Search Results

Overview

Uniprot IDQ9Y224
Protein NametRNA-splicing ligase complex subunit RTRAF
Gene NameRTRAF
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
108 DLVPDNSKTADNATK
115 KTADNATKNAEPLIN
171 LTQDAVAKANQTKEG
234 QAIIADPKTDHRLGK

Function

Accessory 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 (PubMed:21311021, PubMed:24870230). RNA-binding protein involved in modulation of mRNA transcription by Polymerase II (PubMed:16950395). Could also play a role in RNA transport (PubMed:24608264)

Protein Sequence

10 MFRRKLTALD 20 YHNPAGFNCK 30 DETEFRNFIV 40 WLEDQKIRHY 50 KIEDRGNLRN 60 IHSSDWPKFF 70 EKYLRDVNCP 80 FKIQDRQEAI 90 DWLLGLAVRL 100 EYGDNAEKYK 110 DLVPDNSKTA 120 DNATKNAEPL 130 INLDVNNPDF 140 KAGVMALANL 150 LQIQRHDDYL 160 VMLKAIRILV 170 QERLTQDAVA 180 KANQTKEGLP 190 VALDKHILGF 200 DTGDAVLNEA 210 AQILRLLHIE 220 ELRELQTKIN 230 EAIVAVQAII 240 ADPKTDHRLG KVGR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005813 centrosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0072686 mitotic spindle
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0072669 tRNA-splicing ligase complex
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0000993 RNA polymerase II complex binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006469 negative regulation of protein kinase activity
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0050658 RNA transport
Biological Process GO:0006388 tRNA splicing, via endonucleolytic cleavage and ligation

Reference

[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.