UniProt Accession

 RTCB_MOUSE; Q99LF4; Q3TA04; Q3TI25; Q3UDW6 

Genbank Protein ID

 AY424364; AK145891; AK145916; AK149885; AK150376; AK150470; AK151042; AK151182; AK151932; AK152144; AK153434; AK168038; AK172175; BC003288 

Genbank Nucleotide ID

 AAR02005.1; BAE26729.1; BAE26747.1; BAE29145.1; BAE29508.1; BAE29587.1; BAE30059.1; BAE30183.1; BAE30808.1; BAE30981.1; BAE31991.1; BAE40021.1; BAE42866.1; AAH03288.1 

Protein Name

 tRNA-splicing ligase RtcB homolog 

Protein Synonyms/Alias

 Focal adhesion-associated protein; FAAP 

Gene Name

 D10Wsu52e 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
67	GGFLPAMKQIGNVAA	ubiquitination	[1]
279	DALVAMEKAMKRDKI	ubiquitination	[1]
285	EKAMKRDKIIVNDRQ	ubiquitination	[1]
366	EQHVVDGKERTLLVH	ubiquitination	[1]
465	AIRVASPKLVMEEAP	ubiquitination	[1]
492	CHDAGISKKAIKLRP	ubiquitination	[1]
496	GISKKAIKLRPIAVI	acetylation	[2, 3]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

Functional 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 a RNA ligase with broad substrate specificity, and may function toward other RNAs (By similarity). Essential during post-implantation development of embryos. 

Sequence Annotation

 METAL 122 122 Zinc (Potential).
 METAL 227 227 Zinc (Potential).
 METAL 259 259 Zinc (Potential).  

Keyword

 ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Reference proteome; tRNA processing; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 505 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0072669; C:tRNA-splicing ligase complex; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003972; F:RNA ligase (ATP) activity; ISS:UniProtKB.
 GO:0001701; P:in utero embryonic development; IMP:MGI.
 GO:0001890; P:placenta development; IMP:MGI.
 GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:UniProtKB. 

Interpro

 IPR027513; RtcB_euk.
 IPR001233; RtcB_family. 

Pfam

 PF01139; UPF0027 

SMART

  

PROSITE

 PS01288; UPF0027 

PRINTS