MAX_FELCA
ID MAX_FELCA Reviewed; 160 AA.
AC P61245; P25912; P52163;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein max {ECO:0000250|UniProtKB:P61244};
DE AltName: Full=Myc-associated factor X {ECO:0000250|UniProtKB:P61244};
GN Name=MAX {ECO:0000250|UniProtKB:P61244};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=7579579; DOI=10.3109/10425179509030979;
RA Gallagher R.C., Neil J.C., Fulton R.;
RT "Cloning and sequence of the feline max, and max 9 transcripts.";
RL DNA Seq. 5:269-271(1995).
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. May repress
CC transcription via the recruitment of a chromatin remodeling complex
CC containing H3 'Lys-9' histone methyltransferase activity (By
CC similarity). Represses MYC transcriptional activity from E-box elements
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61244}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MYC or MAD. Part of the
CC E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3,
CC BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some
CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1,
CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with SPAG9.
CC The heterodimer MYC:MAX interacts with ABI1; the interaction may
CC enhance MYC:MAX transcriptional activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC Cell projection, dendrite {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR EMBL; D37786; BAA07038.1; -; mRNA.
DR RefSeq; NP_001009866.1; NM_001009866.1.
DR AlphaFoldDB; P61245; -.
DR BMRB; P61245; -.
DR SMR; P61245; -.
DR STRING; 9685.ENSFCAP00000009607; -.
DR Ensembl; ENSFCAT00000062463; ENSFCAP00000041492; ENSFCAG00000010347.
DR GeneID; 493947; -.
DR KEGG; fca:493947; -.
DR CTD; 4149; -.
DR VGNC; VGNC:80920; MAX.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00530000064011; -.
DR HOGENOM; CLU_109424_1_0_1; -.
DR InParanoid; P61245; -.
DR OrthoDB; 1545748at2759; -.
DR TreeFam; TF318841; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000010347; Expressed in uterus and 10 other tissues.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Activator; Cell projection; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT CHAIN 2..160
FT /note="Protein max"
FT /id="PRO_0000127268"
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 103..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 103..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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 153
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
SQ SEQUENCE 160 AA; 18275 MW; EB10F3137727A56F CRC64;
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN
SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS
