Literature search services are currently unavailable. During our hosting provider's UPS upgrade we experienced a hardware failure and are currently working to resolve the issue.

Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Identification of a novel SNF2/SWI2 protein family member, SRCAP, which interacts with CREB-binding protein.

The ability of cAMP response-element binding protein (CREB)-binding protein (CBP) to function as a co-activator for a number of transcription factors appears to be mediated by its ability to act as a histone acetyltransferase and through its interaction with a number of other proteins (general transcription factors, histone acetyltransferases, and other co-activators). Here we report that CBP also interacts with a novel ATPase termed Snf2-Related CBP Activator Protein (SRCAP). Consistent with this activity, SRCAP contains the conserved ATPase domain found within members of the Snf2 family. Transfection experiments demonstrate that SRCAP is able to activate transcription when expressed as a Gal-SRCAP chimera and that SRCAP also enhances the ability of CBP to activate transcription. The adenoviral protein E1A was found to disrupt interaction between SRCAP and CBP possibly representing a mechanism for E1A-mediated transcriptional repression.

Pubmed ID: 10347196


  • Johnston H
  • Kneer J
  • Chackalaparampil I
  • Yaciuk P
  • Chrivia J


The Journal of biological chemistry

Publication Data

June 4, 1999

Associated Grants


Mesh Terms

  • Adenosine Triphosphatases
  • Adenovirus E1A Proteins
  • Amino Acid Sequence
  • CREB-Binding Protein
  • Gene Library
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins
  • Trans-Activators
  • Transcriptional Activation