P05221 (NUPL_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Nucleoplasmin
Organism	Xenopus laevis (African clawed frog)
Taxonomic identifier	8355 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	200 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.5 Ref.6
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.
Sequence similarities	Belongs to the nucleoplasmin family.
Biophysicochemical properties	Temperature dependence: Thermostable.

Ontologies

Keywords
Biological process	Fertilization
Cellular component	Nucleus
Molecular function	Chaperone Chromatin regulator Developmental protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	chromatin 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_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 200

199

Nucleoplasmin

PRO_0000219486

Regions

Region

35 – 39

5

Acidic tract A1

Region

128 – 148

21

Acidic tract A2

Region

174 – 176

3

Acidic tract A3

Motif

155 – 170

16

Bipartite nuclear localization signal

Compositional bias

138 – 145

8

Poly-Glu

Sites

Site

58

1

Interaction between pentamers By similarity

Site

82

1

Interaction between pentamers By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3

Modified residue

3

1

Phosphoserine Ref.3

Modified residue

4

1

Phosphothreonine Ref.3

Modified residue

6

1

Phosphoserine Ref.3

Modified residue

8

1

Phosphothreonine Ref.3

Modified residue

149

1

Phosphoserine Ref.3

Modified residue

177

1

Phosphoserine Ref.3

Modified residue

178

1

Phosphoserine Ref.3

Modified residue

182

1

Phosphoserine Ref.3

Experimental info

Sequence conflict

11

1

L → V in CAA68363. Ref.2

Sequence conflict

27

1

D → N in CAA68363. Ref.2

Sequence conflict

31

1

E → A in CAA68363. Ref.2

Sequence conflict

34

1

V → I in CAA68363. Ref.2

Sequence conflict

61

1

N → H in CAA68363. Ref.2

Sequence conflict

72

1

A → K in CAA68363. Ref.2

Sequence conflict

75

1

S → P in CAA68363. Ref.2

Sequence conflict

80

1

T → S in CAA68363. Ref.2

Sequence conflict

111

1

L → V in CAA68363. Ref.2

Sequence conflict

134 – 137

4

Missing Ref.2

Sequence conflict

147

1

Q → P in CAA68363. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

200

Helix Strand Turn

Details...

Beta strand

18 – 23

6

Beta strand

29 – 32

4

Beta strand

44 – 52

9

Beta strand

61 – 67

7

Beta strand

74 – 82

9

Turn

83 – 85

3

Beta strand

88 – 90

3

Beta strand

100 – 106

7

Beta strand

111 – 118

8

Sequences

	Sequence		Length	Mass (Da)
	P05221 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: A91DD110F2965812	FASTA	200	22,024
	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

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]	"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.
[5]	"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.
[6]	"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.

PIR

A26169.
A26630.

UniGene

Xl.1262.
Xl.1264.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00217.

ProteinModelPortal

P05221.

SMR

P05221. Positions 16-119.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48470N.

MINT

MINT-6623126.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG045601.

Family and domain databases

Gene3D

2.60.120.340. 1 hit.

InterPro

IPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]

PANTHER

PTHR22747. PTHR22747. 1 hit.

SUPFAM

SSF69203. Nucleoplasmin. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P05221.

Entry information

Entry name

NUPL_XENLA

Accession

Primary (citable) accession number: P05221

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program