NHP2

Last update 08 May 2025

Basic Info

Synonyms

FLJ20479, H/ACA ribonucleoprotein complex subunit 2, NHP2

+ [4]

Introduction

Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.

100 Clinical Results associated with NHP2

100 Translational Medicine associated with NHP2

0 Patents (Medical) associated with NHP2

109

Literatures (Medical) associated with NHP2

01 Sep 2025·Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

A smart photosensitive fluorescent probe for sensing Co2+ in extremely alkaline aqueous solution

Article

Author: Xiao, Nao ; Wei, Shaoyin ; Shi, Ruilin ; Huang, Bingxuan ; Wang, Yujie ; Zhang, Yiming ; Wang, Yuji

A novel pH-, viscosity-, and photo-sensitive polymorphic fluorescence probe NHP for sensing Co²⁺ has been developed. The hydrazone-based NHP can be synthesized by only one step of reflux reaction and purified by washing with poor solvents. Three single crystals of NHP-1, NHP-2, and NHP-3 with different conformations were resolved. As a photo acid generator (PAG), the hydrogen atom on the imino group of the probe NHP can be shed with 365 nm ultraviolet (UV) light illumination or in alkaline conditions. Due to the above two conditions, the negatively charged ligand obtained after dehydrogenation of NHP can accelerate its chelation with Co²⁺. When irradiated with 365 nm UV light, the product (NHP₂-Co²⁺ (I)) of NHP chelating with Co²⁺ appears yellowish in aqueous solution. In a strong alkali aqueous solution, the chelate product (NHP₂-Co²⁺ (II)) of NHP and Co²⁺ showed bright blue-green fluorescence. The formed divalent Co(II) complex NHP₂-Co²⁺ can be oxidized to trivalent Co(III) complex NHP₃-Co³⁺, as confirmed by the resolution of single crystals of NHP₃-Co³⁺.

01 Jan 2024·Journal of Family Medicine and Primary Care

In silico characterization and identification of compound heterozygous variants in H/ACA Ribonucleoprotein Assembly Factor (SHQ1) from Indian population

Article

Author: Ghali, Noor ; Srivastava, Sudhanshu ; Gowda, Vykuntaraju K. ; Srivastava, Anshika ; Shamnur, Asha ; Srinivasan, Varunvenkat M. ; Kinhal, Uddhav

ABSTRACTBackground:H/ACA small nucleolar ribonucleoproteins (snoRNP) form a complex with multiple proteins to accomplish the pseudouridylation of rRNA. The assembly of H/ACA small nucleolar ribonucleoproteins (snoRNP) is initiated by H/ACA ribonucleoprotein Assembly factor, that is, SHQ1. Mutations in SHQ1 have been reported to cause two disorders namely, dystonia-35 childhood onset (OMIM*619921) and neurodevelopmental disorder with seizures and dystonia (OMIM*619922), both of which are inherited in an autosomal recessive manner. Considering the high genetic and clinical diversity of SHQ1-related clinical features and the importance of SHQ1 in the assembly of the H/ACA snoRNP complex, it is important to take a systematic approach to delineate the genetic diagnosis and impact of mutations on protein structure and stability.Methods:Whole exome sequencing followed by Sanger validation was performed in an individual with the clinical features of neurodevelopmental disorder with seizures and dystonia (OMIM*619922). Protein modeling studies of all the reported SHQ1 variants to date were performed using freely available web servers Interactive Tree of Life, String, BioGrid, ShinyGO, DAVID, and Pathvix. Protein structures were visualized using Pymol.Results and Discussion:We identified compound heterozygous variants, one known frameshift deletion c. 828_831del, p.(Asp277Serfs*27) and the other novel missense variant c. 1157A>C, p.(Tyr386Ser) found in an individual with neurodevelopmental disorder, seizures, movement disorder, and hypomyelination leukodystrophy on neuroimaging. Protein-interactome studies identified potential genetic interactors that include GAR1, NAF1, TRUB1, UTP15, DKC1, NOP10, NPHOSPH 10, KRR1, NOP58, NOP56, FBL, RRP9, NHP2, RUVBL1, and RUVBL2. Ribosome biogenesis in eukaryotes, RNA polymerase, RNA transport, spliceosome, ribosome, cytosolic DNA-sensing pathway, DNA replication, mismatch repair, base excision repair, nucleotide excision repair, and basal transcription factors process were identified as the linked pathways with the prioritized genes.Conclusion:In conclusion, a sophisticated genotype and phenotype correlation followed by linking the genes to the key biological pathways opens new avenues to understand disease pathology and plan for therapeutic interventions.

16 Sep 2023·Human molecular genetics

Novel pathological variants of NHP2 affect N-terminal domain flexibility, protein stability, H/ACA Ribonucleoprotein (RNP) complex formation and telomerase activity.

Article

Author: Vertemara, Jacopo ; Baliakas, Panagiotis ; von Castelmur, Eleonore ; Norberg, Anna ; Lottersberger, Francisca ; Cammenga, Jörg ; Faustini, Elena ; Maliński, Bartosz ; Tisi, Renata ; Zhang, Yuming ; Ladenvall, Claes

Telomere biology disorders (TBDs) are characterized by short telomeres, premature aging, bone marrow failure and cancer predisposition. Germline mutations in NHP2, encoding for one component of the telomerase cofactor H/ACA RNA binding complex together with Dyskerin, NOP10 and GAR1, have been previously reported in rare cases of TBDs. Here, we report two novel NHP2 variants (NHP2-A39T and NHP2-T44M) identified in a compound heterozygous patient affected by premature aging, bone marrow failure/myelodysplastic syndrome and gastric cancer. Although still able to support cell viability, both variants reduce the levels of hTR, the telomerase RNA component, and telomerase activity, expanding the panel of NHP2 pathological variants. Furthermore, both variants fail to be incorporated in the H/ACA RNA binding complex when in competition with wild-type endogenous NHP2, and the lack of incorporation causes their drastic proteasomal degradation. By RoseTTAFold prediction followed by molecular dynamics simulations, we reveal a dramatic distortion of residues 33-41, which normally position on top of the NHP2 core, as the main defect of NHP2-A39T, and high flexibility and the misplacement of the N-terminal region (residues 1-24) in NHP2-T44M and, to a lower degree, in NHP2-A39T. Because deletion of amino acids 2-24 causes a reduction in NHP2 levels only in the presence of wild-type NHP2, while deletion of amino acids 2-38 completely disrupts NHP2 stability, we propose that the two variants are mis-incorporated into the H/ACA binding complex due to the altered dynamics of the first 23 amino acids and/or the distortion of the residues 25-41 loop.

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NHP2

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