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Overview

Uniprot IDP19338
Protein NameNucleolin
Gene NameNCL
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
102 KKTVTPAKAVTTPGK
109 KAVTTPGKKGATPGK
110 AVTTPGKKGATPGKA
116 KKGATPGKALVATPG
124 ALVATPGKKGAAIPA
125 LVATPGKKGAAIPAK
132 KGAAIPAKGAKNGKN
15 GKNQGDPKKMAPPPK
16 KNQGDPKKMAPPPKE
223 AKGKKAAKVVPVKAK
228 AAKVVPVKAKNVAED
288 KKEMAKQKAAPEAKK
294 QKAAPEAKKQKVEGT
295 KAAPEAKKQKVEGTE
297 APEAKKQKVEGTEPT
324 NKSAPELKTGISDVF
348 VRIGMTRKFGYVDFE
370 ALELTGLKVFGNEIK
377 KVFGNEIKLEKPKGK
398 DARTLLAKNLPYKVT
403 LAKNLPYKVTQDELK
424 AEIRLVSKDGKSKGI
429 VSKDGKSKGIAYIEF
444 KTEADAEKTFEEKQG
449 AEKTFEEKQGTEIDG
467 SLYYTGEKGQNQDYR
477 NQDYRGGKNSTWSGE
513 FEKATFIKVPQNQNG
523 QNQNGKSKGYAFIEF
545 EALNSCNKREIEGRA
55 IPQKKGKKAAATSAK
572 NARSQPSKTLFVKGL
577 PSKTLFVKGLSEDTT
6 **MVKLAKAGKNQGD
610 DRETGSSKGFGFVDF
62 KAAATSAKKVVVSPT
624 FNSEEDAKAAKEAME
627 EEDAKAAKEAMEDGE
63 AAATSAKKVVVSPTK
646 KVTLDWAKPKGEGGF
70 KVVVSPTKKVAVATP
71 VVVSPTKKVAVATPA
79 VAVATPAKKAAVTPG
80 AVATPAKKAAVTPGK
87 KAAVTPGKKAAATPA
88 AAVTPGKKAAATPAK
9 VKLAKAGKNQGDPKK
95 KAAATPAKKTVTPAK
96 AAATPAKKTVTPAKA

Function

Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats

Protein Sequence

10 MVKLAKAGKN 20 QGDPKKMAPP 30 PKEVEEDSED 40 EEMSEDEEDD 50 SSGEEVVIPQ 60 KKGKKAAATS 70 AKKVVVSPTK 80 KVAVATPAKK 90 AAVTPGKKAA 100 ATPAKKTVTP 110 AKAVTTPGKK 120 GATPGKALVA 130 TPGKKGAAIP 140 AKGAKNGKNA 150 KKEDSDEEED 160 DDSEEDEEDD 170 EDEDEDEDEI 180 EPAAMKAAAA 190 APASEDEDDE 200 DDEDDEDDDD 210 DEEDDSEEEA 220 METTPAKGKK 230 AAKVVPVKAK 240 NVAEDEDEEE 250 DDEDEDDDDD 260 EDDEDDDDED 270 DEEEEEEEEE 280 EPVKEAPGKR 290 KKEMAKQKAA 300 PEAKKQKVEG 310 TEPTTAFNLF 320 VGNLNFNKSA 330 PELKTGISDV 340 FAKNDLAVVD 350 VRIGMTRKFG 360 YVDFESAEDL 370 EKALELTGLK 380 VFGNEIKLEK 390 PKGKDSKKER 400 DARTLLAKNL 410 PYKVTQDELK 420 EVFEDAAEIR 430 LVSKDGKSKG 440 IAYIEFKTEA 450 DAEKTFEEKQ 460 GTEIDGRSIS 470 LYYTGEKGQN 480 QDYRGGKNST 490 WSGESKTLVL 500 SNLSYSATEE 510 TLQEVFEKAT 520 FIKVPQNQNG 530 KSKGYAFIEF 540 ASFEDAKEAL 550 NSCNKREIEG 560 RAIRLELQGP 570 RGSPNARSQP 580 SKTLFVKGLS 590 EDTTEETLKE 600 SFDGSVRARI 610 VTDRETGSSK 620 GFGFVDFNSE 630 EDAKAAKEAM 640 EDGEIDGNKV 650 TLDWAKPKGE 660 GGFGGRGGGR 670 GGFGGRGGGR 680 GGRGGFGGRG 690 RGGFGGRGGF 700 RGGRGGGGDH 710 KPQGKKTKFE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005938 cell cortex
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0005681 spliceosomal complex
Molecular Function GO:0044547 DNA topoisomerase binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0043560 insulin receptor substrate binding
Molecular Function GO:0048027 mRNA 5'-UTR binding
Molecular Function GO:0042731 PH domain binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0042162 telomeric DNA binding
Biological Process GO:0001525 angiogenesis
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0017148 negative regulation of translation
Biological Process GO:1901838 positive regulation of transcription of nucleolar large rRNA by RNA polymerase I
Cellular Component GO:0005694 chromosome
Cellular Component GO:0001533 cornified envelope
Cellular Component GO:0036464 cytoplasmic ribonucleoprotein granule
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0160056 macropinosome membrane

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.