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Q9ULX9

- MAFF_HUMAN

UniProt

Q9ULX9 - MAFF_HUMAN

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Protein
Transcription factor MafF
Gene
MAFF
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Interacts with the upstream promoter region of the oxytocin receptor gene. May be a transcriptional enhancer in the up-regulation of the oxytocin receptor gene at parturition. Since it lacks a putative transactivation domain, it may behave as a transcriptional repressor when it dimerize among himself. May also serve as a transcriptional activator by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. May be involved in the cellular stress response.

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
  2. sequence-specific DNA binding transcription factor activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. in utero embryonic development Source: Ensembl
  3. parturition Source: ProtInc
  4. regulation of epidermal cell differentiation Source: Ensembl
  5. skeletal muscle cell differentiation Source: Ensembl
  6. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ9ULX9.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor MafF
Alternative name(s):
U-Maf
V-maf musculoaponeurotic fibrosarcoma oncogene homolog F
Gene namesi
Name:MAFF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:6780. MAFF.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Transcription factor MafF
PRO_0000076497Add
BLAST

Proteomic databases

MaxQBiQ9ULX9.
PaxDbiQ9ULX9.
PRIDEiQ9ULX9.

PTM databases

PhosphoSiteiQ9ULX9.

Expressioni

Tissue specificityi

Expressed in the term myometrium and kidney.

Inductioni

By oxidative stress.1 Publication

Gene expression databases

ArrayExpressiQ9ULX9.
BgeeiQ9ULX9.
CleanExiHS_MAFF.
GenevestigatoriQ9ULX9.

Organism-specific databases

HPAiCAB025341.

Interactioni

Subunit structurei

Monomer and homo- or heterodimer. Interacts with MIP.1 Publication

Protein-protein interaction databases

BioGridi117264. 25 interactions.
IntActiQ9ULX9. 4 interactions.
MINTiMINT-1413410.
STRINGi9606.ENSP00000345393.

Structurei

3D structure databases

ProteinModelPortaliQ9ULX9.
SMRiQ9ULX9. Positions 24-110.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 11464bZIP
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 7626Basic motif By similarity
Add
BLAST
Regioni79 – 9315Leucine-zipper By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the bZIP family. Maf subfamily.

Phylogenomic databases

eggNOGiNOG315640.
HOGENOMiHOG000045475.
HOVERGENiHBG001725.
InParanoidiQ9ULX9.
KOiK09037.
OMAiHGPASCS.
OrthoDBiEOG7BGHMQ.
PhylomeDBiQ9ULX9.
TreeFamiTF325689.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9ULX9-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSVDPLSSKA LKIKRELSEN TPHLSDEALM GLSVRELNRH LRGLSAEEVT    50
RLKQRRRTLK NRGYAASCRV KRVCQKEELQ KQKSELEREV DKLARENAAM 100
RLELDALRGK CEALQGFARS VAAARGPATL VAPASVITIV KSTPGSGSGP 150
AHGPDPAHGP ASCS 164
Length:164
Mass (Da):17,760
Last modified:June 20, 2002 - v2
Checksum:iFC34D9FF317E5EE1
GO
Isoform 2 (identifier: Q9ULX9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Note: No experimental confirmation available.

Show »
Length:135
Mass (Da):14,569
Checksum:i54E949F996CCE45A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2.
VSP_043029Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161G → A in BAA86871. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB025247 mRNA. Translation: BAA86871.1.
AJ010857 mRNA. Translation: CAB52435.1.
AK002001 mRNA. Translation: BAA92029.1.
AK300932 mRNA. Translation: BAG62561.1.
AL021977 Genomic DNA. Translation: CAB45266.1.
BC015037 mRNA. Translation: AAH15037.1.
BC067751 mRNA. Translation: AAH67751.1.
CCDSiCCDS13968.1. [Q9ULX9-1]
CCDS54528.1. [Q9ULX9-2]
PIRiJC7112.
RefSeqiNP_001155044.1. NM_001161572.1. [Q9ULX9-1]
NP_001155045.1. NM_001161573.1. [Q9ULX9-1]
NP_001155046.1. NM_001161574.1. [Q9ULX9-2]
NP_036455.1. NM_012323.3. [Q9ULX9-1]
UniGeneiHs.517617.

Genome annotation databases

EnsembliENST00000338483; ENSP00000345393; ENSG00000185022. [Q9ULX9-1]
ENST00000407965; ENSP00000384094; ENSG00000185022. [Q9ULX9-1]
ENST00000426621; ENSP00000388882; ENSG00000185022. [Q9ULX9-1]
ENST00000538320; ENSP00000442060; ENSG00000185022. [Q9ULX9-1]
ENST00000538999; ENSP00000441482; ENSG00000185022. [Q9ULX9-2]
GeneIDi23764.
KEGGihsa:23764.
UCSCiuc003avc.3. human. [Q9ULX9-1]

Polymorphism databases

DMDMi21542145.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB025247 mRNA. Translation: BAA86871.1 .
AJ010857 mRNA. Translation: CAB52435.1 .
AK002001 mRNA. Translation: BAA92029.1 .
AK300932 mRNA. Translation: BAG62561.1 .
AL021977 Genomic DNA. Translation: CAB45266.1 .
BC015037 mRNA. Translation: AAH15037.1 .
BC067751 mRNA. Translation: AAH67751.1 .
CCDSi CCDS13968.1. [Q9ULX9-1 ]
CCDS54528.1. [Q9ULX9-2 ]
PIRi JC7112.
RefSeqi NP_001155044.1. NM_001161572.1. [Q9ULX9-1 ]
NP_001155045.1. NM_001161573.1. [Q9ULX9-1 ]
NP_001155046.1. NM_001161574.1. [Q9ULX9-2 ]
NP_036455.1. NM_012323.3. [Q9ULX9-1 ]
UniGenei Hs.517617.

3D structure databases

ProteinModelPortali Q9ULX9.
SMRi Q9ULX9. Positions 24-110.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117264. 25 interactions.
IntActi Q9ULX9. 4 interactions.
MINTi MINT-1413410.
STRINGi 9606.ENSP00000345393.

PTM databases

PhosphoSitei Q9ULX9.

Polymorphism databases

DMDMi 21542145.

Proteomic databases

MaxQBi Q9ULX9.
PaxDbi Q9ULX9.
PRIDEi Q9ULX9.

Protocols and materials databases

DNASUi 23764.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338483 ; ENSP00000345393 ; ENSG00000185022 . [Q9ULX9-1 ]
ENST00000407965 ; ENSP00000384094 ; ENSG00000185022 . [Q9ULX9-1 ]
ENST00000426621 ; ENSP00000388882 ; ENSG00000185022 . [Q9ULX9-1 ]
ENST00000538320 ; ENSP00000442060 ; ENSG00000185022 . [Q9ULX9-1 ]
ENST00000538999 ; ENSP00000441482 ; ENSG00000185022 . [Q9ULX9-2 ]
GeneIDi 23764.
KEGGi hsa:23764.
UCSCi uc003avc.3. human. [Q9ULX9-1 ]

Organism-specific databases

CTDi 23764.
GeneCardsi GC22P038597.
HGNCi HGNC:6780. MAFF.
HPAi CAB025341.
MIMi 604877. gene.
neXtProti NX_Q9ULX9.
PharmGKBi PA30538.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG315640.
HOGENOMi HOG000045475.
HOVERGENi HBG001725.
InParanoidi Q9ULX9.
KOi K09037.
OMAi HGPASCS.
OrthoDBi EOG7BGHMQ.
PhylomeDBi Q9ULX9.
TreeFami TF325689.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinki Q9ULX9.

Miscellaneous databases

ChiTaRSi MAFF. human.
GeneWikii MAFF_(gene).
GenomeRNAii 23764.
NextBioi 46719.
PROi Q9ULX9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ULX9.
Bgeei Q9ULX9.
CleanExi HS_MAFF.
Genevestigatori Q9ULX9.

Family and domain databases

Gene3Di 1.10.880.10. 1 hit.
InterProi IPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view ]
PANTHERi PTHR10129. PTHR10129. 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. "Molecular cloning of a human MafF homologue, which specifically binds to the oxytocin receptor gene in term myometrium."
    Kimura T., Ivell R., Rust W., Mizumoto Y., Ogita K., Kusui C., Matsumura Y., Azuma C., Murata Y.
    Biochem. Biophys. Res. Commun. 264:86-92(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Term myometrium.
  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] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Small intestine.
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Placenta and Skin.
  5. "Differential induction of mafF, mafG and mafK expression by electrophile-response-element activators."
    Moran J.A., Dahl E.L., Mulcahy R.T.
    Biochem. J. 361:371-377(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "The novel human gene MIP functions as a co-activator of hMafF."
    Ye X., Li Y., Huang Q., Yu Y., Yuan H., Wang P., Wan D., Gu J., Huo K., Li Y.-Y., Lu H.
    Arch. Biochem. Biophys. 449:87-93(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIP.

Entry informationi

Entry nameiMAFF_HUMAN
AccessioniPrimary (citable) accession number: Q9ULX9
Secondary accession number(s): B4DV49, Q9Y525
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 20, 2002
Last modified: September 3, 2014
This is version 124 of the entry and version 2 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 22
    Human chromosome 22: 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

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