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P05221

- NUPL_XENLA

UniProt

P05221 - NUPL_XENLA

Protein

Nucleoplasmin

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Nucleoplasmin is an acidic protein which is able to assemble nucleosomes by binding histones and transferring them to DNA.

    Temperature dependencei

    Thermostable.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei58 – 581Interaction between pentamersBy similarity
    Sitei82 – 821Interaction between pentamersBy similarity

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. multicellular organismal development Source: UniProtKB-KW
    3. single fertilization Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone, Chromatin regulator, Developmental protein

    Keywords - Biological processi

    Fertilization

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoplasmin
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi192 – 1921R → A: Abolishes arginine methylation. 1 Publication
    Mutagenesisi194 – 1941R → A: Reduces arginine methylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 200199NucleoplasminPRO_0000219486Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei3 – 31Phosphoserine2 Publications
    Modified residuei4 – 41Phosphothreonine2 Publications
    Modified residuei6 – 61Phosphoserine2 Publications
    Modified residuei8 – 81Phosphothreonine2 Publications
    Modified residuei149 – 1491Phosphoserine2 Publications
    Modified residuei177 – 1771Phosphoserine2 Publications
    Modified residuei178 – 1781Phosphoserine2 Publications
    Modified residuei182 – 1821Phosphoserine2 Publications
    Modified residuei192 – 1921Omega-N-methylarginine; by PRMT5; alternate1 Publication
    Modified residuei192 – 1921Symmetric dimethylarginine; by PRMT5; alternate1 Publication

    Post-translational modificationi

    Activated by phosphorylation of multiple serine/threonine residues, along both core and tail domains. The level of phosphorylation gradually increases during egg maturation, reaching an average of 7-10 phosphates per monomer, so that at the time of fertilization the activity of the protein is maximum.2 Publications
    Methylated by prmt5, yielding both monomethylated and symmetrically dimethylated Arg-192.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Interactioni

    Subunit structurei

    Homopentamer, when bound to H2A-H2B dimers only. Homodecamer of two stacked pentamers, when bound to H2A-H2B dimers and H3-H4 tetramers simultaneously. Interacts with the heterotetramer formed by wdr77 and prmt5.4 Publications

    Protein-protein interaction databases

    DIPiDIP-48470N.
    IntActiP05221. 1 interaction.
    MINTiMINT-6623126.

    Structurei

    Secondary structure

    1
    200
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 236
    Beta strandi29 – 324
    Beta strandi44 – 529
    Beta strandi61 – 677
    Beta strandi74 – 829
    Turni83 – 853
    Beta strandi88 – 903
    Beta strandi100 – 1067
    Beta strandi111 – 1188

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EE5X-ray2.40B153-171[»]
    1EJYX-ray2.90N155-170[»]
    1K5JX-ray2.30A/B/C/D/E1-124[»]
    2VTXX-ray2.50A/B/C/D/E/G/H/I/J/K10-120[»]
    3UL1X-ray1.90A153-172[»]
    4BPLX-ray2.30B153-172[»]
    DisProtiDP00217.
    ProteinModelPortaliP05221.
    SMRiP05221. Positions 16-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05221.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 395Acidic tract A1
    Regioni128 – 14821Acidic tract A2Add
    BLAST
    Regioni174 – 1763Acidic tract A3

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi155 – 17016Bipartite nuclear localization signalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi138 – 1458Poly-Glu

    Sequence similaritiesi

    Belongs to the nucleoplasmin family.Curated

    Phylogenomic databases

    HOVERGENiHBG045601.

    Family and domain databases

    Gene3Di2.60.120.340. 1 hit.
    InterProiIPR004301. Nucleoplasmin.
    IPR024057. Nucleoplasmin_core_dom.
    [Graphical view]
    PANTHERiPTHR22747. PTHR22747. 1 hit.
    SUPFAMiSSF69203. SSF69203. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05221-1 [UniParc]FASTAAdd to Basket

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    MASTVSNTSK LEKPVSLIWG CELNEQDKTF EFKVEDDEEK CEHQLALRTV    50
    CLGDKAKDEF NIVEIVTQEE GAEKSVPIAT LKPSILPMAT MVGIELTPPV 100
    TFRLKAGSGP LYISGQHVAM EEDYSWAEEE DEGEAEGEEE EEEEEDQESP 150
    PKAVKRPAAT KKAGQAKKKK LDKEDESSEE DSPTKKGKGA GRGRKPAAKK 200
    Length:200
    Mass (Da):22,024
    Last modified:August 13, 1987 - v1
    Checksum:iA91DD110F2965812
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111L → V in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti27 – 271D → N in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti31 – 311E → A in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti34 – 341V → I in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti61 – 611N → H in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti72 – 721A → K in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti75 – 751S → P in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti80 – 801T → S in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti111 – 1111L → V in CAA68363. (PubMed:3428591)Curated
    Sequence conflicti134 – 1374Missing(PubMed:3428591)Curated
    Sequence conflicti147 – 1471Q → P in CAA68363. (PubMed:3428591)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04766 mRNA. Translation: CAA28460.1.
    Y00204 mRNA. Translation: CAA68363.1.
    PIRiA26169.
    A26630.
    UniGeneiXl.1262.
    Xl.1264.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04766 mRNA. Translation: CAA28460.1 .
    Y00204 mRNA. Translation: CAA68363.1 .
    PIRi A26169.
    A26630.
    UniGenei Xl.1262.
    Xl.1264.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EE5 X-ray 2.40 B 153-171 [» ]
    1EJY X-ray 2.90 N 155-170 [» ]
    1K5J X-ray 2.30 A/B/C/D/E 1-124 [» ]
    2VTX X-ray 2.50 A/B/C/D/E/G/H/I/J/K 10-120 [» ]
    3UL1 X-ray 1.90 A 153-172 [» ]
    4BPL X-ray 2.30 B 153-172 [» ]
    DisProti DP00217.
    ProteinModelPortali P05221.
    SMRi P05221. Positions 16-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48470N.
    IntActi P05221. 1 interaction.
    MINTi MINT-6623126.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG045601.

    Miscellaneous databases

    EvolutionaryTracei P05221.

    Family and domain databases

    Gene3Di 2.60.120.340. 1 hit.
    InterProi IPR004301. Nucleoplasmin.
    IPR024057. Nucleoplasmin_core_dom.
    [Graphical view ]
    PANTHERi PTHR22747. PTHR22747. 1 hit.
    SUPFAMi SSF69203. SSF69203. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals."
      Dingwall C., Dilworth S.M., Black S.J., Kearsey S.E., Cox L.S., Laskey R.A.
      EMBO J. 6:69-74(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of nucleoplasmin from Xenopus laevis oocytes and analysis of its developmental expression."
      Buerglin T.R., Mattaj I.W., Newmeyer D.D., Zeller R., De Robertis E.M.
      Genes Dev. 1:97-107(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-200.
    3. "Phosphorylation of both nucleoplasmin domains is required for activation of its chromatin decondensation activity."
      Banuelos S., Omaetxebarria M.J., Ramos I., Larsen M.R., Arregi I., Jensen O.N., Arizmendi J.M., Prado A., Muga A.
      J. Biol. Chem. 282:21213-21221(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-3; THR-4; SER-6; THR-8; SER-149; SER-177; SER-178 AND SER-182.
    4. "Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs."
      Wilczek C., Chitta R., Woo E., Shabanowitz J., Chait B.T., Hunt D.F., Shechter D.
      J. Biol. Chem. 286:42221-42231(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT5 AND WDR77, MUTAGENESIS OF ARG-192 AND ARG-194, IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION AT ARG-192.
    5. "Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha."
      Conti E., Kuriyan J.
      Structure 8:329-338(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 153-171 IN COMPLEX WITH KARYOPHERIN ALPHA, NUCLEAR LOCALIZATION SIGNAL.
    6. "The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly."
      Dutta S., Akey I.V., Dingwall C., Hartman K.L., Laue T., Nolte R.T., Head J.F., Akey C.W.
      Mol. Cell 8:841-853(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-124, SUBUNIT.
    7. "Activation of nucleoplasmin, an oligomeric histone chaperone, challenges its stability."
      Taneva S.G., Munoz I.G., Franco G., Falces J., Arregi I., Muga A., Montoya G., Urbaneja M.A., Banuelos S.
      Biochemistry 47:13897-13906(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 10-120, PHOSPHORYLATION, SUBUNIT.

    Entry informationi

    Entry nameiNUPL_XENLA
    AccessioniPrimary (citable) accession number: P05221
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3