Q9ULX9 (MAFF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor MafF

Alternative name(s):
U-Maf
V-maf musculoaponeurotic fibrosarcoma oncogene homolog F

Gene names

Name:

MAFF

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Monomer and homo- or heterodimer. Interacts with MIP. Ref.6
Subcellular location	Nucleus.
Tissue specificity	Expressed in the term myometrium and kidney.
Induction	By oxidative stress. Ref.5
Sequence similarities	Belongs to the bZIP family. Maf subfamily. Contains 1 bZIP domain.

Ontologies

Keywords
Biological process	Stress response Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome parturition Traceable author statement. Source: ProtInc transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	nucleoplasm Traceable author statement. Source: Reactome
Molecular function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 164	164	Transcription factor MafF		PRO_0000076497
Regions
	Domain	86 – 114	29	Leucine-zipper
	DNA binding	53 – 83	31	Basic motif
Experimental info
	Sequence conflict	116	1	G → A in BAA86871. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9ULX9 [UniParc]. Last modified June 20, 2002. Version 2. Checksum: FC34D9FF317E5EE1	FASTA	164	17,760
	10 20 30 40 50 60 MSVDPLSSKA LKIKRELSEN TPHLSDEALM GLSVRELNRH LRGLSAEEVT RLKQRRRTLK 70 80 90 100 110 120 NRGYAASCRV KRVCQKEELQ KQKSELEREV DKLARENAAM RLELDALRGK CEALQGFARS 130 140 150 160 VAAARGPATL VAPASVITIV KSTPGSGSGP AHGPDPAHGP ASCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10527846] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[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: 10591208] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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: 11772409] [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: 16549056] [Abstract] Cited for: INTERACTION WITH MIP.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB025247 mRNA. Translation: BAA86871.1. AJ010857 mRNA. Translation: CAB52435.1. AK002001 mRNA. Translation: BAA92029.1. AL021977 Genomic DNA. Translation: CAB45266.1. BC015037 mRNA. Translation: AAH15037.1. BC067751 mRNA. Translation: AAH67751.1.
IPI	IPI00099497.
PIR	JC7112.
RefSeq	NP_001155044.1. NM_001161572.1. NP_001155045.1. NM_001161573.1. NP_001155046.1. NM_001161574.1. NP_036455.1. NM_012323.3.
UniGene	Hs.517617.
3D structure databases
ProteinModelPortal	Q9ULX9.
SMR	Q9ULX9. Positions 24-110.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ULX9. 4 interactions.
MINT	MINT-1413410.
STRING	Q9ULX9.
PTM databases
PhosphoSite	Q9ULX9.
Polymorphism databases
DMDM	21542145.
Proteomic databases
PRIDE	Q9ULX9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000338483; ENSP00000345393; ENSG00000185022. ENST00000407965; ENSP00000384094; ENSG00000185022. ENST00000426621; ENSP00000388882; ENSG00000185022.
GeneID	23764.
KEGG	hsa:23764.
UCSC	uc003avc.1. human.
Organism-specific databases
CTD	23764.
GeneCards	GC22P038597.
H-InvDB	HIX0016465.
HGNC	HGNC:6780. MAFF.
HPA	CAB025341.
MIM	604877. gene.
neXtProt	NX_Q9ULX9.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20041.
GeneTree	ENSGT00550000074549.
HOGENOM	HBG715194.
HOVERGEN	HBG001725.
InParanoid	Q9ULX9.
OMA	KYEALQG.
OrthoDB	EOG4G1MHT.
PhylomeDB	Q9ULX9.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q9ULX9.
Bgee	Q9ULX9.
CleanEx	HS_MAFF.
Genevestigator	Q9ULX9.
GermOnline	ENSG00000185022. Homo sapiens.
Family and domain databases
InterPro	IPR004827. bZIP. IPR004826. bZIP_Maf. IPR008917. Euk_TF_DNA-bd. IPR024874. Transciption_factor_Maf. [Graphical view]
Gene3D	G3DSA:1.10.880.10. G3DSA:1.10.880.10. 1 hit.
KO	K09037.
PANTHER	PTHR10129. PTHR10129. 1 hit.
Pfam	PF03131. bZIP_Maf. 1 hit. [Graphical view]
SMART	SM00338. BRLZ. 1 hit. [Graphical view]
SUPFAM	SSF47454. Euk_transcr_DNA. 1 hit.
PROSITE	PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	46719.
SOURCE	Search...

Entry information

Entry name

MAFF_HUMAN

Accession

Primary (citable) accession number: Q9ULX9
Secondary accession number(s): Q9Y525

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	June 20, 2002
Last modified:	January 25, 2012
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.