PGBM_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PGBM_MOUSE
• UniProt AC: Q05793
• Protein Name: Basement membrane-specific heparan sulfate proteoglycan core protein
• Gene Name: Hspg2
• Organism: Mus musculus (Mouse).
• Sequence Length: 3707
• Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane.
• Protein Description: Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development (By similarity).; Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6 (By similarity).; The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity..
• Protein Sequence: MGQRAVGSLLLGLLLHARLLAVTHGLRAYDGLSLPEDTETVTASRYGWTYSYLSDDEDLLADDASGDGLGSGDVGSGDFQMVYFRALVNFTRSIEYSPQLEDASAKEFREVSEAVVEKLEPEYRKIPGDQIVSVVFIKELDGWVFVELDVGSEGNADGSQIQEVLHTVVSSGSIGPYVTSPWGFKFRRLGTVPQFPRVCTETEFACHSYNECVALEYRCDRRPDCRDMSDELNCEEPVPELSSSTPAVGKVSPLPLWPEAATTPPPPVTHGPQFLLPSVPGPSACGPQEASCHSGHCIPRDYLCDGQEDCRDGSDELGCASPPPCEPNEFACENGHCALKLWRCDGDFDCEDRTDEANCSVKQPGEVCGPTHFQCVSTNRCIPASFHCDEESDCPDRSDEFGCMPPQVVTPPQQSIQASRGQTVTFTCVATGVPTPIINWRLNWGHIPAHPRVTMTSEGGRGTLIIRDVKEADQGAYTCEAMNSRGMVFGIPDGVLELVPQRGPCPDGHFYLEDSASCLPCFCFGVTNVCQSSLRFRDQIRLSFDQPNDFKGVNVTMPSQPGVPPLSSTQLQIDPALQEFQLVDLSRRFLVHDAFWALPKQFLGNKVDSYGGFLRYKVRYELARGMLEPVQKPDVILVGAGYRLHSRGHTPTHPGTLNQRQVQLSEEHWVHESGRPVQRAEMLQALASLEAVLLQTVYNTKMASVGLSDIVMDTTVTHTTIHGRAHSVEECRCPIGYSGLSCESCDAHFTRVPGGPYLGTCSGCNCNGHASSCDPVYGHCLNCQHNTEGPQCDKCKPGFFGDATKATATACRPCPCPYIDASRRFSDTCFLDTDGQATCDACAPGYTGRRCESCAPGYEGNPIQPGGKCRPTTQEIVRCDERGSLGTSGETCRCKNNVVGRLCNECSDGSFHLSKQNPDGCLKCFCMGVSRQCSSSSWSRAQVLGASEQPSQFSLSNAAGTHTTSEGVSSPAPGELSFSSFHNLLSEPYFWSLPASFRGDKVTSYGGELRFTVMQRPRPSSAPLHRQPLVVLQGNNIVLEHHASRDPSPGQPSNFIVPFQEQAWQRPDGQPATREHLLMALAGIDALLIQASYTQQPAESRLSGISMDVAVPENTGQDSAREVEQCTCPPGYRGPSCQDCDTGYTRVPSGLYLGTCERCNCHGHSETCEPETGACQSCQHHTEGASCEQCQPGYYGDAQRGTPQDCQPCPCYGAPAAGQAAHTCFLDTDGHPTCDSCSPGHSGRHCERCAPGYYGNPSQGQPCHRDGQVPEVLGCGCDPHGSISSQCDAAGQCQCKAQVEGRSCSHCRPHHFHLSASNPEGCLPCFCMGVTQQCASSSYSRQLISTHFAPGDFQGFALVNPQRNSQLTGGFTVEPVHDGARLSFSNFAHLGQESFYWQLPEIYQGDKVAAYGGKLRYTLSYTAGPQGSPLLDPDIQITGNNIMLVASQPALQGPERRSYEIIFREEFWRRPDGQPATREHLLMALADLDELLVRATFSSVPRAASISAVSLEGAQPGPSSGPRALEVEECRCPPGYVGLSCQDCAPGYTRTGSGLYLGQCELCECNGHSDLCHPETGACSRCQHNTAGEFCELCATGYYGDATAGTPEDCQPCACPLTNPENMFSRTCESLGAGGYRCTACEPGYTGQYCEQCAPGYEGDPNVQGGRCQPLTKESLEVQIHPSRSVVPQGGPHSLRCQVSGSPPHYFYWSREDGRPLPSSAQQRHQGSELHFPSVQPSDAGVYICTCRNLIHTSNSRAELLVAEAPSKPIMVTVEEQRSQSVRPGADVTFICTAKSKSPAYTLVWTRLHNGKLPSRAMDFNGILTIRNVQPSDAGTYVCTGSNMFAMDQGTATLHVQVSGTSTAPVASIHPPQLTVQPGQQAEFRCSATGNPTPMLEWIGGPSGQLPAKAQIHNGILRLPAIEPSDQGQYLCRALSSAGQHVARAMLQVHGGSGPRVQVSPERTQVHEGRTVRLYCRAAGVPSASITWRKEGGSLPFRHQAHGSRLRLHHMSVADSGEYVCRANNNIDAQETSIMISVSPSTNSPPAPASPAPIRIESSSSRVAEGQTLDLNCVVPGHAHAQVTWHKRGGSLPTHHQTHGSRLRLYQVSSADSGEYVCSVLSSSGPLEASVLVSITPAAANVHIPGVVPPIRIETSSSRVAEGQTLDLSCVVPGQAHAQVTWHKRGGSLPAGHQVHGHMLRLNRVSPADSGEYSCQVTGSSGTLEASVLVTIEASEPSPIPAPGLAQPVYIESSSSHLTEGQTVDLKCVVPGQAHAQVTWHKRGSSLPARHQTHGSLLRLYQLSPADSGEYVCQVAGSSHPEHEASFKLTVPSSQNSSFRLRSPVISIEPPSSTVQQGQDASFKCLIHEGAMPIKVEWKIRDQELEDNVHISPNGSIITIVAPGPATMEPTACVASNVYGMAQSVVNLSVHGPPTVSVLPEGPVHVKMGKDITLECISSGEPRSSPRWTRLGIPVKLEPRMFGLMNSHAMLKIASVKPSDAGTYVCQAQNALGTAQKQVELIVDTGTVAPGTPQVQVEESELTLEAGHTATLHCSATGNPPPTIHWSKLRAPLPWQHRIEGNTLVIPRVAQQDSGQYICNATNSAGHTEATVVLHVESPPYATIIPEHTSAQPGNLVQLQCLAHGTPPLTYQWSLVGGVLPEKAVVRNQLLRLEPTVPEDSGRYRCQVSNRVGSAEAFAQVLVQGSSSNLPDTSIPGGSTPTVQVTPQLETRNIGASVEFHCAVPNERGTHLRWLKEGGQLPPGHSVQDGVLRIQNLDQNCQGTYVCQAHGPWGQAQATAQLIVQALPSVLINVRTSVHSVVVGHSVEFECLALGDPKPQVTWSKVGGHLRPGIVQSGTIIRIAHVELADAGQYRCAATNAAGTTQSHVLLLVQALPQISTPPEIRVPAGSAAVFPCMASGYPTPAITWSKVDGDLPPDSRLENNMLMLPSVRPEDAGTYVCTATNRQGKVKAFAYLQVPERVIPYFTQTPYSFLPLPTIKDAYRKFEIKITFRPDSADGMLLYNGQKRSPTNLANRQPDFISFGLVGGRPEFRFDAGSGMATIRHPTPLALGQFHTVTLLRSLTQGSLIVGNLAPVNGTSQGKFQGLDLNEELYLGGYPDYGAIPKAGLSSGFVGCVRELRIQGEEIVFHDVNLTTHGISHCPTCQDRPCQNGGQCQDSESSSYTCVCPAGFTAAAVNIRKPCTATPSLWADATCVNRPDGRGYTCRCHLGRSGVRCEEGVTVTTPSMSGAGSYLALPALTNTHHELRLDVEFKPLEPNGILLFSGGKSGPVEDFVSLAMVGGHLEFRYELGSGLAVLRSHEPLALGRWHRVSAERLNKDGSLRVDGGRPVLRSSPGKSQGLNLHTLLYLGGVEPSVQLSPATNMSAHFHGCVGEVSVNGKRLDLTYSFLGSQGVGQCYDSSPCERQPCRNGATCMPAGEYEFQCLCQDGFKGDLCEHEENPCQLHEPCLNGGTCRGARCLCLPGFSGPRCQQGAGYGVVESDWHPEGSGGNDAPGQYGAYFYDNGFLGLPGNSFSRSLPEVPETIEFEVRTSTADGLLLWQGVVREASRSKDFISLGLQDGHLVFSYQLGSGEARLVSGDPINDGEWHRITALREGQRGSIQVDGEDLVTGRSPGPNVAVNTKDIIYIGGAPDVATLTRGKFSSGITGCIKNLVLHTARPGAPPPQPLDLQHRAQAGANTRPCPS

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
29	Phosphorylation	VTHGLRAYDGLSLPE HHCCHHHCCCCCCCC	12.24	25367039
33	Phosphorylation	LRAYDGLSLPEDTET HHHCCCCCCCCCCCE	47.62	25367039
38	Phosphorylation	GLSLPEDTETVTASR CCCCCCCCCEEEEHH	31.71	25367039
40	Phosphorylation	SLPEDTETVTASRYG CCCCCCCEEEEHHCC	25.83	25367039
42	Phosphorylation	PEDTETVTASRYGWT CCCCCEEEEHHCCEE	26.74	25367039
44	Phosphorylation	DTETVTASRYGWTYS CCCEEEEHHCCEEEE	19.37	25367039
46	Phosphorylation	ETVTASRYGWTYSYL CEEEEHHCCEEEEEC	17.96	25367039
49	Phosphorylation	TASRYGWTYSYLSDD EEHHCCEEEEECCCC	9.76	25367039
50	Phosphorylation	ASRYGWTYSYLSDDE EHHCCEEEEECCCCH	6.71	25367039
51	Phosphorylation	SRYGWTYSYLSDDED HHCCEEEEECCCCHH	16.54	25367039
52	Phosphorylation	RYGWTYSYLSDDEDL HCCEEEEECCCCHHH	10.38	25367039
54	Phosphorylation	GWTYSYLSDDEDLLA CEEEEECCCCHHHCC	34.48	25367039
65	O-linked_Glycosylation	DLLADDASGDGLGSG HHCCCCCCCCCCCCC	44.40	-
65	Phosphorylation	DLLADDASGDGLGSG HHCCCCCCCCCCCCC	44.40	25367039
71	O-linked_Glycosylation	ASGDGLGSGDVGSGD CCCCCCCCCCCCCCC	36.54	-
71	Phosphorylation	ASGDGLGSGDVGSGD CCCCCCCCCCCCCCC	36.54	25367039
76	Phosphorylation	LGSGDVGSGDFQMVY CCCCCCCCCCCEEEE	34.73	25367039
76	O-linked_Glycosylation	LGSGDVGSGDFQMVY CCCCCCCCCCCEEEE	34.73	-
83	Phosphorylation	SGDFQMVYFRALVNF CCCCEEEEEEHHHHH	5.08	25367039
89	N-linked_Glycosylation	VYFRALVNFTRSIEY EEEEHHHHHHHCCCC	33.16	19656770
91	Phosphorylation	FRALVNFTRSIEYSP EEHHHHHHHCCCCCC	20.50	25367039
106	Ubiquitination	QLEDASAKEFREVSE CCCCCCHHHHHHHHH	55.69	-
358	N-linked_Glycosylation	EDRTDEANCSVKQPG CCCCCCCCCCCCCCC	19.29	-
554	N-linked_Glycosylation	PNDFKGVNVTMPSQP CCCCCCCEEECCCCC	32.01	-
586	Phosphorylation	EFQLVDLSRRFLVHD HHCHHCCHHHHHHHH	19.56	29899451
847	O-linked_Glycosylation	DACAPGYTGRRCESC CCCCCCCCCCCCCCC	30.08	22645316
884	Phosphorylation	VRCDERGSLGTSGET EECCCCCCCCCCCCC	29.82	23737553
887	Phosphorylation	DERGSLGTSGETCRC CCCCCCCCCCCCCCC	38.56	23737553
888	Phosphorylation	ERGSLGTSGETCRCK CCCCCCCCCCCCCCC	32.60	26824392
891	Phosphorylation	SLGTSGETCRCKNNV CCCCCCCCCCCCCCH	14.58	23737553
1628	S-palmitoylation	ENMFSRTCESLGAGG HHHHHHHHHHCCCCC	3.04	28526873
1746	O-linked_Glycosylation	DAGVYICTCRNLIHT CCEEEEEEECCEEEC	12.63	55412281
1960	Phosphorylation	SGPRVQVSPERTQVH CCCCEEECCCCCEEE	12.17	26643407
1964	Phosphorylation	VQVSPERTQVHEGRT EEECCCCCEEECCCE	33.03	26643407
1987	Phosphorylation	GVPSASITWRKEGGS CCCCCEEEEEECCCC	19.40	28059163
2336	N-linked_Glycosylation	LTVPSSQNSSFRLRS EECCCCCCCCEEEEC	41.38	19656770
2394	N-linked_Glycosylation	DNVHISPNGSIITIV CCEEECCCCCEEEEE	50.48	-
2427	N-linked_Glycosylation	GMAQSVVNLSVHGPP CCCEEEEEEECCCCC	25.17	-
2497	Acetylation	MLKIASVKPSDAGTY EEEEEECCHHHCCHH	35.99	22826441
2600	N-linked_Glycosylation	DSGQYICNATNSAGH CCCCEEEECCCCCCC	40.00	-
2694	Phosphorylation	QVSNRVGSAEAFAQV EEECCCCCHHHHHHH	21.78	-
3030	Phosphorylation	LYNGQKRSPTNLANR EECCCCCCCCCHHHC	43.01	28059163
3098	N-linked_Glycosylation	VGNLAPVNGTSQGKF EEEEECCCCCCCCEE	47.14	19656770
3154	N-linked_Glycosylation	EIVFHDVNLTTHGIS EEEEEEEECCCCCCC	37.41	19656770
3385	N-linked_Glycosylation	VQLSPATNMSAHFHG CEECCCCCCCEECCC	25.23	-

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

Oops, there are no upstream regulatory protein records of PGBM_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PGBM_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 PGBM_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of PGBM_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

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2336 AND ASN-3098, ANDMASS SPECTROMETRY.
PubMed: 19349973

"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-89; ASN-2336; ASN-3098 ANDASN-3154, AND MASS SPECTROMETRY.
PubMed: 19656770