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Q9UH92

- MLX_HUMAN

UniProt

Q9UH92 - MLX_HUMAN

Protein

Max-like protein X

Gene

MLX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (01 Oct 2001)
      Previous versions | rss
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    Functioni

    Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4, TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation.3 Publications

    GO - Molecular functioni

    1. DNA binding Source: BHF-UCL
    2. protein heterodimerization activity Source: BHF-UCL
    3. protein homodimerization activity Source: BHF-UCL
    4. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
    5. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
    6. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    7. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. energy reserve metabolic process Source: Reactome
    2. negative regulation of transcription, DNA-templated Source: BHF-UCL
    3. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    4. nucleocytoplasmic transport Source: Ensembl
    5. positive regulation of cellular metabolic process Source: Reactome
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_2122. ChREBP activates metabolic gene expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Max-like protein X
    Alternative name(s):
    Class D basic helix-loop-helix protein 13
    Short name:
    bHLHd13
    Max-like bHLHZip protein
    Protein BigMax
    Transcription factor-like protein 4
    Gene namesi
    Name:MLX
    Synonyms:BHLHD13, TCFL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11645. MLX.

    Subcellular locationi

    Isoform Alpha : Cytoplasm
    Note: Found predominantly in the cytoplasm.
    Isoform Beta : Cytoplasm
    Note: Found predominantly in the cytoplasm.
    Isoform Gamma : Nucleus
    Note: Found predominantly in the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti3287. Takayasu arteritis.
    PharmGKBiPA36397.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 298298Max-like protein XPRO_0000127279Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei45 – 451PhosphoserineBy similarity
    Modified residuei48 – 481PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UH92.
    PaxDbiQ9UH92.
    PRIDEiQ9UH92.

    PTM databases

    PhosphoSiteiQ9UH92.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested, including spleen, thymus, prostate, ovary, intestine, colon, peripheral blood leukocyte, heart, liver, skeletal muscle and kidney. Lower levels of expression in testis, brain, placenta and lung.1 Publication

    Gene expression databases

    ArrayExpressiQ9UH92.
    BgeeiQ9UH92.
    CleanExiHS_MLX.
    GenevestigatoriQ9UH92.

    Organism-specific databases

    HPAiCAB025329.

    Interactioni

    Subunit structurei

    Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAD1, MAD4, MNT, WBSCR14 and MLXIP. Can also bind DNA as a homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi112805. 14 interactions.
    IntActiQ9UH92. 7 interactions.
    MINTiMINT-1475792.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UH92.
    SMRiQ9UH92. Positions 125-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 18759bHLHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni140 – 16021Leucine-zipperAdd
    BLAST

    Sequence similaritiesi

    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG259028.
    HOVERGENiHBG019061.
    InParanoidiQ9UH92.
    KOiK09113.
    OMAiPHILRNI.
    OrthoDBiEOG73805M.
    PhylomeDBiQ9UH92.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Gamma (identifier: Q9UH92-1) [UniParc]FASTAAdd to Basket

    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

    MTEPGASPED PWVKASPVGA HAGEGRAGRA RARRGAGRRG ASLLSPKSPT    50
    LSVPRGCRED SSHPACAKVE YAYSDNSLDP GLFVESTRKG SVVSRANSIG 100
    STSASSVPNT DDEDSDYHQE AYKESYKDRR RRAHTQAEQK RRDAIKRGYD 150
    DLQTIVPTCQ QQDFSIGSQK LSKAIVLQKT IDYIQFLHKE KKKQEEEVST 200
    LRKDVTALKI MKVNYEQIVK AHQDNPHEGE DQVSDQVKFN VFQGIMDSLF 250
    QSFNASISVA SFQELSACVF SWIEEHCKPQ TLREIVIGVL HQLKNQLY 298
    Length:298
    Mass (Da):33,300
    Last modified:October 1, 2001 - v2
    Checksum:iD1981730051473C5
    GO
    Isoform Alpha (identifier: Q9UH92-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         15-68: Missing.
         81-110: Missing.

    Show »
    Length:214
    Mass (Da):24,905
    Checksum:i025F90C6F253E56D
    GO
    Isoform Beta (identifier: Q9UH92-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         15-68: Missing.

    Show »
    Length:244
    Mass (Da):27,883
    Checksum:i63EED502A9FA082D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti247 – 2471D → V in AAF14638. (PubMed:10593926)Curated
    Sequence conflicti298 – 2981Y → C in BAA90977. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti223 – 2231Q → R.
    Corresponds to variant rs665268 [ dbSNP | Ensembl ].
    VAR_049547

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei15 – 6854Missing in isoform Alpha and isoform Beta. 5 PublicationsVSP_002137Add
    BLAST
    Alternative sequencei81 – 11030Missing in isoform Alpha. 2 PublicationsVSP_002138Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF203978 mRNA. Translation: AAF14638.1.
    AF213666 mRNA. Translation: AAG40145.1.
    AF213667 mRNA. Translation: AAG40146.1.
    AF213668 mRNA. Translation: AAG40147.1.
    AK000150 mRNA. Translation: BAA90977.1.
    AK290258 mRNA. Translation: BAF82947.1.
    AK314378 mRNA. Translation: BAG37005.1.
    AK315432 mRNA. Translation: BAG37820.1.
    BT009812 mRNA. Translation: AAP88814.1.
    BC010689 mRNA. Translation: AAH10689.1.
    CCDSiCCDS11430.1. [Q9UH92-1]
    CCDS42341.1. [Q9UH92-2]
    CCDS45687.1. [Q9UH92-3]
    PIRiJC5333.
    RefSeqiNP_733752.1. NM_170607.2. [Q9UH92-1]
    NP_937847.1. NM_198204.1. [Q9UH92-3]
    NP_937848.1. NM_198205.1. [Q9UH92-2]
    UniGeneiHs.383019.
    Hs.714749.

    Genome annotation databases

    EnsembliENST00000246912; ENSP00000246912; ENSG00000108788. [Q9UH92-1]
    ENST00000346833; ENSP00000320913; ENSG00000108788. [Q9UH92-2]
    ENST00000435881; ENSP00000416627; ENSG00000108788. [Q9UH92-3]
    GeneIDi6945.
    KEGGihsa:6945.
    UCSCiuc002iaf.3. human. [Q9UH92-3]
    uc002iag.3. human. [Q9UH92-1]
    uc002iah.3. human. [Q9UH92-2]

    Polymorphism databases

    DMDMi20138856.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF203978 mRNA. Translation: AAF14638.1 .
    AF213666 mRNA. Translation: AAG40145.1 .
    AF213667 mRNA. Translation: AAG40146.1 .
    AF213668 mRNA. Translation: AAG40147.1 .
    AK000150 mRNA. Translation: BAA90977.1 .
    AK290258 mRNA. Translation: BAF82947.1 .
    AK314378 mRNA. Translation: BAG37005.1 .
    AK315432 mRNA. Translation: BAG37820.1 .
    BT009812 mRNA. Translation: AAP88814.1 .
    BC010689 mRNA. Translation: AAH10689.1 .
    CCDSi CCDS11430.1. [Q9UH92-1 ]
    CCDS42341.1. [Q9UH92-2 ]
    CCDS45687.1. [Q9UH92-3 ]
    PIRi JC5333.
    RefSeqi NP_733752.1. NM_170607.2. [Q9UH92-1 ]
    NP_937847.1. NM_198204.1. [Q9UH92-3 ]
    NP_937848.1. NM_198205.1. [Q9UH92-2 ]
    UniGenei Hs.383019.
    Hs.714749.

    3D structure databases

    ProteinModelPortali Q9UH92.
    SMRi Q9UH92. Positions 125-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112805. 14 interactions.
    IntActi Q9UH92. 7 interactions.
    MINTi MINT-1475792.

    Chemistry

    ChEMBLi CHEMBL2062357.

    PTM databases

    PhosphoSitei Q9UH92.

    Polymorphism databases

    DMDMi 20138856.

    Proteomic databases

    MaxQBi Q9UH92.
    PaxDbi Q9UH92.
    PRIDEi Q9UH92.

    Protocols and materials databases

    DNASUi 6945.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246912 ; ENSP00000246912 ; ENSG00000108788 . [Q9UH92-1 ]
    ENST00000346833 ; ENSP00000320913 ; ENSG00000108788 . [Q9UH92-2 ]
    ENST00000435881 ; ENSP00000416627 ; ENSG00000108788 . [Q9UH92-3 ]
    GeneIDi 6945.
    KEGGi hsa:6945.
    UCSCi uc002iaf.3. human. [Q9UH92-3 ]
    uc002iag.3. human. [Q9UH92-1 ]
    uc002iah.3. human. [Q9UH92-2 ]

    Organism-specific databases

    CTDi 6945.
    GeneCardsi GC17P040719.
    HGNCi HGNC:11645. MLX.
    HPAi CAB025329.
    MIMi 602976. gene.
    neXtProti NX_Q9UH92.
    Orphaneti 3287. Takayasu arteritis.
    PharmGKBi PA36397.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259028.
    HOVERGENi HBG019061.
    InParanoidi Q9UH92.
    KOi K09113.
    OMAi PHILRNI.
    OrthoDBi EOG73805M.
    PhylomeDBi Q9UH92.
    TreeFami TF318841.

    Enzyme and pathway databases

    Reactomei REACT_2122. ChREBP activates metabolic gene expression.

    Miscellaneous databases

    ChiTaRSi MLX. human.
    GeneWikii MLX_(gene).
    GenomeRNAii 6945.
    NextBioi 27189.
    PROi Q9UH92.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UH92.
    Bgeei Q9UH92.
    CleanExi HS_MLX.
    Genevestigatori Q9UH92.

    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. "Mlx, a novel Max-like bHLHZip protein that interacts with the Max network of transcription factors."
      Billin A.N., Eilers A.L., Queva C., Ayer D.E.
      J. Biol. Chem. 274:36344-36350(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Promyelocyte.
    2. "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?"
      Meroni G., Cairo S., Merla G., Messali S., Brent R., Ballabio A., Reymond A.
      Oncogene 19:3266-3277(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), SUBCELLULAR LOCATION.
    3. "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 ALPHA; BETA AND GAMMA).
      Tissue: Brain and Colon.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
    5. "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] (ISOFORM BETA).
      Tissue: Eye.
    6. "A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex."
      Eilers A.L., Sundwall E., Lin M., Sullivan A.A., Ayer D.E.
      Mol. Cell. Biol. 22:8514-8526(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MLXIP.
    7. "MondoA-Mlx heterodimers are candidate sensors of cellular energy status: mitochondrial localization and direct regulation of glycolysis."
      Sans C.L., Satterwhite D.J., Stoltzman C.A., Breen K.T., Ayer D.E.
      Mol. Cell. Biol. 26:4863-4871(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMLX_HUMAN
    AccessioniPrimary (citable) accession number: Q9UH92
    Secondary accession number(s): A8K2J3
    , B2RAV8, B2RD73, Q53XM6, Q96FL2, Q9H2V0, Q9H2V1, Q9H2V2, Q9NXN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3