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O60675 (MAFK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor MafK
Alternative name(s):
Erythroid transcription factor NF-E2 p18 subunit
Gene names
Name:MAFK
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor.

Subunit structure

Homodimer or heterodimer. It can form high affinity heterodimers with members of the CNC-bZIP family such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the bZIP family. Maf subfamily.

Contains 1 bZIP domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processblood coagulation

Traceable author statement. Source: Reactome

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleoplasm

Traceable author statement. Source: Reactome

   Molecular functionsequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Non-traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 156156Transcription factor MafK
PRO_0000076503

Regions

Domain86 – 11429Leucine-zipper
DNA binding51 – 7626Basic motif

Amino acid modifications

Modified residue251Phosphoserine Ref.3 Ref.4 Ref.5

Sequences

Sequence LengthMass (Da)Tools
O60675 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 39F98F8D550C168E

FASTA15617,523
        10         20         30         40         50         60 
MTTNPKPNKA LKVKKEAGEN APVLSDDELV SMSVRELNQH LRGLTKEEVT RLKQRRRTLK 

        70         80         90        100        110        120 
NRGYAASCRI KRVTQKEELE RQRVELQQEV EKLARENSSM RLELDALRSK YEALQTFART 

       130        140        150 
VARGPVAPSK VATTSVITIV KSTELSSTSV PFSAAS 

« Hide

References

« Hide 'large scale' references
[1]"Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif."
Toki T., Itoh J., Kitazawa J., Arai K., Hatakeyama K., Akasaka J., Igarashi K., Nomura N., Yokoyama M., Yamamoto M., Ito E.
Oncogene 14:1901-1910(1997) [PubMed: 9150357] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[4]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF059194 mRNA. Translation: AAC14426.1.
AC093734 Genomic DNA. Translation: AAP21866.1.
IPIIPI00031018.
RefSeqNP_002351.1. NM_002360.3.
UniGeneHs.520612.

3D structure databases

ProteinModelPortalO60675.
SMRO60675. Positions 24-111.
ModBaseSearch...

Protein-protein interaction databases

IntActO60675. 2 interactions.
STRINGO60675.

PTM databases

PhosphoSiteO60675.

Proteomic databases

PRIDEO60675.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343242; ENSP00000344903; ENSG00000198517.
ENST00000403150; ENSP00000386009; ENSG00000198517.
ENST00000406174; ENSP00000385437; ENSG00000198517.
GeneID7975.
KEGGhsa:7975.
UCSCuc003skr.1. human.

Organism-specific databases

CTD7975.
GeneCardsGC07P001536.
H-InvDBHIX0006420.
HGNCHGNC:6782. MAFK.
HPACAB026820.
MIM600197. gene.
neXtProtNX_O60675.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00550000074549.
HOVERGENHBG001725.
InParanoidO60675.
OMARGPVTPT.
OrthoDBEOG4X3H2R.
PhylomeDBO60675.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO60675.
BgeeO60675.
CleanExHS_MAFK.
GenevestigatorO60675.
GermOnlineENSG00000198517. Homo sapiens.

Family and domain databases

InterProIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR008917. Euk_TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
Gene3DG3DSA:1.10.880.10. G3DSA:1.10.880.10. 1 hit.
KOK09037.
PANTHERPTHR10129. PTHR10129. 1 hit.
PfamPF03131. bZIP_Maf. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. Euk_transcr_DNA. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio30491.
SOURCESearch...

Entry information

Entry nameMAFK_HUMAN
AccessionPrimary (citable) accession number: O60675
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 93 of the entry and version 1 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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families