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P61244

- MAX_HUMAN

UniProt

P61244 - MAX_HUMAN

Protein

Protein max

Gene

MAX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    1. protein binding Source: UniProtKB
    2. sequence-specific DNA binding Source: Ensembl
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. transcription coactivator activity Source: ProtInc
    5. transcription cofactor activity Source: ProtInc

    GO - Biological processi

    1. cellular response to peptide hormone stimulus Source: Ensembl
    2. cellular response to starvation Source: Ensembl
    3. negative regulation of gene expression Source: Ensembl
    4. neuron apoptotic process Source: Ensembl
    5. protein complex assembly Source: Ensembl
    6. response to axon injury Source: Ensembl
    7. response to insulin Source: Ensembl
    8. retina development in camera-type eye Source: Ensembl
    9. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_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: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:6913. MAX.

    Subcellular locationi

    Nucleus. Cell projectiondendrite By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. dendrite Source: UniProtKB-SubCell
    3. MLL1 complex Source: UniProtKB
    4. nucleus Source: BHF-UCL
    5. PML body Source: Ensembl

    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.

    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.4 Publications

    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

    ArrayExpressiP61244.
    BgeeiP61244.
    CleanExiHS_MAX.
    GenevestigatoriP61244.

    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
    EPAS1Q998142EBI-751711,EBI-447470
    FTH1P027942EBI-751711,EBI-713259
    GABBR1Q9UBS53EBI-751711,EBI-724156
    MAD1L1Q9Y6D92EBI-751711,EBI-742610
    MYCP0110621EBI-751711,EBI-447544
    MYCNP041984EBI-751711,EBI-878369

    Protein-protein interaction databases

    BioGridi110319. 62 interactions.
    DIPiDIP-28145N.
    IntActiP61244. 46 interactions.
    MINTiMINT-1468374.
    STRINGi9606.ENSP00000351490.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000293257.
    HOVERGENiHBG008542.
    InParanoidiP61244.
    KOiK04453.
    OMAiFPYEHLP.
    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. Align

    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

    MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV    50
    PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR 100
    ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ 150
    SRKKLRMEAS 160
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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]

    Polymorphism databases

    DMDMi47117704.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS41965.1. [P61244-3 ]
    CCDS9770.1. [P61244-6 ]
    CCDS9771.1.
    CCDS9772.1. [P61244-2 ]
    CCDS9774.1. [P61244-5 ]
    PIRi A38431.
    A42611.
    B38431.
    S33118.
    RefSeqi NP_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 ]
    UniGenei Hs.285354.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AN2 X-ray 2.90 A 22-107 [» ]
    1HLO X-ray 2.80 A/B 20-92 [» ]
    1NKP X-ray 1.80 B/E 23-102 [» ]
    1NLW X-ray 2.00 B/E 24-99 [» ]
    1R05 NMR - A/B 22-103 [» ]
    DisProti DP00084.
    ProteinModelPortali P61244.
    SMRi P61244. Positions 23-102.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110319. 62 interactions.
    DIPi DIP-28145N.
    IntActi P61244. 46 interactions.
    MINTi MINT-1468374.
    STRINGi 9606.ENSP00000351490.

    Chemistry

    BindingDBi P61244.
    ChEMBLi CHEMBL1250363.

    PTM databases

    PhosphoSitei P61244.

    Polymorphism databases

    DMDMi 47117704.

    Proteomic databases

    MaxQBi P61244.
    PaxDbi P61244.
    PRIDEi P61244.

    Protocols and materials databases

    DNASUi 4149.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246163 ; 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 ]
    GeneIDi 4149.
    KEGGi hsa:4149.
    UCSCi uc001xie.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

    CTDi 4149.
    GeneCardsi GC14M065472.
    GeneReviewsi MAX.
    HGNCi HGNC:6913. MAX.
    HPAi CAB000328.
    HPA003474.
    MIMi 154950. gene.
    neXtProti NX_P61244.
    Orphaneti 29072. Hereditary pheochromocytoma-paraganglioma.
    PharmGKBi PA30656.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239807.
    HOGENOMi HOG000293257.
    HOVERGENi HBG008542.
    InParanoidi P61244.
    KOi K04453.
    OMAi FPYEHLP.
    OrthoDBi EOG7XPZ7J.
    PhylomeDBi P61244.
    TreeFami TF318841.

    Enzyme and pathway databases

    Reactomei REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinki P61244.

    Miscellaneous databases

    ChiTaRSi MAX. human.
    EvolutionaryTracei P61244.
    GeneWikii MAX_(gene).
    GenomeRNAii 4149.
    NextBioi 16302.
    PMAP-CutDB P61244.
    PROi P61244.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61244.
    Bgeei P61244.
    CleanExi HS_MAX.
    Genevestigatori P61244.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    [Graphical view ]
    Pfami PF00010. HLH. 1 hit.
    [Graphical view ]
    SMARTi SM00353. HLH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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, 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, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, IDENTIFICATION BY MASS SPECTROMETRY [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, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, IDENTIFICATION BY MASS SPECTROMETRY [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: October 1, 2014
    This is version 131 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