Search Results

Overview

Uniprot IDP82979
Protein NameSAP domain-containing ribonucleoprotein
Gene NameSARNP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 TETVELHKLKLAELK
119 VPVSLESKKAARAAR
12 TVELHKLKLAELKQE
120 PVSLESKKAARAARF
135 GISSVPTKGLSSDNK
149 KPMVNLDKLKERAQR
151 MVNLDKLKERAQRFG
17 KLKLAELKQECLARG
31 GLETKGIKQDLIHRL
88 TVDVAAEKKVVKITS
89 VDVAAEKKVVKITSE
92 AAEKKVVKITSEIPQ

Function

Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15338056, PubMed:17196963, PubMed:20844015). The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15338056, PubMed:17196963, PubMed:20844015). Associates with DDX39B, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export (PubMed:37578863)

Protein Sequence

10 MATETVELHK 20 LKLAELKQEC 30 LARGLETKGI 40 KQDLIHRLQA 50 YLEEHAEEEA 60 NEEDVLGDET 70 EEEETKPIEL 80 PVKEEEPPEK 90 TVDVAAEKKV 100 VKITSEIPQT 110 ERMQKRAERF 120 NVPVSLESKK 130 AARAARFGIS 140 SVPTKGLSSD 150 NKPMVNLDKL 160 KERAQRFGLN 170 VSSISRKSED 180 DEKLKKRKER 190 FGIVTSSAGT 200 GTTEDTEAKK 210 RKRAERFGIA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000346 transcription export complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006406 mRNA export from nucleus
Biological Process GO:0016973 poly(A)+ mRNA export from nucleus
Biological Process GO:0006417 regulation of translation

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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[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] 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.

[7] 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.

[8] 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.

[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.