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Protein

Probable rRNA-processing protein EBP2

Gene

EBNA1BP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for the processing of the 27S pre-rRNA.By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Probable rRNA-processing protein EBP2
Alternative name(s):
EBNA1-binding protein 2
Nucleolar protein p40
Gene namesi
Name:EBNA1BP2
Synonyms:EBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:15531. EBNA1BP2.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: ProtInc
  • nucleolus Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27586.

Polymorphism and mutation databases

BioMutaiEBNA1BP2.
DMDMi116241344.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Probable rRNA-processing protein EBP2PRO_0000119993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei3 – 31Phosphothreonine1 Publication
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei11 – 111Phosphoserine1 Publication
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei16 – 161Phosphoserine2 Publications
Modified residuei270 – 2701Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99848.
PaxDbiQ99848.
PRIDEiQ99848.

2D gel databases

SWISS-2DPAGEQ99848.

PTM databases

PhosphoSiteiQ99848.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ99848.
CleanExiHS_EBNA1BP2.
ExpressionAtlasiQ99848. baseline and differential.
GenevisibleiQ99848. HS.

Organism-specific databases

HPAiHPA026512.
HPA028277.

Interactioni

Subunit structurei

Specifically interacts with EBV EBNA1. The EBNA1-EBP2 interaction is important for the stable segregation of EBV episomes during cell division (PubMed:10074103). Interacts with WDR46.2 Publications

Protein-protein interaction databases

BioGridi116166. 77 interactions.
IntActiQ99848. 16 interactions.
MINTiMINT-86910.
STRINGi9606.ENSP00000407323.

Structurei

3D structure databases

ProteinModelPortaliQ99848.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili138 – 16932Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the EBP2 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG263447.
GeneTreeiENSGT00390000014984.
HOGENOMiHOG000231281.
HOVERGENiHBG031528.
InParanoidiQ99848.
KOiK14823.
PhylomeDBiQ99848.

Family and domain databases

InterProiIPR008610. Ebp2.
[Graphical view]
PANTHERiPTHR13028. PTHR13028. 1 hit.
PfamiPF05890. Ebp2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99848-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTPPLSDSE SESDESLVTD RELQDAFSRG LLKPGLNVVL EGPKKAVNDV
60 70 80 90 100
NGLKQCLAEF KRDLEWVERL DVTLGPVPEI GGSEAPAPQN KDQKAVDPED
110 120 130 140 150
DFQREMSFYR QAQAAVLAVL PRLHQLKVPT KRPTDYFAEM AKSDLQMQKI
160 170 180 190 200
RQKLQTKQAA MERSEKAKQL RALRKYGKKV QTEVLQKRQQ EKAHMMNAIK
210 220 230 240 250
KYQKGFSDKL DFLEGDQKPL AQRKKAGAKG QQMRKGPSAK RRYKNQKFGF
260 270 280 290 300
GGKKKGSKWN TRESYDDVSS FRAKTAHGRG LKRPGKKGSN KRPGKRTREK

MKNRTH
Length:306
Mass (Da):34,852
Last modified:October 17, 2006 - v2
Checksum:i1212FC2E9442FA2E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471M → V in AAB46731 (PubMed:11327720).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti223 – 2231R → H.
Corresponds to variant rs7163 [ dbSNP | Ensembl ].
VAR_024437

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86602 mRNA. Translation: AAB46731.1.
BC009175 mRNA. Translation: AAH09175.1.
CCDSiCCDS478.1.
PIRiJC7687.
RefSeqiNP_001153408.1. NM_001159936.1.
NP_006815.2. NM_006824.2.
UniGeneiHs.346868.

Genome annotation databases

EnsembliENST00000236051; ENSP00000236051; ENSG00000117395.
GeneIDi10969.
KEGGihsa:10969.
UCSCiuc001cin.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86602 mRNA. Translation: AAB46731.1.
BC009175 mRNA. Translation: AAH09175.1.
CCDSiCCDS478.1.
PIRiJC7687.
RefSeqiNP_001153408.1. NM_001159936.1.
NP_006815.2. NM_006824.2.
UniGeneiHs.346868.

3D structure databases

ProteinModelPortaliQ99848.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116166. 77 interactions.
IntActiQ99848. 16 interactions.
MINTiMINT-86910.
STRINGi9606.ENSP00000407323.

PTM databases

PhosphoSiteiQ99848.

Polymorphism and mutation databases

BioMutaiEBNA1BP2.
DMDMi116241344.

2D gel databases

SWISS-2DPAGEQ99848.

Proteomic databases

MaxQBiQ99848.
PaxDbiQ99848.
PRIDEiQ99848.

Protocols and materials databases

DNASUi10969.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236051; ENSP00000236051; ENSG00000117395.
GeneIDi10969.
KEGGihsa:10969.
UCSCiuc001cin.3. human.

Organism-specific databases

CTDi10969.
GeneCardsiGC01M043572.
HGNCiHGNC:15531. EBNA1BP2.
HPAiHPA026512.
HPA028277.
MIMi614443. gene.
neXtProtiNX_Q99848.
PharmGKBiPA27586.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG263447.
GeneTreeiENSGT00390000014984.
HOGENOMiHOG000231281.
HOVERGENiHBG031528.
InParanoidiQ99848.
KOiK14823.
PhylomeDBiQ99848.

Miscellaneous databases

ChiTaRSiEBNA1BP2. human.
GeneWikiiEBNA1BP2.
GenomeRNAii10969.
NextBioi41678.
PROiQ99848.
SOURCEiSearch...

Gene expression databases

BgeeiQ99848.
CleanExiHS_EBNA1BP2.
ExpressionAtlasiQ99848. baseline and differential.
GenevisibleiQ99848. HS.

Family and domain databases

InterProiIPR008610. Ebp2.
[Graphical view]
PANTHERiPTHR13028. PTHR13028. 1 hit.
PfamiPF05890. Ebp2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "EBP2, a human protein that interacts with sequences of the Epstein-Barr virus nuclear antigen 1 important for plasmid maintenance."
    Shire K., Ceccarelli D.F.J., Avolio-Hunter T.M., Frappier L.
    J. Virol. 73:2587-2595(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EBNA1.
  2. "Expression of p40/Epstein-Barr virus nuclear antigen 1 binding protein 2."
    Henning D., Valdez B.C.
    Biochem. Biophys. Res. Commun. 283:430-436(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  4. "Identification and partial characterization of a Mr 40,000 nucleolar antigen associated with cell proliferation."
    Chatterjee A., Freeman J.W., Busch H.
    Cancer Res. 47:1123-1129(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Proteomic and targeted analytical identification of BXDC1 and EBNA1BP2 as dynamic scaffold proteins in the nucleolus."
    Hirano Y., Ishii K., Kumeta M., Furukawa K., Takeyasu K., Horigome T.
    Genes Cells 14:155-166(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-7; SER-9; SER-11; SER-13 AND SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Nucleolar scaffold protein, WDR46, determines the granular compartmental localization of nucleolin and DDX21."
    Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T., Takeyasu K.
    Genes Cells 18:780-797(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WDR46.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEBP2_HUMAN
AccessioniPrimary (citable) accession number: Q99848
Secondary accession number(s): Q96A66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 17, 2006
Last modified: June 24, 2015
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.