DP00356: Cbp/p300-interacting transactivator 2 [Isoform 1]FASTA viewXML view

General information
DisProt:DP00356
Name:Cbp/p300-interacting transactivator 2 [Isoform 1]
Synonym(s):CITE2_HUMAN
MSG-related protein 1
MRG-1
P35srj
First appeared in release:Release 3.0 (02/17/2006)
UniProt:Q99967-1
UniGene:Hs.82071
SwissProt: CITE2_HUMAN
TrEMBL:  
NCBI (GI): 21542403
Source organism:Homo sapiens (Human)
Sequence length:270
Percent disordered:19%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MADHMMAMNH GRFPDGTNGL HHHPAHRMGM GQFPSPHHHQ QQQPQHAFNA LMGEHIHYGA - 60
GNMNATSGIR HAMGPGTVNG GHPPSALAPA ARFNNSQFMG PPVASQGGSL PASMQLQKLN - 120
NQYFNHHPYP HNHYMPDLHP AAGHQMNGTN QHFRDCNPKH SGGSSTPGGS GGSSTPGGSG - 180
SSSGGGAGSS NSGGGSGSGN MPASVAHVPA AMLPPNVIDT DFIDEEVLMS LVIEMGLDRI - 240
KELPELWLGQ NEFDFMTDFV CKQQPSRVSC



Functional narrative    

Cbp/p300-interacting transactivator 2 is a ubiquitously expressed nuclear protein that competes with HIF-1 alpha for binding to the CBP/p300 TAZ1 domain. Expression is directly induced by HIF-1, implicating the protein as a negative feedback regulator of HIF-1 alpha and a fundamental component of the cellular mechanism for attenuation of the hypoxic response. The activation domain is unstructured when free and folds upon binding, forming a helix (termed alpha A) and an extended structure that wraps around TAZ1.

Region 1: 220-270

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:Activation domain
Location:220 - 270
Length:51
Region sequence:

TDFIDEEVLMSLVIEMGLDRIKELPELWLGQNEFDFMTDFVCKQQPSRVSC

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

  2. Nuclear magnetic resonance (NMR)

References:
  1. De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. "Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites." J Biol Chem. 2004; 279(4): 3042-9. PubMed: 14594809

Comments:
 



References

  1. De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. "Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites." J Biol Chem. 2004; 279(4): 3042-9. PubMed: 14594809


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