DP00136: Histone H1.2FASTA viewXML view

General information
DisProt:DP00136
Name:Histone H1.2
Synonym(s):H12_RAT
H1d
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P15865
UniGene:Rn.196361
SwissProt: H12_RAT
TrEMBL:  
NCBI (GI): 1170152
Source organism:Rattus norvegicus (Rat)
Sequence length:217
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSETAPAAPA APAPAEKTPI KKKARKAAGG AKRKASGPPV SELITKAVAA SKERSGVSLA - 60
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA - 120
KKAGAAKAKK PAGAAKKPKK ATGTATPKKS TKKTPKKAKK PAAGAKKAKS PKKAKATKAK - 180
KAPKSPAKAR AVKPKAAKPK TSKPKAAKPK KTAAKKK



Functional narrative    

Histone H1d is essential for the condensation of DNA into inactive solenoid-like structures. H1d is a member of the histone H1/H5 family and located in the nucleus. H1d appears to contain a molten globular structure flanked by two disordered regions. These regions appear to become ordered when H1d interacts with ATP, and subsequently DNA.

Region 1: 1-30 Region 2: 31-119 Region 3: 120-217

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 - Extended
Name: 
Location:1 - 30
Length:30
Region sequence:

MSETAPAAPAAPAPAEKTPIKKKARKAAGG

Modification type: Complex
Engineered
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-DNA binding
Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, near-UV (pH: 7.5; )
References:
  1. Cole KD, Kandala JC, Kremer E, Kistler WS. "Isolation of a genomic clone encoding the rat histone variant, H1d." Gene. 1990; 89(2): 265-9. PubMed: 2373370

  2. Tarkka T, Oikarinen J, Grundstrom T. "Nucleotide and calcium-induced conformational changes in histone H1." FEBS Lett. 1997; 406(1-2): 56-60. PubMed: 9109385
Comments:
 



Region 2
Type:Disordered - Molten Globule
Name: 
Location:31 - 119
Length:89
Region sequence:

AKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSK
GTLVQTKGTGASGSFKLNKKAASGEAKPK

Modification type: Complex
Engineered
PDB:  
Structural/functional type: Function arises via a molten globule to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-DNA binding
Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, near-UV (pH: 7.5; )
References:
  1. Cole KD, Kandala JC, Kremer E, Kistler WS. "Isolation of a genomic clone encoding the rat histone variant, H1d." Gene. 1990; 89(2): 265-9. PubMed: 2373370

  2. Tarkka T, Oikarinen J, Grundstrom T. "Nucleotide and calcium-induced conformational changes in histone H1." FEBS Lett. 1997; 406(1-2): 56-60. PubMed: 9109385
Comments:
 



Region 3
Type:Disordered - Extended
Name: 
Location:120 - 217
Length:98
Region sequence:

AKKAGAAKAKKPAGAAKKPKKATGTATPKKSTKKTPKKAKKPAAGAKKAKSPKKAKATKA
KKAPKSPAKARAVKPKAAKPKTSKPKAAKPKKTAAKKK

Modification type: Complex
Engineered
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-DNA binding
Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, near-UV (pH: 7.5; )
References:
  1. Cole KD, Kandala JC, Kremer E, Kistler WS. "Isolation of a genomic clone encoding the rat histone variant, H1d." Gene. 1990; 89(2): 265-9. PubMed: 2373370

  2. Tarkka T, Oikarinen J, Grundstrom T. "Nucleotide and calcium-induced conformational changes in histone H1." FEBS Lett. 1997; 406(1-2): 56-60. PubMed: 9109385
Comments:
 


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