LIN7C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIN7C_HUMAN
• UniProt AC: Q9NUP9
• Protein Name: Protein lin-7 homolog C
• Gene Name: LIN7C
• Organism: Homo sapiens (Human).
• Sequence Length: 197
• Subcellular Localization: Cell membrane ; Peripheral membrane protein . Basolateral cell membrane ; Peripheral membrane protein . Cell junction. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density; Peripheral membrane protein. Cell junction, tight junction. Ce
• Protein Description: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells..
• Protein Sequence: MAALGEPVRLERDICRAIELLEKLQRSGEVPPQKLQALQRVLQSEFCNAVREVYEHVYETVDISSSPEVRANATAKATVAAFAASEGHSHPRVVELPKTEEGLGFNIMGGKEQNSPIYISRIIPGGIADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGKVKLVVRYTPKVLEEMESRFEKMRSAKRRQQT

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
2	Acetylation	------MAALGEPVR ------CCCCCCCCC	16.05	22814378
9	Methylation	AALGEPVRLERDICR CCCCCCCCCHHHHHH	41.36	115482139
23	Ubiquitination	RAIELLEKLQRSGEV HHHHHHHHHHHCCCC	50.30	23000965
34	Ubiquitination	SGEVPPQKLQALQRV CCCCCHHHHHHHHHH	48.63	21906983
44	Phosphorylation	ALQRVLQSEFCNAVR HHHHHHHHHHHHHHH	28.60	24670416
47	Glutathionylation	RVLQSEFCNAVREVY HHHHHHHHHHHHHHH	2.54	22555962
54	Phosphorylation	CNAVREVYEHVYETV HHHHHHHHHHHHHHC	8.79	28152594
58	Phosphorylation	REVYEHVYETVDISS HHHHHHHHHHCCCCC	14.06	28152594
60	Phosphorylation	VYEHVYETVDISSSP HHHHHHHHCCCCCCH	13.04	28152594
64	Phosphorylation	VYETVDISSSPEVRA HHHHCCCCCCHHHHC	21.94	27134283
65	Phosphorylation	YETVDISSSPEVRAN HHHCCCCCCHHHHCH	50.69	28348404
66	Phosphorylation	ETVDISSSPEVRANA HHCCCCCCHHHHCHH	20.49	28348404
76	Ubiquitination	VRANATAKATVAAFA HHCHHHHHHHHHHHH	39.99	23000965
78	Phosphorylation	ANATAKATVAAFAAS CHHHHHHHHHHHHHH	15.24	-
85	Phosphorylation	TVAAFAASEGHSHPR HHHHHHHHCCCCCCE	40.45	28857561
89	Phosphorylation	FAASEGHSHPRVVEL HHHHCCCCCCEEEEC	46.15	28857561
108	Sulfoxidation	EGLGFNIMGGKEQNS CCCCCEECCCCCCCC	6.42	21406390
111	Ubiquitination	GFNIMGGKEQNSPIY CCEECCCCCCCCCEE	50.85	32015554
115	Phosphorylation	MGGKEQNSPIYISRI CCCCCCCCCEEEEEE	16.63	21815630
118	Phosphorylation	KEQNSPIYISRIIPG CCCCCCEEEEEECCC	9.02	28152594
120	Phosphorylation	QNSPIYISRIIPGGI CCCCEEEEEECCCCC	10.64	28152594
130	Methylation	IPGGIADRHGGLKRG CCCCCCCCCCCCCCC	22.71	115482147
161	Ubiquitination	EKAVELLKAAQGKVK HHHHHHHHHCCCCEE	55.06	32015554
161	Malonylation	EKAVELLKAAQGKVK HHHHHHHHHCCCCEE	55.06	26320211
176	Ubiquitination	LVVRYTPKVLEEMES EEEEECHHHHHHHHH	52.21	23000965
190	Phosphorylation	SRFEKMRSAKRRQQT HHHHHHHHHHHHHCC	34.34	-

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

Oops, there are no upstream regulatory protein records of LIN7C_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LIN7C_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 LIN7C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSKP_HUMAN	CASK	physical	14960569
APBA1_HUMAN	APBA1	physical	14960569
DLG1_HUMAN	DLG1	physical	14960569
MPDZ_HUMAN	MPDZ	physical	26186194
INADL_HUMAN	INADL	physical	26186194
MPP2_HUMAN	MPP2	physical	26186194
MPP6_HUMAN	MPP6	physical	26186194
ABLM1_HUMAN	ABLIM1	physical	26186194
MPP7_HUMAN	MPP7	physical	26186194
MPP3_HUMAN	MPP3	physical	26186194
DLG1_HUMAN	DLG1	physical	26186194
KI26B_HUMAN	KIF26B	physical	26186194
MPP5_HUMAN	MPP5	physical	26186194
LIN7B_HUMAN	LIN7B	physical	26186194
CSKP_HUMAN	CASK	physical	26186194
ABLM2_HUMAN	ABLIM2	physical	26186194
APBA1_HUMAN	APBA1	physical	26186194
ARHGQ_HUMAN	ARHGEF26	physical	26186194
APC_HUMAN	APC	physical	26186194
PXDC1_HUMAN	PXDC1	physical	26186194
MPP7_HUMAN	MPP7	physical	28514442
CSKP_HUMAN	CASK	physical	28514442
MPDZ_HUMAN	MPDZ	physical	28514442
INADL_HUMAN	INADL	physical	28514442
DLG1_HUMAN	DLG1	physical	28514442
MPP6_HUMAN	MPP6	physical	28514442
KI26B_HUMAN	KIF26B	physical	28514442
APBA1_HUMAN	APBA1	physical	28514442
ARHGQ_HUMAN	ARHGEF26	physical	28514442
ABLM2_HUMAN	ABLIM2	physical	28514442
LIN7B_HUMAN	LIN7B	physical	28514442
ABLM1_HUMAN	ABLIM1	physical	28514442
PXDC1_HUMAN	PXDC1	physical	28514442
MPP3_HUMAN	MPP3	physical	28514442
APC_HUMAN	APC	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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330