Annotation for this protein is in progress - please check future releases for more complete information


DP00224: Transcription factor 4FASTA viewXML view

General information
DisProt:DP00224
Name:Transcription factor 4
Synonym(s):ITF2_HUMAN
Immunoglobulin transcription factor 2
ITF-2
SL3-3 enhancer factor 2
SEF-2
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P15884
UniGene:Hs.605153
SwissProt: ITF2_HUMAN
TrEMBL:  
NCBI (GI): 3915747
Source organism:Homo sapiens (Human)
Sequence length:667
Percent disordered:19%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MHHQQRMAAL GTDKELSDLL DFSAMFSPPV SSGKNGPTSL ASGHFTGSNV EDRSSSGSWG - 60
NGGHPSPSRN YGDGTPYDHM TSRDLGSHDN LSPPFVNSRI QSKTERGSYS SYGRESNLQG - 120
CHQQSLLGGD MDMGNPGTLS PTKPGSQYYQ YSSNNPRRRP LHSSAMEVQT KKVRKVPPGL - 180
PSSVYAPSAS TADYNRDSPG YPSSKPATST FPSSFFMQDG HHSSDPWSSS SGMNQPGYAG - 240
MLGNSSHIPQ SSSYCSLHPH ERLSYPSHSS ADINSSLPPM STFHRSGTNH YSTSSCTPPA - 300
NGTDSIMANR GSGAAGSSQT GDALGKALAS IYSPDHTNNS FSSNPSTPVG SPPSLSAGTA - 360
VWSRNGGQAS SSPNYEGPLH SLQSRIEDRL ERLDDAIHVL RNHAVGPSTA MPGGHGDMHG - 420
IIGPSHNGAM GGLGSGYGTG LLSANRHSLM VGTHREDGVA LRGSHSLLPN QVPVPQLPVQ - 480
SATSPDLNPP QDPYRGMPPG LQGQSVSSGS SEIKSDDEGD ENLQDTKSSE DKKLDDDKKD - 540
IKSITSNNDD EDLTPEQKAE REKERRMANN ARERLRVRDI NEAFKELGRM VQLHLKSDKP - 600
QTKLLILHQA VAVILSLEQQ VRERNLNPKA ACLKRREEEK VSSEPPPLSL AGPHPGMGDA - 660
SNHMGQM

Region 1: 1-53 Region 2: 1-56 Region 3: 1-130

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:1 - 53
Length:53
Region sequence:

MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDR

Modification type: Fragment
Native
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, far-UV

  2. Fluorescence, intrinsic (pH: 7.4; DTT 2 mM; sodium chloride 100 mM; sodium phosphate (buffer) 50 mM)
References:
  1. Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. "Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin." J Mol Biol. 2001; 306(5): 1179-1189. PubMed: 11237626
Comments:
 



Region 2
Type:Disordered
Name: 
Location:1 - 56
Length:56
Region sequence:

MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSS

Modification type: Fragment
Native
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, far-UV

  2. Fluorescence, intrinsic (pH: 7.4; DTT 2 mM; sodium chloride 100 mM; sodium phosphate (buffer) 50 mM)
References:
  1. Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. "Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin." J Mol Biol. 2001; 306(5): 1179-1189. PubMed: 11237626
Comments:
 



Region 3
Type:Disordered
Name: 
Location:1 - 130
Length:130
Region sequence:

MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWG
NGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQG
CHQQSLLGGD

Modification type: Fragment
Native
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, far-UV

  2. Fluorescence, intrinsic (pH: 7.4; DTT 2 mM; sodium chloride 100 mM; sodium phosphate (buffer) 50 mM)
References:
  1. Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. "Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin." J Mol Biol. 2001; 306(5): 1179-1189. PubMed: 11237626
Comments:
 



References

  1. Corneliussen B, Thornell A, Hallberg B, Grundström T. "Helix-loop-helix transcriptional activators bind to a sequence in glucocorticoid response elements of retrovirus enhancers." J Virol. 1991; 65(11): 6084-93. PubMed: 1681116



Comments


Three constructs of TCF4 were used in the Knapp paper. They extended from residues 1-53, 1-56, and 1-130. Each was found to be disordered in solution.


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