RN181_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN181_HUMAN
• UniProt AC: Q9P0P0
• Protein Name: E3 ubiquitin-protein ligase RNF181
• Gene Name: RNF181
• Organism: Homo sapiens (Human).
• Sequence Length: 153
• Protein Description: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates..
• Protein Sequence: MASYFDEHDCEPSDPEQETRTNMLLELARSLFNRMDFEDLGLVVDWDHHLPPPAAKTVVENLPRTVIRGSQAELKCPVCLLEFEEEETAIEMPCHHLFHSSCILPWLSKTNSCPLCRYELPTDDDTYEEHRRDKARKQQQQHRLENLHGAMYT

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	------MASYFDEHD ------CCCCCCCCC	16.97	-
3	Phosphorylation	-----MASYFDEHDC -----CCCCCCCCCC	25.65	23663014
4	Phosphorylation	----MASYFDEHDCE ----CCCCCCCCCCC	12.91	23663014
13	Phosphorylation	DEHDCEPSDPEQETR CCCCCCCCCHHHHHH	43.43	23663014
19	Phosphorylation	PSDPEQETRTNMLLE CCCHHHHHHHHHHHH	42.35	26552605
23	Sulfoxidation	EQETRTNMLLELARS HHHHHHHHHHHHHHH	4.46	21406390
65	Phosphorylation	VVENLPRTVIRGSQA HHHCCCCCEECCCHH	20.53	21949786
70	Phosphorylation	PRTVIRGSQAELKCP CCCEECCCHHHHCCC	19.17	17525332
126	Phosphorylation	ELPTDDDTYEEHRRD CCCCCCCHHHHHHHH	39.57	28796482
127	Phosphorylation	LPTDDDTYEEHRRDK CCCCCCHHHHHHHHH	26.72	28796482
137	Ubiquitination	HRRDKARKQQQQHRL HHHHHHHHHHHHHHH	58.27	29967540
152	Phosphorylation	ENLHGAMYT------ HHHHHHCCC------	14.57	29978859
153	Phosphorylation	NLHGAMYT------- HHHHHCCC-------	21.03	25159151

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

Oops, there are no upstream regulatory protein records of RN181_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN181_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 RN181_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ITA2B_HUMAN	ITGA2B	physical	15075326
ITA2B_HUMAN	ITGA2B	physical	18331836
TRIM8_HUMAN	TRIM8	physical	22493164
VPS11_HUMAN	VPS11	physical	22493164
ZMY10_HUMAN	ZMYND10	physical	21988832
RN181_HUMAN	RNF181	physical	18331836
UB2D1_HUMAN	UBE2D1	physical	18331836
CAR11_HUMAN	CARD11	physical	26711259
UBC_HUMAN	UBC	physical	26711259
UB2D1_HUMAN	UBE2D1	physical	26711259
UB2D2_HUMAN	UBE2D2	physical	26711259
UB2D3_HUMAN	UBE2D3	physical	26711259
UB2E1_HUMAN	UBE2E1	physical	26711259
UBE2N_HUMAN	UBE2N	physical	26711259
BCL10_HUMAN	BCL10	physical	26711259

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

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASSSPECTROMETRY.
PubMed: 17525332

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, AND MASSSPECTROMETRY.
PubMed: 18669648