DP00087: Tegument protein VP16FASTA viewXML view

General information
DisProt:DP00087
Name:Tegument protein VP16
Synonym(s):VP16_HHV2H
Alpha trans-inducing protein
Alpha-TIF
Vmw65
ICP25
Transcriptional activator VP16
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P68336
UniGene: 
SwissProt: VP16_HHV2H
TrEMBL:  
NCBI (GI): 55584017
Source organism:Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Sequence length:490
Percent disordered:27%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MDLLVDDLFA DADGVSPPPP RPAGGPKNTP AAPPLYATGR LSQAQLMPSP PMPVPPAALF - 60
NRLLDDLGFS AGPALCTMLD TWNEDLFSGF PTNADMYREC KFLSTLPSDV IDWGDAHVPE - 120
RSPIDIRAHG DVAFPTLPAT RDELPSYYEA MAQFFRGELR AREESYRTVL ANFCSALYRY - 180
LRASVRQLHR QAHMRGRNRD LREMLRTTIA DRYYRETARL ARVLFLHLYL FLSREILWAA - 240
YAEQMMRPDL FDGLCCDLES WRQLACLFQP LMFINGSLTV RGVPVEARRL RELNHIREHL - 300
NLPLVRSAAA EEPGAPLTTP PVLQGNQARS SGYFMLLIRA KLDSYSSVAT SEGESVMREH - 360
AYSRGRTRNN YGSTIEGLLD LPDDDDAPAE AGLVAPRMSF LSAGQRPRRL STTAPITDVS - 420
LGDELRLDGE EVDMTPADAL DDFDLEMLGD VESPSPGMTH DPVSYGALDV DDFEFEQMFT - 480
DAMGIDDFGG

Region 1: 350-394 Region 2: 403-490

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: 
Location:350 - 394
Length:45
Region sequence:

TSEGESVMREHAYSRGRTRNNYGSTIEGLLDLPDDDDAPAEAGLV

Modification type: Native
PDB: 16VP:A
Structural/functional type:  
Functional classes:  
Functional subclasses: Protein-DNA binding
Protein-protein binding
Detection methods:
  1. X-ray crystallography (289 K; pH: 4; polyethylene glycol 8000 (w/v) 20 %; potassium phosphate 50 mM)

  2. Sensitivity to proteolysis
References:
  1. Liu Y, Gong W, Huang CC, Herr W, Cheng X. "Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16." Genes Dev. 1999; 13(13): 1692-703. PubMed: 10398682
Comments:
 



Region 2
Type:Disordered
Name:C terminal
Location:403 - 490
Length:88
Region sequence:

AGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDP
VSYGALDVDDFEFEQMFTDAMGIDDFGG

Modification type: Native
PDB: 16VP:A
Structural/functional type:  
Functional classes:  
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (289 K; pH: 4; polyethylene glycol 8000 (w/v) 20 %; potassium phosphate 50 mM)

  2. Sensitivity to proteolysis
References:
  1. Liu Y, Gong W, Huang CC, Herr W, Cheng X. "Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16." Genes Dev. 1999; 13(13): 1692-703. PubMed: 10398682
Comments:
 



References

  1. Donaldson L, Capone JP. "Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type 1." J Biol Chem. 1992; 267(3): 1411-4. PubMed: 1309782

  2. Hayes S, O'Hare P. "Mapping of a major surface-exposed site in herpes simplex virus protein Vmw65 to a region of direct interaction in a transcription complex assembly." J Virol. 1993; 67(2): 852-62. PubMed: 8380468

  3. O'Hare P, Williams G. "Structural studies of the acidic transactivation domain of the Vmw65 protein of herpes simplex virus using 1H NMR." Biochemistry. 1992; 31(16): 4150-6. PubMed: 1314658

  4. Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. "Critical amino acids in the transcriptional activation domain of the herpesvirus protein VP16 are solvent-exposed in highly mobile protein segments. An intrinsic fluorescence study." J Biol Chem. 1996; 271(9): 4819-26. PubMed: 8617751

  5. Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. "Induced alpha helix in the VP16 activation domain upon binding to a human TAF." Science. 1997; 277(5330): 1310-3. PubMed: 9271577


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