Search Results

Overview

Uniprot ID	Q9Y5U2
Protein Name	U5 small nuclear ribonucleoprotein TSSC4
Gene Name	TSSC4
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
123	MSDNGGFKRPLAPSG
217	EGRVIFTKPVRGVEA
234	ERKRVLGKVGEPGRG
318	SRDHFRNKSSSPEDP

Function

Protein associated with the U5 snRNP, during its maturation and its post-splicing recycling and which is required for spliceosomal tri-snRNP complex assembly in the nucleus (PubMed:34131137, PubMed:35188580). Has a molecular sequestering activity and transiently hinders SNRNP200 binding sites for constitutive splicing factors that intervene later during the assembly of the spliceosome and splicing (PubMed:35188580). Together with its molecular sequestering activity, may also function as a molecular adapter and placeholder, coordinating the assembly of the U5 snRNP and its association with the U4/U6 di-snRNP (PubMed:34131137)

Protein Sequence

10 MAEAGTGEPS 20 PSVEGEHGTE 30 YDTLPSDTVS 40 LSDSDSDLSL 50 PGGAEVEALS 60 PMGLPGEEDS 70 GPDEPPSPPS 80 GLLPATVQPF 90 HLRGMSSTFS 100 QRSRDIFDCL 110 EGAARRAPSS 120 VAHTSMSDNG 130 GFKRPLAPSG 140 RSPVEGLGRA 150 HRSPASPRVP 160 PVPDYVAHPE 170 RWTKYSLEDV 180 TEVSEQSNQA 190 TALAFLGSQS 200 LAAPTDCVSS 210 FNQDPSSCGE 220 GRVIFTKPVR 230 GVEARHERKR 240 VLGKVGEPGR 250 GGLGNPATDR 260 GEGPVELAHL 270 AGPGSPEAEE 280 WGSHHGGLQE 290 VEALSGSVHS 300 GSVPGLPPVE 310 TVGFHGSRKR 320 SRDHFRNKSS SPEDPGAEV

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005681	spliceosomal complex
Cellular Component	GO:0005682	U5 snRNP
Molecular Function	GO:0140313	molecular sequestering activity
Molecular Function	GO:0044877	protein-containing complex binding
Biological Process	GO:0000387	spliceosomal snRNP assembly
Biological Process	GO:0000244	spliceosomal tri-snRNP complex assembly

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[5] 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.

[6] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[7] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[8] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.