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Protein Page:
MAX (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
MAX a transcription factor. Forms a DNA- binding protein complex with MYC or MAD. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. CPG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC/MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3-K9 histone methyltransferase activity. Three alternatively spliced isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: DNA-binding; Transcription factor
Chromosomal Location of Human Ortholog: 14q23
Cellular Component: cytoplasm; dendrite; nucleoplasm; nucleus; PML body
Molecular Function: protein binding; protein complex binding; protein heterodimerization activity; protein homodimerization activity; transcription coactivator activity; transcription cofactor activity; transcription factor activity
Biological Process: cellular response to starvation; neuron apoptosis; protein complex assembly; regulation of transcription from RNA polymerase II promoter; response to axon injury; response to insulin stimulus; retina development in camera-type eye; transcription from RNA polymerase II promoter
Reference #:  P61244 (UniProtKB)
Gene Symbols: MAX
Molecular weight: 18,275 Da
Basal Isoelectric point: 5.88  Predict pI for various phosphorylation states
CST Pathways:  Regulation of P38 MAPKs
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

MAX

Protein Structure Not Found.
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Sites Implicated In
transcription, altered: S2‑p, S11‑p
activity, inhibited: S2‑p, S11‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
4 26 S2‑p ______MsDNDDIEV
4 22 S11‑p NDDIEVEsDEEQPRF
1 0 K40‑ac RKRRDHIkDsFHsLR
0 1 K40‑ub RKRRDHIkDsFHsLR
0 2 S42‑p RRDHIkDsFHsLRDS
0 1 S45‑p HIkDsFHsLRDSVPS
0 1 K57‑ub VPSLQGEkASRAQIL
1 1 K66‑ac SRAQILDkAtEyIQy
0 4 T68‑p AQILDkAtEyIQyMR
0 19 Y70‑p ILDkAtEyIQyMRRK
0 25 Y73‑p kAtEyIQyMRRKNHT
0 3 S107‑p RALEKARsSAQLQTN
0 1 Y115‑p SAQLQTNyPSsDNsL
0 1 S118‑p LQTNyPSsDNsLytN
0 3 S121‑p NyPSsDNsLytNAKG
0 65 Y123‑p PSsDNsLytNAKGST
0 1 T124‑p SsDNsLytNAKGSTI
0 1 T130 ytNAKGSTIsAFDGG
0 1 S132‑p NAKGSTIsAFDGGsD
0 1 S138‑p IsAFDGGsDsssEsE
0 2 S140‑p AFDGGsDsssEsEPE
0 1 S141‑p FDGGsDsssEsEPEE
0 1 S142‑p DGGsDsssEsEPEEP
0 4 S144‑p GsDsssEsEPEEPQS
1 0 K153‑ac PEEPQSRkkLRMEAS
1 0 K154‑ac EEPQSRkkLRMEAS_
  MAX iso2  
S2‑p ______MsDNDDIEV
S11‑p NDDIEVEsDADKRAH
K31 RKRRDHIKDSFHSLR
K31 RKRRDHIKDSFHSLR
S33 RRDHIKDSFHSLRDS
S36 HIKDSFHSLRDSVPS
K48 VPSLQGEKASRAQIL
K57 SRAQILDKATEyIQY
T59 AQILDKATEyIQYMR
Y61‑p ILDKATEyIQYMRRK
Y64 KATEyIQYMRRKNHT
S98 RALEKARSSAQLQTN
Y106 SAQLQTNYPSSDNSL
S109 LQTNYPSSDNSLyTN
S112 NYPSSDNSLyTNAKG
Y114‑p PSSDNSLyTNAKGST
T115 SSDNSLyTNAKGSTI
T121 yTNAKGSTISAFDGG
S123 NAKGSTISAFDGGSD
S129 ISAFDGGSDSSSESE
S131 AFDGGSDSSSESEPE
S132 FDGGSDSSSESEPEE
S133 DGGSDSSSESEPEEP
S135 GSDSSSESEPEEPQS
K144 PEEPQSRKKLRMEAS
K145 EEPQSRKKLRMEAS_
  mouse

► Hide Isoforms
 
S2‑p ______MsDNDDIEV
S11‑p NDDIEVEsDEEQARF
K40 RKRRDHIKDSFHSLR
K40 RKRRDHIKDSFHSLR
S42 RRDHIKDSFHSLRDS
S45 HIKDSFHSLRDSVPS
K57 VPSLQGEKASRAQIL
K66 SRAQILDKATEYIQY
T68 AQILDKATEYIQYMR
Y70 ILDKATEYIQYMRRK
Y73 KATEYIQYMRRKNDT
S107 RALEKARSSAQLQTN
Y115 SAQLQTNYPSSDNSL
S118 LQTNYPSSDNSLYTN
S121 NYPSSDNSLYTNAKG
Y123 PSSDNSLYTNAKGGt
T124 SSDNSLYTNAKGGtI
T130‑p YTNAKGGtISAFDGG
S132 NAKGGtISAFDGGSD
S138 ISAFDGGSDSSSEsE
S140 AFDGGSDSSSEsEPE
S141 FDGGSDSSSEsEPEE
S142 DGGSDSSSEsEPEEP
S144‑p GSDSSSEsEPEEPQS
K153 PEEPQSRKKLRMEAS
K154 EEPQSRKKLRMEAS_
  MAX iso2  
S2‑p ______MsDNDDIEV
S11‑p NDDIEVEsDADKRAH
K31 RKRRDHIKDSFHSLR
K31 RKRRDHIKDSFHSLR
S33 RRDHIKDSFHSLRDS
S36 HIKDSFHSLRDSVPS
K48 VPSLQGEKASRAQIL
K57 SRAQILDKATEYIQY
T59 AQILDKATEYIQYMR
Y61 ILDKATEYIQYMRRK
Y64 KATEYIQYMRRKNHT
S98 RALEKARSSAQLQTN
Y106 SAQLQTNYPSSDNSL
S109 LQTNYPSSDNSLYTN
S112 NYPSSDNSLYTNAKG
Y114 PSSDNSLYTNAKGGT
T115 SSDNSLYTNAKGGTI
T121 YTNAKGGTISAFDGG
S123 NAKGGTISAFDGGSD
S129 ISAFDGGSDSSSESE
S131 AFDGGSDSSSESEPE
S132 FDGGSDSSSESEPEE
S133 DGGSDSSSESEPEEP
S135 GSDSSSESEPEEPQS
K144 PEEPQSRKKLRMEAS
K145 EEPQSRKKLRMEAS_
  rat

► Hide Isoforms
 
S2‑p ______MsDNDDIEV
S11‑p NDDIEVEsDEEQPRF
K40 RKRRDHIKDSFHSLR
K40 RKRRDHIKDSFHSLR
S42 RRDHIKDSFHSLRDS
S45 HIKDSFHSLRDSVPS
K57 VPSLQGEKASRAQIL
K66‑ac SRAQILDkATEYIQY
T68 AQILDkATEYIQYMR
Y70 ILDkATEYIQYMRRK
Y73 kATEYIQYMRRKNHT
S107 RALEKARSSAQLQTN
Y115 SAQLQTNYPSSDNSL
S118 LQTNYPSSDNSLYTN
S121 NYPSSDNSLYTNAKG
Y123 PSSDNSLYTNAKGGT
T124 SSDNSLYTNAKGGTI
T130 YTNAKGGTISAFDGG
S132 NAKGGTISAFDGGSD
S138 ISAFDGGSDSSSESE
S140 AFDGGSDSSSESEPE
S141 FDGGSDSSSESEPEE
S142 DGGSDSSSESEPEEP
S144 GSDSSSESEPEEPQN
K153 PEEPQNRKKLRMEAS
K154 EEPQNRKKLRMEAS_
  MAX iso2  
S2‑p ______MsDNDDIEV
S11‑p NDDIEVEsDADKRAH
K31 RKRRDHIKDSFHSLR
K31 RKRRDHIKDSFHSLR
S33 RRDHIKDSFHSLRDS
S36 HIKDSFHSLRDSVPS
K48 VPSLQGEKASRAQIL
K57 SRAQILDKATEYIQY
T59 AQILDKATEYIQYMR
Y61 ILDKATEYIQYMRRK
Y64 KATEYIQYMRRKNHT
S98 RALEKARSSAQLQTN
Y106 SAQLQTNYPSSDNSL
S109 LQTNYPSSDNSLYTN
S112 NYPSSDNSLYTNAKG
Y114 PSSDNSLYTNAKGGT
T115 SSDNSLYTNAKGGTI
T121 YTNAKGGTISAFDGG
S123 NAKGGTISAFDGGSD
S129 ISAFDGGSDSSSESE
S131 AFDGGSDSSSESEPE
S132 FDGGSDSSSESEPEE
S133 DGGSDSSSESEPEEP
S135 GSDSSSESEPEEPQN
K144 PEEPQNRKKLRMEAS
K145 EEPQNRKKLRMEAS_
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