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InterPro: IPR011616 bZIP transcription factor, bZIP-1

Protein matches Help

UniProtKB

Matches:

2579 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR011616 bZIP_1

Secondary

IPR001871 , IPR004827

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00170	bZIP_1	2579
Signatures in BioMart

InterPro Relationships Help

Parent

IPR004827 Basic-leucine zipper (bZIP) transcription factor

Found in

IPR000837 Fos transforming protein
IPR001630 cAMP response element binding (CREB) protein
IPR002112 Transcription factor Jun
IPR015558 c-Jun Transcription Factor
IPR016378 Transcription factor, cyclic AMP-dependent
IPR017339 Trans-activator protein BZLF1, human herpesvirus 4

GO Term annotation Help

Process

GO:0006355 regulation of transcription, DNA-dependent

Function

GO:0003700 transcription factor activity
GO:0043565 sequence-specific DNA binding
GO:0046983 protein dimerization activity

InterPro annotation

Entry Details in BioMart

Abstract

The basic-leucine zipper (bZIP) transcription factors [1, 2] of eukaryotic are proteins that contain a basic region mediating sequence-specific DNA-binding followed by a leucine zipper region (see IPR002158) required for dimerization.

Structural links Help

PDB - click here

SCOP: h.1.26.1 , h.1.3.1 , h.1.5.1 , h.3.2.1 , k.1.1.1 , k.31.1.1 , k.6.1.1

CATH: 1.10.287.210 , 1.20.5.170

Database links Help

PANDIT: PF00170

Blocks: IPB011616

Pfam Clan: CL0018.11

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011616

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A8MPH9 Transcription factor kayak, isoforms D/sro

O14867 Transcription regulator protein BACH1

O24646 Transcription factor HY5

P03069 General control protein GCN4

P97302 Transcription regulator protein BACH1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013089	Kelch related
IPR013069	BTB/POZ
IPR011333	BTB/POZ fold
IPR000837	Fos transforming protein
IPR000210	BTB/POZ-like
IPR004827	Basic-leucine zipper (bZIP) transcription factor
IPR008917	Eukaryotic transcription factor, Skn-1-like, DNA-binding
IPR001630	cAMP response element binding (CREB) protein
IPR011616	bZIP transcription factor, bZIP-1
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Hurst HC. Transcription factors 1: bZIP proteins. 2 101-68 1995 [PubMed: 7780801]
2.	Ellenberger T. Getting a grip in DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains. Curr. Opin. Struct. Biol. 4 12-21 1994

Additional Reading Open in usermanual
	Deng Y, Liu J, Zheng Q, Li Q, Kallenbach NR, Lu M. A heterospecific leucine zipper tetramer. Chem. Biol. 15 2008 908-19 [PubMed: 18804028] http://dx.doi.org/10.1016/j.chembiol.2008.07.008
	Deng Y, Liu J, Zheng Q, Eliezer D, Kallenbach NR, Lu M. Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat. Structure 14 2006 247-55 [PubMed: 16472744] http://dx.doi.org/10.1016/j.str.2005.10.010
	Brown JH, Yang Y, Reshetnikova L, Gourinath S, Suveges D, Kardos J, Hobor F, Reutzel R, Nyitray L, Cohen C. An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins. J. Mol. Biol. 375 2008 1434-43 [PubMed: 18155233] http://dx.doi.org/10.1016/j.jmb.2007.11.071
	Shen H, Cao K, Wang X. AtbZIP16 and AtbZIP68, two new members of GBFs, can interact with other G group bZIPs in Arabidopsis thaliana. 41 2008 132-8 [PubMed: 18315949]
	Blankenfeldt W, Thoma NH, Wray JS, Gautel M, Schlichting I. Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment. Proc. Natl. Acad. Sci. U.S.A. 103 2006 17713-7 [PubMed: 17095604] http://dx.doi.org/10.1073/pnas.0606741103
	Yadav MK, Leman LJ, Price DJ, Brooks CL 3rd, Stout CD, Ghadiri MR. Coiled coils at the edge of configurational heterogeneity. Structural analyses of parallel and antiparallel homotetrameric coiled coils reveal configurational sensitivity to a single solvent-exposed amino acid substitution. Biochemistry 45 2006 4463-73 [PubMed: 16584182] http://dx.doi.org/10.1021/bi060092q

InterPro 23.1