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Protein

Protein max

Gene

MAX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity.

GO - Molecular functioni

  • sequence-specific DNA binding Source: Ensembl
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • transcription coactivator activity Source: ProtInc
  • transcription cofactor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1574. Cyclin E associated events during G1/S transition.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP61244.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein max
Alternative name(s):
Class D basic helix-loop-helix protein 4
Short name:
bHLHd4
Myc-associated factor X
Gene namesi
Name:MAX
Synonyms:BHLHD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:6913. MAX.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • dendrite Source: UniProtKB-SubCell
  • MLL1 complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: BHF-UCL
  • PML body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661K → Q: Kept nuclear localization. Loss of nuclear localization; when associated with Q-153 and Q-154. 1 Publication
Mutagenesisi66 – 661K → R: Loss of acetylation, kept nuclear localization; when associated with R-153 and R-154. 1 Publication
Mutagenesisi153 – 1531K → Q: Loss of nuclear localization; when associated with Q-66 and Q-154. Kept nuclear localization; when associated with Q-154. 1 Publication
Mutagenesisi153 – 1531K → R: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-154. 1 Publication
Mutagenesisi154 – 1541K → Q: Loss of nuclear localization; when associated with Q-66 and Q-153. Kept nuclear localization; when associated with Q-153. 1 Publication
Mutagenesisi154 – 1541K → R: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-153. 1 Publication

Organism-specific databases

Orphaneti29072. Hereditary pheochromocytoma-paraganglioma.
PharmGKBiPA30656.

Polymorphism and mutation databases

DMDMi47117704.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 160159Protein maxPRO_0000127269Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei2 – 21Phosphoserine3 Publications
Modified residuei11 – 111Phosphoserine3 Publications
Modified residuei66 – 661N6-acetyllysine1 Publication
Modified residuei153 – 1531N6-acetyllysine1 Publication
Modified residuei154 – 1541N6-acetyllysine1 Publication

Post-translational modificationi

Reversible lysine acetylation might regulate the nuclear-cytoplasmic shuttling of specific Max complexes.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP61244.
PaxDbiP61244.
PRIDEiP61244.

PTM databases

PhosphoSiteiP61244.

Miscellaneous databases

PMAP-CutDBP61244.

Expressioni

Tissue specificityi

High levels found in the brain, heart and lung while lower levels are seen in the liver, kidney and skeletal muscle.

Gene expression databases

BgeeiP61244.
CleanExiHS_MAX.
ExpressionAtlasiP61244. baseline and differential.
GenevisibleiP61244. HS.

Organism-specific databases

HPAiCAB000328.
HPA003474.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MYC or MAD. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with SPAG9. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BANPQ8N9N53EBI-751711,EBI-744695
EPAS1Q998142EBI-751711,EBI-447470
FTH1P027942EBI-751711,EBI-713259
GABBR1Q9UBS53EBI-751711,EBI-724156
MXD1Q051952EBI-751711,EBI-8833637
MXI1P505394EBI-751711,EBI-752241
MYCP0110623EBI-751711,EBI-447544
MYCNP041985EBI-751711,EBI-878369
UNC45AQ9H3U13EBI-10218525,EBI-1048763

Protein-protein interaction databases

BioGridi110319. 67 interactions.
DIPiDIP-28145N.
IntActiP61244. 48 interactions.
MINTiMINT-1468374.
STRINGi9606.ENSP00000351490.

Structurei

Secondary structure

1
160
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 4724Combined sources
Helixi51 – 533Combined sources
Helixi60 – 10041Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AN2X-ray2.90A22-107[»]
1HLOX-ray2.80A/B20-92[»]
1NKPX-ray1.80B/E23-102[»]
1NLWX-ray2.00B/E24-99[»]
1R05NMR-A/B22-103[»]
DisProtiDP00084.
ProteinModelPortaliP61244.
SMRiP61244. Positions 23-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61244.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 7452bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 10222Leucine-zipperAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi152 – 1565Nuclear localization signal

Sequence similaritiesi

Belongs to the MAX family.Curated
Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG239807.
GeneTreeiENSGT00530000064011.
HOGENOMiHOG000293257.
HOVERGENiHBG008542.
InParanoidiP61244.
KOiK04453.
OMAiENXRALE.
OrthoDBiEOG7XPZ7J.
PhylomeDBiP61244.
TreeFamiTF318841.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P61244-1) [UniParc]FASTAAdd to basket

Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV
60 70 80 90 100
PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR
110 120 130 140 150
ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ
160
SRKKLRMEAS
Length:160
Mass (Da):18,275
Last modified:May 10, 2004 - v1
Checksum:iEB10F3137727A56F
GO
Isoform 2 (identifier: P61244-2) [UniParc] [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     13-21: Missing.

Note: Contains a phosphoserine at position 2. Initiator Met-1 is removed. Contains a N-acetylserine at position 2. Contains a phosphoserine at position 11.4 Publications
Show »
Length:151
Mass (Da):17,202
Checksum:iCB69F6F5F39793FA
GO
Isoform 3 (identifier: P61244-3) [UniParc] [UniParc]FASTAAdd to basket

Also known as: Delta-Max

The sequence of this isoform differs from the canonical sequence as follows:
     99-160: VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS → GESES

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:103
Mass (Da):12,099
Checksum:i49DC1A0441FFA301
GO
Isoform 4 (identifier: P61244-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     99-160: VRALEKARSS...SRKKLRMEAS → GEHPSSWGSW...VRASHGVCAQ

Show »
Length:134
Mass (Da):15,395
Checksum:iA2FFD0B98CF93275
GO
Isoform 5 (identifier: P61244-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-160: ASRAQILDKA...SRKKLRMEAS → LYFLFWKLCT...QVHKKKECKI

Note: No experimental confirmation available.
Show »
Length:96
Mass (Da):11,455
Checksum:iD380F721DCF2D6C8
GO
Isoform 6 (identifier: P61244-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-160: ASRAQILDKA...SRKKLRMEAS → GTKMKLTLPPVFPYEHLPFPTVFCHG

Note: No experimental confirmation available.
Show »
Length:83
Mass (Da):9,599
Checksum:iFE0E966237003D47
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei13 – 219Missing in isoform 2. 3 PublicationsVSP_002117
Alternative sequencei58 – 160103ASRAQ…RMEAS → LYFLFWKLCTPVLHRQSLMQ KCHTFISSYQVHKKKECKI in isoform 5. 1 PublicationVSP_043430Add
BLAST
Alternative sequencei58 – 160103ASRAQ…RMEAS → GTKMKLTLPPVFPYEHLPFP TVFCHG in isoform 6. CuratedVSP_047661Add
BLAST
Alternative sequencei99 – 16062VRALE…RMEAS → GESES in isoform 3. 2 PublicationsVSP_002118Add
BLAST
Alternative sequencei99 – 16062VRALE…RMEAS → GEHPSSWGSWPCCAPARSGF GTWACRVRASHGVCAQ in isoform 4. 1 PublicationVSP_043183Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64240 mRNA. Translation: AAA36200.1.
M64240 mRNA. Translation: AAA36201.1.
X66867 Genomic DNA. Translation: CAA47337.1.
X66867 Genomic DNA. Translation: CAA47338.1.
X66867 Genomic DNA. Translation: CAA47339.1.
X60287 mRNA. Translation: CAA42827.1.
AK290130 mRNA. Translation: BAF82819.1.
AK290929 mRNA. Translation: BAF83618.1.
AK292189 mRNA. Translation: BAF84878.1.
AK292630 mRNA. Translation: BAF85319.1.
AL139022 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80899.1.
CH471061 Genomic DNA. Translation: EAW80901.1.
CH471061 Genomic DNA. Translation: EAW80903.1.
CH471061 Genomic DNA. Translation: EAW80904.1.
BC003525 mRNA. Translation: AAH03525.1.
BC004516 mRNA. Translation: AAH04516.1.
BC013669 mRNA. Translation: AAH13669.1.
BC027924 mRNA. Translation: AAH27924.1.
CCDSiCCDS41965.1. [P61244-3]
CCDS9770.1. [P61244-6]
CCDS9771.1.
CCDS9772.1. [P61244-2]
CCDS9774.1. [P61244-5]
PIRiA38431.
A42611.
B38431.
S33118.
RefSeqiNP_001257997.1. NM_001271068.1.
NP_002373.3. NM_002382.4. [P61244-1]
NP_660087.1. NM_145112.2. [P61244-2]
NP_660088.1. NM_145113.2. [P61244-3]
NP_660089.1. NM_145114.2. [P61244-5]
NP_932061.1. NM_197957.3. [P61244-6]
UniGeneiHs.285354.

Genome annotation databases

EnsembliENST00000246163; ENSP00000246163; ENSG00000125952. [P61244-5]
ENST00000284165; ENSP00000284165; ENSG00000125952. [P61244-4]
ENST00000341653; ENSP00000342482; ENSG00000125952. [P61244-6]
ENST00000358402; ENSP00000351175; ENSG00000125952. [P61244-2]
ENST00000358664; ENSP00000351490; ENSG00000125952. [P61244-1]
ENST00000394606; ENSP00000378104; ENSG00000125952. [P61244-3]
ENST00000553928; ENSP00000451907; ENSG00000125952. [P61244-3]
ENST00000556979; ENSP00000452378; ENSG00000125952. [P61244-3]
ENST00000618858; ENSP00000480127; ENSG00000125952. [P61244-3]
GeneIDi4149.
KEGGihsa:4149.
UCSCiuc001xie.2. human. [P61244-3]
uc001xif.2. human.
uc001xig.2. human. [P61244-2]
uc001xij.2. human. [P61244-4]
uc001xik.4. human. [P61244-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64240 mRNA. Translation: AAA36200.1.
M64240 mRNA. Translation: AAA36201.1.
X66867 Genomic DNA. Translation: CAA47337.1.
X66867 Genomic DNA. Translation: CAA47338.1.
X66867 Genomic DNA. Translation: CAA47339.1.
X60287 mRNA. Translation: CAA42827.1.
AK290130 mRNA. Translation: BAF82819.1.
AK290929 mRNA. Translation: BAF83618.1.
AK292189 mRNA. Translation: BAF84878.1.
AK292630 mRNA. Translation: BAF85319.1.
AL139022 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80899.1.
CH471061 Genomic DNA. Translation: EAW80901.1.
CH471061 Genomic DNA. Translation: EAW80903.1.
CH471061 Genomic DNA. Translation: EAW80904.1.
BC003525 mRNA. Translation: AAH03525.1.
BC004516 mRNA. Translation: AAH04516.1.
BC013669 mRNA. Translation: AAH13669.1.
BC027924 mRNA. Translation: AAH27924.1.
CCDSiCCDS41965.1. [P61244-3]
CCDS9770.1. [P61244-6]
CCDS9771.1.
CCDS9772.1. [P61244-2]
CCDS9774.1. [P61244-5]
PIRiA38431.
A42611.
B38431.
S33118.
RefSeqiNP_001257997.1. NM_001271068.1.
NP_002373.3. NM_002382.4. [P61244-1]
NP_660087.1. NM_145112.2. [P61244-2]
NP_660088.1. NM_145113.2. [P61244-3]
NP_660089.1. NM_145114.2. [P61244-5]
NP_932061.1. NM_197957.3. [P61244-6]
UniGeneiHs.285354.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AN2X-ray2.90A22-107[»]
1HLOX-ray2.80A/B20-92[»]
1NKPX-ray1.80B/E23-102[»]
1NLWX-ray2.00B/E24-99[»]
1R05NMR-A/B22-103[»]
DisProtiDP00084.
ProteinModelPortaliP61244.
SMRiP61244. Positions 23-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110319. 67 interactions.
DIPiDIP-28145N.
IntActiP61244. 48 interactions.
MINTiMINT-1468374.
STRINGi9606.ENSP00000351490.

Chemistry

BindingDBiP61244.
ChEMBLiCHEMBL3301395.

PTM databases

PhosphoSiteiP61244.

Polymorphism and mutation databases

DMDMi47117704.

Proteomic databases

MaxQBiP61244.
PaxDbiP61244.
PRIDEiP61244.

Protocols and materials databases

DNASUi4149.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000246163; ENSP00000246163; ENSG00000125952. [P61244-5]
ENST00000284165; ENSP00000284165; ENSG00000125952. [P61244-4]
ENST00000341653; ENSP00000342482; ENSG00000125952. [P61244-6]
ENST00000358402; ENSP00000351175; ENSG00000125952. [P61244-2]
ENST00000358664; ENSP00000351490; ENSG00000125952. [P61244-1]
ENST00000394606; ENSP00000378104; ENSG00000125952. [P61244-3]
ENST00000553928; ENSP00000451907; ENSG00000125952. [P61244-3]
ENST00000556979; ENSP00000452378; ENSG00000125952. [P61244-3]
ENST00000618858; ENSP00000480127; ENSG00000125952. [P61244-3]
GeneIDi4149.
KEGGihsa:4149.
UCSCiuc001xie.2. human. [P61244-3]
uc001xif.2. human.
uc001xig.2. human. [P61244-2]
uc001xij.2. human. [P61244-4]
uc001xik.4. human. [P61244-5]

Organism-specific databases

CTDi4149.
GeneCardsiGC14M065472.
GeneReviewsiMAX.
HGNCiHGNC:6913. MAX.
HPAiCAB000328.
HPA003474.
MIMi154950. gene.
neXtProtiNX_P61244.
Orphaneti29072. Hereditary pheochromocytoma-paraganglioma.
PharmGKBiPA30656.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239807.
GeneTreeiENSGT00530000064011.
HOGENOMiHOG000293257.
HOVERGENiHBG008542.
InParanoidiP61244.
KOiK04453.
OMAiENXRALE.
OrthoDBiEOG7XPZ7J.
PhylomeDBiP61244.
TreeFamiTF318841.

Enzyme and pathway databases

ReactomeiREACT_1574. Cyclin E associated events during G1/S transition.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP61244.

Miscellaneous databases

ChiTaRSiMAX. human.
EvolutionaryTraceiP61244.
GeneWikiiMAX_(gene).
GenomeRNAii4149.
NextBioi16302.
PMAP-CutDBP61244.
PROiP61244.
SOURCEiSearch...

Gene expression databases

BgeeiP61244.
CleanExiHS_MAX.
ExpressionAtlasiP61244. baseline and differential.
GenevisibleiP61244. HS.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc."
    Blackwood E.M., Eisenman R.N.
    Science 251:1211-1217(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "Alternative mRNA forms and open reading frames of the max gene."
    Vaestrik I., Koskinen P.J., Alitalo R., Maekelae T.P.
    Oncogene 8:503-507(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation."
    Maekelae T.P., Koskinen P.J., Vaestrik I., Alitalo K.
    Science 256:373-377(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Mammary gland, Thalamus and Thymus.
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
    Tissue: Brain, Lung and Uterus.
  8. "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
    Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
    Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MGA; EUHMTASE1; BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
  9. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  10. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Max is acetylated by p300 at several nuclear localization residues."
    Faiola F., Wu Y.-T., Pan S., Zhang K., Farina A., Martinez E.
    Biochem. J. 403:397-407(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-66; LYS-153 AND LYS-154, MUTAGENESIS OF LYS-66; LYS-153 AND LYS-154.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain."
    Ferre-D'Amare A.R., Prendergast G.C., Ziff E.B., Burley S.K.
    Nature 363:38-45(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-107.
  20. "The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control."
    Brownlie P., Ceska T., Lamers M., Romier C., Stier G., Teo H., Suck D.
    Structure 5:509-520(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiMAX_HUMAN
AccessioniPrimary (citable) accession number: P61244
Secondary accession number(s): A6NH73
, A8K265, A8K4G4, A8K824, P25912, P52163, Q14803, Q96CY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: June 24, 2015
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.