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Protein

H/ACA ribonucleoprotein complex subunit 2

Gene

NHP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for ribosome biogenesis. Part of a 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. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs. Essential for growth. Directly binds H/ACA snoRNAs.3 Publications

GO - Molecular functioni

  • box H/ACA snoRNA binding Source: GO_Central
  • snoRNA binding Source: UniProtKB

GO - Biological processi

  • cleavage involved in rRNA processing Source: SGD
  • maturation of LSU-rRNA Source: GO_Central
  • rRNA pseudouridine synthesis Source: SGD
  • snRNA pseudouridine synthesis Source: SGD
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
H/ACA ribonucleoprotein complex subunit 2
Alternative name(s):
H/ACA snoRNP protein NHP2
High mobility group-like nuclear protein 2
Gene namesi
Name:NHP2
Ordered Locus Names:YDL208W
ORF Names:D1045
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL208W.
SGDiS000002367. NHP2.

Subcellular locationi

GO - Cellular componenti

  • box H/ACA snoRNP complex Source: SGD
  • small nucleolar ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561V → K: No effect. 1 Publication
Mutagenesisi59 – 591G → E: Significant growth impairment at 30 and 37 degrees Celsius. Impaired association with H/ACA snoRNAs. 1 Publication
Mutagenesisi68 – 681R → A: No effect. 1 Publication
Mutagenesisi76 – 772Missing : Lethal. Impaired association with H/ACA snoRNAs. Accumulation of NHP2 within the nucleolus. 1 Publication
Mutagenesisi80 – 801D → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156H/ACA ribonucleoprotein complex subunit 2PRO_0000136776Add
BLAST

Proteomic databases

MaxQBiP32495.

Interactioni

Subunit structurei

Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs). The protein component of the H/ACA snoRNP contains CBF5, GAR1, NHP2 and NOP10. The complex contains a stable core composed of CBF5 and NOP10, to which GAR1 and NHP2 subsequently bind. Interacts with SHQ1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBF5P3332211EBI-12014,EBI-4105
GAR1P280073EBI-12014,EBI-7321
NAF1P539193EBI-12014,EBI-28887

Protein-protein interaction databases

BioGridi31838. 79 interactions.
DIPiDIP-5134N.
IntActiP32495. 49 interactions.
MINTiMINT-8285526.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 5115Combined sources
Turni52 – 543Combined sources
Beta strandi56 – 594Combined sources
Helixi60 – 6910Combined sources
Beta strandi74 – 774Combined sources
Helixi86 – 9611Combined sources
Beta strandi101 – 1033Combined sources
Helixi107 – 1148Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi121 – 1255Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1373Combined sources
Helixi139 – 15517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LBWNMR-A36-156[»]
2LBXNMR-A36-156[»]
ProteinModelPortaliP32495.
SMRiP32495. Positions 36-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32495.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L7Ae family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074939.
HOGENOMiHOG000055227.
InParanoidiP32495.
KOiK11129.
OMAiCVKKAAK.
OrthoDBiEOG790GCX.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR002415. H/ACA_rnp_Nhp2_euk.
IPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSiPR00881. L7ARS6FAMILY.
PR00883. NUCLEARHMG.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32495-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKDNKEHKE SKESKTVDNY EARMPAVLPF AKPLASKKLN KKVLKTVKKA
60 70 80 90 100
SKAKNVKRGV KEVVKALRKG EKGLVVIAGD ISPADVISHI PVLCEDHSVP
110 120 130 140 150
YIFIPSKQDL GAAGATKRPT SVVFIVPGSN KKKDGKNKEE EYKESFNEVV

KEVQAL
Length:156
Mass (Da):17,122
Last modified:February 1, 2005 - v2
Checksum:i008188132B494E5D
GO

Sequence cautioni

The sequence CAA40885.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA67483.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA98786.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57714 Genomic DNA. Translation: CAA40885.1. Different initiation.
X99000 Genomic DNA. Translation: CAA67483.1. Different initiation.
Z74256 Genomic DNA. Translation: CAA98786.1. Different initiation.
BK006938 Genomic DNA. Translation: DAA11656.1.
PIRiS67767.
RefSeqiNP_010073.2. NM_001180268.1.

Genome annotation databases

EnsemblFungiiYDL208W; YDL208W; YDL208W.
GeneIDi851319.
KEGGisce:YDL208W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57714 Genomic DNA. Translation: CAA40885.1. Different initiation.
X99000 Genomic DNA. Translation: CAA67483.1. Different initiation.
Z74256 Genomic DNA. Translation: CAA98786.1. Different initiation.
BK006938 Genomic DNA. Translation: DAA11656.1.
PIRiS67767.
RefSeqiNP_010073.2. NM_001180268.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LBWNMR-A36-156[»]
2LBXNMR-A36-156[»]
ProteinModelPortaliP32495.
SMRiP32495. Positions 36-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31838. 79 interactions.
DIPiDIP-5134N.
IntActiP32495. 49 interactions.
MINTiMINT-8285526.

Proteomic databases

MaxQBiP32495.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL208W; YDL208W; YDL208W.
GeneIDi851319.
KEGGisce:YDL208W.

Organism-specific databases

EuPathDBiFungiDB:YDL208W.
SGDiS000002367. NHP2.

Phylogenomic databases

GeneTreeiENSGT00550000074939.
HOGENOMiHOG000055227.
InParanoidiP32495.
KOiK11129.
OMAiCVKKAAK.
OrthoDBiEOG790GCX.

Enzyme and pathway databases

BioCyciYEAST:G3O-29590-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32495.
PROiP32495.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR002415. H/ACA_rnp_Nhp2_euk.
IPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSiPR00881. L7ARS6FAMILY.
PR00883. NUCLEARHMG.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and genetic analysis of NHP2: a moderately abundant high mobility group-like nuclear protein with an essential function in Saccharomyces cerevisiae."
    Kolodrubetz D., Burgum A.
    Yeast 7:79-90(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new open reading frames, nine known genes and one gene for Gly-tRNA."
    Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U., Schmidt E.R.
    Yeast 13:163-169(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: PROTEIN SEQUENCE OF 1-9, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN H/ACA SNORNP COMPLEXES.
  6. "Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure."
    Watkins N.J., Gottschalk A., Neubauer G., Kastner B., Fabrizio P., Mann M., Luehrmann R.
    RNA 4:1549-1568(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN H/ACA SNORNP COMPLEXES.
  7. "Accumulation of H/ACA snoRNPs depends on the integrity of the conserved central domain of the RNA-binding protein Nhp2p."
    Henras A., Dez C., Noaillac-Depeyre J., Henry Y., Caizergues-Ferrer M.
    Nucleic Acids Res. 29:2733-2746(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, MUTAGENESIS OF VAL-56; GLY-59; ARG-68; 76-VAL-ILE-77 AND ASP-80.
  8. "The Shq1p.Naf1p complex is required for box H/ACA small nucleolar ribonucleoprotein particle biogenesis."
    Yang P.K., Rotondo G., Porras T., Legrain P., Chanfreau G.
    J. Biol. Chem. 277:45235-45242(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHQ1.
  9. "Naf1 p is a box H/ACA snoRNP assembly factor."
    Fatica A., Dlakic M., Tollervey D.
    RNA 8:1502-1514(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NAF1.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. "Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA snoRNAs."
    Henras A.K., Capeyrou R., Henry Y., Caizergues-Ferrer M.
    RNA 10:1704-1712(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
  12. "Structure of H/ACA RNP protein Nhp2p reveals cis/trans isomerization of a conserved proline at the RNA and Nop10 binding interface."
    Koo B.K., Park C.J., Fernandez C.F., Chim N., Ding Y., Chanfreau G., Feigon J.
    J. Mol. Biol. 411:927-942(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 36-156, SUBUNIT.

Entry informationi

Entry nameiNHP2_YEAST
AccessioniPrimary (citable) accession number: P32495
Secondary accession number(s): D6VRE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 2005
Last modified: July 6, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.