCC	35.69	29255136
2274	Phosphorylation	GLAGDTETFRKVEPG CCCCCCCCCCCCCCC	30.72	29255136
2277	Ubiquitination	GDTETFRKVEPGQAI CCCCCCCCCCCCCCC	46.92	29967540
2310	Phosphorylation	ELLQFCRTPNPALKN HHHHHCCCCCCCCCC	28.71	29255136
2316	Ubiquitination	RTPNPALKNGQYWV- CCCCCCCCCCCCCC-	62.23	21963094
2320	Phosphorylation	PALKNGQYWV----- CCCCCCCCCC-----	14.99	22461510

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
2252	T	Phosphorylation	Kinase	PRKCA	P17252	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CSPG4_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRIP2_HUMAN	GRIP2	physical	12458226
CDC42_HUMAN	CDC42	physical	10587647
GRIP1_HUMAN	GRIP1	physical	12458226

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2075, AND MASSSPECTROMETRY.
PubMed: 16335952

Phosphorylation

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND MASSSPECTROMETRY.
PubMed: 18187866