RN187_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN187_HUMAN
• UniProt AC: Q5TA31
• Protein Name: E3 ubiquitin-protein ligase RNF187
• Gene Name: RNF187
• Organism: Homo sapiens (Human).
• Sequence Length: 235
• Subcellular Localization: Cytoplasm . Nucleus . Predominantly located in the cytoplasm. Shuttles between the cytoplasm and the nucleus.
• Protein Description: E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8..
• Protein Sequence: MALPAGPAEAACALCQRAPREPVRADCGHRFCRACVVRFWAEEDGPFPCPECADDCWQRAVEPGRPPLSRRLLALEEAAAAPARDGPASEAALQLLCRADAGPLCAACRMAAGPEPPEWEPRWRKALRGKENKGSVEIMRKDLNDARDLHGQAESAAAVWKGHVMDRRKKALTDYKKLRAFFVEEEEHFLQEAEKEEGLPEDELADPTERFRSLLQAVSELEKKHRNLGLSMLLQ

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
52	Ubiquitination	GPFPCPECADDCWQR CCCCCCHHCHHHHHH	2.80	21906983
98	Asymmetric dimethylarginine	AALQLLCRADAGPLC HHHHHHHHCCCHHHH	35.16	-
98	Methylation	AALQLLCRADAGPLC HHHHHHHHCCCHHHH	35.16	23624934
109	Asymmetric dimethylarginine	GPLCAACRMAAGPEP HHHHHHHHHHCCCCC	17.04	-
109	Methylation	GPLCAACRMAAGPEP HHHHHHHHHHCCCCC	17.04	23624934
114	Ubiquitination	ACRMAAGPEPPEWEP HHHHHCCCCCCCCCH	46.31	21906983
130	Ubiquitination	WRKALRGKENKGSVE HHHHHCCCCCCCCHH	52.24	-
133	Sumoylation	ALRGKENKGSVEIMR HHCCCCCCCCHHHHH	54.37	-
133	Ubiquitination	ALRGKENKGSVEIMR HHCCCCCCCCHHHHH	54.37	33845483
133	Sumoylation	ALRGKENKGSVEIMR HHCCCCCCCCHHHHH	54.37	-
141	Ubiquitination	GSVEIMRKDLNDARD CCHHHHHCCHHCHHH	49.54	29967540
155	Phosphorylation	DLHGQAESAAAVWKG HHHCCHHHHHHHHHH	26.65	27050516
161	Ubiquitination	ESAAAVWKGHVMDRR HHHHHHHHHHHHHHH	32.32	21906983
170	Ubiquitination	HVMDRRKKALTDYKK HHHHHHHHHHCCHHH	46.98	29967540
176	Ubiquitination	KKALTDYKKLRAFFV HHHHCCHHHHHHHHH	48.41	27667366
177	Ubiquitination	KALTDYKKLRAFFVE HHHCCHHHHHHHHHH	36.66	-
195	Ubiquitination	HFLQEAEKEEGLPED HHHHHHHHHCCCCHH	69.02	PubMed
223	Ubiquitination	QAVSELEKKHRNLGL HHHHHHHHHHHHCCH	67.51	21963094
224	Ubiquitination	AVSELEKKHRNLGLS HHHHHHHHHHHCCHH	38.12	20852630PubMed

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

Oops, there are no upstream regulatory protein records of RN187_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
48	K	ubiquitylation	'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-223 and Lys-224) and are thus mutually exclusive.	20852630
48	K	ubiquitylation	Lys-48'-autoubiquitination leads to degradation by the proteasome, while MAP3K1-induced 'Lys-63'-linked polyubiquitination results in the stabilization of the protein.	20852630
195	K	ubiquitylation	'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-223 and Lys-224) and are thus mutually exclusive.	20852630
223	K	ubiquitylation	'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-223 and Lys-224) and are thus mutually exclusive.	20852630
224	K	ubiquitylation	'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-223 and Lys-224) and are thus mutually exclusive.	20852630

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RN187_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JUN_HUMAN	JUN	physical	20852630
RN187_HUMAN	RNF187	physical	23624934
ANM1_HUMAN	PRMT1	physical	23624934

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.