P36049 (EBP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
rRNA-processing protein EBP2

Alternative name(s):
EBNA1-binding protein homolog

Gene names

Name:	EBP2
Ordered Locus Names:	YKL172W
ORF Names:	YKL636

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	427 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the processing of the 27S pre-rRNA. Probably involved in the step of the processing of the 27 SA precursor into the 27 SB intermediate. Ref.4 Ref.5
Subunit structure	Interacts with LOC1, NOP12, SIZ2, ULS1 and WSS1. Ref.8
Subcellular location	Nucleus › nucleolus Ref.4 Ref.5.
Post-translational modification	Sumoylated. Ref.8
Sequence similarities	Belongs to the EBP2 family.

Ontologies

Keywords
Biological process	Ribosome biogenesis
Cellular component	Nucleus
Domain	Coiled coil
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nuclear division Inferred from mutant phenotype. Source: SGD rRNA processing Inferred from mutant phenotype Ref.5. Source: SGD
Cellular component	nuclear periphery Inferred from direct assay. Source: SGD nucleolus Inferred from direct assay Ref.5. Source: SGD preribosome, large subunit precursor Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 427	427	rRNA-processing protein EBP2		PRO_0000120000
Regions
	Coiled coil	45 – 174	130	Potential
	Coiled coil	234 – 265	32	Potential
	Coiled coil	291 – 348	58	Potential
Amino acid modifications
	Modified residue	104	1	Phosphoserine Ref.6 Ref.9
	Modified residue	110	1	Phosphoserine Ref.6 Ref.9
	Modified residue	177	1	Phosphoserine Ref.6 Ref.7
	Modified residue	183	1	Phosphoserine Ref.6 Ref.7
Experimental info
	Mutagenesis	36 – 37	2	KK → RR: Reduces sumoylation and impairs interaction with SIZ2, WSS1 and ULS1, when associated with R-61 and R-62. Ref.8
	Mutagenesis	61 – 62	2	KK → RR: Reduces sumoylation and impairs interaction with SIZ2, WSS1 and ULS1, when associated with R-36 and R-37. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P36049 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 4A11F6CDF779DB5A	FASTA	427	49,734
	10 20 30 40 50 60 MAKGFKLKEL LSHQKEIEKA EKLENDLKKK KSQELKKEEP TIVTASNLKK LEKKEKKADV 70 80 90 100 110 120 KKEVAADTEE YQSQALSKKE KRKLKKELKK MQEQDATEAQ KHMSGDEDES GDDREEEEEE 130 140 150 160 170 180 EEEEEGRLDL EKLAKSDSES EDDSESENDS EEDEDVVAKE ESEEKEEQEE EQDVPLSDVE 190 200 210 220 230 240 FDSDADVVPH HKLTVNNTKA MKHALERVQL PWKKHSFQEH QSVTSETNTD EHIKDIYDDT 250 260 270 280 290 300 ERELAFYKQS LDAVLVARDE LKRLKVPFKR PLDYFAEMVK SDEHMDKIKG KLIEEASDKK 310 320 330 340 350 360 AREEARRQRQ LKKFGKQVQN ATLQKRQLEK RETLEKIKSL KNKRKHNEID HSEFNVGVEE 370 380 390 400 410 420 EVEGKRFDRG RPNGKRAAKN AKYGQGGMKR FKRKNDATSS ADVSGFSSRK MKGKTNRPGK SRRARRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and analysis of a 20.5 kb DNA segment located on the left arm of yeast chromosome XI." Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F. Yeast 10:S25-S33(1994) [PubMed: 8091858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Ebp2p, yeast homologue of a human protein that interacts with Epstein-Barr virus nuclear antigen 1, is required for pre-rRNA processing and ribosomal subunit assembly." Tsujii R., Miyoshi K., Tsuno A., Matsui Y., Toh-e A., Miyakawa T., Mizuta K. Genes Cells 5:543-553(2000) [PubMed: 10947841] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"The budding yeast homolog of the human EBNA1-binding protein 2 (Ebp2p) is an essential nucleolar protein required for pre-rRNA processing." Huber M.D., Dworet J.H., Shire K., Frappier L., McAlear M.A. J. Biol. Chem. 275:28764-28773(2000) [PubMed: 10849420] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-110; SER-177 AND SER-183, MASS SPECTROMETRY. Strain: ADR376.
[7]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-183, MASS SPECTROMETRY.
[8]	"SUMO mediates interaction of Ebp2p, the yeast homolog of Epstein-Barr virus nuclear antigen 1-binding protein 2, with a RING finger protein Ris1p." Shirai C., Mizuta K. Biosci. Biotechnol. Biochem. 72:1881-1886(2008) [PubMed: 18603780] [Abstract] Cited for: INTERACTION WITH LOC1, NOP12, SIZ2; ULS1 AND WSS1, SUMOYLATION, MUTAGENESIS OF 36-LYS-LYS-37 AND 61-LYS-LYS-62.
[9]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-110, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z26878 Genomic DNA. Translation: CAA81515.1. Z28172 Genomic DNA. Translation: CAA82014.1. BK006944 Genomic DNA. Translation: DAA08994.1.
PIR	S38002.
RefSeq	NP_012749.1. NM_001179738.1.
3D structure databases
ProteinModelPortal	P36049.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6507N.
IntAct	P36049. 25 interactions.
MINT	MINT-671580.
STRING	P36049.
Proteomic databases
PeptideAtlas	P36049.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL172W; YKL172W; YKL172W.
GeneID	853682.
KEGG	sce:YKL172W.
NMPDR	fig|4932.3.peg.3727.
Organism-specific databases
CYGD	YKL172w.
SGD	S000001655. EBP2.
Phylogenomic databases
eggNOG	fuNOG05214.
GeneTree	EFGT00050000000016.
HOGENOM	HBG714721.
OMA	KSDEHME.
OrthoDB	EOG408RJ7.
Gene expression databases
ArrayExpress	P36049.
Genevestigator	P36049.
GermOnline	YKL172W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008610. Ebp2. [Graphical view]
KO	K14823.
PANTHER	PTHR13028. Ebp2. 1 hit.
Pfam	PF05890. Ebp2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974646.

Entry information

Entry name

EBP2_YEAST

Accession

Primary (citable) accession number: P36049
Secondary accession number(s): D6VX28

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program