DP00213: Histone-binding protein N1/N2FASTA viewXML view

General information
DisProt:DP00213
Name:Histone-binding protein N1/N2
Synonym(s):HIBN_XENLA
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P06180
UniGene:Xl.48795
SwissProt: HIBN_XENLA
TrEMBL:  
NCBI (GI): 123127
Source organism:Xenopus laevis (African clawed frog)
Sequence length:590
Percent disordered:4%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MAEETAALST EKTEDTSTAP STSAEKADGI DIDTEAKRLM GAGQKHLVMK DVRSAVNLFQ - 60
EASSLLAKQY GETADECAEA FYSYGMSLLE LARLENGVLG NALEGMPEDD EEEAEKEEDP - 120
NIPSADNLDE KEREQLREQV YDAMAEDQRA PDDTSESEAK GKPEGDSKDK EADEKMKNGQ - 180
KETEKVTDDL KIDSASRDVP MDKSGKGEPP ESKDAETLVE QKESKPETLK EKSIETKEKD - 240
LSKEKTDAKE TANQSPDSTE VAEEKMDSEA SESKESTSIP PTENEANKPD DPEKMEEEEE - 300
GEDSEENEDG TEENEGTEEK ETEEEDVGNL QLAWEMLDLC KTIFKRQQSK EAQLKAAQAH - 360
QKLGEVCIES ENYSQAVEDF LACLNIQKEH LEEHDRLLAE THYHLGLAYQ YSSKHEEAIS - 420
HFTQSIGVIE KRMDVLTKQL EASVGELVDE VKKEMDELKD LLPDIKEKIE DSKEAQKNAT - 480
VTEKALKETL VGGSSGFSKE NGSTSSSSAV EKSGDSTVPV TNCVSDISHL VRKKRKTEEE - 540
SPLKDKDAKK SKQEPVANGA GNGDAVVPTN EEAEKAEEAS METATVESTA



Functional narrative    

This protein is involved in nucleosome assembly. It is bound to H3 and H4 in the absence of DNA, but released from H3 and H4 in the presence of DNA. (UniProt).

Region 1: 532-552

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:nuclear location sequence (NLS)
Location:532 - 552
Length:21
Region sequence:

RKKRKTEEESPLKDKAKKSKG

Modification type: Complex
Engineered
Fragment
PDB: 1PJN:A
Structural/functional type: Function arises from the disordered state
Functional classes: Chaperones
Functional subclasses: Nuclear localization
Flexible linkers/spacers
Detection methods:
  1. X-ray crystallography (293 K; pH: 6; DTT; Sodium citrate)

References:
  1. Fontes MR, Teh T, Jans D, Brinkworth RI, Kobe B. "Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha." J. Biol. Chem.. 2003; 278(30): 27981-7. PubMed: 12695505

Comments:
The numbering used by Fontes et al (2003) for the NLS--aa 335-355--differs slightly from UniProt--aa 532-552--for the same sequence. UniProt numbering is used in DP00213. Additionally, the authors used a synthetically constructed peptide which varies from UniProt (listed first) at these positions: D547A, A548K, K550S, S551K, K552G.


The Fontes et al (2003) experiment was performed in complex with importin-alpha.




References

  1. Fontes MR, Teh T, Jans D, Brinkworth RI, Kobe B. "Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha." J. Biol. Chem.. 2003; 278(30): 27981-7. PubMed: 12695505

  2. Kleinschmidt JA, Dingwall C, Maier G, Franke WW. "Molecular characterization of a karyophilic, histone-binding protein: cDNA cloning, amino acid sequence and expression of nuclear protein N1/N2 of Xenopus laevis." Embo J. 1986; 5(13): 3547-52. PubMed: 3549279



Comments


According to Kleinschmidt et al (1986), this protein shows aberrant migration on SDS-PAGE gels and is heat stable. These two properties strongly suggest that the protein is totally disordered but are not considered definitive evidence that it is, in fact, disordered.


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