dbPTM

P3H3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P3H3_HUMAN
UniProt AC	Q8IVL6
Protein Name	Prolyl 3-hydroxylase 3 {ECO:0000312\|HGNC:HGNC:19318}
Gene Name	P3H3 {ECO:0000312\|HGNC:HGNC:19318}
Organism	Homo sapiens (Human).
Sequence Length	736
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-linkling of collagen fibrils. Required for normal hydroxylation of lysine residues in type I collagen chains in skin, bone, tendon, aorta and cornea. Required for normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly. Apparently not required for normal prolyl 3-hydroxylation on collagen chains, possibly because it functions redundantly with other prolyl 3-hydroxylases..
Protein Sequence	MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALLREALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALRRADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTFFVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLEEALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGETATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQAQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREKLREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGVLLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSERVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWREPPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWAVTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQRVQDKTGRAPRVREEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
145	Phosphorylation	AARLRVGSALRDAFR HHHHHHHHHHHHHHH	22.67	-
201	Phosphorylation	MAKYRRMSGVRPQSF HHHHHHHHCCCCCCC	32.12	28555341
331	N-linked_Glycosylation	EAHAQVGNLSQAIEN HHHHHHCCHHHHHHH	37.35	UniProtKB CARBOHYD
462	N-linked_Glycosylation	TQDSRQLNGSERAVL CCCHHHCCCCHHHHH	43.54	UniProtKB CARBOHYD
478	Glutathionylation	GLLTPAECGVLLQLA CCCCHHHHHHHHHHH	5.05	22555962
497	Phosphorylation	GAGARSGYRGRRSPH CCCCCCCCCCCCCCC	15.90	20736484
517	Ubiquitination	FEGLTVLKAAQLARA CCCHHHHHHHHHHHC	37.02	-
662	Phosphorylation	PHGVWAVTRGRRCAL CCCCEEEECCCCCHH	21.47	24719451
694	Phosphorylation	AKELLQESQEEEEEE HHHHHHHHHHHHHHH	29.90	26657352

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 P3H3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of P3H3_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 P3H3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLOD1_HUMAN	PLOD1	physical	28514442
KEAP1_HUMAN	KEAP1	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442
IDE_HUMAN	IDE	physical	28514442

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
DB00172	L-Proline
DB00139	Succinic acid
DB00126	Vitamin C

Regulatory Network of P3H3_HUMAN

Related Literatures of Post-Translational Modification