P37261 (FRM2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fatty acid repression mutant protein 2

Gene names

Name:	FRM2
Ordered Locus Names:	YCL026C-A
ORF Names:	YCLX08C, YCLX8C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in negative regulation of fatty acid metabolism. Ref.5
Subcellular location	Cytoplasm. Nucleus Ref.6.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to oxidative stress Inferred from mutant phenotype PubMed 19904831. Source: SGD fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of fatty acid metabolic process Inferred from mutant phenotype Ref.5. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.6. Source: SGD nucleus Inferred from direct assay Ref.6. Source: SGD
Molecular_function	oxidoreductase activity, acting on NAD(P)H, nitrogenous group as acceptor Inferred from direct assay PubMed 22687599. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 193	193	Fatty acid repression mutant protein 2		PRO_0000087340
Amino acid modifications
	Modified residue	2	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P37261 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: 2F555CE7D9DBCE15	FASTA	193	21,232
	10 20 30 40 50 60 MSPTGNYLNA ITNRRTIYNL KPELPQGVGL DDVKRTVHVI LKNTPTAFNS QVNRAVIIVG 70 80 90 100 110 120 DTHKRIWDAV ASAMPTAEAK KRPESCRDEA YGSVIFFTDE GPTEKLQRDF PALAAAFPTC 130 140 150 160 170 180 AAHTTGAVQI QSWTALELLG LGANLQHYND YVKSALPQDV PIAWTVQSQL VFGVPTALPE 190 EKTFINNVIN VYH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Valles G., Volckaerts G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 105-115.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Yeast chromosome III: new gene functions." Koonin E.V., Bork P., Sander C. EMBO J. 13:493-503(1994) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, SIMILARITY.
[5]	"Identification of a class of Saccharomyces cerevisiae mutants defective in fatty acid repression of gene transcription and analysis of the frm2 gene." McHale M.W., Kroening K.D., Bernlohr D.A. Yeast 12:319-331(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59720 Genomic DNA. Translation: CAC42960.1. BK006937 Genomic DNA. Translation: DAA07459.1.
PIR	S53591.
RefSeq	NP_009904.2. NM_001178713.1.
3D structure databases
ProteinModelPortal	P37261.
SMR	P37261. Positions 6-187.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3881N.
IntAct	P37261. 1 interaction.
MINT	MINT-552319.
STRING	4932.YCL026C-A.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCL026C-A; YCL026C-A; YCL026C-A.
GeneID	850332.
KEGG	sce:YCL026C-A.
Organism-specific databases
CYGD	YCL026c-a.
SGD	S000000589. FRM2.
Phylogenomic databases
eggNOG	COG3560.
GeneTree	ENSGT00390000005422.
HOGENOM	HOG000089187.
KO	K07078.
OMA	IPRIASR.
OrthoDB	EOG4C2MKS.
Enzyme and pathway databases
BioCyc	YEAST:G3O-29320-MONOMER.
Gene expression databases
Genevestigator	P37261.
GermOnline	YCL026C-A. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.109.10. 1 hit.
InterPro	IPR000415. Nitroreductase-like. [Graphical view]
Pfam	PF00881. Nitroreductase. 1 hit. [Graphical view]
SUPFAM	SSF55469. Nitroreductase. 1 hit.
ProtoNet	Search...
Other
NextBio	965766.

Entry information

Entry name

FRM2_YEAST

Accession

Primary (citable) accession number: P37261
Secondary accession number(s): D6VQZ0, Q8NIM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	August 16, 2005
Last modified:	May 29, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program