Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q99848 (EBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable rRNA-processing protein EBP2
Alternative name(s):
EBNA1-binding protein 2
Nucleolar protein p40
Gene names
Name:EBNA1BP2
Synonyms:EBP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Specifically interacts with EBV EBNA1. The EBNA1-EBP2 interaction is important for the stable segregation of EBV episomes during cell division. Ref.1

Subcellular location

Nucleusnucleolus. Note: Associated with the nucleolus in an RNA-dependent manner. Ref.4 Ref.7

Tissue specificity

Ubiquitous. Ref.2

Sequence similarities

Belongs to the EBP2 family.

Ontologies

Keywords
   Biological processRibosome biogenesis
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processribosome biogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmembrane

Traceable author statement PubMed 7596406. Source: ProtInc

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Probable rRNA-processing protein EBP2
PRO_0000119993

Regions

Coiled coil138 – 16932 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.10
Modified residue31Phosphothreonine Ref.8
Modified residue71Phosphoserine Ref.8
Modified residue91Phosphoserine Ref.8
Modified residue111Phosphoserine Ref.8
Modified residue131Phosphoserine Ref.8
Modified residue161Phosphoserine Ref.5 Ref.8
Modified residue2701Phosphoserine Ref.6

Natural variations

Natural variant2231R → H.
Corresponds to variant rs7163 [ dbSNP | Ensembl ].
VAR_024437

Experimental info

Sequence conflict1471M → V in AAB46731. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99848 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 1212FC2E9442FA2E

FASTA30634,852
        10         20         30         40         50         60 
MDTPPLSDSE SESDESLVTD RELQDAFSRG LLKPGLNVVL EGPKKAVNDV NGLKQCLAEF 

        70         80         90        100        110        120 
KRDLEWVERL DVTLGPVPEI GGSEAPAPQN KDQKAVDPED DFQREMSFYR QAQAAVLAVL 

       130        140        150        160        170        180 
PRLHQLKVPT KRPTDYFAEM AKSDLQMQKI RQKLQTKQAA MERSEKAKQL RALRKYGKKV 

       190        200        210        220        230        240 
QTEVLQKRQQ EKAHMMNAIK KYQKGFSDKL DFLEGDQKPL AQRKKAGAKG QQMRKGPSAK 

       250        260        270        280        290        300 
RRYKNQKFGF GGKKKGSKWN TRESYDDVSS FRAKTAHGRG LKRPGKKGSN KRPGKRTREK 


MKNRTH 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U86602 mRNA. Translation: AAB46731.1.
BC009175 mRNA. Translation: AAH09175.1.
PIRJC7687.
RefSeqNP_001153408.1. NM_001159936.1.
NP_006815.2. NM_006824.2.
UniGeneHs.346868.

3D structure databases

ProteinModelPortalQ99848.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116166. 41 interactions.
IntActQ99848. 14 interactions.
MINTMINT-86910.
STRING9606.ENSP00000236051.

PTM databases

PhosphoSiteQ99848.

Polymorphism databases

DMDM116241344.

2D gel databases

SWISS-2DPAGEQ99848.

Proteomic databases

PaxDbQ99848.
PRIDEQ99848.

Protocols and materials databases

DNASU10969.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000236051; ENSP00000236051; ENSG00000117395.
GeneID10969.
KEGGhsa:10969.
UCSCuc001cin.3. human.

Organism-specific databases

CTD10969.
GeneCardsGC01M043572.
HGNCHGNC:15531. EBNA1BP2.
HPAHPA026512.
HPA028277.
MIM614443. gene.
neXtProtNX_Q99848.
PharmGKBPA27586.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263447.
HOGENOMHOG000231281.
HOVERGENHBG031528.
InParanoidQ99848.
KOK14823.
PhylomeDBQ99848.

Gene expression databases

ArrayExpressQ99848.
BgeeQ99848.
CleanExHS_EBNA1BP2.
GenevestigatorQ99848.

Family and domain databases

InterProIPR008610. Ebp2.
[Graphical view]
PANTHERPTHR13028. PTHR13028. 1 hit.
PfamPF05890. Ebp2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEBNA1BP2. human.
GeneWikiEBNA1BP2.
GenomeRNAi10969.
NextBio41678.
PROQ99848.
SOURCESearch...

Entry information

Entry nameEBP2_HUMAN
AccessionPrimary (citable) accession number: Q99848
Secondary accession number(s): Q96A66
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM