EPYC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EPYC_HUMAN
• UniProt AC: Q99645
• Protein Name: Epiphycan
• Gene Name: EPYC
• Organism: Homo sapiens (Human).
• Sequence Length: 322
• Subcellular Localization: Secreted, extracellular space, extracellular matrix.
• Protein Description: May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization..
• Protein Sequence: MKTLAGLVLGLVIFDAAVTAPTLESINYDSETYDATLEDLDNLYNYENIPVDKVEIEIATVMPSGNRELLTPPPQPEKAQEEEEEEESTPRLIDGSSPQEPEFTGVLGPHTNEDFPTCLLCTCISTTVYCDDHELDAIPPLPKNTAYFYSRFNRIKKINKNDFASLSDLKRIDLTSNLISEIDEDAFRKLPQLRELVLRDNKIRQLPELPTTLTFIDISNNRLGRKGIKQEAFKDMYDLHHLYLTDNNLDHIPLPLPENLRALHLQNNNILEMHEDTFCNVKNLTYIRKALEDIRLDGNPINLSKTPQAYMCLPRLPVGSLV

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
60	O-linked_Glycosylation	KVEIEIATVMPSGNR EEEEEEEEECCCCCC	24.01	UniProtKB CARBOHYD
60	Phosphorylation	KVEIEIATVMPSGNR EEEEEEEEECCCCCC	24.01	26074081
64	O-linked_Glycosylation	EIATVMPSGNRELLT EEEEECCCCCCCCCC	30.51	-
64	Phosphorylation	EIATVMPSGNRELLT EEEEECCCCCCCCCC	30.51	26074081
71	Phosphorylation	SGNRELLTPPPQPEK CCCCCCCCCCCCCHH	46.50	26074081
96	O-linked_Glycosylation	TPRLIDGSSPQEPEF CCCCCCCCCCCCCCC	34.79	UniProtKB CARBOHYD
165	Phosphorylation	INKNDFASLSDLKRI CCCCCCCCHHHHHHC	28.53	24719451
167	Phosphorylation	KNDFASLSDLKRIDL CCCCCCHHHHHHCCC	38.10	21130716
176	Phosphorylation	LKRIDLTSNLISEID HHHCCCCCCHHHHCC	36.62	-
283	N-linked_Glycosylation	DTFCNVKNLTYIRKA CCCCCCCCHHHHHHH	33.08	UniProtKB CARBOHYD
302	N-linked_Glycosylation	RLDGNPINLSKTPQA CCCCCCCCCCCCCCE	39.25	UniProtKB CARBOHYD

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
64	S	Glycosylation	There is one glycosaminoglycan chain, known to be dermatan sulfate, and it is probably the O-glycosylation at Ser-64 (By similarity).	-
64	S	Sulfation	There is one glycosaminoglycan chain, known to be dermatan sulfate, and it is probably the O-glycosylation at Ser-64 (By similarity).	-

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of EPYC_HUMAN !!

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.