MAX_XENLA
ID MAX_XENLA Reviewed; 163 AA.
AC Q07016;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein max;
DE Short=xMAX;
DE AltName: Full=Myc-associated factor X;
GN Name=max;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XMAX1; XMAX2; XMAX3 AND XMAX4).
RX PubMed=8302600;
RA Tonissen K.F., Krieg P.A.;
RT "Analysis of a variant Max sequence expressed in Xenopus laevis.";
RL Oncogene 9:33-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XMAX2 AND XMAX4).
RX PubMed=8494787;
RA King M.W., Blackwood E.M., Eisenman R.N.;
RT "Expression of two distinct homologues of Xenopus Max during early
RT development.";
RL Cell Growth Differ. 4:85-92(1993).
CC -!- FUNCTION: Transcription regulator. Forms a sequence-specific DNA-
CC binding protein complex with MYC or MAD which recognizes the core
CC sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional
CC activator, whereas the MAD-MAX complex is a repressor (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. MYC/MAX heterodimers bind to target DNA with high affinity.
CC MAX may also form homodimers which recognize the same target sequence,
CC but which are unable to function as transcription activators. Component
CC of some MLL1/MLL complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=XMAX4; Synonyms=XMAX2;
CC IsoId=Q07016-1; Sequence=Displayed;
CC Name=XMAX1;
CC IsoId=Q07016-2; Sequence=VSP_002122, VSP_002123;
CC Name=XMAX2; Synonyms=XMAX1;
CC IsoId=Q07016-3; Sequence=VSP_002123;
CC Name=XMAX3;
CC IsoId=Q07016-4; Sequence=VSP_002122;
CC -!- TISSUE SPECIFICITY: All four alternatively spliced forms are present
CC during development and in all adult tissues examined.
CC -!- PTM: Phosphorylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR EMBL; L09739; AAA17425.1; -; mRNA.
DR EMBL; L09738; AAA17424.1; -; mRNA.
DR EMBL; L04923; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; L04924; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B56883; B56883.
DR PIR; I51586; I51586.
DR PIR; I51587; I51587.
DR RefSeq; NP_001079118.1; NM_001085649.1. [Q07016-1]
DR RefSeq; NP_001089042.1; NM_001095573.1.
DR AlphaFoldDB; Q07016; -.
DR SMR; Q07016; -.
DR MaxQB; Q07016; -.
DR DNASU; 504192; -.
DR GeneID; 373652; -.
DR GeneID; 504192; -.
DR KEGG; xla:373652; -.
DR CTD; 373652; -.
DR CTD; 504192; -.
DR Xenbase; XB-GENE-6255913; max.L.
DR Xenbase; XB-GENE-6252877; max.S.
DR OrthoDB; 1545748at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 373652; Expressed in testis and 19 other tissues.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR037933; MAX-like.
DR PANTHER; PTHR10328; PTHR10328; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..163
FT /note="Protein max"
FT /id="PRO_0000127274"
FT DOMAIN 23..74
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 13..21
FT /note="Missing (in isoform XMAX1 and isoform XMAX3)"
FT /evidence="ECO:0000303|PubMed:8302600"
FT /id="VSP_002122"
FT VAR_SEQ 99..125
FT /note="Missing (in isoform XMAX1 and isoform XMAX2)"
FT /evidence="ECO:0000303|PubMed:8302600,
FT ECO:0000303|PubMed:8494787"
FT /id="VSP_002123"
FT CONFLICT 52
FT /note="S -> A (in Ref. 1; AAA17424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 163 AA; 18685 MW; 94ABC1D67A564D6A CRC64;
MSDNDDIEVE SDEDSSRFPY SADKRAHHNA LERKRRDHIK DSFHGLRDSV PSLQGEKASR
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVQ ISNPKPPSNG APEQKNVLQL
LSPSKVRALE KAKSSSQLQS NYSSSESETE EPQSRKKLRM DAS
