PGS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PGS1_HUMAN
• UniProt AC: P21810
• Protein Name: Biglycan
• Gene Name: BGN
• Organism: Homo sapiens (Human).
• Sequence Length: 368
• Subcellular Localization: Secreted, extracellular space, extracellular matrix.
• Protein Description: May be involved in collagen fiber assembly..
• Protein Sequence: MWPLWRLVSLLALSQALPFEQRGFWDFTLDDGPFMMNDEEASGADTSGVLDPDSVTPTYSAMCPFGCHCHLRVVQCSDLGLKSVPKEISPDTTLLDLQNNDISELRKDDFKGLQHLYALVLVNNKISKIHEKAFSPLRKLQKLYISKNHLVEIPPNLPSSLVELRIHDNRIRKVPKGVFSGLRNMNCIEMGGNPLENSGFEPGAFDGLKLNYLRISEAKLTGIPKDLPETLNELHLDHNKIQAIELEDLLRYSKLYRLGLGHNQIRMIENGSLSFLPTLRELHLDNNKLARVPSGLPDLKLLQVVYLHSNNITKVGVNDFCPMGFGVKRAYYNGISLFNNPVPYWEVQPATFRCVTDRLAIQFGNYKK

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
9	Phosphorylation	WPLWRLVSLLALSQA CHHHHHHHHHHHHHC	23.43	28857561
14	Phosphorylation	LVSLLALSQALPFEQ HHHHHHHHHCCCHHH	14.06	24043423
42	O-linked_Glycosylation	MMNDEEASGADTSGV CCCHHHCCCCCCCCC	37.48	2590169
47	O-linked_Glycosylation	EASGADTSGVLDPDS HCCCCCCCCCCCCCC	27.70	2590169
56	O-linked_Glycosylation	VLDPDSVTPTYSAMC CCCCCCCCCCCCCCC	17.54	OGP
58	O-linked_Glycosylation	DPDSVTPTYSAMCPF CCCCCCCCCCCCCCC	22.27	OGP
77	Phosphorylation	HLRVVQCSDLGLKSV EEEEEECHHHCCCCC	20.83	-
103	Phosphorylation	DLQNNDISELRKDDF ECCCCCHHHHCCCCC	33.18	24719451
111	Acetylation	ELRKDDFKGLQHLYA HHCCCCCCHHHHHHH	66.75	30587191
142	Acetylation	SPLRKLQKLYISKNH CHHHHHHHHEECCCC	54.41	27178108
180	O-linked_Glycosylation	KVPKGVFSGLRNMNC CCCCCHHHCCCCCCC	34.21	-
198	O-linked_Glycosylation	GGNPLENSGFEPGAF CCCCCCCCCCCCCCC	35.17	-
212	Phosphorylation	FDGLKLNYLRISEAK CCCCCCEEEEEEEHH	14.06	29083192
216	Phosphorylation	KLNYLRISEAKLTGI CCEEEEEEEHHHHCC	25.68	29083192
253	Phosphorylation	LEDLLRYSKLYRLGL HHHHHHHHHHHHCCC	15.11	27251275
270	N-linked_Glycosylation	NQIRMIENGSLSFLP CEEEEEECCCCCCCC	34.13	19159218
311	N-linked_Glycosylation	VVYLHSNNITKVGVN EEEECCCCEEEEECC	46.45	19159218
328	Acetylation	CPMGFGVKRAYYNGI CCCCCCCCEEEECCE	31.52	24889065
367	Acetylation	AIQFGNYKK------ HHHCCCCCC------	56.88	30587197

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

Oops, there are no upstream regulatory protein records of PGS1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PGS1_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 PGS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JPH3_HUMAN	JPH3	physical	11145944

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

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-270 AND ASN-311, AND MASSSPECTROMETRY.
PubMed: 19159218

O-linked Glycosylation

"Dermatan sulphate proteoglycans of human articular cartilage. Theproperties of dermatan sulphate proteoglycans I and II.";
Roughley P.J., White R.J.;
Biochem. J. 262:823-827(1989).
Cited for: PROTEIN SEQUENCE OF 38-57.
PubMed: 2590169