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Overview

Uniprot IDQ8IYB3
Protein NameSerine/arginine repetitive matrix protein 1
Gene NameSRRM1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
140 QRQIEQEKLASMKKQ
246 TSTSDILKVPKPEPI
257 PEPIPEPKEPSPEKN
29 KKLLKQLKFAECLEK
36 KFAECLEKKVDMSKV
459 SPAPKPRKVELSESE
472 SEEDKGGKMAAADSV
513 RPKRSHVKNGEVGRR
735 PEPKKIKKAASPSPQ

Function

Part of pre- and post-splicing multiprotein mRNP complexes. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates

Protein Sequence

10 MDAGFFRGTS 20 AEQDNRFSNK 30 QKKLLKQLKF 40 AECLEKKVDM 50 SKVNLEVIKP 60 WITKRVTEIL 70 GFEDDVVIEF 80 IFNQLEVKNP 90 DSKMMQINLT 100 GFLNGKNARE 110 FMGELWPLLL 120 SAQENIAGIP 130 SAFLELKKEE 140 IKQRQIEQEK 150 LASMKKQDED 160 KDKRDKEEKE 170 SSREKRERSR 180 SPRRRKSRSP 190 SPRRRSSPVR 200 RERKRSHSRS 210 PRHRTKSRSP 220 SPAPEKKEKT 230 PELPEPSVKV 240 KEPSVQEATS 250 TSDILKVPKP 260 EPIPEPKEPS 270 PEKNSKKEKE 280 KEKTRPRSRS 290 RSKSRSRTRS 300 RSPSHTRPRR 310 RHRSRSRSYS 320 PRRRPSPRRR 330 PSPRRRTPPR 340 RMPPPPRHRR 350 SRSPVRRRRR 360 SSASLSGSSS 370 SSSSSRSRSP 380 PKKPPKRTSS 390 PPRKTRRLSP 400 SASPPRRRHR 410 PSPPATPPPK 420 TRHSPTPQQS 430 NRTRKSRVSV 440 SPGRTSGKVT 450 KHKGTEKRES 460 PSPAPKPRKV 470 ELSESEEDKG 480 GKMAAADSVQ 490 QRRQYRRQNQ 500 QSSSDSGSSS 510 SSEDERPKRS 520 HVKNGEVGRR 530 RRHSPSRSAS 540 PSPRKRQKET 550 SPRGRRRRSP 560 SPPPTRRRRS 570 PSPAPPPRRR 580 RTPTPPPRRR 590 TPSPPPRRRS 600 PSPRRYSPPI 610 QRRYSPSPPP 620 KRRTASPPPP 630 PKRRASPSPP 640 PKRRVSHSPP 650 PKQRSSPVTK 660 RRSPSLSSKH 670 RKGSSPSRST 680 REARSPQPNK 690 RHSPSPRPRA 700 PQTSSSPPPV 710 RRGASSSPQR 720 RQSPSPSTRP 730 IRRVSRTPEP 740 KKIKKAASPS 750 PQSVRRVSSS 760 RSVSGSPEPA 770 AKKPPAPPSP 780 VQSQSPSTNW 790 SPAVPVKKAK 800 SPTPSPSPPR 810 NSDQEGGGKK 820 KKKKKDKKHK 830 KDKKHKKHKK 840 HKKEKAVAAA 850 AAAAVTPAAI 860 AAATTTLAQE 870 EPVAAPEPKK 880 ETESEAEDNL 890 DDLEKHLREK 900 ALRSMRKAQV SPQS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005681 spliceosomal complex
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0048024 regulation of mRNA splicing, via spliceosome
Biological Process GO:0008380 RNA splicing
Biological Process GO:0000375 RNA splicing, via transesterification reactions

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] 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.

[5] 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.

[6] 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.

[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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[9] 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.