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P05221

- NUPL_XENLA

UniProt

P05221 - NUPL_XENLA

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Protein

Nucleoplasmin

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 31Phosphoserine1 Publication
Modified residuei4 – 41Phosphothreonine1 Publication
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei8 – 81Phosphothreonine1 Publication
Modified residuei149 – 1491Phosphoserine1 Publication
Modified residuei177 – 1771Phosphoserine1 Publication
Modified residuei178 – 1781Phosphoserine1 Publication
Modified residuei182 – 1821Phosphoserine1 Publication
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 – 236Combined sources
Beta strandi29 – 324Combined sources
Beta strandi44 – 529Combined sources
Beta strandi61 – 677Combined sources
Beta strandi74 – 829Combined sources
Turni83 – 853Combined sources
Beta strandi88 – 903Combined sources
Beta strandi100 – 1067Combined sources
Beta strandi111 – 1188Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

« Hide

        10         20         30         40         50
MASTVSNTSK LEKPVSLIWG CELNEQDKTF EFKVEDDEEK CEHQLALRTV
60 70 80 90 100
CLGDKAKDEF NIVEIVTQEE GAEKSVPIAT LKPSILPMAT MVGIELTPPV
110 120 130 140 150
TFRLKAGSGP LYISGQHVAM EEDYSWAEEE DEGEAEGEEE EEEEEDQESP
160 170 180 190 200
PKAVKRPAAT KKAGQAKKKK LDKEDESSEE DSPTKKGKGA GRGRKPAAKK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 84 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