RN103_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN103_HUMAN
• UniProt AC: O00237
• Protein Name: E3 ubiquitin-protein ligase RNF103
• Gene Name: RNF103
• Organism: Homo sapiens (Human).
• Sequence Length: 685
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway..
• Protein Sequence: MWLKLFFLLLYFLVLFVLARFFEAIVWYETGIFATQLVDPVALSFKKLKTILECRGLGYSGLPEKKDVRELVEKSGDLMEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQVIANDRSPLVGKIHWEKMVKKVSRFGIRTGTFNCSSDPRYCRRRGWVRSTLIMSVPQTSTSKGKVMLKEYSGRKIEVEHIFKWITAHAASRIKTIYNAEHLKEEWNKSDQYWLKIYLFANLDQPPAFFSALSIKFTGRVEFIFVNVENWDNKSYMTDIGIYNMPSYILRTPEGIYRYGNHTGEFISLQAMDSFLRSLQPEVNDLFVLSLVLVNLMAWMDLFITQGATIKRFVVLISTLGTYNSLLIISWLPVLGFLQLPYLDSFYEYSLKLLRYSNTTTLASWVRADWMFYSSHPALFLSTYLGHGLLIDYFEKKRRRNNNNDEVNANNLEWLSSLWDWYTSYLFHPIASFQNFPVESDWDEDPDLFLERLAFPDLWLHPLIPTDYIKNLPMWRFKCLGVQSEEEMSEGSQDTENDSESENTDTLSSEKEVFEDKQSVLHNSPGTASHCDAEACSCANKYCQTSPCERKGRSYGSYNTNEDMEPDWLTWPADMLHCTECVVCLENFENGCLLMGLPCGHVFHQNCIVMWLAGGRHCCPVCRWPSYKKKQPYAQHQPLSNDVPS

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
44	Phosphorylation	LVDPVALSFKKLKTI CCCHHHHCHHHHHHH	25.86	24719451
45	Ubiquitination	VDPVALSFKKLKTIL CCHHHHCHHHHHHHH	9.34	33845483
47	Acetylation	PVALSFKKLKTILEC HHHHCHHHHHHHHHH	53.88	19827411
49	Ubiquitination	ALSFKKLKTILECRG HHCHHHHHHHHHHCC	42.26	33845483
59	Phosphorylation	LECRGLGYSGLPEKK HHHCCCCCCCCCCHH	12.47	24719451
60	Phosphorylation	ECRGLGYSGLPEKKD HHCCCCCCCCCCHHC	31.86	24719451
61	Ubiquitination	CRGLGYSGLPEKKDV HCCCCCCCCCCHHCH	36.45	33845483
62	Ubiquitination	RGLGYSGLPEKKDVR CCCCCCCCCCHHCHH	3.99	22817900
65	Acetylation	GYSGLPEKKDVRELV CCCCCCCHHCHHHHH	52.94	19827419
65	Ubiquitination	GYSGLPEKKDVRELV CCCCCCCHHCHHHHH	52.94	27667366
66	Ubiquitination	YSGLPEKKDVRELVE CCCCCCHHCHHHHHH	60.85	22817900
66	Acetylation	YSGLPEKKDVRELVE CCCCCCHHCHHHHHH	60.85	19827427
85	Phosphorylation	LMEGELYSALKEEEA CCHHHHHHHHCHHHH	39.49	24719451
130	Ubiquitination	VIANDRSPLVGKIHW EECCCCCCCCCEEHH	31.77	33845483
134	Ubiquitination	DRSPLVGKIHWEKMV CCCCCCCEEHHHHHH	24.74	33845483
186	Ubiquitination	QTSTSKGKVMLKEYS CCCCCCCEEEEEECC	28.36	33845483
190	Ubiquitination	SKGKVMLKEYSGRKI CCCEEEEEECCCCEE	36.19	33845483
211	Ubiquitination	KWITAHAASRIKTIY HHHHHHHHHHCHHHH	6.89	33845483
215	Ubiquitination	AHAASRIKTIYNAEH HHHHHHCHHHHCHHH	27.97	33845483
233	Phosphorylation	EWNKSDQYWLKIYLF HHCCCCCHHHHHEEE	20.07	22817900
390	Phosphorylation	LDSFYEYSLKLLRYS CHHHHHHHHHHHHHC	13.69	24719451
524	Phosphorylation	FKCLGVQSEEEMSEG EEECCCCCHHHHCCC	44.56	-

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

Oops, there are no upstream regulatory protein records of RN103_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN103_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 RN103_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DERL1_HUMAN	DERL1	physical	18675248
TERA_HUMAN	VCP	physical	18675248
UBE2N_HUMAN	UBE2N	physical	18615712
UB2L3_HUMAN	UBE2L3	physical	18615712
UB2E2_HUMAN	UBE2E2	physical	18615712
UB2E1_HUMAN	UBE2E1	physical	18615712

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.