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Overview

Uniprot IDQ14103
Protein NameHeterogeneous nuclear ribonucleoprotein D0
Gene NameHNRNPD
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
110 GLSWDTTKKDLKDYF
129 EVVDCTLKLDPITGR
153 KESESVDKVMDQKEH
183 KTKEPVKKIFVGGLS
197 SPDTPEEKIREYFGG
218 IELPMDNKTNKRRGF
221 PMDNKTNKRRGFCFI
243 VKKIMEKKYHNVGLS
251 YHNVGLSKCEIKVAM

Function

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. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation

Protein Sequence

10 MSEEQFGGDG 20 AAAAATAAVG 30 GSAGEQEGAM 40 VAATQGAAAA 50 AGSGAGTGGG 60 TASGGTEGGS 70 AESEGAKIDA 80 SKNEEDEGHS 90 NSSPRHSEAA 100 TAQREEWKMF 110 IGGLSWDTTK 120 KDLKDYFSKF 130 GEVVDCTLKL 140 DPITGRSRGF 150 GFVLFKESES 160 VDKVMDQKEH 170 KLNGKVIDPK 180 RAKAMKTKEP 190 VKKIFVGGLS 200 PDTPEEKIRE 210 YFGGFGEVES 220 IELPMDNKTN 230 KRRGFCFITF 240 KEEEPVKKIM 250 EKKYHNVGLS 260 KCEIKVAMSK 270 EQYQQQQQWG 280 SRGGFAGRAR 290 GRGGGPSQNW 300 NQGYSNYWNQ 310 GYGNYGYNSQ 320 GYGGYGGYDY 330 TGYNNYYGYG 340 DYSNQQSGYG 350 KVSRRGGHQN SYKPY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005829 cytosol
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0014069 postsynaptic density
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0042826 histone deacetylase binding
Molecular Function GO:0003680 minor groove of adenine-thymine-rich DNA binding
Molecular Function GO:0035925 mRNA 3'-UTR AU-rich region binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0042162 telomeric DNA binding
Biological Process GO:0061158 3'-UTR-mediated mRNA destabilization
Biological Process GO:0071230 cellular response to amino acid stimulus
Biological Process GO:0071392 cellular response to estradiol stimulus
Biological Process GO:0071732 cellular response to nitric oxide
Biological Process GO:1904586 cellular response to putrescine
Biological Process GO:0021549 cerebellum development
Biological Process GO:0097167 circadian regulation of translation
Biological Process GO:0070934 CRD-mediated mRNA stabilization
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:1990828 hepatocyte dedifferentiation
Biological Process GO:0001889 liver development
Biological Process GO:1900152 negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
Biological Process GO:2000767 positive regulation of cytoplasmic translation
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:1904355 positive regulation of telomere capping
Biological Process GO:0032212 positive regulation of telomere maintenance via telomerase
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:0042752 regulation of circadian rhythm
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0010468 regulation of gene expression
Biological Process GO:0051592 response to calcium ion
Biological Process GO:0051602 response to electrical stimulus
Biological Process GO:1901355 response to rapamycin
Biological Process GO:1904383 response to sodium phosphate
Biological Process GO:0006401 RNA catabolic process
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] 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.

[4] 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.

[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] 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.

[8] 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.

[9] 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.

[10] 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.

[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.