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P54843

- MAF_MOUSE

UniProt

P54843 - MAF_MOUSE

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Protein

Transcription factor Maf

Gene

Maf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  3. sequence-specific DNA binding Source: MGI
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP54843.
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

        10         20         30         40         50
MASELAMNNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI
60 70 80 90 100
AGGSLSSTPM STPCSSVPPS PSFSAPSPGS GSEQKAHLED YYWMTGYPQQ
110 120 130 140 150
LNPEALGFSP EDAVEALISN SHQLQGGFDG YARGAQQLAA AAGAGAGASL
160 170 180 190 200
GGSGEEMGPA AAVVSAVIAA AAAQSGAAPH YHHHHHHAAG HHHHPTAGAP
210 220 230 240 250
GAAGGASASA SGAGGAGGGG PASAGGGGGG GGGGGTAGAG GALHPHHAAG
260 270 280 290 300
GLHFDDRFSD EQLVTMSVRE LNRQLRGVSK EEVIRLKQKR RTLKNRGYAQ
310 320 330 340 350
SCRFKRVQQR HVLESEKNQL LQQVDHLKQE ISRLVRERDA YKEKYEKLVS
360 370
NGFRENGSSS DNPSSPEFFM
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 P54843.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 123 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