RN138_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN138_MOUSE
• UniProt AC: Q9CQE0
• Protein Name: E3 ubiquitin-protein ligase RNF138 {ECO:0000305}
• Gene Name: Rnf138 {ECO:0000312|MGI:MGI:1929211}
• Organism: Mus musculus (Mouse).
• Sequence Length: 245
• 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: MSEELSAATSYTEDDFYCPVCQEVLKTPVRTAACQHVFCRKCFLTAMRESGIHCPLCRGSVTRRERACPERALDLENIMRRFSGSCRCCSKKIKFYRMRHHYKSCKKYQDEYGVSSVIPNFKISQDSVRSSNRSETSASDNTETYQEDTSSSGHPTFKCPLCQESNFTRQRLLDHCNSNHLFQIVPVTCPICVSLPWGDPSQITRNFVSHLNQRHQFDYGEFVNLQLDEETQYQTAVEESFQVNM

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
96	Phosphorylation	CSKKIKFYRMRHHYK CHHHHHHHHHHHHHH	9.86	20139300
122	Ubiquitination	SSVIPNFKISQDSVR CCCCCCCEECHHHHC	48.35	-
136	Phosphorylation	RSSNRSETSASDNTE CCCCCCCCCCCCCCC	30.73	25338131
137	Phosphorylation	SSNRSETSASDNTET CCCCCCCCCCCCCCC	23.02	25338131
139	Phosphorylation	NRSETSASDNTETYQ CCCCCCCCCCCCCCC	31.03	25338131
142	Phosphorylation	ETSASDNTETYQEDT CCCCCCCCCCCCCCC	34.39	-

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

Oops, there are no upstream regulatory protein records of RN138_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN138_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RN138_MOUSE !!

Drug and Disease Associations

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