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P54841 (MAFB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Mafb
Synonyms:Krml, Maf1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17 Ref.18

Subunit structure

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. Ref.8 Ref.10 Ref.14

Subcellular location

Nucleus Ref.10.

Tissue specificity

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. Ref.11 Ref.12 Ref.14

Developmental stage

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. Ref.7 Ref.11 Ref.14

Domain

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

Post-translational modification

Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its transcriptional repression activity and promotes macrophage differentiation from myeloid progenitors. Ref.15

Disruption phenotype

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. Ref.9 Ref.12 Ref.13 Ref.16 Ref.17

Sequence similarities

Belongs to the bZIP family. Maf subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseProto-oncogene
Tumor suppressor
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation in thymus

Inferred from mutant phenotype PubMed 19164599. Source: MGI

brain segmentation

Inferred from mutant phenotype PubMed 7925021. Source: MGI

inner ear morphogenesis

Inferred from mutant phenotype PubMed 16325169. Source: MGI

negative regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12798298. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12701106. Source: MGI

respiratory gaseous exchange

Inferred from mutant phenotype Ref.9. Source: MGI

rhombomere 5 development

Inferred from mutant phenotype PubMed 7925021. Source: MGI

rhombomere 6 development

Inferred from mutant phenotype PubMed 7925021. Source: MGI

segment specification

Inferred from mutant phenotype PubMed 12701106. Source: MGI

thymus development

Inferred from mutant phenotype PubMed 19164599. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from direct assay PubMed 12917329. Source: MGI

transcription factor complex

Inferred from direct assay PubMed 12798298. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12701106PubMed 12798298. Source: MGI

protein binding

Inferred from physical interaction PubMed 12798298. Source: MGI

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Transcription factor MafB
PRO_0000076495

Regions

Domain238 – 30164bZIP
Region238 – 26326Basic motif By similarity
Region266 – 28722Leucine-zipper By similarity
Compositional bias131 – 14313Poly-His
Compositional bias158 – 16710Poly-His

Amino acid modifications

Cross-link32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.15
Cross-link297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.15

Experimental info

Mutagenesis321K → R: Loss of SUMO modification, increases transactivation activity, increases macrophage differentiation and inhibits myeloid progenitor growth; when associated with R-297. Ref.15
Mutagenesis2481N → A: Reduces ability to activate insulin and glucagon gene expression. Ref.17
Mutagenesis2481N → S: Loss of transcriptional activity. Ref.17
Mutagenesis2971K → R: Loss of SUMO modification, increases transactivation activity, increases macrophage differentiation and inhibits myeloid progenitor growth; when associated with R-32. Ref.15
Sequence conflict2751Q → K in BAE32860. Ref.3

Secondary structure

......... 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54841 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D77AE07ABD9C2AD2

FASTA32335,809
        10         20         30         40         50         60 
MAAELSMGQE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ PAGSVSSTPL 

        70         80         90        100        110        120 
STPCSSVPSS PSFSPTEPKT HLEDLYWMAS NYQQMNPEAL NLTPEDAVEA LIGSHPVPQP 

       130        140        150        160        170        180 
LQSFDGFRSA HHHHHHHHPH PHHGYPGAGV THDDLGQHAH PHHHHHHQAS PPPSSAASPA 

       190        200        210        220        230        240 
QQLPTSHPGP GPHATAAATA AGGNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK 

       250        260        270        280        290        300 
QKRRTLKNRG YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK 

       310        320 
LANSGFREAG STSDSPSSPE FFL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"MafB is essential for renal development and F4/80 expression in macrophages."
Moriguchi T., Hamada M., Morito N., Terunuma T., Hasegawa K., Zhang C., Yokomizo T., Esaki R., Kuroda E., Yoh K., Kudo T., Nagata M., Greaves D.R., Engel J.D., Yamamoto M., Takahashi S.
Mol. Cell. Biol. 26:5715-5727(2006) [PubMed] [Europe PMC] [Abstract]
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]"MafB is required for islet beta cell maturation."
Artner I., Blanchi B., Raum J.C., Guo M., Kaneko T., Cordes S., Sieweke M., Stein R.
Proc. Natl. Acad. Sci. U.S.A. 104:3853-3858(2007) [PubMed] [Europe PMC] [Abstract]
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]"A new MAFia in cancer."
Eychene A., Rocques N., Pouponnot C.
Nat. Rev. Cancer 8:683-693(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS16994.1.
PIRI49529.
RefSeqNP_034788.1. NM_010658.3.
UniGeneMm.330745.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WT7X-ray2.30B214-303[»]
2WTYX-ray2.90A/B211-306[»]
4AUWX-ray2.90A/B/E/F211-305[»]
ProteinModelPortalP54841.
SMRP54841. Positions 211-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201014. 5 interactions.
DIPDIP-60663N.

PTM databases

PhosphoSiteP54841.

Proteomic databases

MaxQBP54841.
PRIDEP54841.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099126; ENSMUSP00000096728; ENSMUSG00000074622.
GeneID16658.
KEGGmmu:16658.
UCSCuc008nqw.2. mouse.

Organism-specific databases

CTD9935.
MGIMGI:104555. Mafb.

Phylogenomic databases

eggNOGNOG241084.
GeneTreeENSGT00550000074549.
HOGENOMHOG000261683.
HOVERGENHBG000313.
InParanoidQ3U3C8.
KOK09036.
OMAHPHHGYP.
OrthoDBEOG7BGHMQ.
PhylomeDBP54841.
TreeFamTF325689.

Gene expression databases

ArrayExpressP54841.
BgeeP54841.
CleanExMM_MAF1.
GenevestigatorP54841.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028571. MafB.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF10. PTHR10129:SF10. 1 hit.
PfamPF03131. bZIP_Maf. 1 hit.
PF08383. Maf_N. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAFB. mouse.
NextBio290353.
PROP54841.
SOURCESearch...

Entry information

Entry nameMAFB_MOUSE
AccessionPrimary (citable) accession number: P54841
Secondary accession number(s): Q3U3C8, Q3UPT9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot