Search Results

Overview

Uniprot IDP05455
Protein NameLupus La protein
Gene NameSSB
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
105 PEVTDEYKNDVKNRS
166 DSIESAKKFVETPGQ
174 FVETPGQKYKETDLL
191 FKDDYFAKKNEERKQ
192 KDDYFAKKNEERKQN
200 NEERKQNKVEAKLRA
208 VEAKLRAKQEQEAKQ
216 QEQEAKQKLEEDAEM
269 IDFVRGAKEGIILFK
278 GIILFKEKAKEALGK
287 KEALGKAKDANNGNL
317 VEKEALKKIIEDQQE
328 DQQESLNKWKSKGRR
330 QESLNKWKSKGRRFK
344 KGKGKGNKAAQPGSG
352 AAQPGSGKGKVQFQG
354 QPGSGKGKVQFQGKK
360 GKVQFQGKKTKFASD
363 QFQGKKTKFASDDEH
383 NGATGPVKRAREETD
397 DKEEPASKQQKTENG
76 VEALSKSKAELMEIS

Function

Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation (PubMed:2470590, PubMed:3192525). In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:12384597)

Protein Sequence

10 MAENGDNEKM 20 AALEAKICHQ 30 IEYYFGDFNL 40 PRDKFLKEQI 50 KLDEGWVPLE 60 IMIKFNRLNR 70 LTTDFNVIVE 80 ALSKSKAELM 90 EISEDKTKIR 100 RSPSKPLPEV 110 TDEYKNDVKN 120 RSVYIKGFPT 130 DATLDDIKEW 140 LEDKGQVLNI 150 QMRRTLHKAF 160 KGSIFVVFDS 170 IESAKKFVET 180 PGQKYKETDL 190 LILFKDDYFA 200 KKNEERKQNK 210 VEAKLRAKQE 220 QEAKQKLEED 230 AEMKSLEEKI 240 GCLLKFSGDL 250 DDQTCREDLH 260 ILFSNHGEIK 270 WIDFVRGAKE 280 GIILFKEKAK 290 EALGKAKDAN 300 NGNLQLRNKE 310 VTWEVLEGEV 320 EKEALKKIIE 330 DQQESLNKWK 340 SKGRRFKGKG 350 KGNKAAQPGS 360 GKGKVQFQGK 370 KTKFASDDEH 380 DEHDENGATG 390 PVKRAREETD 400 KEEPASKQQK TENGAGDQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0010494 cytoplasmic stress granule
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0008266 poly(U) RNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:1990825 sequence-specific mRNA binding
Molecular Function GO:0000049 tRNA binding
Biological Process GO:0008334 histone mRNA metabolic process
Biological Process GO:0075522 IRES-dependent viral translational initiation
Biological Process GO:0071045 nuclear histone mRNA catabolic process
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:1903608 protein localization to cytoplasmic stress granule
Biological Process GO:0042780 tRNA 3'-end processing
Biological Process GO:0001682 tRNA 5'-leader removal
Biological Process GO:0006409 tRNA export from nucleus
Biological Process GO:0006400 tRNA modification
Biological Process GO:0008033 tRNA processing

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] 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.

[5] 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.

[6] 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.

[7] 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.

[8] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[9] 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.

[10] 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.

[11] 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.