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Protein

Regulatory protein ADR1

Gene

ADR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri104 – 12623C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri132 – 15524C2H2-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular response to oleic acid Source: SGD
  • chromatin organization Source: SGD
  • negative regulation of chromatin silencing Source: SGD
  • peroxisome organization Source: SGD
  • positive regulation of ethanol catabolic process by positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of fatty acid beta-oxidation by positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of peroxisome organization by positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter by oleic acid Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter in response to ethanol Source: SGD
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29797-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein ADR1
Gene namesi
Name:ADR1
Ordered Locus Names:YDR216W
ORF Names:YD8142.16, YD8142B.08
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR216W.
SGDiS000002624. ADR1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061C → Y: Suppresses activity.
Mutagenesisi109 – 1091C → Y: Suppresses activity.
Mutagenesisi114 – 1141A → V: Lowers activity.
Mutagenesisi118 – 1181H → Y: Suppresses activity.
Mutagenesisi122 – 1221H → Y: Suppresses activity.
Mutagenesisi134 – 1341C → Y: Suppresses activity.
Mutagenesisi142 – 1421T → I: Lowers activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13231323Regulatory protein ADR1PRO_0000046801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541PhosphoserineCombined sources
Modified residuei188 – 1881PhosphothreonineCombined sources
Modified residuei193 – 1931PhosphothreonineCombined sources
Modified residuei230 – 2301Phosphoserine; by PKA; in vitroCombined sources1 Publication
Modified residuei258 – 2581PhosphoserineCombined sources
Modified residuei259 – 2591PhosphothreonineCombined sources
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei323 – 3231PhosphoserineCombined sources
Modified residuei325 – 3251PhosphoserineCombined sources
Modified residuei327 – 3271PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylation at Ser-230 by cAMP-dependent protein kinase A does not affect DNA binding but appears to prevent transcription of ADH2 during glucose repression.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07248.
PeptideAtlasiP07248.

PTM databases

iPTMnetiP07248.

Interactioni

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: SGD
  • TFIIB-class transcription factor binding Source: SGD
  • TFIID-class transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi32269. 101 interactions.
DIPiDIP-7N.
IntActiP07248. 26 interactions.
MINTiMINT-406601.

Structurei

Secondary structure

1
1323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi104 – 1063Combined sources
Turni107 – 1093Combined sources
Beta strandi111 – 1155Combined sources
Helixi116 – 12611Combined sources
Beta strandi131 – 1333Combined sources
Turni135 – 1373Combined sources
Beta strandi142 – 1443Combined sources
Helixi145 – 1517Combined sources
Turni152 – 1543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ARDNMR-A102-130[»]
1ARENMR-A102-130[»]
1ARFNMR-A102-130[»]
1PAANMR-A130-159[»]
2ADRNMR-A102-161[»]
5A7Uelectron microscopy4.80A130-158[»]
DisProtiDP00077.
ProteinModelPortaliP07248.
SMRiP07248. Positions 102-161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07248.

Family & Domainsi

Sequence similaritiesi

Contains 2 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri104 – 12623C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri132 – 15524C2H2-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00840000130382.
InParanoidiP07248.
KOiK09466.
OMAiIMDFERT.
OrthoDBiEOG7MPRP5.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANVEKPNDC SGFPVVDLNS CFSNGFNNEK QEIEMETDDS PILLMSSSAS
60 70 80 90 100
RENSNTFSVI QRTPDGKIIT TNNNMNSKIN KQLDKLPENL RLNGRTPSGK
110 120 130 140 150
LRSFVCEVCT RAFARQEHLK RHYRSHTNEK PYPCGLCNRC FTRRDLLIRH
160 170 180 190 200
AQKIHSGNLG ETISHTKKVS RTITKARKNS ASSVKFQTPT YGTPDNGNFL
210 220 230 240 250
NRTTANTRRK ASPEANVKRK YLKKLTRRAS FSAQSASSYA LPDQSSLEQH
260 270 280 290 300
PKDRVKFSTP ELVPLDLKNP ELDSSFDLNM NLDLNLNLDS NFNIALNRSD
310 320 330 340 350
SSGSTMNLDY KLPESANNYT YSSGSPTRAY VGANTNSKNA SFNDADLLSS
360 370 380 390 400
SYWIKAYNDH LFSVSESDET SPMNSELNDT KLIVPDFKST IHHLKDSRSS
410 420 430 440 450
SWTVAIDNNS NNNKVSDNQP DFVDFQELLD NDTLGNDLLE TTAVLKEFEL
460 470 480 490 500
LHDDSVSATA TSNEIDLSHL NLSNSPISPH KLIYKNKEGT NDDMLISFGL
510 520 530 540 550
DHPSNREDDL DKLCNMTRDV QAIFSQYLKG EESKRSLEDF LSTSNRKEKP
560 570 580 590 600
DSGNYTFYGL DCLTLSKISR ALPASTVNNN QPSHSIESKL FNEPMRNMCI
610 620 630 640 650
KVLRYYEKFS HDSSESVMDS NPNLLSKELL MPAVSELNEY LDLFKNNFLP
660 670 680 690 700
HFPIIHPSLL DLDLDSLQRY TNEDGYDDAE NAQLFDRLSQ GTDKEYDYEH
710 720 730 740 750
YQILSISKIV CLPLFMATFG SLHKFGYKSQ TIELYEMSRR ILHSFLETKR
760 770 780 790 800
RCRSTTVNDS YQNIWLMQSL ILSFMFALVA DYLEKIDSSL MKRQLSALCS
810 820 830 840 850
TIRSNCLPTI SANSEKSINN NNEPLTFGSP LQYIIFESKI RCTLMAYDFC
860 870 880 890 900
QFLKCFFHIK FDLSIKEKDV ETIYIPDNES KWASESIICN GHVVQKQNFY
910 920 930 940 950
DFRNFYYSFT YGHLHSIPEF LGSSMIYYEY DLRKGTKSHV FLDRIDTKRL
960 970 980 990 1000
ERSLDTSSYG NDNMAATNKN IAILIDDTII LKNNLMSMRF IKQIDRSFTE
1010 1020 1030 1040 1050
KVRKGQIAKI YDSFLNSVRL NFLKNYSVEV LCEFLVALNF SIRNISSLYV
1060 1070 1080 1090 1100
EEESDCSQRM NSPELPRIHL NNQALSVFNL QGYYYCFILI IKFLLDFEAT
1110 1120 1130 1140 1150
PNFKLLRIFI ELRSLANSIL LPTLSRLYPQ EFSGFPDVVF TQQFINKDNG
1160 1170 1180 1190 1200
MLVPGLSANE HHNGASAAVK TKLAKKINVE GLAMFINEIL VNSFNDTSFL
1210 1220 1230 1240 1250
NMEDPIRNEF SFDNGDRAVT DLPRSAHFLS DTGLEGINFS GLNDSHQTVS
1260 1270 1280 1290 1300
TLNLLRYGEN HSSKHKNGGK GQGFAEKYQL SLKYVTIAKL FFTNVKENYI
1310 1320
HCHMLDKMAS DFHTLENHLK GNS
Length:1,323
Mass (Da):150,941
Last modified:December 21, 2004 - v2
Checksum:iEE807290EA6CC5C2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1216 – 12161D → H in AAA73863 (PubMed:3515197).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28414 Genomic DNA. Translation: AAA73863.1.
Z48612 Genomic DNA. Translation: CAA88496.1.
Z68194 Genomic DNA. Translation: CAA92359.1.
Z68195 Genomic DNA. Translation: CAA92367.1.
BK006938 Genomic DNA. Translation: DAA12059.1.
PIRiA24534.
RefSeqiNP_010502.3. NM_001180524.3.

Genome annotation databases

EnsemblFungiiYDR216W; YDR216W; YDR216W.
GeneIDi851802.
KEGGisce:YDR216W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28414 Genomic DNA. Translation: AAA73863.1.
Z48612 Genomic DNA. Translation: CAA88496.1.
Z68194 Genomic DNA. Translation: CAA92359.1.
Z68195 Genomic DNA. Translation: CAA92367.1.
BK006938 Genomic DNA. Translation: DAA12059.1.
PIRiA24534.
RefSeqiNP_010502.3. NM_001180524.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ARDNMR-A102-130[»]
1ARENMR-A102-130[»]
1ARFNMR-A102-130[»]
1PAANMR-A130-159[»]
2ADRNMR-A102-161[»]
5A7Uelectron microscopy4.80A130-158[»]
DisProtiDP00077.
ProteinModelPortaliP07248.
SMRiP07248. Positions 102-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32269. 101 interactions.
DIPiDIP-7N.
IntActiP07248. 26 interactions.
MINTiMINT-406601.

PTM databases

iPTMnetiP07248.

Proteomic databases

MaxQBiP07248.
PeptideAtlasiP07248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR216W; YDR216W; YDR216W.
GeneIDi851802.
KEGGisce:YDR216W.

Organism-specific databases

EuPathDBiFungiDB:YDR216W.
SGDiS000002624. ADR1.

Phylogenomic databases

GeneTreeiENSGT00840000130382.
InParanoidiP07248.
KOiK09466.
OMAiIMDFERT.
OrthoDBiEOG7MPRP5.

Enzyme and pathway databases

BioCyciYEAST:G3O-29797-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07248.
NextBioi969641.
PROiP07248.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence homology of the yeast regulatory protein ADR1 with Xenopus transcription factor TFIIIA."
    Hartshorne T.A., Blumberg H., Young E.T.
    Nature 320:283-287(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  5. "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-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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-323 AND THR-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-188; THR-193; SER-230; SER-258; THR-259; SER-299 AND SER-325, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Zinc-dependent structure of a single-finger domain of yeast ADR1."
    Parraga G., Horvath S.J., Eisen A., Taylor W.E., Hood L., Young E.T., Klevit R.E.
    Science 241:1489-1492(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF ZINC-FINGERS.
  9. "ADR1a, a zinc finger peptide, exists in two folded conformations."
    Xu R.X., Horvath S.J., Klevit R.E.
    Biochemistry 30:3365-3371(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 131-159.
  10. "A folding transition and novel zinc finger accessory domain in the transcription factor ADR1."
    Bowers P.M., Schaufler L.E., Klevit R.E.
    Nat. Struct. Biol. 6:478-485(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 102-161.
  11. "Two zinc fingers of a yeast regulatory protein shown by genetic evidence to be essential for its function."
    Blumberg H., Eisen A., Sledziewski A., Bader D., Young E.T.
    Nature 328:443-445(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  12. "Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: residues that contact DNA and that transactivate."
    Thukral S.K., Morrison M.L., Young E.T.
    Proc. Natl. Acad. Sci. U.S.A. 88:9188-9192(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  13. "Mutations in the zinc fingers of ADR1 that change the specificity of DNA binding and transactivation."
    Thukral S.K., Morrison M.L., Young E.T.
    Mol. Cell. Biol. 12:2784-2792(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  14. "ADR1c mutations enhance the ability of ADR1 to activate transcription by a mechanism that is independent of effects on cyclic AMP-dependent protein kinase phosphorylation of Ser-230."
    Denis C.L., Fontaine S.C., Chase D., Kemp B.E., Bemis L.T.
    Mol. Cell. Biol. 12:1507-1514(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, PHOSPHORYLATION AT SER-230.
  15. "A mutation outside the two zinc fingers of ADR1 can suppress defects in either finger."
    Camier S., Kacherovsky N., Young E.T.
    Mol. Cell. Biol. 12:5758-5767(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  16. "Mutations in the zinc-finger region of the yeast regulatory protein ADR1 affect both DNA binding and transcriptional activation."
    Cook W.J., Mosley S.P., Audino D.C., Mullaney D.L., Rovelli A., Stewart G., Denis C.L.
    J. Biol. Chem. 269:9374-9379(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiADR1_YEAST
AccessioniPrimary (citable) accession number: P07248
Secondary accession number(s): D6VSJ9, Q04919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 21, 2004
Last modified: May 11, 2016
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.