UniProtKB - P05221 (NUPL_XENLA)
Protein
Nucleoplasmin
Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Functioni
Acts as a chaperone for histones, such as histone H2A-H2B, and thus regulates the assembly of nucleosome cores (PubMed:11684019, PubMed:19055325). Involved in chromatin remodeling, especially during fertilization and early embryonic development (By similarity). May be involved in sperm chromatin decondensation during fertilization (PubMed:17510054).By similarity3 Publications
Temperature dependencei
Thermostable.
GO - Molecular functioni
- nucleosome binding Source: CAFA
GO - Biological processi
- chromosome decondensation Source: CAFA
- multicellular organism development Source: UniProtKB-KW
- sperm chromatin decondensation Source: CAFA
Keywordsi
Molecular function | Chaperone, Chromatin regulator, Developmental protein |
Biological process | Fertilization |
Names & Taxonomyi
Protein namesi | Recommended name: Nucleoplasmin |
Organismi | Xenopus laevis (African clawed frog) |
Taxonomic identifieri | 8355 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 192 | R → A: Abolishes arginine methylation. 1 Publication | 1 | |
Mutagenesisi | 194 | R → A: Reduces arginine methylation. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000219486 | 2 – 200 | NucleoplasminAdd BLAST | 199 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanine1 Publication | 1 | |
Modified residuei | 3 | Phosphoserine1 Publication | 1 | |
Modified residuei | 4 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 6 | Phosphoserine1 Publication | 1 | |
Modified residuei | 8 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 149 | Phosphoserine1 Publication | 1 | |
Modified residuei | 177 | Phosphoserine1 Publication | 1 | |
Modified residuei | 178 | Phosphoserine1 Publication | 1 | |
Modified residuei | 182 | Phosphoserine1 Publication | 1 | |
Modified residuei | 192 | Omega-N-methylarginine; by PRMT5; alternate1 Publication | 1 | |
Modified residuei | 192 | Symmetric dimethylarginine; by PRMT5; alternate1 Publication | 1 |
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, PhosphoproteinPTM databases
iPTMneti | P05221 |
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 PublicationsSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 58 | Interaction between pentamers1 Publication | 1 | |
Sitei | 82 | Interaction between pentamers1 Publication | 1 |
Binary interactionsi
P05221
With | #Exp. | IntAct |
---|---|---|
SRP1 [Q02821] from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). | 2 | EBI-7261813,EBI-1797 |
Protein-protein interaction databases
DIPi | DIP-48470N |
ELMi | P05221 |
IntActi | P05221, 2 interactors |
MINTi | P05221 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P05221 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P05221 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 35 – 39 | Acidic tract A11 Publication | 5 | |
Regioni | 128 – 148 | Acidic tract A21 PublicationAdd BLAST | 21 | |
Regioni | 174 – 176 | Acidic tract A31 Publication | 3 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 155 – 170 | Bipartite nuclear localization signal1 PublicationAdd BLAST | 16 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 138 – 145 | Poly-Glu | 8 |
Sequence similaritiesi
Belongs to the nucleoplasmin family.Curated
Family and domain databases
DisProti | DP00217 |
IDEALi | IID50001 |
InterProi | View protein in InterPro IPR004301, Nucleoplasmin IPR024057, Nucleoplasmin_core_dom IPR036824, Nucleoplasmin_core_dom_sf |
PANTHERi | PTHR22747, PTHR22747, 1 hit |
Pfami | View protein in Pfam PF03066, Nucleoplasmin, 1 hit |
SUPFAMi | SSF69203, SSF69203, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P05221-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 11 | L → V in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 27 | D → N in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 31 | E → A in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 34 | V → I in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 61 | N → H in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 72 | A → K in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 75 | S → P in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 80 | T → S in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 111 | L → V in CAA68363 (PubMed:3428591).Curated | 1 | |
Sequence conflicti | 134 – 137 | Missing in CAA68363 (PubMed:3428591).Curated | 4 | |
Sequence conflicti | 147 | Q → P in CAA68363 (PubMed:3428591).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X04766 mRNA Translation: CAA28460.1 Y00204 mRNA Translation: CAA68363.1 |
PIRi | A26169 A26630 |
Similar proteinsi
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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | 1-120 | [»] | |
3UL1 | X-ray | 1.90 | A | 153-172 | [»] | |
4BPL | X-ray | 2.30 | B | 153-172 | [»] | |
SMRi | P05221 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-48470N |
ELMi | P05221 |
IntActi | P05221, 2 interactors |
MINTi | P05221 |
PTM databases
iPTMneti | P05221 |
Protocols and materials databases
ABCDi | P05221, 1 sequenced antibody |
Miscellaneous databases
EvolutionaryTracei | P05221 |
Family and domain databases
DisProti | DP00217 |
IDEALi | IID50001 |
InterProi | View protein in InterPro IPR004301, Nucleoplasmin IPR024057, Nucleoplasmin_core_dom IPR036824, Nucleoplasmin_core_dom_sf |
PANTHERi | PTHR22747, PTHR22747, 1 hit |
Pfami | View protein in Pfam PF03066, Nucleoplasmin, 1 hit |
SUPFAMi | SSF69203, SSF69203, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NUPL_XENLA | |
Accessioni | P05221Primary (citable) accession number: P05221 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 13, 1987 |
Last sequence update: | August 13, 1987 | |
Last modified: | December 2, 2020 | |
This is version 109 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families