Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper class of transcription factors, see pfam00010. Myc forms a heterodimer with Max, and this complex regulates cell growth through direct activation of genes involved in cell replication. Mutations in the C-terminal 20 residues of this domain cause unique changes in the induction of apoptosis, transformation, and G2 arrest.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174247702   9 IDVVTLAEANE-SESSTESSTETSEEHCKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKRLKLDS-GRVLKQISNN 86
Cdd:pfam01056 254 IDVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNN 333

                  ....*.
gi 1174247702  87 RKCLSP 92
Cdd:pfam01056 334 RKCSSP 339

Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper class of transcription factors, see pfam00010. Myc forms a heterodimer with Max, and this complex regulates cell growth through direct activation of genes involved in cell replication. Mutations in the C-terminal 20 residues of this domain cause unique changes in the induction of apoptosis, transformation, and G2 arrest.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174247702   9 IDVVTLAEANE-SESSTESSTETSEEHCKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKRLKLDS-GRVLKQISNN 86
Cdd:pfam01056 254 IDVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNN 333

                  ....*.
gi 1174247702  87 RKCLSP 92
Cdd:pfam01056 334 RKCSSP 339

Helix-loop-helix DNA-binding domain;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1174247702 102 KRRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSIQ 154
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53

Myc amino-terminal region; The myc family belongs to the basic helix-loop-helix leucine zipper class of transcription factors, see pfam00010. Myc forms a heterodimer with Max, and this complex regulates cell growth through direct activation of genes involved in cell replication. Mutations in the C-terminal 20 residues of this domain cause unique changes in the induction of apoptosis, transformation, and G2 arrest.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174247702   9 IDVVTLAEANE-SESSTESSTETSEEHCKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKRLKLDS-GRVLKQISNN 86
Cdd:pfam01056 254 IDVVTVEKRQPsSKRKEVSTLTTALGHSRPQHSPLVLKRCHVIIHQHNYAAPPSTRSEDPPQKRLKLESsGRVLKQISNN 333

                  ....*.
gi 1174247702  87 RKCLSP 92
Cdd:pfam01056 334 RKCSSP 339

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in N-Myc and similar proteins; N-Myc, also termed Class E basic helix-loop-helix protein 37 (bHLHe37), is a bHLHZip proto-oncogene protein that positively regulates the transcription of MYCNOS in neuroblastoma cells. It is also essential during embryonic development. N-Myc has a critical role in regulating the switch between proliferation and differentiation of progenitor cells. It binds DNA as a heterodimer with MAX. The family also includes S-Myc, encoded by rat or mouse intronless myc gene, which has apoptosis-inducing activity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174247702  98 EENDKRRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHK 177
Cdd:cd11456     1 EDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEQKLLLEKEKLQARQQQLLKK 80

                  ....*
gi 1174247702 178 LEQLR 182
Cdd:cd11456    81 IEQAR 85

helix loop helix domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1174247702  107 NVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSIQSDEH 158
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQEELQ 52

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, also termed Class D basic helix-loop-helix protein 4 (bHLHd4), or Myc-associated factor X, is a bHLHZip transcription regulator that forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a transcriptional repressor. Max homodimer bind DNA but is transcriptionally inactive. Targeted deletion of max results in early embryonic lethality in mice.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1174247702 102 KRRTHNVLERQRRNELKLSFFALRDEIPEVAnNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRR 169
Cdd:cd11406     1 KRAHHNALERKRRDHIKDSFHSLRDSVPSLQ-GEKASRAQILKKATEYIQYMRRKNHTHQQDIDDLKR 67

Myc leucine zipper domain; This family consists of the leucine zipper dimerization domain found in both cellular c-Myc proto-oncogenes and viral v-Myc oncogenes. dimerization via the leucine zipper motif with other basic helix-loop-helix-leucine zipper (b/HLH/lz) proteins such as Max is required for efficient DNA binding. The Myc-Max dimer is a transactivating complex activating expression of growth related genes promoting cell proliferation. The dimerization is facilitated via interdigitating leucine residues every 7th position of the alpha helix. Like charge repulsion of adjacent residues in this region perturbs the formation of homodimers with heterodimers being promoted by opposing charge attractions.

                          10        20
                  ....*....|....*....|....*..
gi 1174247702 155 SDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:pfam02344   1 ADEQRLISEKDQLRKRREQLKHRLEQL 27

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar proteins; Mnt, also termed Class D basic helix-loop-helix protein 3 (bHLHd3), or Myc antagonist MNT, or protein ROX, is a bHLHZip transcriptional repressor that binds DNA as a heterodimer with MAX. It binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'. Mnt has an important role as an antagonist and regulator of Myc activities and it is a potential tumor suppressor. Mnt is ubiquitously expressed. Mnt-deficient mice shown to exhibit early postnatal lethality.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174247702 103 RRTHNVLERQRRNELKLSFFALRDEIPEvANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKL 178
Cdd:cd11402     3 REVHNKLEKNRRAHLKECFETLKRQIPN-LDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREKIALQQRL 77

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) family; The MGA family includes MGA, Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins. MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites. spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174247702 103 RRTHNVLERQRRNELKLSFFALRDEIPEvANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLR 168
Cdd:cd19682     1 RLRHKKRERERRSELRELFDKLKQLLGL-DSDEKASKLAVLTEAIEEIQQLKREEDELQKEKARLT 65

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) and similar proteins; Mad1, also termed Max dimerization protein 1 (MXD1), or Max dimerizer 1, or protein MAD, is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174247702 103 RRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd18931     2 RSTHNEMEKNRRAHLRLCLEKLKMLVPLGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRHLKRQLEKL 80

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family and similar proteins; The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box. The family also includes Saccharomyces cerevisiae transcription factor HMS1 (also termed high-copy MEP suppressor protein 1) and serine-rich protein TYE7. HMS1 is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation. TYE7, also termed basic-helix-loop-helix protein SGC1, is a putative bHLHzip transcription activator required for Ty1-mediated glycolytic gene expression. TYE7 N-terminal is extremely rich in serine residues. It binds DNA on E-box motifs, 5'-CANNTG-3'. TYE7 is not essential for growth.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174247702 102 KRRTHNVLERQRRNELKLSFFALRDEIP---------------EVANNEKAPKVVILKKATEYVLSIQSdehrliaEKEQ 166
Cdd:cd11395     3 KRLPHNAIEKRYRSNLNTKIERLRDAIPslrspegksddgglgGLAPTTKLSKATILTKAIEYIRHLEQ-------ENER 75

                          90
                  ....*....|..
gi 1174247702 167 LRRRREQLKHKL 178
Cdd:cd11395    76 LEEENEELRQQV 87

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), MLX-interacting protein-like (MLXIPL) and similar proteins; The family includes MLXIP and MLXIPL. MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm. MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1174247702 102 KRRTHNVLERQRRNELKLSFFALRDEIPEVAN--NEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRR 170
Cdd:cd11405     3 RRLSHISAEQKRRFNIKSGFDTLQSLIPSLGQnpNQKVSKAAMLQKAAEYIKSLKRERQQMQEEAEQLRQE 73

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and similar proteins; MXI1, also termed Max interactor 1, or Class C basic helix-loop-helix protein 11 (bHLHc11), is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX. It plays an important role in the regulation of cell proliferation.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174247702 103 RRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd18930     2 RSTHNELEKNRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQRFLKRRLEQL 80

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 2 (SREBP2) and similar proteins; SREBP2, also termed Class D basic helix-loop-helix protein 2 (bHLHd2), or sterol regulatory element-binding transcription factor 2 (SREBF2), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcription activator of cholesterol biosynthesis.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174247702  99 ENDKRRTHNVLERQRRNELKLSFFALRDEIpeVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLR 168
Cdd:cd18922     3 EGERRTTHNIIEKRYRSSINDKIIELKDLV--MGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMALK 70

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae centromere-binding protein 1 (CBP-1) and similar proteins; CBP-1, also termed centromere promoter factor 1 (CPF1), or centromere-binding factor 1 (CBF1), is a bHLHzip protein that is required for chromosome stability and methionine prototrophy. It binds as a homodimer to the centromere DNA elements I (CDEI, GTCACATG) region of the centromere that is required for optimal centromere function.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174247702 102 KRRTHNVLERQRRNELKLSFFALRDEIPevANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQL 181
Cdd:cd11398     7 RRDNHKEVERRRRENINEGINELAALVP--GNAREKNKGAILARAVEYIQELQETEAKNIEKWTLEKLLTDQAIAELAAL 84

                  .
gi 1174247702 182 R 182
Cdd:cd11398    85 N 85

basic helix-loop-helix (bHLH) domain found in protein atonal homolog 8 (ATOH8) and similar proteins; ATOH8, also termed Class A basic helix-loop-helix protein 21 (bHLHa21), or helix-loop-helix protein hATH-6 (hATH6), is a bHLH shear-stress-responsive transcription factor expressed in activated satellite cells and proliferating myoblasts of human skeletal muscle tissue. It regulates endothelial cell proliferation, migration and tube-like structures formation. ATOH8 binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1174247702 101 DKRRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSI 153
Cdd:cd11421     7 QRRIEANARERTRVHTISAAFEALRKAVPSYSYNQKLSKLAILRIACSYILAL 59

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein ABA-INDUCIBLE bHLH-TYPE (AIB) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as AIB and MYC proteins (MYC2, MYC3 and MYC4). AIB, also termed AtbHLH17, or EN 35, is a transcription activator that regulates positively abscisic acid (ABA) response. MYC2, also termed protein jasmonate insensitive 1, or R-homologous Arabidopsis protein 1 (RAP-1), or AtbHLH6, or EN 38, or Z-box binding factor 1 protein, is a transcriptional activator involved in abscisic acid (ABA), jasmonic acid (JA), and light signaling pathways. MYC3, also termed protein altered tryptophan regulation 2, or AtbHLH5, or transcription factor ATR2, or EN 36, is a transcription factor involved in tryptophan, jasmonic acid (JA) and other stress-responsive gene regulation. MYC4, also termed AtbHLH4, or EN 37, is a transcription factor involved in jasmonic acid (JA) gene regulation. MYC2, together with MYC3 and MYC4, controls additively subsets of JA-dependent responses.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174247702 110 ERQRRNELKLSFFALRDEIPEVANNEKAPkvvILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLK 175
Cdd:cd11449    13 ERQRREKLNQRFYALRAVVPNVSKMDKAS---LLGDAISYINELKSKVQDMETEKKEMKRQESEKK 75

basic helix-loop-helix (bHLH) domain found in achaete-scute-like protein 2 (ASCL-2) and similar proteins; ASCL-2, also termed achaete-scute homolog 2 (ASH-2), or Class A basic helix-loop-helix protein 45 (bHLHa45), or mammalian achaete scute homolog 2 (Mash2), is a bHLH transcription factor that is involved in Schwann cell differentiation and control of proliferation in adult peripheral nerves.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1174247702 107 NVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSIQS 155
Cdd:cd19743     8 NERERNRVKLVNLGFAALRQHVPQGGASKKMSKVETLRSAVEYIRALQR 56

basic helix-loop-helix (bHLH) domain found in Drosophila melanogaster achaete-scute complex (AS-C) proteins, achaete-scute-like proteins, ASCL1-2, and similar proteins; This subfamily includes Drosophila melanogaster AS-C proteins and two ASCL family of transcription factors, ASCL-1 and ASCL-2. Drosophila melanogaster AS-C proteins includes lethal of scute (also known as achaete-scute complex protein T3 or AST3), scute (also known as achaete-scute complex protein T4 or AST4), achaete (also known as achaete-scute complex protein T5 or AST5), and asense (also known as achaete-scute complex protein T8 or AST8). They are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system, as well as in sex determination and dosage compensation. ASCL-1, also termed Class A basic helix-loop-helix protein 46 (bHLHa46), or achaete-scute homolog 1 (ASH-1), or mammalian achaete scute homolog 1 (Mash1), is expressed in subsets of neural progenitors in both the central and peripheral nervous system. It plays a key role in neuronal differentiation and specification in the nervous system. ASCL-2, also termed achaete-scute homolog 2 (ASH-2), or Class A basic helix-loop-helix protein 45 (bHLHa45), or mammalian achaete scute homolog 2 (Mash2), is involved in Schwann cell differentiation and control of proliferation in adult peripheral nerves.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1174247702 107 NVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSIQ 154
Cdd:cd19723     6 NERERNRVKLVNLGFATLREHVPNGRANKKMSKVETLRSAVEYIRQLQ 53

basic helix-loop-helix (bHLH) domain found in muscle, intestine and stomach expression 1 (MIST-1) and similar proteins; MIST-1, also termed Class A basic helix-loop-helix protein 15 (bHLHa15), or Class B basic helix-loop-helix protein 8 (bHLHb8), is a bHLH transcription factor expressed in pancreatic acinar cells and other serous exocrine cells. It is essential for cytoskeletal organization and secretory activity. It also functions as a potent endoplasmic reticulum (ER) stress-inducible transcriptional regulator. MIST-1 is capable of binding to E-box (CANNTG) motifs as a homodimer or a heterodimer with E-proteins (E12 and E47) to regulate transcription.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1174247702 102 KRRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAPKVVILKKATEYVLSIQS 155
Cdd:cd19711     1 RRLESNERERQRMHKLNNAFQALREVIPHVRAEKKLSKIETLTLAKNYIKSLTT 54

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 1 (SREBP1) and similar proteins; SREBP1, also termed Class D basic helix-loop-helix protein 1 (bHLHd1), or sterol regulatory element-binding transcription factor 1 (SREBF1), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcriptional activator required for lipid homeostasis. It may control transcription of the low-density lipoprotein receptor gene as well as the fatty acid. SREBP1 has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3').

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1174247702 101 DKRRTHNVLERQRRNELKLSFFALRDEIpeVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLR 168
Cdd:cd18921     5 EKRTAHNAIEKRYRSSINDKIIELKDLV--VGTEAKLNKSAVLRKAIDYIRFLQQSNQKLKQENMALK 70