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MAX_CHICK
ID   MAX_CHICK               Reviewed;         160 AA.
AC   P52162;
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   AltName: Full=Myc-associated factor X;
GN   Name=MAX;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS LONG AND SHORT).
RC   TISSUE=Fibroblast;
RX   PubMed=8290277;
RA   Sollenberger K.G., Kao T.L., Taparowsky E.J.;
RT   "Structural analysis of the chicken max gene.";
RL   Oncogene 9:661-664(1994).
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. Binds DNA as a heterodimer with MYC or MAD. Component of some
CC       MLL1/MLL complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P52162-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P52162-2; Sequence=VSP_002120;
CC   -!- PTM: Phosphorylated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR   EMBL; L12469; AAA16834.1; -; Unassigned_DNA.
DR   PIR; I50379; I50379.
DR   RefSeq; XP_015141578.1; XM_015286092.1. [P52162-1]
DR   AlphaFoldDB; P52162; -.
DR   BMRB; P52162; -.
DR   SMR; P52162; -.
DR   MINT; P52162; -.
DR   STRING; 9031.ENSGALP00000040991; -.
DR   Ensembl; ENSGALT00000052061; ENSGALP00000057649; ENSGALG00000032249. [P52162-2]
DR   Ensembl; ENSGALT00000065978; ENSGALP00000044694; ENSGALG00000032249. [P52162-1]
DR   GeneID; 100858676; -.
DR   KEGG; gga:100858676; -.
DR   CTD; 4149; -.
DR   VEuPathDB; HostDB:geneid_100858676; -.
DR   eggNOG; KOG2483; Eukaryota.
DR   GeneTree; ENSGT00530000064011; -.
DR   HOGENOM; CLU_109424_1_0_1; -.
DR   InParanoid; P52162; -.
DR   OMA; QIQTNYS; -.
DR   OrthoDB; 1545748at2759; -.
DR   PhylomeDB; P52162; -.
DR   PRO; PR:P52162; -.
DR   Proteomes; UP000000539; Chromosome 5.
DR   Bgee; ENSGALG00000032249; Expressed in cerebellum and 13 other tissues.
DR   ExpressionAtlas; P52162; baseline and differential.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   3: Inferred from homology;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..160
FT                   /note="Protein max"
FT                   /id="PRO_0000127272"
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          81..102
FT                   /note="Leucine-zipper"
FT   REGION          105..160
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        105..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         13..21
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002120"
SQ   SEQUENCE   160 AA;  18184 MW;  F09B16D1AB379A7E CRC64;
     MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR
     AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQANYPAADS
     SLYTNPKGST ISAFDGGSDS SSDSEPDEPQ SRKKLRMEAS
 
 
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