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Overview

Uniprot IDQ52LJ0
Protein NametRNA-splicing ligase complex subunit FAM98B
Gene NameFAM98B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
292 SSGTSREKTACAINK
299 KTACAINKVLMGRVP
327 PEMPPWQKRQEGGGG

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. May act as an RNA ligase with broad substrate specificity and may function toward other RNAs (PubMed:21311021, PubMed:24870230). Could regulate the expression of PRMT1, a protein arginine N-methyltransferase (PubMed:28040436)

Protein Sequence

10 MRGPEPGPQP 20 TMEGDVLDTL 30 EALGYKGPLL 40 EEQALTKAAE 50 GGLSSPEFSE 60 LCIWLGSQIK 70 SLCNLEESIT 80 SAGRDDLESF 90 QLEISGFLKE 100 MACPYSVLIS 110 GDIKDRLKKK 120 EDCLKLLLFL 130 STELQASQIL 140 QNKKHKNSQL 150 DKNSEVYQEV 160 QAMFDTLGIP 170 KSTTSDIPHM 180 LNQVESKVKD 190 ILSKVQKNHV 200 GKPLLKMDLN 210 SEQAEQLERI 220 NDALSCEYEC 230 RRRMLMKRLD 240 VTVQSFGWSD 250 RAKVKTDDIA 260 RIYQPKRYAL 270 SPKTTITMAH 280 LLAAREDLSK 290 IIRTSSGTSR 300 EKTACAINKV 310 LMGRVPDRGG 320 RPNEIEPPPP 330 EMPPWQKRQE 340 GGGGRGGWGG 350 GGGGGGRGGG 360 GGGGGRGGWG 370 GGGGGWGGGG 380 GGGGGWGGGG 390 GGGRGGFQGR 400 GDYGGRGGYG 410 GRGGYGGRGY 420 GDPYGGGGGG 430 GGGGGGGGGY RRY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0072669 tRNA-splicing ligase complex
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008276 protein methyltransferase activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0008284 positive regulation of cell population proliferation
Biological Process GO:0010628 positive regulation of gene expression
Biological Process GO:0006479 protein methylation
Biological Process GO:0006388 tRNA splicing, via endonucleolytic cleavage and ligation

Reference

[1] 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.