P32495 (NHP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
H/ACA ribonucleoprotein complex subunit 2

Alternative name(s):
H/ACA snoRNP protein NHP2
High mobility group-like nuclear protein 2

Gene names

Name:	NHP2
Ordered Locus Names:	YDL208W
ORF Names:	D1045

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.7
Subunit structure	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. Ref.8 Ref.9
Subcellular location	Nucleus › nucleolus Ref.5 Ref.10.
Sequence similarities	Belongs to the ribosomal protein L7Ae family.
Sequence caution	The sequence CAA40885.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA67483.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA98786.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cleavage involved in rRNA processing Inferred from mutant phenotype Ref.5. Source: SGD rRNA pseudouridine synthesis Inferred from mutant phenotype Ref.5. Source: SGD snRNA pseudouridine synthesis Inferred from direct assay. Source: SGD
Cellular component	box H/ACA snoRNP complex Inferred from physical interaction Ref.5. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct snoRNA binding Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBF5	P33322	3	EBI-12014,EBI-4105
NAF1	P53919	3	EBI-12014,EBI-28887

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

H/ACA ribonucleoprotein complex subunit 2

PRO_0000136776

Experimental info

Mutagenesis

56

1

V → K: No effect. Ref.7

Mutagenesis

59

1

G → E: Significant growth impairment at 30 and 37 degrees Celsius. Impaired association with H/ACA snoRNAs. Ref.7

Mutagenesis

68

1

R → A: No effect. Ref.7

Mutagenesis

76 – 77

2

Missing: Lethal. Impaired association with H/ACA snoRNAs. Accumulation of NHP2 within the nucleolus.

Mutagenesis

80

1

D → A: No effect. Ref.7

Secondary structure

1

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156

Helix Strand Turn

Details...

Helix

37 – 51

15

Turn

52 – 54

3

Helix

61 – 68

8

Beta strand

75 – 77

3

Helix

86 – 96

11

Beta strand

101 – 103

3

Turn

107 – 109

3

Beta strand

121 – 125

5

Turn

130 – 133

4

Helix

139 – 155

17

Sequences

	Sequence		Length	Mass (Da)
	P32495 [UniParc]. Last modified February 1, 2005. Version 2. Checksum: 008188132B494E5D	FASTA	156	17,122
	10 20 30 40 50 60 MGKDNKEHKE SKESKTVDNY EARMPAVLPF AKPLASKKLN KKVLKTVKKA SKAKNVKRGV 70 80 90 100 110 120 KEVVKALRKG EKGLVVIAGD ISPADVISHI PVLCEDHSVP YIFIPSKQDL GAAGATKRPT 130 140 150 SVVFIVPGSN KKKDGKNKEE EYKESFNEVV KEVQAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2063628] [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: 9046097] [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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs." Henras A., Henry Y., Bousquet-Antonelli C., Noaillac-Depeyre J., Gelugne J.-P., Caizergues-Ferrer M. EMBO J. 17:7078-7090(1998) [PubMed: 9843512] [Abstract] 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: 9848653] [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: 11433018] [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: 12228251] [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: 12515383] [Abstract] Cited for: INTERACTION WITH NAF1.
[10]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] 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: 15388873] [Abstract] Cited for: CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

S67767.

RefSeq

NP_010073.2. NM_001180268.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LBW	NMR	-	A	36-156	[»]
2LBX	NMR	-	A	36-156	[»]

ProteinModelPortal

P32495.

SMR

P32495. Positions 36-156.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5134N.

IntAct

P32495. 46 interactions.

MINT

MINT-501968.

STRING

P32495.

Proteomic databases

PeptideAtlas

P32495.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDL208W; YDL208W; YDL208W.

GeneID

851319.

KEGG

sce:YDL208W.

Organism-specific databases

CYGD

YDL208w.

SGD

S000002367. NHP2.

Phylogenomic databases

eggNOG

fuNOG10048.

GeneTree

EFGT00050000003093.

HOGENOM

HBG739027.

OMA

HLPAVCE.

OrthoDB

EOG473T1W.

Gene expression databases

ArrayExpress

P32495.

Genevestigator

P32495.

GermOnline

YDL208W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002415. H/ACA_rnp_Nhp2_euk.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
[Graphical view]

KO

K11129.

Pfam

PF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]

PRINTS

PR00881. L7ARS6FAMILY.
PR00883. NUCLEARHMG.

PROSITE

PS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

968357.

Entry information

Entry name

NHP2_YEAST

Accession

Primary (citable) accession number: P32495
Secondary accession number(s): D6VRE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 2005
Last modified:	December 14, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program