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O60675

- MAFK_HUMAN

UniProt

O60675 - MAFK_HUMAN

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Protein

Transcription factor MafK

Gene

MAFK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
  2. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. nervous system development Source: Ensembl
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor MafK
Alternative name(s):
Erythroid transcription factor NF-E2 p18 subunit
Gene namesi
Name:MAFK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:6782. MAFK.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30540.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Transcription factor MafKPRO_0000076503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60675.
PaxDbiO60675.
PRIDEiO60675.

PTM databases

PhosphoSiteiO60675.

Expressioni

Gene expression databases

BgeeiO60675.
CleanExiHS_MAFK.
ExpressionAtlasiO60675. baseline.
GenevestigatoriO60675.

Organism-specific databases

HPAiCAB026820.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi113688. 17 interactions.
IntActiO60675. 2 interactions.
STRINGi9606.ENSP00000344903.

Structurei

3D structure databases

ProteinModelPortaliO60675.
SMRiO60675. Positions 24-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 11464bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 7626Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni79 – 9315Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family. Maf subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG236209.
GeneTreeiENSGT00550000074549.
HOVERGENiHBG001725.
InParanoidiO60675.
KOiK09037.
OMAiNASMRLE.
OrthoDBiEOG7BGHMQ.
PhylomeDBiO60675.
TreeFamiTF325689.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR028574. MafK.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERiPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF26. PTHR10129:SF26. 1 hit.
PfamiPF03131. bZIP_Maf. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60675-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTNPKPNKA LKVKKEAGEN APVLSDDELV SMSVRELNQH LRGLTKEEVT
60 70 80 90 100
RLKQRRRTLK NRGYAASCRI KRVTQKEELE RQRVELQQEV EKLARENSSM
110 120 130 140 150
RLELDALRSK YEALQTFART VARGPVAPSK VATTSVITIV KSTELSSTSV

PFSAAS
Length:156
Mass (Da):17,523
Last modified:August 1, 1998 - v1
Checksum:i39F98F8D550C168E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059194 mRNA. Translation: AAC14426.1.
AK092414 mRNA. Translation: BAG52549.1.
AC093734 Genomic DNA. Translation: AAP21866.1.
CH236953 Genomic DNA. Translation: EAL23943.1.
CH471144 Genomic DNA. Translation: EAW87207.1.
BC148265 mRNA. Translation: AAI48266.1.
CCDSiCCDS5325.1.
RefSeqiNP_002351.1. NM_002360.3.
XP_006715836.1. XM_006715773.1.
UniGeneiHs.520612.

Genome annotation databases

EnsembliENST00000343242; ENSP00000344903; ENSG00000198517.
ENST00000403150; ENSP00000386009; ENSG00000198517.
ENST00000406174; ENSP00000385437; ENSG00000198517.
GeneIDi7975.
KEGGihsa:7975.
UCSCiuc003skr.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059194 mRNA. Translation: AAC14426.1 .
AK092414 mRNA. Translation: BAG52549.1 .
AC093734 Genomic DNA. Translation: AAP21866.1 .
CH236953 Genomic DNA. Translation: EAL23943.1 .
CH471144 Genomic DNA. Translation: EAW87207.1 .
BC148265 mRNA. Translation: AAI48266.1 .
CCDSi CCDS5325.1.
RefSeqi NP_002351.1. NM_002360.3.
XP_006715836.1. XM_006715773.1.
UniGenei Hs.520612.

3D structure databases

ProteinModelPortali O60675.
SMRi O60675. Positions 24-111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113688. 17 interactions.
IntActi O60675. 2 interactions.
STRINGi 9606.ENSP00000344903.

Chemistry

ChEMBLi CHEMBL2346484.

PTM databases

PhosphoSitei O60675.

Proteomic databases

MaxQBi O60675.
PaxDbi O60675.
PRIDEi O60675.

Protocols and materials databases

DNASUi 7975.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343242 ; ENSP00000344903 ; ENSG00000198517 .
ENST00000403150 ; ENSP00000386009 ; ENSG00000198517 .
ENST00000406174 ; ENSP00000385437 ; ENSG00000198517 .
GeneIDi 7975.
KEGGi hsa:7975.
UCSCi uc003skr.3. human.

Organism-specific databases

CTDi 7975.
GeneCardsi GC07P001570.
HGNCi HGNC:6782. MAFK.
HPAi CAB026820.
MIMi 600197. gene.
neXtProti NX_O60675.
PharmGKBi PA30540.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236209.
GeneTreei ENSGT00550000074549.
HOVERGENi HBG001725.
InParanoidi O60675.
KOi K09037.
OMAi NASMRLE.
OrthoDBi EOG7BGHMQ.
PhylomeDBi O60675.
TreeFami TF325689.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi MAFK. human.
GeneWikii MAFK.
GenomeRNAii 7975.
NextBioi 30491.
PROi O60675.
SOURCEi Search...

Gene expression databases

Bgeei O60675.
CleanExi HS_MAFK.
ExpressionAtlasi O60675. baseline.
Genevestigatori O60675.

Family and domain databases

Gene3Di 1.10.880.10. 1 hit.
InterProi IPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR028574. MafK.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view ]
PANTHERi PTHR10129. PTHR10129. 1 hit.
PTHR10129:SF26. PTHR10129:SF26. 1 hit.
Pfami PF03131. bZIP_Maf. 1 hit.
[Graphical view ]
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47454. SSF47454. 1 hit.
PROSITEi PS50217. BZIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRANSCRIPTION, INTERACTION WITH NRF1 AND NRF2, TISSUE SPECIFICITY.
  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.
    , 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: Placenta.
  3. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].
  7. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiMAFK_HUMAN
AccessioniPrimary (citable) accession number: O60675
Secondary accession number(s): A4D214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3