RTCB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RTCB_MOUSE
• UniProt AC: Q99LF4
• Protein Name: tRNA-splicing ligase RtcB homolog {ECO:0000255|HAMAP-Rule:MF_03144}
• Gene Name: Rtcb
• Organism: Mus musculus (Mouse).
• Sequence Length: 505
• Subcellular Localization: Nucleus. Cytoplasm . Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low..
• Protein Description: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs (By similarity). Essential during post-implantation development of embryos..
• Protein Sequence: MSRNYNDELQFLDKINKNCWRIKKGFVPNMQVEGVFYVNDALEKLMFEELRNACRGGGVGGFLPAMKQIGNVAALPGIVHRSIGLPDVHSGYGFAIGNMAAFDMNDPEAVVSPGGVGFDINCGVRLLRTNLDESDVQPVKEQLAQAMFDHIPVGVGSKGVIPMNAKDLEEALEMGVDWSLREGYAWAEDKEHCEEYGRMLQADPNKVSPRAKKRGLPQLGTLGAGNHYAEIQVVDEIFNEYAAKKMGIDHKGQVCVMIHSGSRGLGHQVATDALVAMEKAMKRDKIIVNDRQLACARIASPEGQDYLKGMAAAGNYAWVNRSSMTFLTRQAFAKVFNTTPDDLDLHVIYDVSHNIAKVEQHVVDGKERTLLVHRKGSTRAFPPHHPLIAVDYQLTGQPVLIGGTMGTCSYVLTGTEQGMTETFGTTCHGAGRALSRAKSRRNLDFQDVLDKLADMGIAIRVASPKLVMEEAPESYKNVTDVVNTCHDAGISKKAIKLRPIAVIKG

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	Phosphorylation	------MSRNYNDEL ------CCCCCHHHH	29.27	19854140
17	Malonylation	QFLDKINKNCWRIKK HHHHHHHHCCCCCCC	57.88	26320211
67	Ubiquitination	GGFLPAMKQIGNVAA CCHHHHHHHHCCCCC	40.65	-
208	Phosphorylation	QADPNKVSPRAKKRG CCCCCCCCHHHHHCC	15.41	26824392
255	S-nitrosocysteine	IDHKGQVCVMIHSGS CCCCCCEEEEEECCC	1.01	-
279	Ubiquitination	DALVAMEKAMKRDKI HHHHHHHHHHHCCCE	40.47	-
285	Ubiquitination	EKAMKRDKIIVNDRQ HHHHHCCCEEECCHH	38.06	-
285	Malonylation	EKAMKRDKIIVNDRQ HHHHHCCCEEECCHH	38.06	32601280
300	Phosphorylation	LACARIASPEGQDYL HHHHHHCCCCCHHHH	22.55	24719451
366	Acetylation	EQHVVDGKERTLLVH EEEEECCCEEEEEEE	39.29	6568729
366	Ubiquitination	EQHVVDGKERTLLVH EEEEECCCEEEEEEE	39.29	27667366
439	Phosphorylation	RALSRAKSRRNLDFQ HHHHHHHHHCCCCHH	35.17	29550500
465	Ubiquitination	AIRVASPKLVMEEAP EEEECCCHHHHCCCC	51.74	27667366
485	S-palmitoylation	VTDVVNTCHDAGISK HHHHHHHHHHCCCCH	2.00	28526873
492	Ubiquitination	CHDAGISKKAIKLRP HHHCCCCHHHEECEE	44.28	-
492	Malonylation	CHDAGISKKAIKLRP HHHCCCCHHHEECEE	44.28	26320211
496	Acetylation	GISKKAIKLRPIAVI CCCHHHEECEEEEEE	43.22	23864654
496	Malonylation	GISKKAIKLRPIAVI CCCHHHEECEEEEEE	43.22	26320211

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RTCB_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 RTCB_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RTCB_MOUSE !!

Drug and Disease Associations

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