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Protein

Transcription factor MafB

Gene

Mafb

Organism
Mus musculus (Mouse)
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 similarity8 Publications

GO - Molecular functioni

  • DNA binding Source: MGI
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  • transcription factor binding Source: MGI

GO - Biological processi

  • brain segmentation Source: MGI
  • inner ear morphogenesis Source: MGI
  • negative regulation of erythrocyte differentiation Source: MGI
  • negative regulation of osteoclast differentiation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • respiratory gaseous exchange Source: MGI
  • rhombomere 5 development Source: MGI
  • rhombomere 6 development Source: MGI
  • segment specification Source: MGI
  • T cell differentiation in thymus Source: MGI
  • thymus development 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 MafB
Short name:
Maf-B
Alternative name(s):
Kreisler
Segmentation protein Kr
Transcription factor Maf-1
V-maf musculoaponeurotic fibrosarcoma oncogene homolog B
Gene namesi
Name:Mafb
Synonyms:Krml, Maf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:104555. Mafb.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • nucleus Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321K → R: Loss of SUMO modification, increases transactivation activity, increases macrophage differentiation and inhibits myeloid progenitor growth; when associated with R-297. 1 Publication
Mutagenesisi248 – 2481N → A: Reduces ability to activate insulin and glucagon gene expression. 1 Publication
Mutagenesisi248 – 2481N → S: Loss of transcriptional activity. 1 Publication
Mutagenesisi297 – 2971K → R: Loss of SUMO modification, increases transactivation activity, increases macrophage differentiation and inhibits myeloid progenitor growth; when associated with R-32. 1 Publication

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Transcription factor MafBPRO_0000076495Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its transcriptional repression activity and promotes macrophage differentiation from myeloid progenitors.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP54841.
PRIDEiP54841.

PTM databases

PhosphoSiteiP54841.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

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.3 Publications

Gene expression databases

BgeeiP54841.
CleanExiMM_MAF1.
ExpressionAtlasiP54841. baseline and differential.
GenevisibleiP54841. MM.

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). 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.By similarity3 Publications

Protein-protein interaction databases

BioGridi201014. 6 interactions.
DIPiDIP-60663N.
STRINGi10090.ENSMUSP00000096728.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi215 – 2184Combined sources
Helixi221 – 2255Combined sources
Turni228 – 2303Combined sources
Helixi233 – 29967Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WT7X-ray2.30B214-303[»]
2WTYX-ray2.90A/B211-306[»]
4AUWX-ray2.90A/B/E/F211-305[»]
ProteinModelPortaliP54841.
SMRiP54841. Positions 211-297.
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

eggNOGiNOG241084.
GeneTreeiENSGT00550000074549.
HOGENOMiHOG000261683.
HOVERGENiHBG000313.
InParanoidiP54841.
KOiK09036.
OMAiQKNHLEE.
OrthoDBiEOG7BGHMQ.
PhylomeDBiP54841.
TreeFamiTF325689.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028571. MafB.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERiPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF10. PTHR10129:SF10. 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.

P54841-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAELSMGQE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ
60 70 80 90 100
PAGSVSSTPL STPCSSVPSS PSFSPTEPKT HLEDLYWMAS NYQQMNPEAL
110 120 130 140 150
NLTPEDAVEA LIGSHPVPQP LQSFDGFRSA HHHHHHHHPH PHHGYPGAGV
160 170 180 190 200
THDDLGQHAH PHHHHHHQAS PPPSSAASPA QQLPTSHPGP GPHATAAATA
210 220 230 240 250
AGGNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK QKRRTLKNRG
260 270 280 290 300
YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK
310 320
LANSGFREAG STSDSPSSPE FFL
Length:323
Mass (Da):35,809
Last modified:October 1, 1996 - v1
Checksum:iD77AE07ABD9C2AD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti275 – 2751Q → K in BAE32860 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16994.1.
PIRiI49529.
RefSeqiNP_034788.1. NM_010658.3.
UniGeneiMm.330745.

Genome annotation databases

EnsembliENSMUST00000099126; ENSMUSP00000096728; ENSMUSG00000074622.
GeneIDi16658.
KEGGimmu:16658.
UCSCiuc008nqw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16994.1.
PIRiI49529.
RefSeqiNP_034788.1. NM_010658.3.
UniGeneiMm.330745.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WT7X-ray2.30B214-303[»]
2WTYX-ray2.90A/B211-306[»]
4AUWX-ray2.90A/B/E/F211-305[»]
ProteinModelPortaliP54841.
SMRiP54841. Positions 211-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201014. 6 interactions.
DIPiDIP-60663N.
STRINGi10090.ENSMUSP00000096728.

PTM databases

PhosphoSiteiP54841.

Proteomic databases

MaxQBiP54841.
PRIDEiP54841.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000099126; ENSMUSP00000096728; ENSMUSG00000074622.
GeneIDi16658.
KEGGimmu:16658.
UCSCiuc008nqw.2. mouse.

Organism-specific databases

CTDi9935.
MGIiMGI:104555. Mafb.

Phylogenomic databases

eggNOGiNOG241084.
GeneTreeiENSGT00550000074549.
HOGENOMiHOG000261683.
HOVERGENiHBG000313.
InParanoidiP54841.
KOiK09036.
OMAiQKNHLEE.
OrthoDBiEOG7BGHMQ.
PhylomeDBiP54841.
TreeFamiTF325689.

Miscellaneous databases

ChiTaRSiMafb. mouse.
NextBioi290353.
PROiP54841.
SOURCEiSearch...

Gene expression databases

BgeeiP54841.
CleanExiMM_MAF1.
ExpressionAtlasiP54841. baseline and differential.
GenevisibleiP54841. MM.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028571. MafB.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERiPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF10. PTHR10129:SF10. 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. "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.
    , 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. 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. 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. 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. Cited for: REVIEW, FUNCTION.
  19. "Transcription factor C/EBPbeta isoform ratio regulates osteoclastogenesis through MafB."
    Smink J.J., Begay V., Schoenmaker T., Sterneck E., de Vries T.J., Leutz A.
    EMBO J. 28:1769-1781(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMAFB_MOUSE
AccessioniPrimary (citable) accession number: P54841
Secondary accession number(s): Q3U3C8, Q3UPT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 130 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.