RN138_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN138_RAT
• UniProt AC: Q99PD2
• Protein Name: E3 ubiquitin-protein ligase RNF138 {ECO:0000305}
• Gene Name: Rnf138 {ECO:0000312|RGD:621485}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 209
• Subcellular Localization: Chromosome . Recruited at DNA damage sites. Localizes to sites of double-strand break: localization to double-strand break sites is mediated by the zinc fingers.
• Protein Description: E3 ubiquitin-protein ligase involved in DNA damage response by promoting DNA resection and homologous recombination. Recruited to sites of double-strand breaks following DNA damage and specifically promotes double-strand break repair via homologous recombination. Two different, non-exclusive, mechanisms have been proposed. According to a report, regulates the choice of double-strand break repair by favoring homologous recombination over non-homologous end joining (NHEJ): acts by mediating ubiquitination of XRCC5/Ku80, leading to remove the Ku complex from DNA breaks, thereby promoting homologous recombination. According to another report, cooperates with UBE2Ds E2 ubiquitin ligases (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) to promote homologous recombination by mediating ubiquitination of RBBP8/CtIP. Together with NLK, involved in the ubiquitination and degradation of TCF/LEF. Also exhibits auto-ubiquitination activity in combination with UBE2K. May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway..
• Protein Sequence: MSEELSADTSYTEDDFYCPVCQEVLKTPVRTAACQHVFCRKCFLTAMRESGIHCPLCRGSVTRRERACPERAIDLENIMRRVSGSCRCCSKKIKFYRMRHHYKSCKKYQDEYGVSSVIPNVKISQDSVRSSNRSETSASDNTETYQEDTSSSGHPTFKCPLCQESNFTRQRLLDHCNSNHLFQIVPVNLQLDEETQYQTAVEESFQVNM

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
139	Phosphorylation	NRSETSASDNTETYQ CCCCCCCCCCCCCCC	31.03	30181290
142	Phosphorylation	ETSASDNTETYQEDT CCCCCCCCCCCCCCC	34.39	30181290
144	Phosphorylation	SASDNTETYQEDTSS CCCCCCCCCCCCCCC	28.59	30181290
145	Phosphorylation	ASDNTETYQEDTSSS CCCCCCCCCCCCCCC	12.04	30181290
149	Phosphorylation	TETYQEDTSSSGHPT CCCCCCCCCCCCCCC	29.74	30181290
150	Phosphorylation	ETYQEDTSSSGHPTF CCCCCCCCCCCCCCC	34.52	30181290
151	Phosphorylation	TYQEDTSSSGHPTFK CCCCCCCCCCCCCCC	42.29	30181290
152	Phosphorylation	YQEDTSSSGHPTFKC CCCCCCCCCCCCCCC	40.67	30181290
156	Phosphorylation	TSSSGHPTFKCPLCQ CCCCCCCCCCCCCCC	30.01	30181290

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

Oops, there are no upstream regulatory protein records of RN138_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN138_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RN138_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAC1A_HUMAN	CACNA1A	physical	28167673

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.