MYOC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MYOC_HUMAN
• UniProt AC: Q99972
• Protein Name: Myocilin {ECO:0000303|PubMed:9169133}
• Gene Name: MYOC
• Organism: Homo sapiens (Human).
• Sequence Length: 504
• Subcellular Localization: Secreted . Golgi apparatus . Cytoplasmic vesicle . Secreted, extracellular space. Secreted, extracellular space, extracellular matrix . Secreted, exosome . Mitochondrion . Mitochondrion intermembrane space . Mitochondrion inner membrane . Mitochondrion ou
• Protein Description: Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork..
• Protein Sequence: MRFFCARCCSFGPEMPAVQLLLLACLVWDVGARTAQLRKANDQSGRCQYTFSVASPNESSCPEQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRRGQCPQTRDTARAVPPGSREVSTWNLDTLAFQELKSELTEVPASRILKESPSGYLRSGEGDTGCGELVWVGEPLTLRTAETITGKYGVWMRDPKPTYPYTQETTWRIDTVGTDVRQVFEYDLISQFMQGYPSKVHILPRPLESTGAVVYSGSLYFQGAESRTVIRYELNTETVKAEKEIPGAGYHGQFPYSWGGYTDIDLAVDEAGLWVIYSTDEAKGAIVLSKLNPENLELEQTWETNIRKQSVANAFIICGTLYTVSSYTSADATVNFAYDTGTGISKTLTIPFKNRYKYSSMIDYNPLEKKLFAWDNLNMVTYDIKLSKM

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
57	N-linked_Glycosylation	TFSVASPNESSCPEQ EEEECCCCCCCCCCH	60.32	17650508
133	Phosphorylation	RERDQLETQTRELET HHHHHHHHHHHHHHH	43.78	25072903
135	Phosphorylation	RDQLETQTRELETAY HHHHHHHHHHHHHHH	33.27	25072903
142	Phosphorylation	TRELETAYSNLLRDK HHHHHHHHHHHHHCH	12.91	25072903
143	Phosphorylation	RELETAYSNLLRDKS HHHHHHHHHHHHCHH	20.66	25072903
199	Phosphorylation	ARAVPPGSREVSTWN CCCCCCCCCCCEECC	30.92	22673903
203	Phosphorylation	PPGSREVSTWNLDTL CCCCCCCEECCCCHH	23.97	29083192
204	Phosphorylation	PGSREVSTWNLDTLA CCCCCCEECCCCHHH	24.45	22673903
209	Phosphorylation	VSTWNLDTLAFQELK CEECCCCHHHHHHHH	24.13	22673903
217	Phosphorylation	LAFQELKSELTEVPA HHHHHHHHHHCCCCH	50.92	-
479	Phosphorylation	KYSSMIDYNPLEKKL CCCCCCCCCHHHHHH	14.04	-
496	Phosphorylation	WDNLNMVTYDIKLSK ECCCCEEEEEEEECC	12.52	30622161
497	Phosphorylation	DNLNMVTYDIKLSKM CCCCEEEEEEEECCC	12.31	30622161

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MYOC_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 MYOC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NOE3_HUMAN	OLFM3	physical	12019210
FBN1_HUMAN	FBN1	physical	11923248
FINC_HUMAN	FN1	physical	11773026
MYOC_HUMAN	MYOC	physical	16289162
PEDF_HUMAN	SERPINF1	physical	16289162
ACTA_HUMAN	ACTA2	physical	16289162
G3P_HUMAN	GAPDH	physical	16289162
FRIL_HUMAN	FTL	physical	16289162
ACTB_HUMAN	ACTB	physical	16289162
ACTG_HUMAN	ACTG1	physical	16289162
CLIC1_HUMAN	CLIC1	physical	16289162
CO1A2_HUMAN	COL1A2	physical	16289162
CO3A1_HUMAN	COL3A1	physical	16289162
A2MG_HUMAN	A2M	physical	16289162
LAMA5_HUMAN	LAMA5	physical	16289162
ITA7_HUMAN	ITGA7	physical	16289162
TIMP1_HUMAN	TIMP1	physical	16289162
TGFR1_HUMAN	TGFBR1	physical	16289162
TNR1A_HUMAN	TNFRSF1A	physical	16289162
EF1A1_HUMAN	EEF1A1	physical	16289162
GLO2_HUMAN	HAGH	physical	16289162
FUBP1_HUMAN	FUBP1	physical	16289162
LEG3_HUMAN	LGALS3	physical	16289162
NOTC2_HUMAN	NOTCH2	physical	16289162
OLFL3_HUMAN	OLFML3	physical	16289162
CD81_HUMAN	CD81	physical	16289162
RFC1_HUMAN	RFC1	physical	16289162
KCRM_HUMAN	CKM	physical	16289162
IGLL1_HUMAN	IGLL1	physical	16289162
MAEA_HUMAN	MAEA	physical	16289162
ECE1_HUMAN	ECE1	physical	16289162
C1QB_HUMAN	C1QB	physical	16289162
KPYM_HUMAN	PKM	physical	16289162
VIME_HUMAN	VIM	physical	16289162
MYH11_HUMAN	MYH11	physical	16289162
TPM1_HUMAN	TPM1	physical	16289162
HSP74_HUMAN	HSPA4	physical	16289162
TKT_HUMAN	TKT	physical	16289162
CAP1_HUMAN	CAP1	physical	16289162
ENOA_HUMAN	ENO1	physical	16289162
ALDOA_HUMAN	ALDOA	physical	16289162
ANXA2_HUMAN	ANXA2	physical	16289162

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.