dbPTM

SC65_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SC65_HUMAN
UniProt AC	Q92791
Protein Name	Endoplasmic reticulum protein SC65 {ECO:0000303\|PubMed:23959653}
Gene Name	P3H4 {ECO:0000312\|HGNC:HGNC:16946}
Organism	Homo sapiens (Human).
Sequence Length	437
Subcellular Localization	Endoplasmic reticulum .
Protein Description	Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. Required for normal bone density and normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly..
Protein Sequence	MARVAWGLLWLLLGSAGAQYEKYSFRGFPPEDLMPLAAAYGHALEQYEGESWRESARYLEAALRLHRLLRDSEAFCHANCSGPAPAAKPDPDGGRADEWACELRLFGRVLERAACLRRCKRTLPAFQVPYPPRQLLRDFQSRLPYQYLHYALFKANRLEKAVAAAYTFLQRNPKHELTAKYLNYYQGMLDVADESLTDLEAQPYEAVFLRAVKLYNSGDFRSSTEDMERALSEYLAVFARCLAGCEGAHEQVDFKDFYPAIADLFAESLQCKVDCEANLTPNVGGYFVDKFVATMYHYLQFAYYKLNDVRQAARSAASYMLFDPKDSVMQQNLVYYRFHRARWGLEEEDFQPREEAMLYHNQTAELRELLEFTHMYLQSDDEMELEETEPPLEPEDALSDAEFEGEGDYEEGMYADWWQEPDAKGDEAEAEPEPELA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	LGSAGAQYEKYSFRG HHHCCCHHHCCCCCC	17.54	-
23	Phosphorylation	AGAQYEKYSFRGFPP CCCHHHCCCCCCCCH	10.91	-
88	Ubiquitination	SGPAPAAKPDPDGGR CCCCCCCCCCCCCCC	52.65	21963094
160	Ubiquitination	FKANRLEKAVAAAYT HHHHHHHHHHHHHHH	53.40	29967540
174	Ubiquitination	TFLQRNPKHELTAKY HHHHHCCCHHHHHHH	53.94	29967540
186	Ubiquitination	AKYLNYYQGMLDVAD HHHHHHHHHHHHHCC	22.06	21963094
213	Ubiquitination	AVFLRAVKLYNSGDF HHHHHHHHHHCCCCC	44.24	33845483
234	Phosphorylation	MERALSEYLAVFARC HHHHHHHHHHHHHHH	9.15	17053785
315	Phosphorylation	DVRQAARSAASYMLF HHHHHHHHHHHHHHC	24.38	24247654
325	Ubiquitination	SYMLFDPKDSVMQQN HHHHCCCCCCHHHHC	65.56	21963094
335	Phosphorylation	VMQQNLVYYRFHRAR HHHHCHHHHHHHHHH	7.65	24247654
361	N-linked_Glycosylation	EEAMLYHNQTAELRE HHHHHHCCCHHHHHH	27.60	-
423	Ubiquitination	DWWQEPDAKGDEAEA CCCCCCCCCCCCCCC	28.57	21963094

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
Oops, there are no upstream regulatory protein records of SC65_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SC65_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SC65_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SC65_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.

Regulatory Network of SC65_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-234, AND MASSSPECTROMETRY.	17053785 [Abstract]