Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribosome biogenesis protein ENP2

Gene

ENP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in rRNA-processing and ribosome biosynthesis.1 Publication

GO - Biological processi

  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • ribosomal small subunit biogenesis Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-30849-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome biogenesis protein ENP2
Alternative name(s):
Essential nuclear protein 2
Gene namesi
Name:ENP2
Ordered Locus Names:YGR145W
ORF Names:G6623
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR145W.
SGDiS000003377. ENP2.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: SGD
  • small-subunit processome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 707707Ribosome biogenesis protein ENP2PRO_0000051473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei529 – 5291PhosphoserineCombined sources
Modified residuei550 – 5501PhosphoserineCombined sources
Modified residuei555 – 5551PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP48234.

PTM databases

iPTMnetiP48234.

Interactioni

Subunit structurei

Component of the 90S pre-ribosomes.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BFR2Q066318EBI-23354,EBI-36432
HCA4P204483EBI-23354,EBI-5612

Protein-protein interaction databases

BioGridi33393. 43 interactions.
DIPiDIP-5535N.
IntActiP48234. 14 interactions.
MINTiMINT-500380.

Structurei

3D structure databases

ProteinModelPortaliP48234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati54 – 9441WD 1Add
BLAST
Repeati178 – 21740WD 2Add
BLAST
Repeati226 – 26540WD 3Add
BLAST
Repeati269 – 31042WD 4Add
BLAST
Repeati312 – 35140WD 5Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat NOL10/ENP2 family.Curated
Contains 5 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00390000007900.
HOGENOMiHOG000182967.
InParanoidiP48234.
KOiK14788.
OMAiYVEFHSQ.
OrthoDBiEOG75TMNG.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR012580. NUC153.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08159. NUC153. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48234-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLKSTSAND VSVYQVSGTN VSRSLPDWIA KKRKRQLKND LEYQNRVELI
60 70 80 90 100
QDFEFSEASN KIKVSRDGQY CMATGTYKPQ IHVYDFANLS LKFDRHTDAE
110 120 130 140 150
NVDFTILSDD WTKSVHLQND RSIQFQNKGG LHYTTRIPKF GRSLVYNKVN
160 170 180 190 200
CDLYVGASGN ELYRLNLEKG RFLNPFKLDT EGVNHVSINE VNGLLAAGTE
210 220 230 240 250
TNVVEFWDPR SRSRVSKLYL ENNIDNRPFQ VTTTSFRNDG LTFACGTSNG
260 270 280 290 300
YSYIYDLRTS EPSIIKDQGY GFDIKKIIWL DNVGTENKIV TCDKRIAKIW
310 320 330 340 350
DRLDGKAYAS MEPSVDINDI EHVPGTGMFF TANESIPMHT YYIPSLGPSP
360 370 380 390 400
RWCSFLDSIT EELEEKPSDT VYSNYRFITR DDVKKLNLTH LVGSRVLRAY
410 420 430 440 450
MHGFFINTEL YDKVSLIANP DAYKDERERE IRRRIEKERE SRIRSSGAVQ
460 470 480 490 500
KPKIKVNKTL VDKLSQKRGD KVAGKVLTDD RFKEMFEDEE FQVDEDDYDF
510 520 530 540 550
KQLNPVKSIK ETEEGAAKRI RALTAAEESD EERIAMKDGR GHYDYEDEES
560 570 580 590 600
DEEESDDETN QKSNKEELSE KDLRKMEKQK ALIERRKKEK EQSERFMNEM
610 620 630 640 650
KAGTSTSTQR DESAHVTFGE QVGELLEVEN GKKSNESILR RNQRGEAELT
660 670 680 690 700
FIPQRKSKKD GNYKSRRHDN SSDEEGIDEN GNKKDNGRSK PRFENRRRAS

KNAFRGM
Length:707
Mass (Da):81,734
Last modified:September 21, 2011 - v2
Checksum:i6C3DFB372C058A04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti678 – 6781D → E in CAA59803 (PubMed:8585325).Curated
Sequence conflicti678 – 6781D → E in CAA97158 (PubMed:9169869).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85807 Genomic DNA. Translation: CAA59803.1.
Z72930 Genomic DNA. Translation: CAA97158.1.
BK006941 Genomic DNA. Translation: DAA08236.2.
PIRiS60436.
RefSeqiNP_011661.2. NM_001181274.2.

Genome annotation databases

EnsemblFungiiYGR145W; YGR145W; YGR145W.
GeneIDi853048.
KEGGisce:YGR145W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85807 Genomic DNA. Translation: CAA59803.1.
Z72930 Genomic DNA. Translation: CAA97158.1.
BK006941 Genomic DNA. Translation: DAA08236.2.
PIRiS60436.
RefSeqiNP_011661.2. NM_001181274.2.

3D structure databases

ProteinModelPortaliP48234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33393. 43 interactions.
DIPiDIP-5535N.
IntActiP48234. 14 interactions.
MINTiMINT-500380.

PTM databases

iPTMnetiP48234.

Proteomic databases

MaxQBiP48234.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR145W; YGR145W; YGR145W.
GeneIDi853048.
KEGGisce:YGR145W.

Organism-specific databases

EuPathDBiFungiDB:YGR145W.
SGDiS000003377. ENP2.

Phylogenomic databases

GeneTreeiENSGT00390000007900.
HOGENOMiHOG000182967.
InParanoidiP48234.
KOiK14788.
OMAiYVEFHSQ.
OrthoDBiEOG75TMNG.

Enzyme and pathway databases

BioCyciYEAST:G3O-30849-MONOMER.

Miscellaneous databases

PROiP48234.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR012580. NUC153.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08159. NUC153. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames."
    Skala J., Nawrocki A., Goffeau A.
    Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 678.
    Strain: ATCC 204508 / S288c.
  4. "90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit processing factors but predominantly lack 60S synthesis factors."
    Grandi P., Rybin V., Bassler J., Petfalski E., Strauss D., Marzioch M., Schaefer T., Kuster B., Tschochner H., Tollervey D., Gavin A.-C., Hurt E.
    Mol. Cell 10:105-115(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE 90S PRE-RIBOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
  5. Cited for: INTERACTION WITH ESF1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "The small-subunit processome is a ribosome assembly intermediate."
    Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S., Baserga S.J.
    Eukaryot. Cell 3:1619-1626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. Cited for: ASSOCIATION WITH THE 90S PRE-RIBOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains over 200 genes."
    Wade C.H., Umbarger M.A., McAlear M.A.
    Yeast 23:293-306(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529; SER-550 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529; SER-550 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529; SER-550 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNOL10_YEAST
AccessioniPrimary (citable) accession number: P48234
Secondary accession number(s): D6VUS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: September 21, 2011
Last modified: July 6, 2016
This is version 129 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.