DP00041: High mobility group-T proteinFASTA viewXML view

General information
DisProt:DP00041
Name:High mobility group-T protein
Synonym(s):HMGT_ONCMY
HMG-T
HMG-T1
HMG-1
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P07746
UniGene:Omy.32291
SwissProt: HMGT_ONCMY
TrEMBL:  
NCBI (GI): 123382
Source organism:Oncorhynchus mykiss (Rainbow trout)(Salmo gairdneri)
Sequence length:204
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MGKDPRKPRG KMSSYAYFVQ TRREEHKKKH PEASVNFSEF SKKCSERWKT MSAKEKGKFE - 60
DLAKLDKVRY EREMRSYIPP KGEKKKRFKD PNAPKRPSSA FFIFCADFRP QVKGETPGLS - 120
IGDVAKKLGE KWNNLTAEDK VPYEKKASRL KEKYEKDITA YRNKGKVPVS MPAKAAAPAK - 180
DDDDDDDDDD DDEDDDDDDD EDDE



Functional narrative    

Circular dichroism at pH 2 indicates that there is 9% helical content which is very much less than homologous proteins HMG-1 and HMG-2. As pH or salt concentration is increased, the structure proceeds to fold and aggregate into secondary and tertiary structure. According to NMR data, HMG-T lacks a highly acidic domain that suggests that the entire chain binds to DNA. This is different than HMG-1 and HMG-2, which have highly acidic domains that do not bind DNA.

Region 1: 1-204

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 - 204
Length:204
Region sequence:

MGKDPRKPRGKMSSYAYFVQTRREEHKKKHPEASVNFSEFSKKCSERWKTMSAKEKGKFE
DLAKLDKVRYEREMRSYIPPKGEKKKRFKDPNAPKRPSSAFFIFCADFRPQVKGETPGLS
IGDVAKKLGEKWNNLTAEDKVPYEKKASRLKEKYEKDITAYRNKGKVPVSMPAKAAAPAK
DDDDDDDDDDDDEDDDDDDDEDDE

Modification type:  
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-DNA binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (pH: 2; )

  2. Nuclear magnetic resonance (NMR)

References:
  1. Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH. "Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis." Eur J Biochem. 1981; 119(3): 545-51. PubMed: 6273163

Comments:
 



References

  1. Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH. "Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis." Eur J Biochem. 1981; 119(3): 545-51. PubMed: 6273163

  2. Pentecost BT, Wright JM, Dixon GH. "Isolation and sequence of cDNA clones coding for a member of the family of high mobility group proteins (HMG-T) in trout and analysis of HMG-T-mRNA's in trout tissues." Nucleic Acids Res. 1985; 13(13): 4871-4888. PubMed: 4022777

  3. Stros M, Nishikawa S, Dixon GH. "cDNA sequence and structure of a gene encoding trout testis high-mobility-group-1 protein." Eur J Biochem. 1994; 225(2): 581-91. PubMed: 7957172

  4. Watson DC, Dixon GH. "Amino acid sequence homologies between the high-mobility-group proteins, HMG-T from trout testis and HMG-1 and -2 from calf thymus: is the poly-aspartic-glutamic acid polypeptide within the main chain?" Biosci Rep. 1981; 1(2): 167-175. PubMed: 6117336

  5. Watson DC, Peters EH, Dixon GH. "The purification, characterization and partial sequence determination of a trout testis non-histone protein, HMG-T." Eur J Biochem. 1977; 74(1): 53-60. PubMed: 852459


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