Search Results

Overview

Uniprot IDP07910
Protein NameHeterogeneous nuclear ribonucleoproteins C1/C2
Gene NameHNRNPC
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
157 ARAVVPSKRQRVSGN
170 GNTSRRGKSGFNSKS
176 GKSGFNSKSGQRGSS
189 SSKSGKLKGDDLQAI
197 GDDLQAIKKELTQIK
198 DDLQAIKKELTQIKQ
204 KKELTQIKQKVDSLL
206 ELTQIKQKVDSLLEN
223 KIEKEQSKQAVEMKN
229 SKQAVEMKNDKSEEE
232 AVEMKNDKSEEEQSS
243 EQSSSSVKKDETNVK
244 QSSSSVKKDETNVKM
29 NLNTLVVKKSDVEAI
30 LNTLVVKKSDVEAIF
39 DVEAIFSKYGKIVGC
42 AIFSKYGKIVGCSVH
50 IVGCSVHKGFAFVQY
8 MASNVTNKTDPRSMN
89 INLAAEPKVNRGKAG

Function

Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671)

Protein Sequence

10 MASNVTNKTD 20 PRSMNSRVFI 30 GNLNTLVVKK 40 SDVEAIFSKY 50 GKIVGCSVHK 60 GFAFVQYVNE 70 RNARAAVAGE 80 DGRMIAGQVL 90 DINLAAEPKV 100 NRGKAGVKRS 110 AAEMYGSVTE 120 HPSPSPLLSS 130 SFDLDYDFQR 140 DYYDRMYSYP 150 ARVPPPPPIA 160 RAVVPSKRQR 170 VSGNTSRRGK 180 SGFNSKSGQR 190 GSSKSGKLKG 200 DDLQAIKKEL 210 TQIKQKVDSL 220 LENLEKIEKE 230 QSKQAVEMKN 240 DKSEEEQSSS 250 SVKKDETNVK 260 MESEGGADDS 270 AEEGDLLDDD 280 DNEDRGDDQL 290 ELIKDDEKEA 300 EEGEDDRDSA NGEDDS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Molecular Function GO:0008266 poly(U) RNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0070034 telomerase RNA binding
Biological Process GO:0070935 3'-UTR-mediated mRNA stabilization
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0032211 negative regulation of telomere maintenance via telomerase
Biological Process GO:0001649 osteoblast differentiation
Biological Process GO:0008380 RNA splicing
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0005681 spliceosomal complex
Cellular Component GO:0005697 telomerase holoenzyme complex
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:1990247 N6-methyladenosine-containing RNA reader activity
Molecular Function GO:0031492 nucleosomal DNA binding

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] 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.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.

[12] 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.