RN212_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN212_HUMAN
• UniProt AC: Q495C1
• Protein Name: Probable E3 SUMO-protein ligase RNF212
• Gene Name: RNF212
• Organism: Homo sapiens (Human).
• Sequence Length: 297
• Subcellular Localization: Nucleus. Chromosome. Associates to the synaptonemal complex. Localizes to a minority of double-strand breaks (DSBs) sites. Marks crossover sites during midpachynema (By similarity)..
• Protein Description: SUMO E3 ligase that acts as a regulator of crossing-over during meiosis: required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11. May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to enhance their binding to recombination sites. Acts as a limiting factor for crossover designation and/or reinforcement and plays an antagonist role with CCNB1IP1/HEI10 in the regulation of meiotic recombination (By similarity)..
• Protein Sequence: MANWVFCNRCFQPPHRTSCFSLTNCGHVYCDACLGKGKKNECLICKAPCRTVLLSKHTDADIQAFFMSIDSLCKKYSRETSQILEFQEKHRKRLLAFYREKISRLEESLRKSVLQIEQLQSMRSSQQTAFSTIKSSVSTKPHGCLLPPHSSAPDRLESMEVDLSPSPIRKSEIAAGPARISMISPPQDGRMGPHLTASFCFIPWLTLSKPPVPGECVISRGSPCFCIDVCPHWLLLLAFSSGRHGELTNSKTLPIYAEVQRAVLFPFQQAEGTLDTFRTPAVSVVFPLCQFERKKSF

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
35	Ubiquitination	VYCDACLGKGKKNEC EECHHHCCCCCCCCE	36.23	21890473
57	Ubiquitination	RTVLLSKHTDADIQA CEEEEECCCCHHHHH	26.13	21890473
101 (in isoform 5)	Ubiquitination	-	36.66	21890473
101 (in isoform 3)	Ubiquitination	-	36.66	21890473
101 (in isoform 2)	Ubiquitination	-	36.66	21890473
101 (in isoform 1)	Ubiquitination	-	36.66	21890473
101	Ubiquitination	LLAFYREKISRLEES HHHHHHHHHHHHHHH	36.66	21890473
112	Phosphorylation	LEESLRKSVLQIEQL HHHHHHHHHHHHHHH	22.94	22210691
121	Phosphorylation	LQIEQLQSMRSSQQT HHHHHHHHHHHCCHH	25.42	25159151
135	Phosphorylation	TAFSTIKSSVSTKPH HHHHHHHHCCCCCCC	31.93	-
164	Phosphorylation	ESMEVDLSPSPIRKS HHCEEECCCCCCCHH	20.90	24719451
166	Phosphorylation	MEVDLSPSPIRKSEI CEEECCCCCCCHHHC	29.59	26546556
171	Phosphorylation	SPSPIRKSEIAAGPA CCCCCCHHHCCCCCC	25.12	-
246 (in isoform 6)	Phosphorylation	-	46.42	24719451
252	Phosphorylation	GELTNSKTLPIYAEV CCCCCCCCCCEEEEE	37.27	27174698
256	Phosphorylation	NSKTLPIYAEVQRAV CCCCCCEEEEEHHEE	8.51	27174698
256 (in isoform 6)	Phosphorylation	-	8.51	24719451
268 (in isoform 6)	Phosphorylation	-	41.64	24719451

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

Oops, there are no upstream regulatory protein records of RN212_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN212_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 RN212_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of RN212_HUMAN !!

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.