NHP2_YEAST
ID NHP2_YEAST Reviewed; 156 AA.
AC P32495; D6VRE6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit NHP2;
DE AltName: Full=H/ACA snoRNP protein NHP2;
DE AltName: Full=High mobility group-like nuclear protein 2;
GN Name=NHP2; OrderedLocusNames=YDL208W; ORFNames=D1045;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2063628; DOI=10.1002/yea.320070202;
RA Kolodrubetz D., Burgum A.;
RT "Sequence and genetic analysis of NHP2: a moderately abundant high mobility
RT group-like nuclear protein with an essential function in Saccharomyces
RT cerevisiae.";
RL Yeast 7:79-90(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046097;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<163::aid-yea54>3.0.co;2-4;
RA Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
RA Schmidt E.R.;
RT "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new
RT open reading frames, nine known genes and one gene for Gly-tRNA.";
RL Yeast 13:163-169(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 1-9, FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP IN H/ACA SNORNP COMPLEXES.
RX PubMed=9843512; DOI=10.1093/emboj/17.23.7078;
RA Henras A., Henry Y., Bousquet-Antonelli C., Noaillac-Depeyre J.,
RA Gelugne J.-P., Caizergues-Ferrer M.;
RT "Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs.";
RL EMBO J. 17:7078-7090(1998).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN H/ACA
RP SNORNP COMPLEXES.
RX PubMed=9848653; DOI=10.1017/s1355838298980761;
RA Watkins N.J., Gottschalk A., Neubauer G., Kastner B., Fabrizio P., Mann M.,
RA Luehrmann R.;
RT "Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-
RT binding protein, are present together with Gar1p in all H BOX/ACA-motif
RT snoRNPs and constitute a common bipartite structure.";
RL RNA 4:1549-1568(1998).
RN [7]
RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF VAL-56; GLY-59; ARG-68;
RP 76-VAL-ILE-77 AND ASP-80.
RX PubMed=11433018; DOI=10.1093/nar/29.13.2733;
RA Henras A., Dez C., Noaillac-Depeyre J., Henry Y., Caizergues-Ferrer M.;
RT "Accumulation of H/ACA snoRNPs depends on the integrity of the conserved
RT central domain of the RNA-binding protein Nhp2p.";
RL Nucleic Acids Res. 29:2733-2746(2001).
RN [8]
RP INTERACTION WITH SHQ1.
RX PubMed=12228251; DOI=10.1074/jbc.m207669200;
RA Yang P.K., Rotondo G., Porras T., Legrain P., Chanfreau G.;
RT "The Shq1p.Naf1p complex is required for box H/ACA small nucleolar
RT ribonucleoprotein particle biogenesis.";
RL J. Biol. Chem. 277:45235-45242(2002).
RN [9]
RP INTERACTION WITH NAF1.
RX PubMed=12515383;
RA Fatica A., Dlakic M., Tollervey D.;
RT "Naf1 p is a box H/ACA snoRNP assembly factor.";
RL RNA 8:1502-1514(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
RX PubMed=15388873; DOI=10.1261/rna.7770604;
RA Henras A.K., Capeyrou R., Henry Y., Caizergues-Ferrer M.;
RT "Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form
RT a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA
RT snoRNAs.";
RL RNA 10:1704-1712(2004).
RN [12]
RP FUNCTION, AND IDENTIFICATION IN THE H/ACA SNORNP COMPLEX.
RX PubMed=21131909; DOI=10.1038/emboj.2010.316;
RA Wu G., Xiao M., Yang C., Yu Y.T.;
RT "U2 snRNA is inducibly pseudouridylated at novel sites by Pus7p and snR81
RT RNP.";
RL EMBO J. 30:79-89(2011).
RN [13]
RP STRUCTURE BY NMR OF 36-156, AND SUBUNIT.
RX PubMed=21708174; DOI=10.1016/j.jmb.2011.06.022;
RA Koo B.K., Park C.J., Fernandez C.F., Chim N., Ding Y., Chanfreau G.,
RA Feigon J.;
RT "Structure of H/ACA RNP protein Nhp2p reveals cis/trans isomerization of a
RT conserved proline at the RNA and Nop10 binding interface.";
RL J. Mol. Biol. 411:927-942(2011).
CC -!- FUNCTION: Non-catalytic component of the H/ACA small nucleolar
CC ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of
CC rRNA and is required for ribosome biogenesis (PubMed:9843512,
CC PubMed:9848653). This involves the isomerization of uridine such that
CC the ribose is subsequently attached to C5, instead of the normal N1
CC (PubMed:9843512, PubMed:9848653). Pseudouridine ('psi') residues may
CC serve to stabilize the conformation of rRNAs (PubMed:9843512,
CC PubMed:9848653). The H/ACA snoRNP complex also mediates
CC pseudouridylation of other types of RNAs (PubMed:21131909). The H/ACA
CC snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA
CC (PubMed:21131909). Essential for growth (PubMed:9843512). Directly
CC binds H/ACA snoRNAs (PubMed:11433018). {ECO:0000269|PubMed:11433018,
CC ECO:0000269|PubMed:21131909, ECO:0000269|PubMed:9843512,
CC ECO:0000269|PubMed:9848653}.
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs) (PubMed:21708174,
CC PubMed:9843512, PubMed:9848653, PubMed:21131909). The protein component
CC of the H/ACA snoRNP contains CBF5, GAR1, NHP2 and NOP10
CC (PubMed:21708174, PubMed:9843512, PubMed:9848653, PubMed:21131909). The
CC complex contains a stable core composed of CBF5 and NOP10, to which
CC GAR1 and NHP2 subsequently bind (PubMed:21708174, PubMed:9843512,
CC PubMed:9848653, PubMed:21131909). Interacts with SHQ1
CC (PubMed:12228251). Interacts with NAF1 (PubMed:12515383).
CC {ECO:0000269|PubMed:12228251, ECO:0000269|PubMed:12515383,
CC ECO:0000269|PubMed:21131909, ECO:0000269|PubMed:21708174,
CC ECO:0000269|PubMed:9843512, ECO:0000269|PubMed:9848653}.
CC -!- INTERACTION:
CC P32495; P33322: CBF5; NbExp=11; IntAct=EBI-12014, EBI-4105;
CC P32495; P28007: GAR1; NbExp=3; IntAct=EBI-12014, EBI-7321;
CC P32495; P53919: NAF1; NbExp=3; IntAct=EBI-12014, EBI-28887;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9843512}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA67483.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA98786.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X57714; CAA40885.1; ALT_INIT; Genomic_DNA.
DR EMBL; X99000; CAA67483.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74256; CAA98786.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA11656.1; -; Genomic_DNA.
DR PIR; S67767; S67767.
DR RefSeq; NP_010073.2; NM_001180268.1.
DR PDB; 2LBW; NMR; -; A=36-156.
DR PDB; 2LBX; NMR; -; A=36-156.
DR PDBsum; 2LBW; -.
DR PDBsum; 2LBX; -.
DR AlphaFoldDB; P32495; -.
DR BMRB; P32495; -.
DR SMR; P32495; -.
DR BioGRID; 31838; 286.
DR ComplexPortal; CPX-737; Box H/ACA ribonucleoprotein complex.
DR DIP; DIP-5134N; -.
DR IntAct; P32495; 52.
DR MINT; P32495; -.
DR STRING; 4932.YDL208W; -.
DR iPTMnet; P32495; -.
DR MaxQB; P32495; -.
DR PaxDb; P32495; -.
DR PRIDE; P32495; -.
DR EnsemblFungi; YDL208W_mRNA; YDL208W; YDL208W.
DR GeneID; 851319; -.
DR KEGG; sce:YDL208W; -.
DR SGD; S000002367; NHP2.
DR VEuPathDB; FungiDB:YDL208W; -.
DR eggNOG; KOG3167; Eukaryota.
DR GeneTree; ENSGT00550000074939; -.
DR HOGENOM; CLU_084513_1_1_1; -.
DR InParanoid; P32495; -.
DR OMA; IDVYSHI; -.
DR BioCyc; MetaCyc:G3O-29590-MON; -.
DR BioCyc; YEAST:G3O-29590-MON; -.
DR EvolutionaryTrace; P32495; -.
DR PRO; PR:P32495; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32495; protein.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000493; P:box H/ACA snoRNP assembly; IMP:UniProtKB.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IMP:SGD.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IMP:SGD.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IDA:ComplexPortal.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IDA:UniProtKB.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00883; NUCLEARHMG.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..156
FT /note="H/ACA ribonucleoprotein complex subunit NHP2"
FT /id="PRO_0000136776"
FT MUTAGEN 56
FT /note="V->K: No effect."
FT /evidence="ECO:0000269|PubMed:11433018"
FT MUTAGEN 59
FT /note="G->E: Significant growth impairment at 30 and 37
FT degrees Celsius. Impaired association with H/ACA snoRNAs."
FT /evidence="ECO:0000269|PubMed:11433018"
FT MUTAGEN 68
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:11433018"
FT MUTAGEN 76..77
FT /note="Missing: Lethal. Impaired association with H/ACA
FT snoRNAs. Accumulation of NHP2 within the nucleolus."
FT /evidence="ECO:0000269|PubMed:11433018"
FT MUTAGEN 80
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:11433018"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:2LBW"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2LBW"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2LBW"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:2LBW"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2LBW"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:2LBW"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2LBW"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:2LBW"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2LBX"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:2LBW"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2LBW"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2LBX"
FT HELIX 139..155
FT /evidence="ECO:0007829|PDB:2LBW"
SQ SEQUENCE 156 AA; 17122 MW; 008188132B494E5D CRC64;
MGKDNKEHKE SKESKTVDNY EARMPAVLPF AKPLASKKLN KKVLKTVKKA SKAKNVKRGV
KEVVKALRKG EKGLVVIAGD ISPADVISHI PVLCEDHSVP YIFIPSKQDL GAAGATKRPT
SVVFIVPGSN KKKDGKNKEE EYKESFNEVV KEVQAL
