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Overview

Uniprot IDP09012
Protein NameU1 small nuclear ribonucleoprotein A
Gene NameSNRPA
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
112 DRKREKRKPKSQETP
114 KREKRKPKSQETPAT
122 SQETPATKKAVQGGG
123 QETPATKKAVQGGGA
96 TDSDIIAKMKGTFVE
98 SDIIAKMKGTFVERD

Function

Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs

Protein Sequence

10 MAVPETRPNH 20 TIYINNLNEK 30 IKKDELKKSL 40 YAIFSQFGQI 50 LDILVSRSLK 60 MRGQAFVIFK 70 EVSSATNALR 80 SMQGFPFYDK 90 PMRIQYAKTD 100 SDIIAKMKGT 110 FVERDRKREK 120 RKPKSQETPA 130 TKKAVQGGGA 140 TPVVGAVQGP 150 VPGMPPMTQA 160 PRIMHHMPGQ 170 PPYMPPPGMI 180 PPPGLAPGQI 190 PPGAMPPQQL 200 MPGQMPPAQP 210 LSENPPNHIL 220 FLTNLPEETN 230 ELMLSMLFNQ 240 FPGFKEVRLV 250 PGRHDIAFVE 260 FDNEVQAGAA 270 RDALQGFKIT 280 QNNAMKISFA KK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005681 spliceosomal complex
Cellular Component GO:0005685 U1 snRNP
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0030619 U1 snRNA binding
Molecular Function GO:1990446 U1 snRNP binding
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0000387 spliceosomal snRNP 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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] 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.

[7] 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.