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Protein

Nucleoplasmin

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: 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.

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi192R → A: Abolishes arginine methylation. 1 Publication1
Mutagenesisi194R → A: Reduces arginine methylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002194862 – 200NucleoplasminAdd BLAST199

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei3Phosphoserine1 Publication1
Modified residuei4Phosphothreonine1 Publication1
Modified residuei6Phosphoserine1 Publication1
Modified residuei8Phosphothreonine1 Publication1
Modified residuei149Phosphoserine1 Publication1
Modified residuei177Phosphoserine1 Publication1
Modified residuei178Phosphoserine1 Publication1
Modified residuei182Phosphoserine1 Publication1
Modified residuei192Omega-N-methylarginine; by PRMT5; alternate1 Publication1
Modified residuei192Symmetric dimethylarginine; by PRMT5; alternate1 Publication1

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

PTM databases

iPTMnetiP05221.

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei58Interaction between pentamersBy similarity1
Sitei82Interaction between pentamersBy similarity1

Protein-protein interaction databases

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

Structurei

Secondary structure

1200
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 23Combined sources6
Beta strandi29 – 32Combined sources4
Beta strandi44 – 52Combined sources9
Beta strandi61 – 67Combined sources7
Beta strandi74 – 82Combined sources9
Turni83 – 85Combined sources3
Beta strandi88 – 90Combined sources3
Beta strandi100 – 106Combined sources7
Beta strandi111 – 118Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05221.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 39Acidic tract A15
Regioni128 – 148Acidic tract A2Add BLAST21
Regioni174 – 176Acidic tract A33

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi155 – 170Bipartite nuclear localization signalAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi138 – 145Poly-Glu8

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.
PfamiPF03066. Nucleoplasmin. 1 hit.
[Graphical view]
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)DescriptionActionsGraphical viewLength
Sequence conflicti11L → V in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti27D → N in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti31E → A in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti34V → I in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti61N → H in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti72A → K in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti75S → P in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti80T → S in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti111L → V in CAA68363 (PubMed:3428591).Curated1
Sequence conflicti134 – 137Missing (PubMed:3428591).Curated4
Sequence conflicti147Q → P in CAA68363 (PubMed:3428591).Curated1

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.
PIRiA26169.
A26630.
UniGeneiXl.1262.
Xl.1264.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP05221.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG045601.

Miscellaneous databases

EvolutionaryTraceiP05221.

Family and domain databases

Gene3Di2.60.120.340. 1 hit.
InterProiIPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERiPTHR22747. PTHR22747. 1 hit.
PfamiPF03066. Nucleoplasmin. 1 hit.
[Graphical view]
SUPFAMiSSF69203. SSF69203. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 91 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.