Search Results

Overview

Uniprot IDQ4G0J3
Protein NameLa-related protein 7
Gene NameLARP7
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
205 GIFPKTVKNKPIPAL
250 TSNTSISKMKRSRPT
252 NTSISKMKRSRPTSE
318 KVKKIIQKDIIKEAS
556 EKKRGTEKLITKAEK
568 AEKIRLAKTQQASKH
574 AKTQQASKHIRFSEY

Function

RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function (PubMed:18249148, PubMed:32017898). Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II (PubMed:18249148, PubMed:18483487). The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (PubMed:18249148, PubMed:18483487). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (PubMed:28254838). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex (PubMed:18281698, PubMed:18483487). LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing (PubMed:32017898). Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes (PubMed:32017898). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (PubMed:32017898). Binds U6 snRNAs with a 5'-CAGGG-3' sequence motif (PubMed:32017898). U6 snRNA processing is required for spermatogenesis (By similarity)

Protein Sequence

10 METESGNQEK 20 VMEEESTEKK 30 KEVEKKKRSR 40 VKQVLADIAK 50 QVDFWFGDAN 60 LHKDRFLREQ 70 IEKSRDGYVD 80 ISLLVSFNKM 90 KKLTTDGKLI 100 ARALRSSAVV 110 ELDLEGTRIR 120 RKKPLGERPK 130 DEDERTVYVE 140 LLPKNVNHSW 150 IERVFGKCGN 160 VVYISIPHYK 170 STGDPKGFAF 180 VEFETKEQAA 190 KAIEFLNNPP 200 EEAPRKPGIF 210 PKTVKNKPIP 220 ALRVVEEKKK 230 KKKKKGRMKK 240 EDNIQAKEEN 250 MDTSNTSISK 260 MKRSRPTSEG 270 SDIESTEPQK 280 QCSKKKKKRD 290 RVEASSLPEV 300 RTGKRKRSSS 310 EDAESLAPRS 320 KVKKIIQKDI 330 IKEASEASKE 340 NRDIEISTEE 350 EKDTGDLKDS 360 SLLKTKRKHK 370 KKHKERHKMG 380 EEVIPLRVLS 390 KSEWMDLKKE 400 YLALQKASMA 410 SLKKTISQIK 420 SESEMETDSG 430 VPQNTGMKNE 440 KTANREECRT 450 QEKVNATGPQ 460 FVSGVIVKII 470 STEPLPGRKQ 480 VRDTLAAISE 490 VLYVDLLEGD 500 TECHARFKTP 510 EDAQAVINAY 520 TEINKKHCWK 530 LEILSGDHEQ 540 RYWQKILVDR 550 QAKLNQPREK 560 KRGTEKLITK 570 AEKIRLAKTQ 580 QASKHIRFSE YD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0120259 7SK snRNP
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0097322 7SK snRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0017070 U6 snRNA binding
Biological Process GO:0000494 box C/D sno(s)RNA 3'-end processing
Biological Process GO:0030154 cell differentiation
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006397 mRNA processing
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0034244 negative regulation of transcription elongation by RNA polymerase II
Biological Process GO:0032897 negative regulation of viral transcription
Biological Process GO:1904871 positive regulation of protein localization to Cajal body
Biological Process GO:1905382 positive regulation of snRNA transcription by RNA polymerase II
Biological Process GO:0048024 regulation of mRNA splicing, via spliceosome
Biological Process GO:0008380 RNA splicing
Biological Process GO:0007283 spermatogenesis
Biological Process GO:1990438 U6 2'-O-snRNA methylation

Reference

[1] 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.

[2] 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.

[3] 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.

[4] 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.

[5] 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.