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Conserved domains on  [gi|187956739|gb|AAI38472|]
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CAMP responsive element binding protein 3-like 2 [Mus musculus]

Protein Classification

bZIP transcription factor( domain architecture ID 10200203)

basic leucine zipper (bZIP) transcription factor similar to Homo sapiens cyclic AMP-responsive element-binding protein 3 (CREB3), an endoplasmic reticulum (ER)-bound transcription factor that plays a role in the unfolded protein response (UPR)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bZIP_CREB3 cd14689
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) ...
305-348 8.02e-19

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of CREB3 (also called LZIP or Luman), and the CREB3-like proteins CREB3L1 (or OASIS), CREB3L2, CREB3L3 (or CREBH), and CREB3L4 (or AIbZIP). They are type II membrane-associated members of the Basic leucine zipper (bZIP) family of transcription factors, with their N-termini facing the cytoplasm and their C-termini penetrating through the ER membrane. They contain an N-terminal transcriptional activation domain followed bZIP and transmembrane domains, and a C-terminal tail. They play important roles in ER stress and the unfolded protein response (UPR), as well as in many other biological processes such as cell secretion, bone and cartilage formation, and carcinogenesis. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


:

Pssm-ID: 269837 [Multi-domain]  Cd Length: 61  Bit Score: 80.27  E-value: 8.02e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 187956739 305 KISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd14689   11 KISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNR 54
 
Name Accession Description Interval E-value
bZIP_CREB3 cd14689
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) ...
305-348 8.02e-19

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of CREB3 (also called LZIP or Luman), and the CREB3-like proteins CREB3L1 (or OASIS), CREB3L2, CREB3L3 (or CREBH), and CREB3L4 (or AIbZIP). They are type II membrane-associated members of the Basic leucine zipper (bZIP) family of transcription factors, with their N-termini facing the cytoplasm and their C-termini penetrating through the ER membrane. They contain an N-terminal transcriptional activation domain followed bZIP and transmembrane domains, and a C-terminal tail. They play important roles in ER stress and the unfolded protein response (UPR), as well as in many other biological processes such as cell secretion, bone and cartilage formation, and carcinogenesis. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269837 [Multi-domain]  Cd Length: 61  Bit Score: 80.27  E-value: 8.02e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 187956739 305 KISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd14689   11 KISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNR 54
BRLZ smart00338
basic region leucin zipper;
305-348 8.44e-07

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 46.40  E-value: 8.44e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 187956739   305 KISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:smart00338  14 REAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELE 57
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
307-347 4.79e-06

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.


Pssm-ID: 395118 [Multi-domain]  Cd Length: 60  Bit Score: 43.91  E-value: 4.79e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 187956739  307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTN 347
Cdd:pfam00170  12 AARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEV 52
 
Name Accession Description Interval E-value
bZIP_CREB3 cd14689
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) ...
305-348 8.02e-19

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of CREB3 (also called LZIP or Luman), and the CREB3-like proteins CREB3L1 (or OASIS), CREB3L2, CREB3L3 (or CREBH), and CREB3L4 (or AIbZIP). They are type II membrane-associated members of the Basic leucine zipper (bZIP) family of transcription factors, with their N-termini facing the cytoplasm and their C-termini penetrating through the ER membrane. They contain an N-terminal transcriptional activation domain followed bZIP and transmembrane domains, and a C-terminal tail. They play important roles in ER stress and the unfolded protein response (UPR), as well as in many other biological processes such as cell secretion, bone and cartilage formation, and carcinogenesis. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269837 [Multi-domain]  Cd Length: 61  Bit Score: 80.27  E-value: 8.02e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 187956739 305 KISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd14689   11 KISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNR 54
bZIP_HY5-like cd14704
Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription ...
307-347 5.14e-10

Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription factors and similar proteins: a DNA-binding and dimerization domain; This subfamily is predominantly composed of plant Basic leucine zipper (bZIP) transcription factors with similarity to Solanum lycopersicum and Arabidopsis thaliana HY5. Also included are the Dictyostelium discoideum bZIP transcription factors E and F. HY5 plays an important role in seedling development and is a positive regulator of photomorphogenesis. Plants with decreased levels of HY5 show defects in light responses including inhibited photomorphogenesis, loss of alkaloid organization, and reduced carotenoid accumulation. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269852 [Multi-domain]  Cd Length: 52  Bit Score: 54.89  E-value: 5.14e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTN 347
Cdd:cd14704   11 SAQLSRQRKKEYLSELEAKCRELEAENAELEARVELLQAEN 51
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
307-348 9.60e-09

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 51.39  E-value: 9.60e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd14686   11 AARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52
bZIP_CREBZF cd14706
Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar ...
308-341 1.01e-07

Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar proteins: a DNA-binding and dimerization domain; CREBZF (also called Zhangfei, ZF, LAZip, or SMILE) is a neuronal bZIP transcription factor that is involved in the infection cycle of herpes simplex virus (HSV) and related cellular processes. It suppresses the ability of the HSV transactivator VP16 to initiate the viral replicative cycle. CREBZF has also been implicated in the regulation of the human nerve growth factor receptor trkA and the tumor suppressor p53. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269854 [Multi-domain]  Cd Length: 54  Bit Score: 48.40  E-value: 1.01e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 187956739 308 AQESRRKKKEYMDSLEKKVESCSTENLELRKKVE 341
Cdd:cd14706   12 ARENRLKKKEYVENLEKSVDKLKSENKELKKANK 45
bZIP_ATF6 cd14700
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar ...
307-343 5.21e-07

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar proteins: a DNA-binding and dimerization domain; ATF-6 is a type I membrane-bound Basic leucine zipper (bZIP) transcription factor that binds to the consensus ER stress response element (ERSE) and enhances the transcription of genes encoding glucose-regulated proteins Grp78, Grp94, and calreticulum. ATF-6 is one of three sensors of the unfolded protein response (UPR) in metazoans; the others being the kinases Ire1 and PERK. It contains an ER-lumenal domain that detects unfolded proteins. In response to ER stress, ATF-6 translocates from the ER to the Golgi with simultaneous cleavage in a process called regulated intramembrane proteolysis (Rip) to its transcriptionally competent form, which enters the nucleus and upregulates target UPR genes. The three UPR sensor branches cross-communicate to form a signaling network. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269848 [Multi-domain]  Cd Length: 52  Bit Score: 46.50  E-value: 5.21e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVL 343
Cdd:cd14700   11 SACLSRKKKKEYVQSLETKLEQLKQENQKLKSENETL 47
BRLZ smart00338
basic region leucin zipper;
305-348 8.44e-07

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 46.40  E-value: 8.44e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 187956739   305 KISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:smart00338  14 REAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELE 57
bZIP_GCN4 cd12193
Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and ...
307-348 2.43e-06

Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and dimerization domain; GCN4 was identified in Saccharomyces cerevisiae from mutations in a deficiency in activation with the general amino acid control pathway. GCN4 encodes a trans-activator of amino acid biosynthetic genes containing 2 acidic activation domains and a C-terminal bZIP domain. In amino acid-deprived cells, GCN4 is up-regulated leading to transcriptional activation of genes encoding amino acid biosynthetic enzymes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269833 [Multi-domain]  Cd Length: 54  Bit Score: 44.48  E-value: 2.43e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd12193   13 AARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLEAEAR 54
bZIP_CREB1 cd14690
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ...
307-343 3.36e-06

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) and similar proteins: a DNA-binding and dimerization domain; CREB1 is a Basic leucine zipper (bZIP) transcription factor that plays a role in propagating signals initiated by receptor activation through the induction of cAMP-responsive genes. Because it responds to many signal transduction pathways, CREB1 is implicated to function in many processes including learning, memory, circadian rhythm, immune response, and reproduction, among others. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269838 [Multi-domain]  Cd Length: 55  Bit Score: 44.16  E-value: 3.36e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVL 343
Cdd:cd14690   12 AARECRRKKKEYVKCLENRVAVLENENKELREELKIL 48
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
307-347 4.79e-06

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.


Pssm-ID: 395118 [Multi-domain]  Cd Length: 60  Bit Score: 43.91  E-value: 4.79e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 187956739  307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTN 347
Cdd:pfam00170  12 AARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEV 52
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
308-345 5.46e-06

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269835 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 5.46e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 187956739 308 AQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLEN 345
Cdd:cd14687   13 ASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLRE 50
bZIP_2 pfam07716
Basic region leucine zipper;
307-345 7.02e-06

Basic region leucine zipper;


Pssm-ID: 462244 [Multi-domain]  Cd Length: 51  Bit Score: 43.36  E-value: 7.02e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 187956739  307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLEN 345
Cdd:pfam07716  12 AAKRSREKKKQKEEELEERVKELERENAQLRQKVEQLEK 50
bZIP_XBP1 cd14691
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ...
305-348 1.05e-05

Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a DNA-binding and dimerization domain; XBP1, a member of the Basic leucine zipper (bZIP) family, is the key transcription factor that orchestrates the unfolded protein response (UPR). It is the most conserved component of the UPR and is critical for cell fate determination in response to ER stress. The inositol-requiring enzyme 1 (IRE1)-XBP1 pathway is one of the three major sensors at the ER membrane that initiates the UPR upon activation. IRE1, a type I transmembrane protein kinase and endoribonuclease, oligomerizes upon ER stress leading to its increased activity. It splices the XBP1 mRNA, producing a variant that translocates to the nucleus and activates its target genes, which are involved in protein folding, degradation, and trafficking. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269839 [Multi-domain]  Cd Length: 58  Bit Score: 42.97  E-value: 1.05e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 187956739 305 KISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd14691   12 RVAAQTARDRKKARMDELEERVRELEEENQKLRAENESLRARNE 55
bZIP_plant_RF2 cd14703
Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and ...
305-348 2.50e-05

Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors with similarity to Oryza sativa RF2a and RF2b, which are important for plant development. They interact with, as homodimers or heterodimers with each other, and activate transcription from the RTBV (rice tungro bacilliform virus) promoter, which is regulated by sequence-specific DNA-binding proteins that bind to the essential cis element BoxII. RF2a and RF2b show differences in binding affinities to BoxII, expression patterns in different rice organs, and subcellular localization. Transgenic rice with increased RF2a and RF2b display increased resistance to rice tungro disease (RTD) with no impact on plant development. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269851 [Multi-domain]  Cd Length: 52  Bit Score: 41.79  E-value: 2.50e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 187956739 305 KISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd14703    9 RQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLEQEKA 52
bZIP_u2 cd14811
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
307-338 3.56e-05

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269873 [Multi-domain]  Cd Length: 52  Bit Score: 41.44  E-value: 3.56e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELRK 338
Cdd:cd14811   11 SARNSRKRKKIYLELLENKVKELQQELEKLKR 42
bZIP_plant_GBF1 cd14702
Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription ...
307-344 3.78e-05

Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors including Arabidopsis thaliana G-box binding factor 1 (GBF1), Zea mays Opaque-2 and Ocs element-binding factor 1 (OCSBF-1), Triticum aestivum Histone-specific transcription factor HBP1 (or HBP-1a), Petroselinum crispum Light-inducible protein CPRF3 and CPRF6, and Nicotiana tabacum BZI-3, among many others. bZIP G-box binding factors (GBFs) contain an N-terminal proline-rich domain in addition to the bZIP domain. GBFs are involved in developmental and physiological processes in response to stimuli such as light or hormones. Opaque-2 plays a role in affecting lysine content and carbohydrate metabolism, acting indirectly on starch/amino acid ratio. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269850 [Multi-domain]  Cd Length: 52  Bit Score: 41.37  E-value: 3.78e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLE 344
Cdd:cd14702   11 SARRSRMRKQAHLEELEAQVEQLRAENSTLRAELNALS 48
bZIP_CREBL2 cd14709
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 ...
307-343 7.74e-05

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 (CREBL2): a DNA-binding and dimerization domain; CREBL2 is a bZIP transcription factor that interacts with CREB and plays a critical role in adipogenesis and lipogenesis. Its overexpression upregulates the expression of PPARgamma and CEBPalpha to promote adipogenesis as well as accelerate lipogenesis by increasing GLUT1 and GLUT4. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269857 [Multi-domain]  Cd Length: 56  Bit Score: 40.39  E-value: 7.74e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVL 343
Cdd:cd14709   12 SARESRDRKKLRYQYLEQLVADREREILLLREELEMY 48
bZIP_AUREO-like cd14809
Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar ...
308-342 1.43e-04

Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar bZIP domains; AUREO is a BL-activated transcription factor specific to phototrophic stramenopiles. It has a bZIP and a BL-sensing light-oxygen voltage (LOV) domain. It has been shown to mediate BL-induced branching and regulate the development of the sex organ in Vaucheria frigida. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. This subgroup also includes the Epstein-Barr virus (EBV) immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). ZEBRA exhibits a variant of the bZIP fold, it has a unique dimer interface and a substantial hydrophobic pocket; it has a C-terminal moiety which stabilizes the coiled coil involved in dimer formation. ZEBRA functions to trigger the switch of EBV's biphasic infection cycle from latent to lytic infection. It activates the promoters of EBV lytic genes by binding ZEBRA response elements (ZREs) and inducing a cascade of expression of over 50 viral genes. It also down regulates latency-associated promoters, is an essential replication factor, induces host cell cycle arrest, and alters cellular immune responses and transcription factor activity.


Pssm-ID: 269871 [Multi-domain]  Cd Length: 52  Bit Score: 39.54  E-value: 1.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 187956739 308 AQESRRKKKEYMDSLEKKVESCSTENLELRKKVEV 342
Cdd:cd14809   12 ARKTRLRKKAYLESLKEQVAALQAENQRLRQQIRQ 46
bZIP_u1 cd14810
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
305-347 3.81e-04

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269872  Cd Length: 52  Bit Score: 38.40  E-value: 3.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 187956739 305 KISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTN 347
Cdd:cd14810    9 KISARNFRARRKEYITQLEEQVADRDAEIEQLRAELRALRNEN 51
bZIP_u3 cd14812
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
307-337 1.59e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269874 [Multi-domain]  Cd Length: 52  Bit Score: 36.81  E-value: 1.59e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 187956739 307 SAQESRRKKKEYMDSLEKKVESCSTENLELR 337
Cdd:cd14812   11 AAQLSRQRKKEEVEELEARVKELEAENRRLR 41
bZIP_YAP cd14688
Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a ...
312-348 3.94e-03

Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed predominantly of AP-1-like transcription factors including Saccharomyces cerevisiae YAPs, Schizosaccharomyces pombe PAP1, and similar proteins. Members of this subfamily belong to the Basic leucine zipper (bZIP) family of transcription factors. The YAP subfamily is composed of eight members (YAP1-8) which may all be involved in stress responses. YAP1 is the major oxidative stress regulator and is also involved in iron metabolism (like YAP5) and detoxification of arsenic (like YAP8). YAP2 is involved in cadmium stress responses while YAP4 and YAP6 play roles in osmotic stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269836 [Multi-domain]  Cd Length: 63  Bit Score: 35.77  E-value: 3.94e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 187956739 312 RRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd14688   18 RERKKERIKELEQRVAELEEELAELEEELQELRAELR 54
bZIP_Zip1 cd14705
Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding ...
312-348 7.29e-03

Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of fungal bZIP transcription factors including Schizosaccharomyces pombe Zip1, Saccharomyces cerevisiae Methionine-requiring protein 28 (Met28p), and Neurospora crassa cys-3, among others. Zip1 is required for the production of key proteins involved in sulfur metabolism and also plays a role in cadmium response. Met28p acts as a cofactor of Met4p, a transcriptional activator of the sulfur metabolic network; it stabilizes DNA:Met4 complexes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269853 [Multi-domain]  Cd Length: 55  Bit Score: 34.81  E-value: 7.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 187956739 312 RRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNR 348
Cdd:cd14705   16 RAKKKQREQELEEKLKELEERIKELERRLDELESENK 52
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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