CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017746
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription factor MafA 
Protein Synonyms/Alias
 Pancreatic beta-cell-specific transcriptional activator; Transcription factor RIPE3b1; V-maf musculoaponeurotic fibrosarcoma oncogene homolog A 
Gene Name
 MAFA 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32DLMKFEVKKEPPEAEsumoylation[1, 2]
Reference
 [1] Sumoylation regulates the transcriptional activity of MafA in pancreatic beta cells.
 Shao C, Cobb MH.
 J Biol Chem. 2009 Jan 30;284(5):3117-24. [PMID: 19029092]
 [2] SUMOylation negatively regulates transcriptional and oncogenic activities of MafA.
 Kanai K, Reza HM, Kamitani A, Hamazaki Y, Han SI, Yasuda K, Kataoka K.
 Genes Cells. 2010 Sep 1;15(9):971-82. [PMID: 20718938
Functional Description
 Acts as a transcriptional factor. Specifically binds the insulin enhancer element RIPE3b and activates insulin gene expression. Cooperates synergistically with NEUROD1 and PDX1. Phosphorylation by GSK3 increases its transcriptional activity and is required for its oncogenic activity. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. 
Sequence Annotation
 DOMAIN 254 317 bZIP.
 REGION 254 279 Basic motif.
 REGION 260 274 Interaction with DNA.
 REGION 282 303 Leucine-zipper.
 MOD_RES 14 14 Phosphoserine; by MAPK1.
 MOD_RES 49 49 Phosphoserine; by GSK3.
 MOD_RES 53 53 Phosphothreonine; by GSK3.
 MOD_RES 57 57 Phosphothreonine; by GSK3.
 MOD_RES 61 61 Phosphoserine; by GSK3.
 MOD_RES 65 65 Phosphoserine; by MAPK1.  
Keyword
 3D-structure; Activator; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 353 AA 
Protein Sequence
MAAELAMGAE LPSSPLAIEY VNDFDLMKFE VKKEPPEAER FCHRLPPGSL SSTPLSTPCS 60
SVPSSPSFCA PSPGTGGGGG AGGGGGSSQA GGAPGPPSGG PGAVGGTSGK PALEDLYWMS 120
GYQHHLNPEA LNLTPEDAVE ALIGSGHHGA HHGAHHPAAA AAYEAFRGPG FAGGGGADDM 180
GAGHHHGAHH AAHHHHAAHH HHHHHHHHGG AGHGGGAGHH VRLEERFSDD QLVSMSVREL 240
NRQLRGFSKE EVIRLKQKRR TLKNRGYAQS CRFKRVQQRH ILESEKCQLQ SQVEQLKLEV 300
GRLAKERDLY KEKYEKLAGR GGPGSAGGAG FPREPSPPQA GPGGAKGTAD FFL 353 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0046982; F:protein heterodimerization activity; NAS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
 GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:UniProtKB.
 GO:0030073; P:insulin secretion; IDA:BHF-UCL.
 GO:0007263; P:nitric oxide mediated signal transduction; IDA:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0009749; P:response to glucose stimulus; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR004827; bZIP.
 IPR004826; bZIP_Maf.
 IPR008917; Euk_TF_DNA-bd.
 IPR013592; Maf_TF_N.
 IPR024874; Transciption_factor_Maf. 
Pfam
 PF03131; bZIP_Maf
 PF08383; Maf_N 
SMART
 SM00338; BRLZ 
PROSITE
 PS50217; BZIP
 PS00036; BZIP_BASIC 
PRINTS