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Conserved domains on  [gi|321400053|ref|NP_001189443|]
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max dimerization protein 1 isoform 3 [Homo sapiens]

Protein Classification

Max dimerization protein 1( domain architecture ID 14441738)

Max dimerization protein 1 is a component of a transcriptional repressor complex together with MAX

Gene Ontology:  GO:0000122|GO:0070443|GO:0000981
PubMed:  16620027

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bHLHzip_Mad1 cd18931
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) ...
 60-126 7.34e-35

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.


:

Pssm-ID: 381501 [Multi-domain]  Cd Length: 80  Bit Score: 118.57  E-value: 7.34e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400053  60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKL 126
Cdd:cd18931   14 AHLRLCLEKLKMLVPLGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRHLKRQLEKL 80
 
Name Accession Description Interval E-value
bHLHzip_Mad1 cd18931
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) ...
 60-126 7.34e-35

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.


Pssm-ID: 381501 [Multi-domain]  Cd Length: 80  Bit Score: 118.57  E-value: 7.34e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400053  60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKL 126
Cdd:cd18931   14 AHLRLCLEKLKMLVPLGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRHLKRQLEKL 80
HLH smart00353
helix loop helix domain;
60-100 2.01e-03

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 35.27  E-value: 2.01e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 321400053    60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLED 100
Cdd:smart00353   9 RKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQE 49
HLH pfam00010
Helix-loop-helix DNA-binding domain;
60-99 7.94e-03

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 33.59  E-value: 7.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 321400053   60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLE 99
Cdd:pfam00010  14 DRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53
 
Name Accession Description Interval E-value
bHLHzip_Mad1 cd18931
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) ...
 60-126 7.34e-35

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.


Pssm-ID: 381501 [Multi-domain]  Cd Length: 80  Bit Score: 118.57  E-value: 7.34e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400053  60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKL 126
Cdd:cd18931   14 AHLRLCLEKLKMLVPLGPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRHLKRQLEKL 80
bHLHzip_Mad cd11401
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad ...
 60-123 2.26e-28

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad family (Mad1, Mxi, Mad3, and Mad4) bear the bHLHzip domain (also known as basic-helix-loop-helix-leucine-zipper or bHLH-LZ domain), which mediates heterodimerization to Max and the sequence-specific DNA binding ability to E-box DNA. Mad family proteins can repress transcription at the E-box through their interaction with co-repressors. Mad family proteins antagonize Myc function in transactivation and transformation and they are growth/tumor suppressors. The developmental phenotypes of the individual Mad family member knockout mice are relatively mild- all these mice have been shown to be viable and normal.


Pssm-ID: 381407 [Multi-domain]  Cd Length: 76  Bit Score: 101.52  E-value: 2.26e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 321400053  60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQL 123
Cdd:cd11401   13 AHLRLCLERLKELVPLGPDATRHTTLSLLTKAKAYIKNLEDKEKRQRQQKEQLRREQRELKRRL 76
bHLHzip_MXI1 cd18930
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-interacting protein 1 (MXI1) and ...
 60-126 2.29e-27

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.


Pssm-ID: 381500 [Multi-domain]  Cd Length: 80  Bit Score: 99.30  E-value: 2.29e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400053  60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKL 126
Cdd:cd18930   14 AHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEADRKSQHQLENLEREQRFLKRRLEQL 80
bHLHzip_Mad4 cd18929
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and ...
 60-129 2.50e-23

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and similar proteins; Mad4, also termed Max dimerization protein 4, or Max dimerizer 4 (MXD4), or Class C basic helix-loop-helix protein 12 (bHLHc12), or Max-interacting transcriptional repressor MAD4, is a bHLHZip Max-interacting transcriptional repressor that suppresses c-myc dependent transformation and is expressed during neural and epidermal differentiation. It is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc.


Pssm-ID: 381499 [Multi-domain]  Cd Length: 88  Bit Score: 89.29  E-value: 2.50e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400053  60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKLGIE 129
Cdd:cd18929   15 AKLRLYLEQLKQLVPLGPDSTRHTTLSLLKRAKMHIKKLEEQDRKALNIKEQLQREHRYLKRRLEQLSVQ 84
bHLHzip_Mad3 cd18932
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 3 (Mad3) and ...
 60-126 1.07e-16

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 3 (Mad3) and similar proteins; Mad3, also termed Max dimerization protein 3, or Max dimerizer 3 (MXD3), or Class C basic helix-loop-helix protein 13 (bHLHc13), or Max-interacting transcriptional repressor MAD3, or Myx, is a bHLHZip Max-interacting transcriptional repressor that plays an important role in cellular proliferation. It suppresses c-myc dependent transformation and is expressed during neural and epidermal differentiation.


Pssm-ID: 381502 [Multi-domain]  Cd Length: 85  Bit Score: 71.76  E-value: 1.07e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400053  60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKL 126
Cdd:cd18932   19 AQLRRCLEQLKQQVPLGADCSRYTTLSLLRRARLHIQKLEEQEQRAQQLKERLRWEQQKLRRRLESL 85
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
 61-126 3.40e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a member of the bHLHzip family of transcription factors that play important roles in the control of normal cell proliferation, growth, survival and differentiation. All Myc isoforms contain two independently functioning polypeptide chain regions: N-terminal transactivating residues and a C-terminal bHLHzip segment. The bHLHzip family of bHLH transcription factors are characterized by a highly conserved N-terminal basic region that may bind DNA at a consensus hexanucleotide sequence known as the E-box (CANNTG) followed by HLH and leucine zipper motifs that may interact with other proteins to form homo- and heterodimers. Myc heterodimerizes with Max enabling specific binding to E-box DNA sequences in the promoters of target genes. The Myc proto-oncoprotein family includes at least five different functional members: c-, N-, L-, S- and B-Myc (which is lacking the bHLH domain).


Pssm-ID: 381406 [Multi-domain]  Cd Length: 80  Bit Score: 37.91  E-value: 3.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321400053  61 HLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKL 126
Cdd:cd11400   15 DLKNSFEKLRDLVPELADNEKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARNEQLRKKLERL 80
bHLHzip_Mnt cd11402
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-binding protein Mnt and similar ...
 60-123 7.35e-04

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.


Pssm-ID: 381408 [Multi-domain]  Cd Length: 77  Bit Score: 36.91  E-value: 7.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 321400053  60 AHLRLCLEKLKGLVPlGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQL 123
Cdd:cd11402   15 AHLKECFETLKRQIP-NLDDKKTSNLNILRSALRYIQILKRKEKEYEHEMERLAREKIALQQRL 77
HLH smart00353
helix loop helix domain;
60-100 2.01e-03

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 35.27  E-value: 2.01e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 321400053    60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLED 100
Cdd:smart00353   9 RKINEAFDELRSLLPTLPKNKKLSKAEILRLAIEYIKSLQE 49
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 61-100 2.84e-03

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


Pssm-ID: 381392 [Multi-domain]  Cd Length: 46  Bit Score: 34.42  E-value: 2.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 321400053  61 HLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLED 100
Cdd:cd00083    7 KINDAFEELKRLLPELPDSKKLSKASILQKAVEYIRELQS 46
HLH pfam00010
Helix-loop-helix DNA-binding domain;
60-99 7.94e-03

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 33.59  E-value: 7.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 321400053   60 AHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLE 99
Cdd:pfam00010  14 DRINDAFDELRELLPTLPPDKKLSKAEILRLAIEYIKHLQ 53
 
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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