Search Results

Overview

Uniprot ID	P08579
Protein Name	U2 small nuclear ribonucleoprotein B''
Gene Name	SNRPB2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
111	KKEKKKAKTVEQTAT
122	QTATTTNKKPGQGTP
123	TATTTNKKPGQGTPN
85	PMRIQYAKTDSDIIS
93	TDSDIISKMRGTFAD

Function

Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA (PubMed:32494006, PubMed:9716128)

Protein Sequence

10 MDIRPNHTIY 20 INNMNDKIKK 30 EELKRSLYAL 40 FSQFGHVVDI 50 VALKTMKMRG 60 QAFVIFKELG 70 SSTNALRQLQ 80 GFPFYGKPMR 90 IQYAKTDSDI 100 ISKMRGTFAD 110 KEKKKEKKKA 120 KTVEQTATTT 130 NKKPGQGTPN 140 SANTQGNSTP 150 NPQVPDYPPN 160 YILFLNNLPE 170 ETNEMMLSML 180 FNQFPGFKEV 190 RLVPGRHDIA 200 FVEFENDGQA 210 GAARDALQGF 220 KITPSHAMKI TYAKK

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0071013	catalytic step 2 spliceosome
Cellular Component	GO:0016607	nuclear speck
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005681	spliceosomal complex
Cellular Component	GO:0005685	U1 snRNP
Cellular Component	GO:0005686	U2 snRNP
Cellular Component	GO:0071007	U2-type catalytic step 2 spliceosome
Cellular Component	GO:0071005	U2-type precatalytic spliceosome
Cellular Component	GO:0005684	U2-type spliceosomal complex
Molecular Function	GO:0030619	U1 snRNA binding
Biological Process	GO:0000398	mRNA splicing, via spliceosome
Biological Process	GO:0000387	spliceosomal snRNP assembly
Biological Process	GO:1903241	U2-type prespliceosome 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] 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.

[4] 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.

[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.