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

P05221 (NUPL_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Nucleoplasmin
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.4 Ref.6 Ref.7

Subcellular location

Nucleus.

Post-translational modification

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.

Methylated by prmt5, yielding both monomethylated and symmetrically dimethylated Arg-192. Ref.4

Sequence similarities

Belongs to the nucleoplasmin family.

Biophysicochemical properties

Temperature dependence:

Thermostable.

Ontologies

Keywords
   Biological processFertilization
   Cellular componentNucleus
   Molecular functionChaperone
Chromatin regulator
Developmental protein
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

single fertilization

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 200199Nucleoplasmin
PRO_0000219486

Regions

Region35 – 395Acidic tract A1
Region128 – 14821Acidic tract A2
Region174 – 1763Acidic tract A3
Motif155 – 17016Bipartite nuclear localization signal
Compositional bias138 – 1458Poly-Glu

Sites

Site581Interaction between pentamers By similarity
Site821Interaction between pentamers By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue31Phosphoserine Ref.3
Modified residue41Phosphothreonine Ref.3
Modified residue61Phosphoserine Ref.3
Modified residue81Phosphothreonine Ref.3
Modified residue1491Phosphoserine Ref.3
Modified residue1771Phosphoserine Ref.3
Modified residue1781Phosphoserine Ref.3
Modified residue1821Phosphoserine Ref.3
Modified residue1921Omega-N-methylarginine; by PRMT5; alternate Ref.4
Modified residue1921Symmetric dimethylarginine; by PRMT5; alternate Ref.4

Experimental info

Mutagenesis1921R → A: Abolishes arginine methylation. Ref.4
Mutagenesis1941R → A: Reduces arginine methylation. Ref.4
Sequence conflict111L → V in CAA68363. Ref.2
Sequence conflict271D → N in CAA68363. Ref.2
Sequence conflict311E → A in CAA68363. Ref.2
Sequence conflict341V → I in CAA68363. Ref.2
Sequence conflict611N → H in CAA68363. Ref.2
Sequence conflict721A → K in CAA68363. Ref.2
Sequence conflict751S → P in CAA68363. Ref.2
Sequence conflict801T → S in CAA68363. Ref.2
Sequence conflict1111L → V in CAA68363. Ref.2
Sequence conflict134 – 1374Missing Ref.2
Sequence conflict1471Q → P in CAA68363. Ref.2

Secondary structure

.................. 200
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05221 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: A91DD110F2965812

FASTA20022,024
        10         20         30         40         50         60 
MASTVSNTSK LEKPVSLIWG CELNEQDKTF EFKVEDDEEK CEHQLALRTV CLGDKAKDEF 

        70         80         90        100        110        120 
NIVEIVTQEE GAEKSVPIAT LKPSILPMAT MVGIELTPPV TFRLKAGSGP LYISGQHVAM 

       130        140        150        160        170        180 
EEDYSWAEEE DEGEAEGEEE EEEEEDQESP PKAVKRPAAT KKAGQAKKKK LDKEDESSEE 

       190        200 
DSPTKKGKGA GRGRKPAAKK 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04766 mRNA. Translation: CAA28460.1.
Y00204 mRNA. Translation: CAA68363.1.
PIRA26169.
A26630.
UniGeneXl.1262.
Xl.1264.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00217.
ProteinModelPortalP05221.
SMRP05221. Positions 16-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48470N.
IntActP05221. 1 interaction.
MINTMINT-6623126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG045601.

Family and domain databases

Gene3D2.60.120.340. 1 hit.
InterProIPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERPTHR22747. PTHR22747. 1 hit.
SUPFAMSSF69203. SSF69203. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP05221.

Entry information

Entry nameNUPL_XENLA
AccessionPrimary (citable) accession number: P05221
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references