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Q99848

- EBP2_HUMAN

UniProt

Q99848 - EBP2_HUMAN

Protein

Probable rRNA-processing protein EBP2

Gene

EBNA1BP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. ribosome biogenesis Source: UniProtKB-KW

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:15531. EBNA1BP2.

    Subcellular locationi

    Nucleusnucleolus 2 Publications
    Note: Associated with the nucleolus in an RNA-dependent manner.

    GO - Cellular componenti

    1. membrane Source: ProtInc
    2. nucleolus Source: HPA
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27586.

    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

    ArrayExpressiQ99848.
    BgeeiQ99848.
    CleanExiHS_EBNA1BP2.
    GenevestigatoriQ99848.

    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.1 Publication

    Protein-protein interaction databases

    BioGridi116166. 49 interactions.
    IntActiQ99848. 14 interactions.
    MINTiMINT-86910.
    STRINGi9606.ENSP00000236051.

    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.
    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

    MDTPPLSDSE SESDESLVTD RELQDAFSRG LLKPGLNVVL EGPKKAVNDV    50
    NGLKQCLAEF KRDLEWVERL DVTLGPVPEI GGSEAPAPQN KDQKAVDPED 100
    DFQREMSFYR QAQAAVLAVL PRLHQLKVPT KRPTDYFAEM AKSDLQMQKI 150
    RQKLQTKQAA MERSEKAKQL RALRKYGKKV QTEVLQKRQQ EKAHMMNAIK 200
    KYQKGFSDKL DFLEGDQKPL AQRKKAGAKG QQMRKGPSAK RRYKNQKFGF 250
    GGKKKGSKWN TRESYDDVSS FRAKTAHGRG LKRPGKKGSN KRPGKRTREK 300
    MKNRTH 306
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi116241344.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86602 mRNA. Translation: AAB46731.1 .
    BC009175 mRNA. Translation: AAH09175.1 .
    CCDSi CCDS478.1.
    PIRi JC7687.
    RefSeqi NP_001153408.1. NM_001159936.1.
    NP_006815.2. NM_006824.2.
    UniGenei Hs.346868.

    3D structure databases

    ProteinModelPortali Q99848.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116166. 49 interactions.
    IntActi Q99848. 14 interactions.
    MINTi MINT-86910.
    STRINGi 9606.ENSP00000236051.

    PTM databases

    PhosphoSitei Q99848.

    Polymorphism databases

    DMDMi 116241344.

    2D gel databases

    SWISS-2DPAGE Q99848.

    Proteomic databases

    MaxQBi Q99848.
    PaxDbi Q99848.
    PRIDEi Q99848.

    Protocols and materials databases

    DNASUi 10969.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000236051 ; ENSP00000236051 ; ENSG00000117395 .
    GeneIDi 10969.
    KEGGi hsa:10969.
    UCSCi uc001cin.3. human.

    Organism-specific databases

    CTDi 10969.
    GeneCardsi GC01M043572.
    HGNCi HGNC:15531. EBNA1BP2.
    HPAi HPA026512.
    HPA028277.
    MIMi 614443. gene.
    neXtProti NX_Q99848.
    PharmGKBi PA27586.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263447.
    HOGENOMi HOG000231281.
    HOVERGENi HBG031528.
    InParanoidi Q99848.
    KOi K14823.
    PhylomeDBi Q99848.

    Miscellaneous databases

    ChiTaRSi EBNA1BP2. human.
    GeneWikii EBNA1BP2.
    GenomeRNAii 10969.
    NextBioi 41678.
    PROi Q99848.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99848.
    Bgeei Q99848.
    CleanExi HS_EBNA1BP2.
    Genevestigatori Q99848.

    Family and domain databases

    InterProi IPR008610. Ebp2.
    [Graphical view ]
    PANTHERi PTHR13028. PTHR13028. 1 hit.
    Pfami PF05890. Ebp2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 126 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