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P54841

- MAFB_MOUSE

UniProt

P54841 - MAFB_MOUSE

Protein

Transcription factor MafB

Gene

Mafb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Acts as a transcriptional activator or repressor. Plays a pivotal role in regulating lineage-specific hematopoiesis by repressing ETS1-mediated transcription of erythroid-specific genes in myeloid cells. Required for monocytic, macrophage, podocyte and islet beta cell differentiation. Involved in renal tubule survival and F4/80 maturation. Activates the insulin and glucagon promoters. Together with PAX6, transactivates weakly the glucagon gene promoter through the G1 element. SUMO modification controls its transcriptional activity and ability to specify macrophage fate. Binds element G1 on the glucagon promoter. Involved either as an oncogene or as a tumor suppressor, depending on the cell context.7 Publications

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. protein binding Source: MGI
    3. sequence-specific DNA binding Source: InterPro
    4. sequence-specific DNA binding transcription factor activity Source: InterPro

    GO - Biological processi

    1. brain segmentation Source: MGI
    2. inner ear morphogenesis Source: MGI
    3. negative regulation of erythrocyte differentiation Source: Ensembl
    4. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    5. regulation of transcription from RNA polymerase II promoter Source: MGI
    6. respiratory gaseous exchange Source: MGI
    7. rhombomere 5 development Source: MGI
    8. rhombomere 6 development Source: MGI
    9. segment specification Source: MGI
    10. T cell differentiation in thymus Source: MGI
    11. thymus development Source: MGI
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor MafB
    Short name:
    Maf-B
    Alternative name(s):
    Kreisler
    Segmentation protein Kr
    Transcription factor Maf-1
    V-maf musculoaponeurotic fibrosarcoma oncogene homolog B
    Gene namesi
    Name:Mafb
    Synonyms:Krml, Maf1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:104555. Mafb.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: MGI
    2. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice show a defect in frequency of respiratory rhythm with a fatal apnea at birth due to lack of neurons from the preBoetC region. They displayed renal dysgenesis with abnormal podocyte differentiation as well as tubular apoptosis. They show altered actin-dependent macrophage morphology. They show a reduced number of cells expressing insulin and glucagon.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321K → R: Loss of SUMO modification, increases transactivation activity, increases macrophage differentiation and inhibits myeloid progenitor growth; when associated with R-297. 1 Publication
    Mutagenesisi248 – 2481N → A: Reduces ability to activate insulin and glucagon gene expression. 1 Publication
    Mutagenesisi248 – 2481N → S: Loss of transcriptional activity. 1 Publication
    Mutagenesisi297 – 2971K → R: Loss of SUMO modification, increases transactivation activity, increases macrophage differentiation and inhibits myeloid progenitor growth; when associated with R-32. 1 Publication

    Keywords - Diseasei

    Proto-oncogene, Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Transcription factor MafBPRO_0000076495Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki32 – 32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its transcriptional repression activity and promotes macrophage differentiation from myeloid progenitors.1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP54841.
    PRIDEiP54841.

    PTM databases

    PhosphoSiteiP54841.

    Expressioni

    Tissue specificityi

    Expressed in pancreatic alpha-cells (glucagon-positive cells), in podocytes of the kidney and macrophages (at protein level). Most abundant in kidney, gut, lung and brain.3 Publications

    Developmental stagei

    Expressed in pancreatic alpha-cells at 10.5 dpc. Expressed in insulin and glucagon islet progenitor cells at 12 dpc onwards (at protein level). Detectable at 8.0 dpc (one somite) as a band in the caudal hindbrain and by 8.5 dpc (six to eight somites) as a sharp rostral edge coincident with the rhombomeres (r) 4 and 5 boundary and a diffuse caudal edge located midway through r6. Expressed in the lens epithelial cells at 10.5 to 14.5 dpc.3 Publications

    Gene expression databases

    ArrayExpressiP54841.
    BgeeiP54841.
    CleanExiMM_MAF1.
    GenevestigatoriP54841.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer with other bHLH-Zip transcription factors. Forms homodimers and heterodimers with FOS, FOSB and FOSL2, but not with JUN proteins (JUN, JUNB and JUND). Interacts with the intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction results in a moderate reduction of MAFB transcriptional potential By similarity. Binds DNA as a homodimer or a heterodimer. Interacts with PAX6; the interaction is direct. Interacts with ETS1 and LRP1.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi201014. 5 interactions.
    DIPiDIP-60663N.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi215 – 2184
    Helixi221 – 2255
    Turni228 – 2303
    Helixi233 – 29967

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WT7X-ray2.30B214-303[»]
    2WTYX-ray2.90A/B211-306[»]
    4AUWX-ray2.90A/B/E/F211-305[»]
    ProteinModelPortaliP54841.
    SMRiP54841. Positions 211-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini238 – 30164bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni238 – 26326Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni266 – 28722Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi131 – 14313Poly-HisAdd
    BLAST
    Compositional biasi158 – 16710Poly-His

    Domaini

    The leucine-zipper domain is involved in the interaction with LRPICD.

    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.
    InParanoidiQ3U3C8.
    KOiK09036.
    OMAiHPHHGYP.
    OrthoDBiEOG7BGHMQ.
    PhylomeDBiP54841.
    TreeFamiTF325689.

    Family and domain databases

    Gene3Di1.10.880.10. 1 hit.
    InterProiIPR004827. bZIP.
    IPR004826. bZIP_Maf.
    IPR013592. Maf_TF_N.
    IPR028571. MafB.
    IPR008917. TF_DNA-bd.
    IPR024874. Transciption_factor_Maf.
    [Graphical view]
    PANTHERiPTHR10129. PTHR10129. 1 hit.
    PTHR10129:SF10. PTHR10129:SF10. 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]

    Sequencei

    Sequence statusi: Complete.

    P54841-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAELSMGQE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ    50
    PAGSVSSTPL STPCSSVPSS PSFSPTEPKT HLEDLYWMAS NYQQMNPEAL 100
    NLTPEDAVEA LIGSHPVPQP LQSFDGFRSA HHHHHHHHPH PHHGYPGAGV 150
    THDDLGQHAH PHHHHHHQAS PPPSSAASPA QQLPTSHPGP GPHATAAATA 200
    AGGNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK QKRRTLKNRG 250
    YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK 300
    LANSGFREAG STSDSPSSPE FFL 323
    Length:323
    Mass (Da):35,809
    Last modified:October 1, 1996 - v1
    Checksum:iD77AE07ABD9C2AD2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti275 – 2751Q → K in BAE32860. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36435 mRNA. Translation: AAA65689.1.
    AF180338 Genomic DNA. Translation: AAD56221.1.
    AK132425 mRNA. Translation: BAE21161.1.
    AK143209 mRNA. Translation: BAE25306.1.
    AK154830 mRNA. Translation: BAE32860.1.
    AL591665 Genomic DNA. Translation: CAM21248.1.
    CH466551 Genomic DNA. Translation: EDL06288.1.
    BC016434 mRNA. Translation: AAH16434.1.
    BC038256 mRNA. Translation: AAH38256.1.
    CCDSiCCDS16994.1.
    PIRiI49529.
    RefSeqiNP_034788.1. NM_010658.3.
    UniGeneiMm.330745.

    Genome annotation databases

    EnsembliENSMUST00000099126; ENSMUSP00000096728; ENSMUSG00000074622.
    GeneIDi16658.
    KEGGimmu:16658.
    UCSCiuc008nqw.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36435 mRNA. Translation: AAA65689.1 .
    AF180338 Genomic DNA. Translation: AAD56221.1 .
    AK132425 mRNA. Translation: BAE21161.1 .
    AK143209 mRNA. Translation: BAE25306.1 .
    AK154830 mRNA. Translation: BAE32860.1 .
    AL591665 Genomic DNA. Translation: CAM21248.1 .
    CH466551 Genomic DNA. Translation: EDL06288.1 .
    BC016434 mRNA. Translation: AAH16434.1 .
    BC038256 mRNA. Translation: AAH38256.1 .
    CCDSi CCDS16994.1.
    PIRi I49529.
    RefSeqi NP_034788.1. NM_010658.3.
    UniGenei Mm.330745.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WT7 X-ray 2.30 B 214-303 [» ]
    2WTY X-ray 2.90 A/B 211-306 [» ]
    4AUW X-ray 2.90 A/B/E/F 211-305 [» ]
    ProteinModelPortali P54841.
    SMRi P54841. Positions 211-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201014. 5 interactions.
    DIPi DIP-60663N.

    PTM databases

    PhosphoSitei P54841.

    Proteomic databases

    MaxQBi P54841.
    PRIDEi P54841.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000099126 ; ENSMUSP00000096728 ; ENSMUSG00000074622 .
    GeneIDi 16658.
    KEGGi mmu:16658.
    UCSCi uc008nqw.2. mouse.

    Organism-specific databases

    CTDi 9935.
    MGIi MGI:104555. Mafb.

    Phylogenomic databases

    eggNOGi NOG241084.
    GeneTreei ENSGT00550000074549.
    HOGENOMi HOG000261683.
    HOVERGENi HBG000313.
    InParanoidi Q3U3C8.
    KOi K09036.
    OMAi HPHHGYP.
    OrthoDBi EOG7BGHMQ.
    PhylomeDBi P54841.
    TreeFami TF325689.

    Miscellaneous databases

    ChiTaRSi MAFB. mouse.
    NextBioi 290353.
    PROi P54841.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54841.
    Bgeei P54841.
    CleanExi MM_MAF1.
    Genevestigatori P54841.

    Family and domain databases

    Gene3Di 1.10.880.10. 1 hit.
    InterProi IPR004827. bZIP.
    IPR004826. bZIP_Maf.
    IPR013592. Maf_TF_N.
    IPR028571. MafB.
    IPR008917. TF_DNA-bd.
    IPR024874. Transciption_factor_Maf.
    [Graphical view ]
    PANTHERi PTHR10129. PTHR10129. 1 hit.
    PTHR10129:SF10. PTHR10129:SF10. 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 mouse segmentation gene kr encodes a novel basic domain-leucine zipper transcription factor."
      Cordes S.P., Barsh G.S.
      Cell 79:1025-1034(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning and functional characterization of the mouse mafB gene."
      Huang K., Serria M.S., Nakabayashi H., Nishi S., Sakai M.
      Gene 242:419-426(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    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].
      Strain: C57BL/6J and NOD.
      Tissue: Eye and Skin.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Strain: FVB/N.
      Tissue: Liver and Mammary gland.
    7. "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: DEVELOPMENTAL STAGE.
    8. "MafB is an inducer of monocytic differentiation."
      Kelly L.M., Englmeier U., Lafon I., Sieweke M.H., Graf T.
      EMBO J. 19:1987-1997(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ETS1.
    9. "MafB deficiency causes defective respiratory rhythmogenesis and fatal central apnea at birth."
      Blanchi B., Kelly L.M., Viemari J.-C., Lafon I., Burnet H., Bevengut M., Tillmanns S., Daniel L., Graf T., Hilaire G., Sieweke M.H.
      Nat. Neurosci. 6:1091-1100(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    10. "Low-density lipoprotein receptor-related protein interacts with MafB, a regulator of hindbrain development."
      Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M., Willnow T.E.
      FEBS Lett. 565:23-27(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRP1, SUBCELLULAR LOCATION.
    11. "MafB: an activator of the glucagon gene expressed in developing islet alpha- and beta-cells."
      Artner I., Le Lay J., Hang Y., Elghazi L., Schisler J.C., Henderson E., Sosa-Pineda B., Stein R.
      Diabetes 55:297-304(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    12. Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    13. "Development of macrophages with altered actin organization in the absence of MafB."
      Aziz A., Vanhille L., Mohideen P., Kelly L.M., Otto C., Bakri Y., Mossadegh N., Sarrazin S., Sieweke M.H.
      Mol. Cell. Biol. 26:6808-6818(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    14. "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.
    15. "SUMO modification regulates MafB-driven macrophage differentiation by enabling Myb-dependent transcriptional repression."
      Tillmanns S., Otto C., Jaffray E., Du Roure C., Bakri Y., Vanhille L., Sarrazin S., Hay R.T., Sieweke M.H.
      Mol. Cell. Biol. 27:5554-5564(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUMOYLATION AT LYS-32 AND LYS-297, MUTAGENESIS OF LYS-32 AND LYS-297.
    16. Cited for: DISRUPTION PHENOTYPE.
    17. "Preferential reduction of beta cells derived from Pax6-MafB pathway in MafB deficient mice."
      Nishimura W., Rowan S., Salameh T., Maas R.L., Bonner-Weir S., Sell S.M., Sharma A.
      Dev. Biol. 314:443-456(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASN-248, DISRUPTION PHENOTYPE.
    18. Cited for: REVIEW, FUNCTION.

    Entry informationi

    Entry nameiMAFB_MOUSE
    AccessioniPrimary (citable) accession number: P54841
    Secondary accession number(s): Q3U3C8, Q3UPT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3