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 (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the SWAP complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. Interacts with AICDA. Interacts with APTX. Interacts with C1QBP. Interacts with ERBB4. Interacts (via C-terminus) with FMR1 isoform 6 (via N-terminus). Interacts with GZF1; this interaction is important for nucleolar localization of GZF1. Interacts with NSUN2. Interacts with NVL. Interacts (via N-terminus domain) with SETX. Interacts (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with TERT; the interaction is important for nucleolar localization of TERT. Interacts with WDR46. Interacts with ZFP36. Interacts with LRRC34. Interacts with RRP1B. Interacts with HNRNPU; this interaction occurs during mitosis. Interacts with RIOK1; RIOK1 recruits NCL to PRMT5 for symmetrically methylation (By similarity). Interacts with ZBTB7B (By similarity). Interacts with MDK; this interaction promotes NCL clustering and lateral movements of this complex into lipid rafts leading to MDK internalization (By similarity). Interacts with HDGF (By similarity). Interacts with ALKBH2. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group (By similarity). Symmetrically methylated by PRMT5 (By similarity).