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Reviewed, UniProtKB/Swiss-Prot Q00816 (HEX2_YEAST)

Last modified December 15, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein HEX2
Alternative name(s):
    Protein SRN1
    Protein REG1
Gene names
Name: HEX2
Synonyms: REG1, SPP43, SRN1
Ordered Locus Names: YDR028C
ORF Names: YD9813.06C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1014 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Subcellular location

Nucleus.

Miscellaneous

Present with 2560 molecules/cell in log phase SD medium. Ref.7

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADE16P541131EBI-8270,EBI-14213

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10141014Protein HEX2
PRO_0000083953

Regions

Motif277 – 2837Nuclear localization signal Potential
Motif595 – 5995Nuclear localization signal Potential
Motif873 – 8797Nuclear localization signal Potential
Compositional bias543 – 55210Ser-rich
Compositional bias742 – 76019Asp/Glu-rich (acidic)
Compositional bias834 – 84411Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21Phosphoserine Ref.8
Modified residue731Phosphothreonine Ref.10
Modified residue751Phosphoserine Ref.8 Ref.10 Ref.9 Ref.11 Ref.12
Modified residue2421Phosphoserine Ref.11 Ref.12
Modified residue2541Phosphoserine Ref.11 Ref.12
Modified residue3111Phosphoserine Ref.12
Modified residue3491Phosphoserine Ref.11
Modified residue4211Phosphoserine Ref.9 Ref.11 Ref.12
Modified residue4801Phosphotyrosine Ref.10
Modified residue4851Phosphoserine Ref.10
Modified residue4901Phosphoserine Ref.10
Modified residue5701Phosphoserine Ref.11 Ref.12 Ref.6
Modified residue5721Phosphoserine Ref.9 Ref.11 Ref.12
Modified residue5761Phosphoserine Ref.9 Ref.11 Ref.12 Ref.6
Modified residue5821Phosphoserine Ref.12
Modified residue5861Phosphoserine Ref.11
Modified residue5871Phosphoserine Ref.11
Modified residue6081Phosphotyrosine Ref.12
Modified residue6101Phosphoserine Ref.12
Modified residue6141Phosphoserine Ref.12
Modified residue6801Phosphoserine Ref.12
Modified residue7671Phosphothreonine Ref.11
Modified residue7691Phosphoserine Ref.8 Ref.11
Modified residue7731Phosphoserine Ref.12
Modified residue7751Phosphoserine Ref.8 Ref.12
Modified residue7761Phosphothreonine Ref.12 Ref.6
Modified residue7781Phosphoserine Ref.12 Ref.6
Modified residue8861Phosphoserine Ref.12
Modified residue8981Phosphoserine Ref.12
Modified residue9251Phosphoserine Ref.12
Modified residue9771Phosphoserine Ref.11 Ref.12
Modified residue10131Phosphoserine Ref.11 Ref.12
Modified residue10141Phosphoserine Ref.11 Ref.12

Experimental info

Sequence conflict376 – 3772DK → EE in AAA34670. Ref.1
Sequence conflict5341N → K in AAA34670. Ref.1
Sequence conflict6571D → H in AAA34670. Ref.1
Sequence conflict8891S → T in AAA34670. Ref.1
Sequence conflict988 – 101427ARGMA…GNDSS → QEVWQASTCTLGKRVTSSHK KMEMTAVRRKNFEVNMKRK Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q00816-1 [UniParc].

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

FASTA1,014112,616
        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' 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: 1889400] [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: 1588964] [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. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"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: 8896275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1014.
[5]"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: 8846786] [Abstract]
Cited for: INTERACTION WITH PP1.
[6]"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: 11875433] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-576; THR-776 AND SER-778, MASS SPECTROMETRY.
[7]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"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: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-75; SER-769 AND SER-775, MASS SPECTROMETRY.
[9]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-421; SER-572 AND SER-576, MASS SPECTROMETRY.
[10]"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: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-73; SER-75; TYR-480; SER-485 AND SER-490, MASS SPECTROMETRY.
[11]"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: 17563356] [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.
[12]"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: 18407956] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
PIRS32613.
RefSeqNP_010311.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2513N.
IntActQ00816. 13 interactions.
STRINGQ00816.

Proteomic databases

PeptideAtlasQ00816.
PRIDEQ00816.

Genome annotation databases

EnsemblYDR028C; YDR028C; YDR028C; Saccharomyces cerevisiae. [Genome view]
GeneID851592.
KEGGsce:YDR028C.
NMPDRfig|4932.3.peg.1054.

Organism-specific databases

CYGDYDR028c.
SGDS000002435. REG1.

Phylogenomic databases

HOGENOMHBG203127.
OMAWAKARNN.
OrthoDBEOG93JDNB.

Gene expression databases

ArrayExpressQ00816.
GenevestigatorQ00816.
GermOnlineYDR028C. Saccharomyces cerevisiae.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio969075.

Entry information

Entry nameHEX2_YEAST
AccessionPrimary (citable) accession number: Q00816
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 15, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Yeast

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents