Search Results

Overview

Uniprot IDQ14978
Protein NameNucleolar and coiled-body phosphoprotein 1
Gene NameNOLC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
104 VQGPPAKKAAVPAKR
110 KKAAVPAKRVGLPPG
148 QKKQPVQKGVKPQAK
186 PPKNQKPKITPVTVK
193 KITPVTVKAQTKAPP
197 VTVKAQTKAPPKPAR
208 KPARAAPKIANGKAA
251 PKKQVVAKAPVKAAT
255 VVAKAPVKAATTPTR
301 PPSAPPPKKSLGTQP
302 PSAPPPKKSLGTQPP
310 SLGTQPPKKAVEKQQ
311 LGTQPPKKAVEKQQP
342 EEKKPPTKAVVSKAT
347 PTKAVVSKATTKPPP
356 TTKPPPAKKAAESSS
396 NKPAVTTKSPAVKPA
407 VKPAAAPKQPVGGGQ
415 QPVGGGQKLLTRKAD
440 SEEEKTKKMVATTKP
448 MVATTKPKATAKAAL
452 TKPKATAKAALSLPA
496 AVKKKPQKVAGGAAP
505 AGGAAPSKPASAKKG
510 PSKPASAKKGKAESS
511 SKPASAKKGKAESSN
572 EEEEEKKKAAVVVSK
579 KAAVVVSKSGSLKKR
593 RKQNEAAKEAETPQA
601 EAETPQAKKIKLQTP
602 AETPQAKKIKLQTPN
604 TPQAKKIKLQTPNTF
613 QTPNTFPKRKKGEKR
615 PNTFPKRKKGEKRAS
647 ADNSFDAKRGAAGDW
663 ERANQVLKFTKGKSF
67 SAKVPERKLQANGPV
76 QANGPVAKKAKKKAS
77 ANGPVAKKAKKKASS

Function

Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:10567578, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus (PubMed:9016786). It has intrinsic GTPase and ATPase activities (PubMed:9016786)

Protein Sequence

10 MADAGIRRVV 20 PSDLYPLVLG 30 FLRDNQLSEV 40 ANKFAKATGA 50 TQQDANASSL 60 LDIYSFWLKS 70 AKVPERKLQA 80 NGPVAKKAKK 90 KASSSDSEDS 100 SEEEEEVQGP 110 PAKKAAVPAK 120 RVGLPPGKAA 130 AKASESSSSE 140 ESSDDDDEED 150 QKKQPVQKGV 160 KPQAKAAKAP 170 PKKAKSSDSD 180 SDSSSEDEPP 190 KNQKPKITPV 200 TVKAQTKAPP 210 KPARAAPKIA 220 NGKAASSSSS 230 SSSSSSSDDS 240 EEEKAAATPK 250 KTVPKKQVVA 260 KAPVKAATTP 270 TRKSSSSEDS 280 SSDEEEEQKK 290 PMKNKPGPYS 300 SVPPPSAPPP 310 KKSLGTQPPK 320 KAVEKQQPVE 330 SSEDSSDESD 340 SSSEEEKKPP 350 TKAVVSKATT 360 KPPPAKKAAE 370 SSSDSSDSDS 380 SEDDEAPSKP 390 AGTTKNSSNK 400 PAVTTKSPAV 410 KPAAAPKQPV 420 GGGQKLLTRK 430 ADSSSSEEES 440 SSSEEEKTKK 450 MVATTKPKAT 460 AKAALSLPAK 470 QAPQGSRDSS 480 SDSDSSSSEE 490 EEEKTSKSAV 500 KKKPQKVAGG 510 AAPSKPASAK 520 KGKAESSNSS 530 SSDDSSEEEE 540 EKLKGKGSPR 550 PQAPKANGTS 560 ALTAQNGKAA 570 KNSEEEEEEK 580 KKAAVVVSKS 590 GSLKKRKQNE 600 AAKEAETPQA 610 KKIKLQTPNT 620 FPKRKKGEKR 630 ASSPFRRVRE 640 EEIEVDSRVA 650 DNSFDAKRGA 660 AGDWGERANQ 670 VLKFTKGKSF 680 RHEKTKKKRG 690 SYRGGSISVQ VNSIKFDSE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015030 Cajal body
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0140678 molecular function inhibitor activity
Molecular Function GO:0046982 protein heterodimerization activity
Molecular Function GO:0004860 protein kinase inhibitor activity
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000278 mitotic cell cycle
Biological Process GO:0071901 negative regulation of protein serine/threonine kinase activity
Biological Process GO:0014032 neural crest cell development
Biological Process GO:0014029 neural crest formation
Biological Process GO:0006417 regulation of translation
Biological Process GO:0042254 ribosome biogenesis
Biological Process GO:0006364 rRNA 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] 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.

[5] 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.

[6] 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.

[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] 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.

[10] 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.