UniProt Accession

 NHP2_HUMAN; Q9NX24; A6NKY8; Q9P095 

Genbank Protein ID

 AJ293309; AF401219; AF161404; AK000486; CR457238; AC136632; BC000009; BC006387 

Genbank Nucleotide ID

 CAC08452.1; AAL02175.1; AAF28964.1; BAA91198.1; CAG33519.1; AAH00009.1; AAH06387.1 

Protein Name

 H/ACA ribonucleoprotein complex subunit 2 

Protein Synonyms/Alias

 Nucleolar protein family A member 2; snoRNP protein NHP2 

Gene Name

 NHP2 

Gene Synonyms/Alias

 NOLA2; HSPC286 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MTKIKADPDGPE	sumoylation	[1, 2, 3, 4]
5	***MTKIKADPDGPE	ubiquitination	[5]
56	KCIKKAVKQKQIRRG	methylation	[6]
111	PYVYIPSKTDLGAAA	ubiquitination	[5]

Reference

 [1] A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58.
 Westman BJ, Verheggen C, Hutten S, Lam YW, Bertrand E, Lamond AI.
 Mol Cell. 2010 Aug 27;39(4):618-31. [PMID: 20797632]
 [2] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [3] A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics.
 Westman BJ, Lamond AI.
 Nucleus. 2011 Jan-Feb;2(1):30-7. [PMID: 21647297]
 [4] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837] 

Functional Description

 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. 

Sequence Annotation

 MOD_RES 19 19 Phosphoserine.
 CROSSLNK 5 5 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 Complete proteome; Disease mutation; Dyskeratosis congenita; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 153 AA 

Protein Sequence

Gene Ontology

 GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005732; C:small nucleolar ribonucleoprotein complex; ISS:UniProtKB.
 GO:0030515; F:snoRNA binding; ISS:UniProtKB.
 GO:0031118; P:rRNA pseudouridine synthesis; ISS:UniProtKB. 

Interpro

 IPR002415; H/ACA_rnp_Nhp2_euk.
 IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
 IPR018492; Ribosomal_L7Ae/L8/Nhp2. 

Pfam

 PF01248; Ribosomal_L7Ae 

SMART

  

PROSITE

 PS01082; RIBOSOMAL_L7AE 

PRINTS

 PR00881; L7ARS6FAMILY.
 PR00883; NUCLEARHMG.