Transcriptional regulatory protein UME6 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P39001 (UME6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transcriptional regulatory protein UME6

Alternative name(s):
Negative transcriptional regulator of IME2
Regulator of inducer of meiosis protein 16
Unscheduled meiotic gene expression protein 6

Gene names

Name:	UME6
Synonyms:	CAR80, CARGR1, NIM2, RIM16
Ordered Locus Names:	YDR207C
ORF Names:	YD8142.04C

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	836 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Binds to the URS1 site (5'-AGCCGCCGA-3') and recruits the RPD3 histone deacetylase complex to the promoters to negatively regulate the expression of many genes including CAR1 (arginase), several required for sporulation, mating type switching, inositol metabolism, and oxidative carbon metabolism. Recruits also the ISW2 chromatin remodeling complex to promoters in a second gene repression pathway. Associates with the master regulator of meiosis IME1 in order to activate the expression of meiosis genes. Has both a positive and negative role in regulating phospholipid biosynthesis. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.27 Ref.29
Subunit structure	Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Interacts with RIM11, MCK1 and IME1. Ref.12 Ref.14 Ref.16 Ref.20 Ref.22 Ref.28
Subcellular location	Nucleus Ref.25.
Post-translational modification	Phosphorylated by RIM11 and MCK1. Ref.16 Ref.20
Miscellaneous	Present with 217 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW lipid particle organization Inferred from mutant phenotype PubMed 18156287. Source: SGD negative regulation of inositol biosynthetic process by negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.13. Source: SGD negative regulation of transcription from RNA polymerase II promoter during meiosis Inferred from mutant phenotype PubMed 21123654 Ref.10. Source: SGD negative regulation of transcription from RNA polymerase II promoter during mitosis Inferred from mutant phenotype Ref.2 Ref.10. Source: SGD nitrogen catabolite repression of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.8. Source: SGD positive regulation of meiosis by negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.10. Source: SGD positive regulation of meiosis by positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.10. Source: SGD positive regulation of phosphatidylcholine biosynthetic process by positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.13. Source: SGD positive regulation of phosphatidylserine biosynthetic process by positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.13. Source: SGD positive regulation of transcription from RNA polymerase II promoter during meiosis Inferred from mutant phenotype PubMed 21123654 Ref.10. Source: SGD pseudohyphal growth Inferred from mutant phenotype PubMed 20876298. Source: SGD spore germination Inferred from mutant phenotype PubMed 21059190. Source: SGD
Cellular_component	Rpd3L complex Inferred from direct assay PubMed 16286007 Ref.28 PubMed 19040720. Source: SGD Rpd3L-Expanded complex Inferred from direct assay PubMed 19040720. Source: SGD
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay Ref.2 Ref.11. Source: SGD RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from direct assay Ref.19 Ref.2. Source: SGD repressing transcription factor binding Inferred from direct assay Ref.19. Source: SGD transcription factor binding transcription factor activity Inferred from genetic interaction Ref.19. Source: SGD zinc ion binding 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 – 836

836

Transcriptional regulatory protein UME6

PRO_0000114987

Regions

DNA binding

771 – 798

Zn(2)-C6 fungal-type Ref.11 Ref.15 Ref.19 Ref.29

Region

508 – 594

SIN3-binding

Amino acid modifications

Modified residue

Phosphoserine Ref.32

Modified residue

Phosphoserine Ref.31

Modified residue

Phosphoserine Ref.32

Modified residue

141

Phosphoserine Ref.31 Ref.32

Modified residue

150

Phosphoserine Ref.31 Ref.32

Modified residue

270

Phosphoserine Ref.32

Modified residue

316

Phosphoserine Ref.32

Modified residue

645

Phosphoserine Ref.30 Ref.31 Ref.32

Modified residue

712

Phosphoserine Ref.32

Experimental info

Mutagenesis

99 – 109

TPVHTPSGSPS → APVHAPAGAPA: Impairs meiotic genes expression, sporulation and interactions with IME1 and RIM11, and abolishes phosphorylation. Ref.16 Ref.20

Mutagenesis

99 – 107

TPVHTPSGS → APVHAPSGA: Impairs meiotic genes expression and sporulation, reduces the interaction with IME1, and abolishes phosphorylation. Ref.16 Ref.20

Mutagenesis

T → N or A: Impairs meiotic genes expression and sporulation, reduces interactions with IME1 and RIM11, and reduces phosphorylation. Ref.16 Ref.20

Mutagenesis

103

T → A: Impairs meiotic genes expression and sporulation, reduces interaction with IME, and reduces phosphorylation. Ref.20

Mutagenesis

107

S → A: Impairs meiotic genes expression and sporulation, reduces interaction with IME, and reduces phosphorylation. Ref.20

Mutagenesis

523

A → S: Impairs SIN3-binding and gene repression activity. Ref.22

Mutagenesis

524

A → T: Impairs gene repression activity. Ref.22

Mutagenesis

525

Missing: Impairs gene repression activity. Ref.22

Mutagenesis

526

V → Q: Impairs gene repression activity. Ref.22

Mutagenesis

527

L → P: Impairs SIN3-binding and gene repression activity. Ref.22

Mutagenesis

528

S → P: Impairs SIN3-binding and gene repression activity. Ref.22

Mutagenesis

530

M → T or V: Impairs SIN3-binding and gene repression activity. Ref.22

Mutagenesis

635

K → E: Impairs gene repression activity. Ref.22

Sequence conflict

101

V → G in BAA04890. Ref.3

Sequence conflict

363

I → V in AAA34471. Ref.1

Sequence conflict

443

N → T in AAA34471. Ref.1

Sequence conflict

465

G → D in AAA34471. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P39001 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 0DDA0A6B4A157182
Show »

FASTA

836

91,124

        10         20         30         40         50         60 
MLDKARSQSK HMDESNAAAS LLSMETTANN HHYLHNKTSR ATLMNSSQDG KKHAEDEVSD 

        70         80         90        100        110        120 
GANSRHPTIS SASIESLKTT YDENPLLSIM KSTCAPNNTP VHTPSGSPSL KVQSGGDIKD 

       130        140        150        160        170        180 
DPKENDTTTT TNTTLQDRRD SDNAVHAAAS PLAPSNTPSD PKSLCNGHVA QATDPQISGA 

       190        200        210        220        230        240 
IQPQYTATNE DVFPYSSTST NSNTATTTIV AGAKKKIHLP PPQAPAVSSP GTTAAGSGAG 

       250        260        270        280        290        300 
TGSGIRSRTG SDLPLIITSA NKNNGKTTNS PMSILSRNNS TNNNDNNSIQ SSDSRESSNN 

       310        320        330        340        350        360 
NEIGGYLRGG TKRGGSPSND SQVQHNVHDD QCAVGVAPRN FYFNKDREIT DPNVKLDENE 

       370        380        390        400        410        420 
SKINISFWLN SKYRDEAYSL NESSSNNASS NTDTPTNSRH ANTSSSITSR NNFQHFRFNQ 

       430        440        450        460        470        480 
IPSQPPTSAS SFTSTNNNNP QRNNINRGED PFATSSRPST GFFYGDLPNR NNRNSPFHTN 

       490        500        510        520        530        540 
EQYIPPPPPK YINSKLDGLR SRLLLGPNSA SSSTKLDDDL GTAAAVLSNM RSSPYRTHDK 

       550        560        570        580        590        600 
PISNVNDMNN TNALGVPASR PHSSSFPSKG VLRPILLRIH NSEQQPIFES NNSTAVFDED 

       610        620        630        640        650        660 
QDQNQDLSPY HLNLNSKKVL DPTFESRTRQ VTWNKNGKRI DRRLSAPEQQ QQLEVPPLKK 

       670        680        690        700        710        720 
SRRSVGNARV ASQTNSDYNS LGESSTSSAP SSPSLKASSG LAYTADYPNA TSPDFAKSKG 

       730        740        750        760        770        780 
KNVKPKAKSK AKQSSKKRPN NTTSKSKANN SQESNNATSS TSQGTRSRTG CWICRLRKKK 

       790        800        810        820        830 
CTEERPHCFN CERLKLDCHY DAFKPDFVSD PKKKQMKLEE IKKKTKEAKR RAMKKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the UME6/CAR80 gene from Saccharomyces cerevisiae." Smart W.C., Park H.-D., Cooper T.G. Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sigma 1278B.
[2]	"UME6 is a key regulator of nitrogen repression and meiotic development." Strich R., Surosky R.T., Steber C.M., Messenguy F., Dubois E., Easton Esposito R. Genes Dev. 8:796-810(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]	Kumeno A. Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Identification of negative regulatory genes that govern the expression of early meiotic genes in yeast." Strich R., Slater M.R., Easton Esposito R. Proc. Natl. Acad. Sci. U.S.A. 86:10018-10022(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Selection for early meiotic mutants in yeast." Mitchell A.P., Bowdish K.S. Genetics 131:65-72(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"The yeast UME6 gene product is required for transcriptional repression mediated by the CAR1 URS1 repressor binding site." Park H.-D., Luche R.M., Cooper T.G. Nucleic Acids Res. 20:1909-1915(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Positive control of yeast meiotic genes by the negative regulator UME6." Bowdish K.S., Yuan H.E., Mitchell A.P. Mol. Cell. Biol. 15:2955-2961(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"UME6 is a central component of a developmental regulatory switch controlling meiosis-specific gene expression." Steber C.M., Easton Esposito R. Proc. Natl. Acad. Sci. U.S.A. 92:12490-12494(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"UME6, a negative regulator of meiosis in Saccharomyces cerevisiae, contains a C-terminal Zn2Cys6 binuclear cluster that binds the URS1 DNA sequence in a zinc-dependent manner." Anderson S.F., Steber C.M., Easton Esposito R., Coleman J.E. Protein Sci. 4:1832-1843(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, DNA-BINDING.
[12]	"Induction of meiosis in Saccharomyces cerevisiae depends on conversion of the transcriptional represssor Ume6 to a positive regulator by its regulated association with the transcriptional activator Ime1." Rubin-Bejerano I., Mandel S., Robzyk K., Kassir Y. Mol. Cell. Biol. 16:2518-2526(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH IME1.
[13]	"The yeast UME6 gene is required for both negative and positive transcriptional regulation of phospholipid biosynthetic gene expression." Jackson J.C., Lopes J.M. Nucleic Acids Res. 24:1322-1329(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters." Kadosh D., Struhl K. Cell 89:365-371(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, INTERACTION WITH SIN3.
[15]	"Role of UME6 in transcriptional regulation of a DNA repair gene in Saccharomyces cerevisiae." Sweet D.H., Jang Y.K., Sancar G.B. Mol. Cell. Biol. 17:6223-6235(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING.
[16]	"Interaction of yeast repressor-activator protein Ume6p with glycogen synthase kinase 3 homolog Rim11p." Malathi K., Xiao Y., Mitchell A.P. Mol. Cell. Biol. 17:7230-7236(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RIM11 AND IME1, PHOSPHORYLATION, MUTAGENESIS OF THR-99 AND 99-THR--SER-109.
[17]	"Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo." Kadosh D., Struhl K. Mol. Cell. Biol. 18:5121-5127(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3." Rundlett S.E., Carmen A.A., Suka N., Turner B.M., Grunstein M. Nature 392:831-835(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"The Isw2 chromatin remodeling complex represses early meiotic genes upon recruitment by Ume6p." Goldmark J.P., Fazzio T.G., Estep P.W., Church G.M., Tsukiyama T. Cell 103:423-433(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING.
[20]	"Shared roles of yeast glycogen synthase kinase 3 family members in nitrogen-responsive phosphorylation of meiotic regulator Ume6p." Xiao Y., Mitchell A.P. Mol. Cell. Biol. 20:5447-5453(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-99; THR-103 AND SER-107, INTERACTION WITH MCK1.
[21]	"Combinatorial regulation of phospholipid biosynthetic gene expression by the UME6, SIN3 and RPD3 genes." Elkhaimi M., Kaadige M.R., Kamath D., Jackson J.C., Biliran H. Jr., Lopes J.M. Nucleic Acids Res. 28:3160-3167(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"Identification of the Sin3-binding site in Ume6 defines a two-step process for conversion of Ume6 from a transcriptional repressor to an activator in yeast." Washburn B.K., Easton Esposito R. Mol. Cell. Biol. 21:2057-2069(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SIN3 AND TEA1, MUTAGENESIS OF ALA-523; ALA-524; ALA-525; VAL-526; LEU-527; SER-528; MET-530 AND LYS-635.
[23]	"The Ume6 regulon coordinates metabolic and meiotic gene expression in yeast." Williams R.M., Primig M., Washburn B.K., Winzeler E.A., Bellis M., Sarrauste de Menthiere C., Davis R.W., Easton Esposito R. Proc. Natl. Acad. Sci. U.S.A. 99:13431-13436(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[24]	"Discovery of novel transcription control relationships with gene regulatory networks generated from multiple-disruption full genome expression libraries." Aburatani S., Tashiro K., Savoie C.J., Nishizawa M., Hayashi K., Ito Y., Muta S., Yamamoto K., Ogawa M., Enomoto A., Masaki M., Watanabe S., Maki Y., Takahashi Y., Eguchi Y., Sakaki Y., Kuhara S. DNA Res. 10:1-8(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[25]	"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].
[26]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[27]	"Yeast Ume6p repressor permits activator binding but restricts TBP binding at the HOP1 promoter." Shimizu M., Takahashi K., Lamb T.M., Shindo H., Mitchell A.P. Nucleic Acids Res. 31:3033-3037(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[28]	"Stable incorporation of sequence specific repressors Ash1 and Ume6 into the Rpd3L complex." Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J., Washburn M.P., Workman J.L. Biochim. Biophys. Acta 1731:77-87(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RPD3C(L) COMPLEX, MASS SPECTROMETRY.
[29]	"Identification of functional transcription factor binding sites using closely related Saccharomyces species." Doniger S.W., Huh J., Fay J.C. Genome Res. 15:701-709(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING.
[30]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, MASS SPECTROMETRY.
[31]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-141; SER-150 AND SER-645, MASS SPECTROMETRY.
[32]	"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-46; SER-73; SER-141; SER-150; SER-270; SER-316; SER-645 AND SER-712, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L32186 Genomic DNA. Translation: AAA34471.1. L24539 Unassigned DNA. Translation: AAC14472.1. D23663 Genomic DNA. Translation: BAA04890.1. Z68194 Genomic DNA. Translation: CAA92346.1. BK006938 Genomic DNA. Translation: DAA12048.1.
PIR	S61570.
RefSeq	NP_010493.1. NM_001180515.1.
3D structure databases
ProteinModelPortal	P39001.
SMR	P39001. Positions 766-821.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-959N.
IntAct	P39001. 8 interactions.
MINT	MINT-387730.
STRING	4932.YDR207C.
Proteomic databases
PaxDb	P39001.
PeptideAtlas	P39001.
PRIDE	P39001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR207C; YDR207C; YDR207C.
GeneID	851788.
KEGG	sce:YDR207C.
Organism-specific databases
CYGD	YDR207c.
SGD	S000002615. UME6.
Phylogenomic databases
eggNOG	NOG41915.
KO	K09243.
OMA	SKINISF.
OrthoDB	EOG4FXVGZ.
Enzyme and pathway databases
BioCyc	YEAST:G3O-29791-MONOMER.
Gene expression databases
Genevestigator	P39001.
GermOnline	YDR207C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	4.10.240.10. 1 hit.
InterPro	IPR001138. Zn2-C6_fun-type_DNA-bd. [Graphical view]
Pfam	PF00172. Zn_clus. 1 hit. [Graphical view]
SMART	SM00066. GAL4. 1 hit. [Graphical view]
SUPFAM	SSF57701. Fungi_TrN. 1 hit.
PROSITE	PS00463. ZN2_CY6_FUNGAL_1. 1 hit. PS50048. ZN2_CY6_FUNGAL_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	969606.

Entry information

Entry name

UME6_YEAST

Accession

Primary (citable) accession number: P39001
Secondary accession number(s): D6VSI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents