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P54843

- MAF_MOUSE

UniProt

P54843 - MAF_MOUSE

Protein

Transcription factor Maf

Gene

Maf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    Acts as a transcriptional activator or repressor. When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters By similarity. Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells. It may interact with additional basic-zipper proteins that determine a subtype of Maf-responsive element binding.By similarity12 Publications

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. protein binding Source: IntAct
    3. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    4. sequence-specific DNA binding Source: MGI
    5. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. cell development Source: MGI
    2. cytokine production Source: MGI
    3. inner ear development Source: MGI
    4. lens development in camera-type eye Source: MGI
    5. lens fiber cell differentiation Source: MGI
    6. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    7. positive regulation of gene expression Source: MGI
    8. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    9. regulation of chondrocyte differentiation Source: MGI
    10. regulation of transcription, DNA-templated Source: MGI

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor Maf
    Alternative name(s):
    Proto-oncogene c-Maf
    V-maf musculoaponeurotic fibrosarcoma oncogene homolog
    Gene namesi
    Name:Maf
    Synonyms:Maf2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:96909. Maf.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Knockout mice lacking this gene exhibit small eyes or microphthalmia with an absence of normal lens structures, an abnormal chondrocyte development, with terminal differentiation of hypertrophic chondrocytes initially delayed, followed by a subsequent expansion of the hypertrophic chondrocyte domain in the growth plates of embryonic and postnatal long bones. They also show a lack of IL4 production.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151S → A: Inhibition on transcriptional activation on CD13 proximal promoter in endothelial cells. 1 Publication
    Mutagenesisi70 – 701S → A: No effect on transcriptional activation on CD13 proximal promoter. Increases liver specific transactivation on the IL-4 promoter. 1 Publication
    Mutagenesisi334 – 3341L → P: Abolishes interaction with USF2. 1 Publication

    Keywords - Diseasei

    Proto-oncogene, Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Transcription factor MafPRO_0000076492Add
    BLAST

    Post-translational modificationi

    Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by glucocorticoids By similarity.By similarity
    Phosphorylated by GSK3 and MAPK13 on serine and threonine residues By similarity. The phosphorylation status can serve to either stimulate or inhibit transcription.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP54843.
    PRIDEiP54843.

    PTM databases

    PhosphoSiteiP54843.

    Expressioni

    Tissue specificityi

    Expressed in tubules of the renal cortex and hepatocytes. Expressed in the lens (at protein level). Expressed in pancreatic islets and endothelial cells.3 Publications

    Developmental stagei

    Expressed in the floor of the diencephalon at 10 dpc (at protein level). Expressed in the midline of the forebrain and in the eye region at 9 dpc. Expressed in the head ectoderm destined to become the lens vesicle at 9 and 10 dpc. Expressed in the lens placode at 10.5 dpc. Expressed in the lens vesicle in both epithelial and fiber cells at 11 dpc. Expressed in secondary fiber cells at the equatorial region that divides the lens into anterior and posterior hemispheres between 11 and 14 dpc. Expressed in the neural tube and in primary fiber cells of the lens at 11.5 dpc. Expressed in proximal tubules of the cortex in the kidney at 16 and 17 dpc. Expressed in hypertrophic chondrocytes at 14.5 to 18.5 dpc. Expressed in the pancreas at 12.5 dpc until the adult stage.5 Publications

    Gene expression databases

    BgeeiP54843.
    GenevestigatoriP54843.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer with other bHLH-Zip transcription factors. Binds DNA as a homodimer or as a heterodimer. Heterotetramer of two MAF and two USF2. Interacts with PAX6; the interaction is direct. Interacts with MYB; interaction takes place weakly in normal T-cells and increases in T-cells following stimulation through the TCR engagement. Interacts with MYB; the ternary complex formed with MYB and the CD13 promoter is regulated in response to differentiating signals. Interacts with USF2; the interaction inhibits its DNA-binding activity on the L7 promoter. Interacts with CREBBP, EP300 and ETS1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Smarca5Q91ZW32EBI-3842521,EBI-927547

    Protein-protein interaction databases

    BioGridi201281. 2 interactions.
    IntActiP54843. 2 interactions.
    MINTiMINT-1131204.

    Structurei

    3D structure databases

    ProteinModelPortaliP54843.
    SMRiP54843. Positions 257-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini285 – 34864bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni126 – 370245Represses ARE-mediated transcriptionBy similarityAdd
    BLAST
    Regioni285 – 31026Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni313 – 33422Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi126 – 251126Gly-richAdd
    BLAST
    Compositional biasi132 – 22493Ala-richAdd
    BLAST
    Compositional biasi180 – 19415His-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the bZIP family. Maf subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG241084.
    GeneTreeiENSGT00550000074549.
    HOGENOMiHOG000261683.
    HOVERGENiHBG000313.
    InParanoidiQ3V1Z2.
    KOiK09035.
    OMAiDRSINQC.
    OrthoDBiEOG7BGHMQ.
    PhylomeDBiP54843.
    TreeFamiTF325689.

    Family and domain databases

    Gene3Di1.10.880.10. 1 hit.
    InterProiIPR004827. bZIP.
    IPR004826. bZIP_Maf.
    IPR013592. Maf_TF_N.
    IPR028573. MafF.
    IPR008917. TF_DNA-bd.
    IPR024874. Transciption_factor_Maf.
    [Graphical view]
    PANTHERiPTHR10129. PTHR10129. 1 hit.
    PTHR10129:SF9. PTHR10129:SF9. 1 hit.
    PfamiPF03131. bZIP_Maf. 1 hit.
    PF08383. Maf_N. 1 hit.
    [Graphical view]
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47454. SSF47454. 1 hit.
    PROSITEiPS50217. BZIP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P54843-1) [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

    MASELAMNNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI    50
    AGGSLSSTPM STPCSSVPPS PSFSAPSPGS GSEQKAHLED YYWMTGYPQQ 100
    LNPEALGFSP EDAVEALISN SHQLQGGFDG YARGAQQLAA AAGAGAGASL 150
    GGSGEEMGPA AAVVSAVIAA AAAQSGAAPH YHHHHHHAAG HHHHPTAGAP 200
    GAAGGASASA SGAGGAGGGG PASAGGGGGG GGGGGTAGAG GALHPHHAAG 250
    GLHFDDRFSD EQLVTMSVRE LNRQLRGVSK EEVIRLKQKR RTLKNRGYAQ 300
    SCRFKRVQQR HVLESEKNQL LQQVDHLKQE ISRLVRERDA YKEKYEKLVS 350
    NGFRENGSSS DNPSSPEFFM 370
    Length:370
    Mass (Da):38,435
    Last modified:February 10, 2009 - v2
    Checksum:i1E8722C8287AAAC9
    GO
    Isoform 2 (identifier: P54843-2) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         370-370: M → MCVCVCALFIL

    Note: No experimental confirmation available.

    Show »
    Length:380
    Mass (Da):39,501
    Checksum:i8A86683B08071901
    GO
    Isoform 3 (identifier: P54843-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         370-370: M → MYPRDSSTSVM

    Note: No experimental confirmation available.

    Show »
    Length:380
    Mass (Da):39,560
    Checksum:i79A6165D907C017B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti202 – 2021A → T in AAB32820. (PubMed:7799931)Curated
    Sequence conflicti208 – 2114ASAS → SSSN in AAB32820. (PubMed:7799931)Curated
    Sequence conflicti223 – 2242SA → NT in AAB32820. (PubMed:7799931)Curated
    Sequence conflicti231 – 2311G → D in AAB32820. (PubMed:7799931)Curated
    Sequence conflicti248 – 2481A → S in AAB32820. (PubMed:7799931)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei370 – 3701M → MCVCVCALFIL in isoform 2. 1 PublicationVSP_036408
    Alternative sequencei370 – 3701M → MYPRDSSTSVM in isoform 3. 1 PublicationVSP_036409

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S74567 mRNA. Translation: AAB32820.1.
    AY560005 mRNA. Translation: AAY81957.1.
    AK132165 mRNA. Translation: BAE21007.1.
    AC113301 Genomic DNA. No translation available.
    CCDSiCCDS40486.1. [P54843-1]
    RefSeqiNP_001020748.2. NM_001025577.2. [P54843-1]
    UniGeneiMm.275549.
    Mm.439772.
    Mm.488377.

    Genome annotation databases

    EnsembliENSMUST00000069009; ENSMUSP00000067704; ENSMUSG00000055435. [P54843-3]
    ENSMUST00000109104; ENSMUSP00000104732; ENSMUSG00000055435. [P54843-1]
    GeneIDi17132.
    KEGGimmu:17132.
    UCSCiuc009noe.2. mouse. [P54843-3]
    uc009nof.1. mouse. [P54843-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S74567 mRNA. Translation: AAB32820.1 .
    AY560005 mRNA. Translation: AAY81957.1 .
    AK132165 mRNA. Translation: BAE21007.1 .
    AC113301 Genomic DNA. No translation available.
    CCDSi CCDS40486.1. [P54843-1 ]
    RefSeqi NP_001020748.2. NM_001025577.2. [P54843-1 ]
    UniGenei Mm.275549.
    Mm.439772.
    Mm.488377.

    3D structure databases

    ProteinModelPortali P54843.
    SMRi P54843. Positions 257-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201281. 2 interactions.
    IntActi P54843. 2 interactions.
    MINTi MINT-1131204.

    PTM databases

    PhosphoSitei P54843.

    Proteomic databases

    MaxQBi P54843.
    PRIDEi P54843.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000069009 ; ENSMUSP00000067704 ; ENSMUSG00000055435 . [P54843-3 ]
    ENSMUST00000109104 ; ENSMUSP00000104732 ; ENSMUSG00000055435 . [P54843-1 ]
    GeneIDi 17132.
    KEGGi mmu:17132.
    UCSCi uc009noe.2. mouse. [P54843-3 ]
    uc009nof.1. mouse. [P54843-1 ]

    Organism-specific databases

    CTDi 4094.
    MGIi MGI:96909. Maf.

    Phylogenomic databases

    eggNOGi NOG241084.
    GeneTreei ENSGT00550000074549.
    HOGENOMi HOG000261683.
    HOVERGENi HBG000313.
    InParanoidi Q3V1Z2.
    KOi K09035.
    OMAi DRSINQC.
    OrthoDBi EOG7BGHMQ.
    PhylomeDBi P54843.
    TreeFami TF325689.

    Miscellaneous databases

    ChiTaRSi MAF. mouse.
    NextBioi 291332.
    PROi P54843.
    SOURCEi Search...

    Gene expression databases

    Bgeei P54843.
    Genevestigatori P54843.

    Family and domain databases

    Gene3Di 1.10.880.10. 1 hit.
    InterProi IPR004827. bZIP.
    IPR004826. bZIP_Maf.
    IPR013592. Maf_TF_N.
    IPR028573. MafF.
    IPR008917. TF_DNA-bd.
    IPR024874. Transciption_factor_Maf.
    [Graphical view ]
    PANTHERi PTHR10129. PTHR10129. 1 hit.
    PTHR10129:SF9. PTHR10129:SF9. 1 hit.
    Pfami PF03131. bZIP_Maf. 1 hit.
    PF08383. Maf_N. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47454. SSF47454. 1 hit.
    PROSITEi PS50217. BZIP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The maf proto-oncogene stimulates transcription from multiple sites in a promoter that directs Purkinje neuron-specific gene expression."
      Kurschner C., Morgan J.I.
      Mol. Cell. Biol. 15:246-254(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
      Tissue: Cerebellum.
    2. "Mafs, Prox1, and Pax6 can regulate chicken betaB1-crystallin gene expression."
      Cui W., Tomarev S.I., Piatigorsky J., Chepelinsky A.B., Duncan M.K.
      J. Biol. Chem. 279:11088-11095(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Strain: C57BL/6J.
      Tissue: Head.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "USF2/FIP associates with the b-Zip transcription factor, c-Maf, via its bHLH domain and inhibits c-Maf DNA binding activity."
      Kurschner C., Morgan J.I.
      Biochem. Biophys. Res. Commun. 231:333-339(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HETEROTETRAMER, INTERACTION WITH USF2, MUTAGENESIS OF LEU-334.
    6. "c-Maf interacts with c-Myb to regulate transcription of an early myeloid gene during differentiation."
      Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.
      Mol. Cell. Biol. 18:2729-2737(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ETS1 AND MYB.
    7. "The transcription factor c-Maf controls the production of interleukin-4 but not other Th2 cytokines."
      Kim J.I., Ho I.-C., Grusby M.J., Glimcher L.H.
      Immunity 10:745-751(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Regulation of lens fiber cell differentiation by transcription factor c-Maf."
      Kawauchi S., Takahashi S., Nakajima O., Ogino H., Morita M., Nishizawa M., Yasuda K., Yamamoto M.
      J. Biol. Chem. 274:19254-19260(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
    9. "Requirement for the c-Maf transcription factor in crystallin gene regulation and lens development."
      Kim J.I., Li T., Ho I.C., Grusby M.J., Glimcher L.H.
      Proc. Natl. Acad. Sci. U.S.A. 96:3781-3785(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    10. "Regulation of mouse lens fiber cell development and differentiation by the Maf gene."
      Ring B.Z., Cordes S.P., Overbeek P.A., Barsh G.S.
      Development 127:307-317(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
    11. "CREB-binding protein/p300 co-activation of crystallin gene expression."
      Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.
      J. Biol. Chem. 277:24081-24089(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CREBBP AND EP300.
    12. "Absence of transcription factor c-maf causes abnormal terminal differentiation of hypertrophic chondrocytes during endochondral bone development."
      MacLean H.E., Kim J.I., Glimcher M.J., Wang J., Kronenberg H.M., Glimcher L.H.
      Dev. Biol. 262:51-63(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
    13. "Developmental contribution of c-maf in the kidney: distribution and developmental study of c-maf mRNA in normal mice kidney and histological study of c-maf knockout mice kidney and liver."
      Imaki J., Tsuchiya K., Mishima T., Onodera H., Kim J.I., Yoshida K., Ikeda H., Sakai M.
      Biochem. Biophys. Res. Commun. 320:1323-1327(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    14. "c-Maf interacts with c-Myb to down-regulate Bcl-2 expression and increase apoptosis in peripheral CD4 cells."
      Peng S., Lalani S., Leavenworth J.W., Ho I.-C., Pauza M.E.
      Eur. J. Immunol. 37:2868-2880(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYB.
    15. "CD13/APN transcription is regulated by the proto-oncogene c-Maf via an atypical response element."
      Mahoney K.M., Petrovic N., Schacke W., Shapiro L.H.
      Gene 403:178-187(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-15 AND SER-70, DNA-BINDING, TISSUE SPECIFICITY.
    16. "Pax-6 and c-Maf functionally interact with the alpha-cell-specific DNA element G1 in vivo to promote glucagon gene expression."
      Gosmain Y., Avril I., Mamin A., Philippe J.
      J. Biol. Chem. 282:35024-35034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PAX6, DNA-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    17. Cited for: REVIEW, FUNCTION.

    Entry informationi

    Entry nameiMAF_MOUSE
    AccessioniPrimary (citable) accession number: P54843
    Secondary accession number(s): Q3V1Z2, Q4QY62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3