Resistance to glucose repression protein 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Resistance to glucose repression protein 1

Alternative name(s):
Protein HEX2
Second-site suppressor of the rna1-1 mutation 1

Gene names

Name:	REG1
Synonyms:	HEX2, PZF240, SPP43, SRN1
Ordered Locus Names:	YDR028C
ORF Names:	YD9813.06C

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	1014 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in RNA processing and negative regulation of glucose repression. Regulates the level of two antigens, P43 and P70. Binds to protein phosphatase type 1. Functions with REG2 and SNF1 protein kinase to regulate growth. Might regulate SNF1 directly or indirectly. Ref.14
Subunit structure	Interacts with SAK1. Ref.6 Ref.14
Subcellular location	Nucleus.
Miscellaneous	Present with 2560 molecules/cell in log phase SD medium.

Ontologies

Keywords
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to glucose starvation Inferred from mutant phenotype PubMed 19723765. Source: SGD glycogen metabolic process Traceable author statement PubMed 10454550. Source: SGD negative regulation of transcription from RNA polymerase II promoter Traceable author statement PubMed 10454550. Source: SGD regulation of carbohydrate metabolic process Inferred from genetic interaction PubMed 12167649. Source: SGD vacuolar protein catabolic process Inferred from mutant phenotype PubMed 14684743. Source: SGD
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell protein phosphatase type 1 complex Traceable author statement PubMed 10454550. Source: SGD
Molecular_function	protein phosphatase type 1 regulator activity Traceable author statement PubMed 11412094. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SNF1	P06782	3	EBI-8270,EBI-17516

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1014

1014

Resistance to glucose repression protein 1

PRO_0000083953

Regions

Motif

277 – 283

7

Nuclear localization signal Potential

Motif

595 – 599

5

Nuclear localization signal Potential

Motif

873 – 879

7

Nuclear localization signal Potential

Compositional bias

543 – 552

10

Ser-rich

Compositional bias

742 – 760

19

Asp/Glu-rich (acidic)

Compositional bias

834 – 844

11

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

2

1

Phosphoserine Ref.9

Modified residue

73

1

Phosphothreonine Ref.11

Modified residue

75

1

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Modified residue

242

1

Phosphoserine Ref.12 Ref.13

Modified residue

254

1

Phosphoserine Ref.12 Ref.13

Modified residue

311

1

Phosphoserine Ref.13

Modified residue

349

1

Phosphoserine Ref.12

Modified residue

421

1

Phosphoserine Ref.10 Ref.12 Ref.13

Modified residue

480

1

Phosphotyrosine Ref.11

Modified residue

485

1

Phosphoserine Ref.11

Modified residue

490

1

Phosphoserine Ref.11

Modified residue

570

1

Phosphoserine Ref.7 Ref.12 Ref.13

Modified residue

572

1

Phosphoserine Ref.10 Ref.12 Ref.13

Modified residue

576

1

Phosphoserine Ref.7 Ref.10 Ref.12 Ref.13

Modified residue

582

1

Phosphoserine Ref.13

Modified residue

586

1

Phosphoserine Ref.12

Modified residue

587

1

Phosphoserine Ref.12

Modified residue

608

1

Phosphotyrosine Ref.13

Modified residue

610

1

Phosphoserine Ref.13

Modified residue

614

1

Phosphoserine Ref.13

Modified residue

680

1

Phosphoserine Ref.13

Modified residue

767

1

Phosphothreonine Ref.12

Modified residue

769

1

Phosphoserine Ref.9 Ref.12

Modified residue

773

1

Phosphoserine Ref.13

Modified residue

775

1

Phosphoserine Ref.9 Ref.13

Modified residue

776

1

Phosphothreonine Ref.7 Ref.13

Modified residue

778

1

Phosphoserine Ref.7 Ref.13

Modified residue

886

1

Phosphoserine Ref.13

Modified residue

898

1

Phosphoserine Ref.13

Modified residue

925

1

Phosphoserine Ref.13

Modified residue

977

1

Phosphoserine Ref.12 Ref.13

Modified residue

1013

1

Phosphoserine Ref.12 Ref.13

Modified residue

1014

1

Phosphoserine Ref.12 Ref.13

Experimental info

Sequence conflict

376 – 377

2

DK → EE in AAA34670. Ref.1

Sequence conflict

534

1

N → K in AAA34670. Ref.1

Sequence conflict

657

1

D → H in AAA34670. Ref.1

Sequence conflict

889

1

S → T in AAA34670. Ref.1

Sequence conflict

988 – 1014

27

ARGMA…GNDSS → QEVWQASTCTLGKRVTSSHK KMEMTAVRRKNFEVNMKRK Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q00816 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 0D4AAC75E111B346
Show »

FASTA

1,014

112,616

        10         20         30         40         50         60 
MSTNLANYFA GKKDIENEHV NRNASHESNS KSDVKISGND NDNDEDMGPS VSMAVQAKND 

        70         80         90        100        110        120 
DDFHKSTFNL KRTRSMGLLD EYIDPTKKLL GRSDDLYDND NEYYDNSSNN SSSNSSDDDY 

       130        140        150        160        170        180 
DDGYQEHSTS VSPPPADNDS YLIPQDDNDV VVEPERHVDY LSHEWKESEI SNSWKYIILK 

       190        200        210        220        230        240 
KKKRDVDLVN AARLENASWR TWAKARNNLK TVSPEVVNWS KDSDVTWLYG PIVRDSEGNA 

       250        260        270        280        290        300 
QSEEEHDLER GYGSDDENSK RISMPTKNSK SIAAAPKPIL KKRTVTEIIE DNALWKLNEA 

       310        320        330        340        350        360 
RKHMTEMKHA SVIMDPNGNK NVHDDFDALA AQVNAQYYHY PKESNSSVSL KSQHSDKKDN 

       370        380        390        400        410        420 
STIPNPVGEN SNGGGDKGEE DLHLKSALHV QNNRSTAQSN KSILENSTND RKANLDQNLN 

       430        440        450        460        470        480 
SPDNNRFPSS TSSSNRDNEN NSMGLSSILT SNPSEKSNKP TKNRHIHFND RVEQCMALRY 

       490        500        510        520        530        540 
PASQSEDDES DDENKQYVDV NNNANVTTIN NNRTPLLAIQ HKSIPINSAT EHLNKNTSDD 

       550        560        570        580        590        600 
DTSSQSSSSS HSDDEEHGGL YINARFSRRS DSGVHSPITD NSSVASSTTS RAHVRPIIKL 

       610        620        630        640        650        660 
LPDTTLNYGS DEESDNGEFN GYGNAVSHNV NTSRGYDYIY DYNSVYTGDT SSFLPVDSCD 

       670        680        690        700        710        720 
IVDVPEGMDL QTAIADDNAS NYEFNNAVES KEKHVPQLHK ASANNTTRQH GSHMLLYDDD 

       730        740        750        760        770        780 
NYSSSSDSEQ QFIEDSQYNS SDDEEEEDDD DQEVDDNHDE GLSLRRTLSL GKSGSTNSLY 

       790        800        810        820        830        840 
DLAQPSLSSA TPQQKNPTNF TGGKTDVDKD AQLAVRPYPL KRNSSSGNFI FNSDSEEESS 

       850        860        870        880        890        900 
SEEEQRPLPA NSQLVNRSVL KGSVTPANIS SQKKKALPKQ PKASDSSQSF RIVNNTPSPA 

       910        920        930        940        950        960 
EVGASDVAIE GYFSPRNESI KSVVSGGNMM DHQDHSEMDT LAKGFENCHI NNASKLKDKK 

       970        980        990       1000       1010 
VDSVQTTRKE ASLTDSSNES LHKVVQNARG MASKYLHSWK KSDVKPQENG NDSS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of Hex2 protein, a negative regulatory element necessary for glucose repression in yeast." Niederacher D., Entian K.-D. Eur. J. Biochem. 200:311-319(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"SRN1, a yeast gene involved in RNA processing, is identical to HEX2/REG1, a negative regulator in glucose repression." Tung K.-S., Norbeck L.L., Nolan S.L., Atkinson N.S., Hopper A.K. Mol. Cell. Biol. 12:2673-2680(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Sequencing and analysis of a 35.4 kb region on the right arm of chromosome IV from Saccharomyces cerevisiae reveal 23 open reading frames." Eide L.G., Sander C., Prydz H. Yeast 12:1085-1090(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1014.
[6]	"REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharomyces cerevisiae." Tu J.L., Carlson M. EMBO J. 14:5939-5946(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PP1.
[7]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-576; THR-776 AND SER-778, MASS SPECTROMETRY. Strain: 2124.
[8]	"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].
[9]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-75; SER-769 AND SER-775, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-421; SER-572 AND SER-576, MASS SPECTROMETRY. Strain: ADR376.
[11]	"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 THR-73; SER-75; TYR-480; SER-485 AND SER-490, MASS SPECTROMETRY.
[12]	"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-75; SER-242; SER-254; SER-349; SER-421; SER-570; SER-572; SER-576; SER-586; SER-587; THR-767; SER-769; SER-977; SER-1013 AND SER-1014, MASS SPECTROMETRY.
[13]	"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-75; SER-242; SER-254; SER-311; SER-421; SER-570; SER-572; SER-576; SER-582; TYR-608; SER-610; SER-614; SER-680; SER-773; SER-775; THR-776; SER-778; SER-886; SER-898; SER-925; SER-977; SER-1013 AND SER-1014, MASS SPECTROMETRY.
[14]	"Interaction of SNF1 protein kinase with its activating kinase Sak1." Liu Y., Xu X., Carlson M. Eukaryot. Cell 10:313-319(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SAK1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M33703 Genomic DNA. Translation: AAA34670.1. M90540 Genomic DNA. Translation: AAB59326.1. Z47814 Genomic DNA. Translation: CAA87807.1. Z74324 Genomic DNA. Translation: CAA98850.1. X95966 Genomic DNA. Translation: CAA65223.1. BK006938 Genomic DNA. Translation: DAA11873.1.
PIR	S32613.
RefSeq	NP_010311.1. NM_001180336.1.
3D structure databases
ProteinModelPortal	Q00816.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2513N.
IntAct	Q00816. 21 interactions.
MINT	MINT-648820.
STRING	4932.YDR028C.
Proteomic databases
PaxDb	Q00816.
PeptideAtlas	Q00816.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR028C; YDR028C; YDR028C.
GeneID	851592.
KEGG	sce:YDR028C.
Organism-specific databases
CYGD	YDR028c.
SGD	S000002435. REG1.
Phylogenomic databases
eggNOG	NOG70919.
OMA	WAKARNN.
OrthoDB	EOG4NPBC1.
Gene expression databases
Genevestigator	Q00816.
GermOnline	YDR028C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013860. DUF1752_fun. [Graphical view]
Pfam	PF08550. DUF1752. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	969075.

Entry information

Entry name

REG1_YEAST

Accession

Primary (citable) accession number: Q00816
Secondary accession number(s): D6VS13

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents