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Overview

Uniprot IDO14979
Protein NameHeterogeneous nuclear ribonucleoprotein D-like
Gene NameHNRNPDL
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
142 GSKINASKNQQDDGK
162 LSWDTSKKDLTEYLS
180 EVVDCTIKTDPVTGR
209 VDKVLELKEHKLDGK
234 KGKEPPKKVFVGGLS
306 GSGKCEIKVAQPKEV
311 EIKVAQPKEVYRQQQ
76 LAGGAAIKGGRRRRP

Function

Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence

Protein Sequence

10 MEVPPRLSHV 20 PPPLFPSAPA 30 TLASRSLSHW 40 RPRPPRQLAP 50 LLPSLAPSSA 60 RQGARRAQRH 70 VTAQQPSRLA 80 GGAAIKGGRR 90 RRPDLFRRHF 100 KSSSIQRSAA 110 AAAATRTARQ 120 HPPADSSVTM 130 EDMNEYSNIE 140 EFAEGSKINA 150 SKNQQDDGKM 160 FIGGLSWDTS 170 KKDLTEYLSR 180 FGEVVDCTIK 190 TDPVTGRSRG 200 FGFVLFKDAA 210 SVDKVLELKE 220 HKLDGKLIDP 230 KRAKALKGKE 240 PPKKVFVGGL 250 SPDTSEEQIK 260 EYFGAFGEIE 270 NIELPMDTKT 280 NERRGFCFIT 290 YTDEEPVKKL 300 LESRYHQIGS 310 GKCEIKVAQP 320 KEVYRQQQQQ 330 QKGGRGAAAG 340 GRGGTRGRGR 350 GQGQNWNQGF 360 NNYYDQGYGN 370 YNSAYGGDQN 380 YSGYGGYDYT 390 GYNYGNYGYG 400 QGYADYSGQQ 410 STYGKASRGG 420 GNHQNNYQPY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005829 cytosol
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:0003690 double-stranded DNA binding
Molecular Function GO:0008143 poly(A) binding
Molecular Function GO:0034046 poly(G) binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0010468 regulation of gene expression
Biological Process GO:0006396 RNA 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] 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] 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.