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Protein

Transcription factor MafB

Gene

Mafb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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, osteoclast, 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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 MafB
Short name:
Maf-B
Alternative name(s):
Transcription factor Maf-1
V-maf musculoaponeurotic fibrosarcoma oncogene homolog B
Gene namesi
Name:Mafb
Synonyms:Maf1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2982. Mafb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Transcription factor MafBPRO_0000076496Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP54842.

Expressioni

Tissue specificityi

Expressed at low levels in a variety of tissues, including liver, muscle and spleen. Strongly expressed in hypertrophic chondrocytes of the femur epiphysis, while expression is very weak in immature proliferating chondrocytes (at protein level).2 Publications

Developmental stagei

Expressed in the cartilage of ribs and limbs, in the eyes and spinal cord at 15 dpc (at protein level). Expressed in the lens epithelium at 13 and 16 dpc; not detected in the fiber cells of the lens. In the eyes, confined in the equator of the lens; not detected in the retina at 15 dpc. In spinal cord, expressed in the ventral part of the dorsal horn and the ventral horn at 15 dpc. Predominantly expressed in post-mitotic cells.2 Publications

Gene expression databases

GenevisibleiP54842. RN.

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). Binds DNA as a homodimer or a heterodimer. Interacts with the intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction results in a moderate reduction of MAFB transcriptional potential. Interacts with PAX6; the interaction is direct. Interacts with ETS1 and LRP1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021452.

Structurei

3D structure databases

ProteinModelPortaliP54842.
SMRiP54842. Positions 211-251.
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

eggNOGiKOG4196. Eukaryota.
ENOG41102C7. LUCA.
GeneTreeiENSGT00550000074549.
HOGENOMiHOG000261683.
HOVERGENiHBG000313.
InParanoidiP54842.
KOiK09036.
OMAiHHAEELS.
OrthoDBiEOG7BGHMQ.
PhylomeDBiP54842.
TreeFamiTF325689.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf_fam.
[Graphical view]
PANTHERiPTHR10129. PTHR10129. 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.

P54842-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAELSMGPE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ
60 70 80 90 100
PAGSVSSTPL STPCSSVPSS PSFSPTEQKT HLEDLYWMAS NYQQMNPEAL
110 120 130 140 150
NLTPEDAVEA LIGSHPVPQP LQSFDGFRSA HHHHHHHHPH PHHGYPGAGV
160 170 180 190 200
THDELGPHAH PHHHHHHQAS PPPSSAASPA QQLPTSHPGP GPHAAAAATA
210 220 230 240 250
AGSNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK QKRRTLKNRG
260 270 280 290 300
YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK
310 320
LANSGFREAG STSDSPSSPE FFL
Length:323
Mass (Da):35,792
Last modified:October 1, 1996 - v1
Checksum:i6E386340D1F840A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56241 mRNA. Translation: AAB50062.1.
RefSeqiNP_062189.1. NM_019316.1.
UniGeneiRn.10725.

Genome annotation databases

EnsembliENSRNOT00000021452; ENSRNOP00000021452; ENSRNOG00000016037.
GeneIDi54264.
KEGGirno:54264.
UCSCiRGD:2982. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56241 mRNA. Translation: AAB50062.1.
RefSeqiNP_062189.1. NM_019316.1.
UniGeneiRn.10725.

3D structure databases

ProteinModelPortaliP54842.
SMRiP54842. Positions 211-251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021452.

Proteomic databases

PaxDbiP54842.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021452; ENSRNOP00000021452; ENSRNOG00000016037.
GeneIDi54264.
KEGGirno:54264.
UCSCiRGD:2982. rat.

Organism-specific databases

CTDi9935.
RGDi2982. Mafb.

Phylogenomic databases

eggNOGiKOG4196. Eukaryota.
ENOG41102C7. LUCA.
GeneTreeiENSGT00550000074549.
HOGENOMiHOG000261683.
HOVERGENiHBG000313.
InParanoidiP54842.
KOiK09036.
OMAiHHAEELS.
OrthoDBiEOG7BGHMQ.
PhylomeDBiP54842.
TreeFamiTF325689.

Miscellaneous databases

PROiP54842.

Gene expression databases

GenevisibleiP54842. RN.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf_fam.
[Graphical view]
PANTHERiPTHR10129. PTHR10129. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat maf related genes: specific expression in chondrocytes, lens and spinal cord."
    Sakai M., Imaki J., Yoshida K., Ogata A., Matsushima-Hibaya Y., Kuboki Y., Nishizawa M., Nishi S.
    Oncogene 14:745-750(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Wistar.
    Tissue: Liver.
  2. "Differential expression of maf-1 and maf-2 genes in the developing rat lens."
    Yoshida K., Imaki J., Koyama Y., Harada T., Shinmei Y., Oishi C., Matsushima-Hibiya Y., Matsuda A., Nishi S., Matsuda H., Sakai M.
    Invest. Ophthalmol. Vis. Sci. 38:2679-2683(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "Rat maf-related factors: the specificities of DNA binding and heterodimer formation."
    Matsushima-Hibiya Y., Nishi S., Sakai M.
    Biochem. Biophys. Res. Commun. 245:412-418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DIMERIZATION, DNA-BINDING.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAFB_RAT
AccessioniPrimary (citable) accession number: P54842
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 120 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.