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HNRNPU

This gene encodes a member of a family of proteins that bind nucleic acids and function in the formation of ribonucleoprotein complexes in the nucleus with heterogeneous nuclear RNA (hnRNA). The encoded protein has affinity for both RNA and DNA, and binds scaffold-attached region (SAR) DNA. Mutations in this gene have been associated with epileptic encephalopathy, early infantile, 54. A pseudogene of this gene has been identified on chromosome 14.
Protein class

Disease related genes, Human disease related genes, Plasma proteins

Predicted location

Intracellular

Single cell type specificity

Low cell type specificity

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

Oligomer (via ATPase domain and RNA-binding RGG-box region); oligomerization occurs upon ATP-binding in a chromatin-associated RNAs (caRNAs)- and transcription-dependent manner and is required for chromatin decompaction (PubMed:28622508). ATP hydrolysis is required to cycle from an oligomeric to monomeric state to compact chromatin (PubMed:28622508). Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 (PubMed:19029303). Identified in the spliceosome C complex (PubMed:11991638). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661, PubMed:19029303). Associates with heterogeneous nuclear ribonucleoprotein (hnRNP) particles (PubMed:8174554, PubMed:9204873, PubMed:9405365, PubMed:11909954). Associates (via middle region) with the C-terminal domain (CTD) RNA polymerase II (Pol II) holoenzyme; this association occurs in a RNA-independent manner (PubMed:10490622). Associates (via middle region) with the core-TFIIH basal transcription factor complex; this association inhibits the CTD phosphorylation of RNA polymerase II holoenzyme by down-regulating TFIIH kinase activity (PubMed:10490622). Associates with the telomerase holoenzyme complex (PubMed:18082603). Associates with spindle microtubules (MTs) in a TPX2-dependent manner (PubMed:21242313). Interacts (via C-terminus) with actin; this interaction is direct and mediates association with the phosphorylated CTD of RNA polymerase II and is disrupted in presence of the long non-coding H19 RNA (PubMed:15711563, PubMed:23811339). Interacts with AURKA (PubMed:21242313, PubMed:25986610). Interacts (via C-terminus) with CBX5; this interaction is, at least in part, RNA-dependent (PubMed:19617346). Interacts with CR2 (PubMed:7753047). Interacts with CRY1 (By similarity). Interacts (via C-terminus) with EP300; this interaction enhances DNA-binding to nuclear scaffold/matrix attachment region (S/MAR) elements (PubMed:11909954). Interacts with ERBB4 (PubMed:20858735). Interacts with GEMIN5 (PubMed:25911097). Interacts with IGF2BP1 (PubMed:17289661, PubMed:23640942). Interacts with IGF2BP2 and IGF2BP3 (PubMed:23640942). Interacts with NCL; this interaction occurs during mitosis (PubMed:21242313). Interacts (via C-terminus) with NR3C1 (via C-terminus) (PubMed:9353307). Interacts with PLK1; this interaction induces phosphorylation of HNRNPU at Ser-59 in mitosis (PubMed:25986610). Interacts with POU3F4 (PubMed:9105675). Interacts with SMARCA4; this interaction occurs in embryonic stem cells and stimulates global Pol II-mediated transcription. Interacts (via C-terminus) with TOP2A; this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA by TOP2A in a RNA-dependent manner (By similarity). Interacts with TPX2; this interaction recruits HNRNPU to spindle microtubules (MTs) (PubMed:21242313, PubMed:25986610). Interacts with UBQLN2 (PubMed:25616961). Interacts (via RNA-binding RGG-box region) with ZBTB7B; the interaction facilitates the recruitment of long non-coding RNA Blnc1 by ZBTB7B (By similarity). Interacts with ERCC6 (PubMed:26030138). (Microbial infection) Interacts with HIV-1 protein Rev.

Molecular function

Activator, Chromatin regulator, Developmental protein, DNA-binding, Repressor, Ribonucleoprotein, RNA-binding

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