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MAF (v-maf musculoaponeurotic fibrosarcoma oncogene homolog (avian))

Written2009-11Alain Eychène, Celio Pouponnot
Institut Curie, CNRS UMR 146, Bat110 Centre Universitaire, F-91405 Orsay, France

(Note : for Links provided by Atlas : click)


Alias (NCBI)C-Maf
HGNC Alias symbc-MAF
HGNC Previous namev-maf avian musculoaponeurotic fibrosarcoma oncogene homolog
LocusID (NCBI) 4094
Atlas_Id 41234
Location 16q23.2  [Link to chromosome band 16q23]
Location_base_pair Starts at 79593838 and ends at 79600737 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping MAF.png]
Local_order WWOX, LOC729251, MAF, DYNLRB2, CDYL2.
  MAF (v-maf musculoaponeurotic fibrosarcoma oncogene homolog (avian)) Hybridization with Vysis LSI IGH/MAF dual color, dual fusion probe (Abbott Molecular, US) showing MAF on 16q23.2 (red signals) - Courtesy Adriana Zamecnikova.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
JCHAIN (4q13.3)::MAF (16q23.2)MAF (16q23.2)::IGFBP7 (4q12)MAF (16q23.2)::PATJ (1p31.3)
NSD2 (4p16.3)::MAF (16q23.2)STPG1 (1p36.11)::MAF (16q23.2)


Note The MAF gene is located on chromosome 16q22-q23. Its paralogs MAFA, MAFB and NRL are located on 8q24.3, 20q11.2-q13.1 and 14q11.1-q11.2, respectively. MAF (c-MAF) was first cloned in chicken as the homolog of the founding member of the family, the viral v-MAF gene, encoded by the AS42 retrovirus that induces Musculo Aponeuorotic Fibrosarcoma (M.A.F.) in chicken. The MAF acronym originates from this tumor.
  The two different MAF transcripts are represented. Variant#2 corresponds to unspliced transcript. Variant#1 corresponds to alternative splicing, which contains two exons. Note that the sequence of these two exons is present on transcript variant#2.
Description The MAF gene encodes two isoforms generated through alternative splicing. These two protein isoforms are called the MAF short form and MAF long form. The MAF short form is translated from the longest mRNA (mRNA variant#2) encoded by one exon while the longest is encoded by two exons (mRNA variant#1) (see diagram). These two products differ in their carboxy terminal part, the long form containing 30 extra amino-acids.
Due to putative alternative polyadenylation signals, other transcripts might encode MAF short form.
Transcription MAF is expressed in many tissues, but its expression is lineage-specific within a given tissue. For example in T cells, MAF is expressed only in the TH2 lineage.


Note The Maf oncoproteins are b-ZIP transcription factors that belong to the AP-1 super-family, which notably includes JUN and FOS. The Maf family contains seven members, which can be subdivided into two subfamilies: the large and small Maf proteins. While the small Maf proteins, MAFF, MAFG and MAFK, are essentially composed of a b-Zip domain, the large Maf proteins, MAFA/L-MAF, MAFB, MAF/c-MAF and NRL contain an additional amino-terminal transactivation domain. Consequently, as homodimers large Maf activate transcription while small Maf repress it. Two different isoforms exist for MAF, which differ in their carboxy-terminus. The short form is constituted of 373 amino acids while the longest form contains 30 additional amino-acids. No specific function has been attributed to these two products.
  Schematic representation of MAF protein structure. The two different isoforms are depicted. The basic, leucine zipper, and EHR domains are indicated. The basic domain contacts directly DNA while the leucine zipper allows dimerization, which is a prerequisite for DNA binding. The EHR domain (extended homology region) is specific for the Maf proteins and is required for Maf binding to DNA. MAF protein is phosphorylated by GSK3, although the residues involved have not been formally identified. Putative GSK3 phosphorylation sites are indicated by analogy with MAFA. Phosphorylation of MAFA transactivation domain by GSK3 induces its ubiquitination and proteasome-dependent degradation. This is coupled to an increase in MAFA transactivating activity. These phosphorylations are required for MAFA transforming activity. Like MAFA and MAFB, MAF is also subjected to sumoylation, which decreases its transactivating activity. The sumoylated Lysine (K33) is indicated.
Description MAF, like all large Maf proteins, contains an amino-terminal transactivation domain and a carboxy-terminal b-ZIP DNA binding domain. Large Maf proteins stimulate transcription of their target genes through their binding to two types of palindromic sequences called TRE- or CRE- type MARE (Maf Responsive Element) (TGCTGACTCAGCA and TGCTGACGTCAGCA, respectively). The Extended Homology Region (EHR, also called ancillary domain, which is specific of the Maf proteins, allows them to recognize a longer palindromic sequence than other AP-1 family members. The MARE sequence is composed of a TRE or CRE core (underlined) flanked by a TGC sequence. While the TGC motif is crucial for Maf binding, the TRE/CRE core can be more degenerate. As other large Maf, MAF is post-translationaly modified by phosphorylation, sumoylation and ubiquitination, mostly occurring in its amino-terminal transactivation domain. Due to posttranslational modifications, notably through GSK3-mediated phosphorylation, MAF apparent molecular weight differs from the calculated one. The protein migrates as different forms ranging from 35 to 50 kDa in SDS-PAGE.
Expression MAF is expressed in many tissues including neural tissue, kidney and lens. However, its expression is lineage-specific within a given tissue. In T cells for example, MAF is expressed only in the TH2 lineage.
Localisation MAF is a nuclear protein.
Function MAF is a transcription factor of the b-Zip family that contacts DNA as homo- or hetero- dimers. MAF knockout mice show peri-natal lethality. They are microphthalmic secondary to defective lens formation. Knockout studies have revealed key roles for MAF in lens terminal differentiation where it regulates the expression of the crystallins, in the specification of the TH2 lineage by regulating the expression of the TH2-specific IL4 cytokine, as well as in chondrocyte terminal differentiation. The role of MAF in lens development is further highlighted by the existence of MAF germinal mutations responsible for congenital cataract in human.
Beside its physiological roles, MAF is an oncogene involved in human cancers (see below).
Homology MAF belongs to the AP-1 superfamilly that includes the JUN, FOS, ATF, CREB and Maf family. The Maf family is composed of seven members: the large Maf: MAF, MAFB, MAFA and NRL and the small Maf: MAFF, MAFG, MAFK that are highly homologous in their EHR- b-ZIP domains. Large Maf are closest to each others, MAF showing 77%, 67% and 53% identities with MAFB, MAFA and NRL, respectively. An ortholog of the large MAF, called TrafficJam, is found in Drosophila.


Germinal Congenital cataract (see below)

Implicated in

Entity Multiple myeloma
Disease Multiple myeloma (cancer of plasma B cells).
Prognosis MAF translocations are of poor prognosis.
Cytogenetics .
Abnormal Protein No fusion protein. These translocations lead to the juxtaposition of a strong immunoglobulin enhancer to the MAF promoter leading to its strong ectopic expression.
Oncogenesis Large Maf proteins, MAFA, MAFB and MAF/c-MAF, are bona fide oncoproteins as demonstrated in tissue culture, animal models and in human cancer. Their oncogenic activity depends on their ability to act as transcription factors, relies on overexpression and does not require activating mutations (no such mutations have been found in human cancers), although it can be enhanced by point mutation. It is noteworthy that the transforming activity of Maf proteins is context-dependent. It is regulated by post-translational modifications, notably phosphorylation. They can occasionally display tumor suppressor-like activity in specific cellular settings. In embryonic fibroblasts, MAFA displays the strongest transforming activity. Its transforming activity depends on its phosphorylation by GSK3. In human, MAF/c-MAF, MAFB and MAFA genes are translocated to the immunoglobulin heavy chain (IgH) locus in 8-10% of multiple myelomas (MM). These translocations lead to overexpression through a strong enhancer effect without any alteration in their coding sequence. MAF translocations are present in 5% of MM. Beside these translocations, MAF is overexpressed in 50% of MM through an unknown mechanism. MAF overexpression plays a causative role in MM by promoting proliferation through cyclinD2 (CCND2) induction. It also promotes the pathological interactions of bone marrow stroma with cancer cells by enhancing integrin B7 (ITGB7) expression. These pathological cellular interactions lead to increased production of the angiogenic cytokine VEGF. MAF also activates the Ser/Thr AKT activity by inducing the expression of DEPTOR (DEPDC6), an inhibitor of mTORC1 and mTORC2 complexes.
While MM is associated with osteolytic lesions, patients with MAF deregulation show low incidence of bone disease. This observation is correlated with low expression by MAF-expressing myeloma cells of DKK1, a Wnt antagonist associated with bone disease in MM.
Chemical screens have identified glucocorticoids as potential therapeutical agents that target MAF activity through ubiquitin dependent degradation.
Entity Angioimmunoblastic T cell lymphoma
Prognosis Not determined.
Oncogenesis MAF has been shown to be overexpressed in 60% of angioimmunoblastic T cell lymphoma. The mechanisms underlying these deregulations are unknown. Although its causative role has not been demonstrated, its deregulation, as in multiple myeloma, is associated to that of CCND2 and ITGB7. MAF has also been found overexpressed in diverse human T cell lymphomas. Accordingly, MAF overexpression in the T cell compartment leads to T cell lymphoma associated with CCND2 and ITGB7 overexpression in transgenic mice.
Entity Congenital cataract
Disease In human, the MAF gene is mutated in congenital cataract that could be associated with microcornea or colomboma. These heterozygote point mutations correspond to residues located in the DNA binding domain and appear to be dominant. They disrupt DNA binding activity by targeting the different conserved basic residues R288P, K297R and R299S. Another mutation in the leucine zipper dimerization domain (K320E) was reported. In support for a role of MAF in congenital cataract, knockout studies in mice have demonstrated an important role of MAF during lens development. Moreover, heterozygote point mutants of murine MAF in its transactivation (D90V) or basic domain (R291Q, corresponding to human residue R294) lead to cataract in mice.
Critical residues mutated in congenital cataract in human and mice are indicated.


Frequent dysregulation of the c-maf proto-oncogene at 16q23 by translocation to an Ig locus in multiple myeloma.
Chesi M, Bergsagel PL, Shonukan OO, Martelli ML, Brents LA, Chen T, Schrock E, Ried T, Kuehl WM.
Blood. 1998 Jun 15;91(12):4457-63.
PMID 9616139
A new MAFia in cancer.
Eychene A, Rocques N, Pouponnot C.
Nat Rev Cancer. 2008 Sep;8(9):683-93. (REVIEW)
PMID 18701893
Maf transcriptionally activates the mouse p53 promoter and causes a p53-dependent cell death.
Hale TK, Myers C, Maitra R, Kolzau T, Nishizawa M, Braithwaite AW.
J Biol Chem. 2000 Jun 16;275(24):17991-9.
PMID 10747965
Novel MAF mutation in a family with congenital cataract-microcornea syndrome.
Hansen L, Eiberg H, Rosenberg T.
Mol Vis. 2007 Oct 18;13:2019-22.
PMID 17982426
Comprehensive mutational screening in a cohort of Danish families with hereditary congenital cataract.
Hansen L, Mikkelsen A, Nurnberg P, Nurnberg G, Anjum I, Eiberg H, Rosenberg T.
Invest Ophthalmol Vis Sci. 2009 Jul;50(7):3291-303. Epub 2009 Jan 31.
PMID 19182255
c-Maf interacts with c-Myb to regulate transcription of an early myeloid gene during differentiation.
Hedge SP, Kumar A, Kurschner C, Shapiro LH.
Mol Cell Biol. 1998 May;18(5):2729-37.
PMID 9566892
Advances in biology of multiple myeloma: clinical applications.
Hideshima T, Bergsagel PL, Kuehl WM, Anderson KC.
Blood. 2004 Aug 1;104(3):607-18. Epub 2004 Apr 15. (REVIEW)
PMID 15090448
The proto-oncogene c-maf is responsible for tissue-specific expression of interleukin-4.
Ho IC, Hodge MR, Rooney JW, Glimcher LH.
Cell. 1996 Jun 28;85(7):973-83.
PMID 8674125
Overexpression of c-maf is a frequent oncogenic event in multiple myeloma that promotes proliferation and pathological interactions with bone marrow stroma.
Hurt EM, Wiestner A, Rosenwald A, Shaffer AL, Campo E, Grogan T, Bergsagel PL, Kuehl WM, Staudt LM.
Cancer Cell. 2004 Feb;5(2):191-9.
PMID 14998494
Domain disruption and mutation of the bZIP transcription factor, MAF, associated with cataract, ocular anterior segment dysgenesis and coloboma.
Jamieson RV, Perveen R, Kerr B, Carette M, Yardley J, Heon E, Wirth MG, van Heyningen V, Donnai D, Munier F, Black GC.
Hum Mol Genet. 2002 Jan 1;11(1):33-42.
PMID 11772997
Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun.
Kataoka K, Noda M, Nishizawa M.
Mol Cell Biol. 1994 Jan;14(1):700-12.
PMID 8264639
Multiple mechanisms and functions of maf transcription factors in the regulation of tissue-specific genes.
Kataoka K.
J Biochem. 2007 Jun;141(6):775-81. (REVIEW)
PMID 17569705
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. 1999 Jul 2;274(27):19254-60.
PMID 10383433
The transcription factor c-Maf controls the production of interleukin-4 but not other Th2 cytokines.
Kim JI, Ho IC, Grusby MJ, Glimcher LH.
Immunity. 1999 Jun;10(6):745-51.
PMID 10403649
Requirement for the c-Maf transcription factor in crystallin gene regulation and lens development.
Kim JI, Li T, Ho IC, Grusby MJ, Glimcher LH.
Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3781-5.
PMID 10097114
Multiple myeloma: evolving genetic events and host interactions.
Kuehl WM, Bergsagel PL.
Nat Rev Cancer. 2002 Mar;2(3):175-87. (REVIEW)
PMID 11990854
SUMO conjugation contributes to immune deviation in nonobese diabetic mice by suppressing c-Maf transactivation of IL-4.
Leavenworth JW, Ma X, Mo YY, Pauza ME.
J Immunol. 2009 Jul 15;183(2):1110-9. Epub 2009 Jun 24.
PMID 19553542
Comparison of maf gene expression patterns during chick embryo development.
Lecoin L, Sii-Felice K, Pouponnot C, Eychene A, Felder-Schmittbuhl MP.
Gene Expr Patterns. 2004 Jan;4(1):35-46.
PMID 14678826
Absence of transcription factor c-maf causes abnormal terminal differentiation of hypertrophic chondrocytes during endochondral bone development.
MacLean HE, Kim JI, Glimcher MJ, Wang J, Kronenberg HM, Glimcher LH.
Dev Biol. 2003 Oct 1;262(1):51-63.
PMID 14512017
A chemical biology screen identifies glucocorticoids that regulate c-maf expression by increasing its proteasomal degradation through up-regulation of ubiquitin.
Mao X, Stewart AK, Hurren R, Datti A, Zhu X, Zhu Y, Shi C, Lee K, Tiedemann R, Eberhard Y, Trudel S, Liang S, Corey SJ, Gillis LC, Barber DL, Wrana JL, Ezzat S, Schimmer AD.
Blood. 2007 Dec 1;110(12):4047-54. Epub 2007 Sep 17.
PMID 17875808
Gene expression profiling of plasma cell dyscrasias reveals molecular patterns associated with distinct IGH translocations in multiple myeloma.
Mattioli M, Agnelli L, Fabris S, Baldini L, Morabito F, Bicciato S, Verdelli D, Intini D, Nobili L, Cro L, Pruneri G, Callea V, Stelitano C, Maiolo AT, Lombardi L, Neri A.
Oncogene. 2005 Apr 7;24(15):2461-73.
PMID 15735737
TACI expression is associated with a mature bone marrow plasma cell signature and C-MAF overexpression in human myeloma cell lines.
Moreaux J, Hose D, Jourdan M, Reme T, Hundemer M, Moos M, Robert N, Moine P, De Vos J, Goldschmidt H, Klein B.
Haematologica. 2007 Jun;92(6):803-11.
PMID 17550853
Overexpression of c-Maf contributes to T-cell lymphoma in both mice and human.
Morito N, Yoh K, Fujioka Y, Nakano T, Shimohata H, Hashimoto Y, Yamada A, Maeda A, Matsuno F, Hata H, Suzuki A, Imagawa S, Mitsuya H, Esumi H, Koyama A, Yamamoto M, Mori N, Takahashi S.
Cancer Res. 2006 Jan 15;66(2):812-9.
PMID 16424013
c-Maf expression in angioimmunoblastic T-cell lymphoma.
Murakami YI, Yatabe Y, Sakaguchi T, Sasaki E, Yamashita Y, Morito N, Yoh K, Fujioka Y, Matsuno F, Hata H, Mitsuya H, Imagawa S, Suzuki A, Esumi H, Sakai M, Takahashi S, Mori N.
Am J Surg Pathol. 2007 Nov;31(11):1695-702.
PMID 18059226
Characterization of c-Maf transcription factor in normal and neoplastic hematolymphoid tissue and its relevance in plasma cell neoplasia.
Natkunam Y, Tedoldi S, Paterson JC, Zhao S, Rodriguez-Justo M, Beck AH, Siebert R, Mason DY, Marafioti T.
Am J Clin Pathol. 2009 Sep;132(3):361-71.
PMID 19687312
MafA has strong cell transforming ability but is a weak transactivator.
Nishizawa M, Kataoka K, Vogt PK.
Oncogene. 2003 Sep 11;22(39):7882-90.
PMID 12970735
DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival.
Peterson TR, Laplante M, Thoreen CC, Sancak Y, Kang SA, Kuehl WM, Gray NS, Sabatini DM.
Cell. 2009 May 29;137(5):873-86. Epub 2009 May 14.
PMID 19446321
Cell context reveals a dual role for Maf in oncogenesis.
Pouponnot C, Sii-Felice K, Hmitou I, Rocques N, Lecoin L, Druillennec S, Felder-Schmittbuhl MP, Eychene A.
Oncogene. 2006 Mar 2;25(9):1299-310.
PMID 16247450
C-MAF oncogene dysregulation in multiple myeloma: frequency and biological relevance.
Rasmussen T, Knudsen LM, Dahl IM, Johnsen HE.
Leuk Lymphoma. 2003 Oct;44(10):1761-6.
PMID 14692531
Regulation of mouse lens fiber cell development and differentiation by the Maf gene.
Ring BZ, Cordes SP, Overbeek PA, Barsh GS.
Development. 2000 Jan;127(2):307-17.
PMID 10603348
Osteopontin dysregulation and lytic bone lesions in multiple myeloma.
Robbiani DF, Colon K, Ely S, Ely S, Chesi M, Bergsagel PL.
Hematol Oncol. 2007 Mar;25(1):16-20.
PMID 17044113
GSK-3-mediated phosphorylation enhances Maf-transforming activity.
Rocques N, Abou Zeid N, Sii-Felice K, Lecoin L, Felder-Schmittbuhl MP, Eychene A, Pouponnot C.
Mol Cell. 2007 Nov 30;28(4):584-97.
PMID 18042454
ARK5 is transcriptionally regulated by the Large-MAF family and mediates IGF-1-induced cell invasion in multiple myeloma: ARK5 as a new molecular determinant of malignant multiple myeloma.
Suzuki A, Iida S, Kato-Uranishi M, Tajima E, Zhan F, Hanamura I, Huang Y, Ogura T, Takahashi S, Ueda R, Barlogie B, Shaughnessy J Jr, Esumi H.
Oncogene. 2005 Oct 20;24(46):6936-44.
PMID 16044163
CS1 promotes multiple myeloma cell adhesion, clonogenic growth, and tumorigenicity via c-maf-mediated interactions with bone marrow stromal cells.
Tai YT, Soydan E, Song W, Fulciniti M, Kim K, Hong F, Li XF, Burger P, Rumizen MJ, Nahar S, Podar K, Hideshima T, Munshi NC, Tonon G, Carrasco RD, Afar DE, Anderson KC.
Blood. 2009 Apr 30;113(18):4309-18. Epub 2009 Feb 4. Erratum in: Blood. 2009 Sep 24;114(13):2852.
PMID 19196658
Genetic aberrations and survival in plasma cell leukemia.
Tiedemann RE, Gonzalez-Paz N, Kyle RA, Santana-Davila R, Price-Troska T, Van Wier SA, Chng WJ, Ketterling RP, Gertz MA, Henderson K, Greipp PR, Dispenzieri A, Lacy MQ, Rajkumar SV, Bergsagel PL, Stewart AK, Fonseca R.
Leukemia. 2008 May;22(5):1044-52. Epub 2008 Jan 24.
PMID 18216867
A novel mutation in the DNA-binding domain of MAF at 16q23.1 associated with autosomal dominant "cerulean cataract" in an Indian family.
Vanita V, Singh D, Robinson PN, Sperling K, Singh JR.
Am J Med Genet A. 2006 Mar 15;140(6):558-66.
PMID 16470690
Large Maf Transcription Factors: Cousins of AP-1 Proteins and Important Regulators of Cellular Differentiation.
Yang Y, Cvekl A.
Einstein J Biol Med. 2007;23(1):2-11. (REVIEW)
PMID 18159220
CKS1B, overexpressed in aggressive disease, regulates multiple myeloma growth and survival through SKP2- and p27Kip1-dependent and -independent mechanisms.
Zhan F, Colla S, Wu X, Chen B, Stewart JP, Kuehl WM, Barlogie B, Shaughnessy JD Jr.
Blood. 2007 Jun 1;109(11):4995-5001. Epub 2007 Feb 15.
PMID 17303695
The molecular classification of multiple myeloma.
Zhan F, Huang Y, Colla S, Stewart JP, Hanamura I, Gupta S, Epstein J, Yaccoby S, Sawyer J, Burington B, Anaissie E, Hollmig K, Pineda-Roman M, Tricot G, van Rhee F, Walker R, Zangari M, Crowley J, Barlogie B, Shaughnessy JD Jr.
Blood. 2006 Sep 15;108(6):2020-8. Epub 2006 May 25.
PMID 16728703
Identification of primary MAFB target genes in multiple myeloma.
van Stralen E, van de Wetering M, Agnelli L, Neri A, Clevers HC, Bast BJ.
Exp Hematol. 2009 Jan;37(1):78-86. Epub 2008 Nov 13.
PMID 19013005


This paper should be referenced as such :
Eychöne, A ; Pouponnot, C
MAF (v-maf musculoaponeurotic fibrosarcoma oncogene homolog (avian))
Atlas Genet Cytogenet Oncol Haematol. 2010;14(9):822-826.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 3 ]
  Multiple myeloma (published in 2004)
Multiple Myeloma
t(14;16)(q32;q23) IGH::MAF

External links


HGNC (Hugo)MAF   6776
Atlas Explorer : (Salamanque)MAF
Entrez_Gene (NCBI)MAF    MAF bZIP transcription factor
AliasesAYGRP; CCA4; CTRCT21; c-MAF
GeneCards (Weizmann)MAF
Ensembl hg19 (Hinxton)ENSG00000178573 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000178573 [Gene_View]  ENSG00000178573 [Sequence]  chr16:79593838-79600737 [Contig_View]  MAF [Vega]
ICGC DataPortalENSG00000178573
TCGA cBioPortalMAF
Genatlas (Paris)MAF
SOURCE (Princeton)MAF
Genetics Home Reference (NIH)MAF
Genomic and cartography
GoldenPath hg38 (UCSC)MAF  -     chr16:79593838-79600737 -  16q23.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)MAF  -     16q23.2   [Description]    (hg19-Feb_2009)
GoldenPathMAF - 16q23.2 [CytoView hg19]  MAF - 16q23.2 [CytoView hg38]
Genome Data Viewer NCBIMAF [Mapview hg19]  
OMIM177075   601088   610202   
Gene and transcription
Genbank (Entrez)AF055376 AF055377 AF447709 AF540388 BC038438
RefSeq transcript (Entrez)NM_001031804 NM_005360
Consensus coding sequences : CCDS (NCBI)MAF
Gene ExpressionMAF [ NCBI-GEO ]   MAF [ EBI - ARRAY_EXPRESS ]   MAF [ SEEK ]   MAF [ MEM ]
Gene Expression Viewer (FireBrowse)MAF [ Firebrowse - Broad ]
GenevisibleExpression of MAF in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)4094
GTEX Portal (Tissue expression)MAF
Human Protein AtlasENSG00000178573-MAF [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO75444   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO75444  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO75444
Domaine pattern : Prosite (Expaxy)BZIP (PS50217)   
Domains : Interpro (EBI)bZIP    bZIP_Maf    Maf/V-MAF    Maf_TF_N    TF_DNA-bd_sf    Transcription_factor_Maf_fam   
Domain families : Pfam (Sanger)bZIP_Maf (PF03131)    Maf_N (PF08383)   
Domain families : Pfam (NCBI)pfam03131    pfam08383   
Domain families : Smart (EMBL)BRLZ (SM00338)  
Conserved Domain (NCBI)MAF
AlphaFold pdb e-kbO75444   
Human Protein Atlas [tissue]ENSG00000178573-MAF [tissue]
Protein Interaction databases
IntAct (EBI)O75444
Ontologies - Pathways
Ontology : AmiGOnegative regulation of transcription by RNA polymerase II  chromatin  RNA polymerase II cis-regulatory region sequence-specific DNA binding  DNA-binding transcription factor activity, RNA polymerase II-specific  DNA-binding transcription factor activity, RNA polymerase II-specific  DNA-binding transcription activator activity, RNA polymerase II-specific  protein binding  nucleus  cytoplasm  regulation of transcription by RNA polymerase II  transcription by RNA polymerase II  positive regulation of gene expression  regulation of chondrocyte differentiation  identical protein binding  positive regulation of transcription by RNA polymerase II  cell development  inner ear development  lens fiber cell differentiation  RNA polymerase II transcription regulator complex  sequence-specific double-stranded DNA binding  
Ontology : EGO-EBInegative regulation of transcription by RNA polymerase II  chromatin  RNA polymerase II cis-regulatory region sequence-specific DNA binding  DNA-binding transcription factor activity, RNA polymerase II-specific  DNA-binding transcription factor activity, RNA polymerase II-specific  DNA-binding transcription activator activity, RNA polymerase II-specific  protein binding  nucleus  cytoplasm  regulation of transcription by RNA polymerase II  transcription by RNA polymerase II  positive regulation of gene expression  regulation of chondrocyte differentiation  identical protein binding  positive regulation of transcription by RNA polymerase II  cell development  inner ear development  lens fiber cell differentiation  RNA polymerase II transcription regulator complex  sequence-specific double-stranded DNA binding  
REACTOMEO75444 [protein]
REACTOME PathwaysR-HSA-8940973 [pathway]   
NDEx NetworkMAF
Atlas of Cancer Signalling NetworkMAF
Wikipedia pathwaysMAF
Orthology - Evolution
GeneTree (enSembl)ENSG00000178573
Phylogenetic Trees/Animal Genes : TreeFamMAF
Homologs : HomoloGeneMAF
Homology/Alignments : Family Browser (UCSC)MAF
Gene fusions - Rearrangements
Fusion : MitelmanIGH::MAF [14q32.33/16q23.2]  
Fusion : MitelmanIGL::MAF [22q11.22/16q23.2]  
Fusion : MitelmanMAF::IGFBP7 [16q23.2/4q12]  
Fusion : FusionHubAC092376.1--MAF    EIF4B--MAF    IGF2--MAF    IGH@--MAF    IGL@--MAF    KLHDC4--MAF    MAF--CPSF3    MAF--CTA    MAF--DNAJC14    MAF--IGF2   
MAF--IGH    MAF--MAFB    MAF--PEX16    MAF--RP11-679B19.2    MAF--SMARCA4    MAF--YY1    MAFB--MAF   
Fusion : QuiverMAF
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerMAF [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)MAF
Exome Variant ServerMAF
GNOMAD BrowserENSG00000178573
Varsome BrowserMAF
ACMGMAF variants
Genomic Variants (DGV)MAF [DGVbeta]
DECIPHERMAF [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisMAF 
ICGC Data PortalMAF 
TCGA Data PortalMAF 
Broad Tumor PortalMAF
OASIS PortalMAF [ Somatic mutations - Copy number]
Cancer Gene: CensusMAF 
Somatic Mutations in Cancer : COSMICMAF  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DMAF
Mutations and Diseases : HGMDMAF
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)MAF
DoCM (Curated mutations)MAF
CIViC (Clinical Interpretations of Variants in Cancer)MAF
NCG (London)MAF
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM177075    601088    610202   
Orphanet1584    3187    14006    14001   
Genetic Testing Registry MAF
NextProtO75444 [Medical]
Target ValidationMAF
Huge Navigator MAF [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDMAF
Pharm GKB GenePA30534
Pharm GKB PathwaysPA165985892   
Clinical trialMAF
DataMed IndexMAF
PubMed115 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Thu Jan 20 14:10:58 CET 2022

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