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Q9Y5Q3 (MAFB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
V-maf musculoaponeurotic fibrosarcoma oncogene homolog B
Gene names
Name:MAFB
Synonyms:KRML
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 By similarity. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Ref.9

Subunit structure

Homodimer or heterodimer with other bHLH-Zip transcription factors. Binds DNA as a homodimer or a heterodimer. Forms homodimers and heterodimers with FOS, FOSB and FOSL2, but not with JUN proteins (JUN, JUNB and JUND). Interacts with PAX6; the interaction is direct. Interacts with ETS1 and LRP1 By similarity. Interacts with the intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction results in a moderate reduction of MAFB transcriptional potential. Ref.6

Subcellular location

Nucleus By similarity.

Tissue specificity

Ubiquitous. Ref.1

Domain

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

Post-translational modification

Phosphorylated by GSK3 and MAPK13 on serine and threonine residues Probable. Ref.7 Ref.8

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

Involvement in disease

Multicentric carpotarsal osteolysis syndrome (MCTO) [MIM:166300]: A rare skeletal disorder, usually presenting in early childhood with a clinical picture mimicking juvenile rheumatoid arthritis. Progressive destruction of the carpal and tarsal bone usually occurs and other bones may also be involved. Chronic renal failure is a frequent component of the syndrome. Mental retardation and minor facial anomalies have been noted in some patients.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Belongs to the bZIP family. Maf subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

brain segmentation

Inferred from electronic annotation. Source: Ensembl

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of erythrocyte differentiation

Inferred from direct assay PubMed 8620536. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

rhombomere 5 development

Inferred from electronic annotation. Source: Ensembl

rhombomere 6 development

Inferred from electronic annotation. Source: Ensembl

segment specification

Inferred from electronic annotation. Source: Ensembl

sensory organ development

Traceable author statement PubMed 8001130. Source: ProtInc

thymus development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Traceable author statement PubMed 8001130. Source: ProtInc

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionsequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding

Inferred from direct assay PubMed 10698492. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IRF3Q146534EBI-3649340,EBI-2650369

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Transcription factor MafB
PRO_0000076494

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) By similarity
Cross-link297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Natural variant541S → L in MCTO. Ref.10
VAR_067979
Natural variant591P → L in MCTO. Ref.10
VAR_067980
Natural variant621T → P in MCTO. Ref.10
VAR_067981
Natural variant631P → R in MCTO. Ref.10
VAR_067982
Natural variant661S → C in MCTO. Ref.10
VAR_067983
Natural variant691S → L in MCTO. Ref.10
VAR_067984
Natural variant701S → A in MCTO. Ref.10
VAR_067985
Natural variant701S → L in MCTO. Ref.10
VAR_067986
Natural variant711P → L in MCTO. Ref.10
VAR_067987
Natural variant711P → S in MCTO. Ref.10
VAR_067988

Experimental info

Sequence conflict521A → V in AAD30106. Ref.1
Sequence conflict2411Q → H in AAD30106. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y5Q3 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: A0F3C09F8936CB16

FASTA32335,792
        10         20         30         40         50         60 
MAAELSMGPE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ PAGSVSSTPL 

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

       130        140        150        160        170        180 
LQSFDSFRGA HHHHHHHHPH PHHAYPGAGV AHDELGPHAH PHHHHHHQAS PPPSSAASPA 

       190        200        210        220        230        240 
QQLPTSHPGP GPHATASATA 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]"Human KRML (MAFB): cDNA cloning, genomic structure, and evaluation as a candidate tumor suppressor gene in myeloid leukemias."
Wang P.W., Eisenbart J.D., Cordes S.P., Barsh G.S., Stoffel M., Le Beau M.M.
Genomics 59:275-281(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Bone marrow.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Brain.
[6]"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.
[7]"MafA transcription factor is phosphorylated by p38 MAP kinase."
Sii-Felice K., Pouponnot C., Gillet S., Lecoin L., Girault J.-A., Eychene A., Felder-Schmittbuhl M.-P.
FEBS Lett. 579:3547-3554(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"GSK-3-mediated phosphorylation enhances Maf-transforming activity."
Rocques N., Abou Zeid N., Sii-Felice K., Lecoin L., Felder-Schmittbuhl M.-P., Eychene A., Pouponnot C.
Mol. Cell 28:584-597(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[9]"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.
[10]"Multicentric carpotarsal osteolysis is caused by mutations clustering in the amino-terminal transcriptional activation domain of MAFB."
Zankl A., Duncan E.L., Leo P.J., Clark G.R., Glazov E.A., Addor M.C., Herlin T., Kim C.A., Leheup B.P., McGill J., McTaggart S., Mittas S., Mitchell A.L., Mortier G.R., Robertson S.P., Schroeder M., Terhal P., Brown M.A.
Am. J. Hum. Genet. 90:494-501(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MCTO LEU-54; LEU-59; PRO-62; ARG-63; CYS-66; LEU-69; ALA-70; LEU-70; SER-71 AND LEU-71.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF134157 mRNA. Translation: AAD30106.1.
AK027324 mRNA. Translation: BAG51303.1.
AL035665 Genomic DNA. Translation: CAB75863.1.
CH471077 Genomic DNA. Translation: EAW76000.1.
BC028098 mRNA. Translation: AAH28098.1.
BC036689 mRNA. Translation: AAH36689.1.
RefSeqNP_005452.2. NM_005461.4.
UniGeneHs.169487.

3D structure databases

ProteinModelPortalQ9Y5Q3.
SMRQ9Y5Q3. Positions 211-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115261. 14 interactions.
IntActQ9Y5Q3. 5 interactions.
STRING9606.ENSP00000362410.

PTM databases

PhosphoSiteQ9Y5Q3.

Polymorphism databases

DMDM21759268.

Proteomic databases

PaxDbQ9Y5Q3.
PRIDEQ9Y5Q3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373313; ENSP00000362410; ENSG00000204103.
ENST00000396967; ENSP00000380167; ENSG00000204103.
GeneID9935.
KEGGhsa:9935.
UCSCuc002xji.3. human.

Organism-specific databases

CTD9935.
GeneCardsGC20M039314.
HGNCHGNC:6408. MAFB.
HPAHPA005653.
MIM166300. phenotype.
608968. gene.
neXtProtNX_Q9Y5Q3.
Orphanet2774. Multicentric carpo-tarsal osteolysis with or without nephropathy.
PharmGKBPA30535.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241084.
HOGENOMHOG000261683.
HOVERGENHBG000313.
InParanoidQ9Y5Q3.
KOK09036.
OMAHPHHGYP.
OrthoDBEOG7BGHMQ.
PhylomeDBQ9Y5Q3.
TreeFamTF325689.

Gene expression databases

BgeeQ9Y5Q3.
CleanExHS_MAFB.
GenevestigatorQ9Y5Q3.

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. human.
GeneWikiMAFB_(gene).
GenomeRNAi9935.
NextBio37480.
PROQ9Y5Q3.
SOURCESearch...

Entry information

Entry nameMAFB_HUMAN
AccessionPrimary (citable) accession number: Q9Y5Q3
Secondary accession number(s): B3KNE1, Q9H1F1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: February 19, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM