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Protein

NADPH--cytochrome P450 reductase

Gene

NCP1

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

This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane.4 Publications

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • FAD1 PublicationNote: Binds 1 FAD per monomer.1 Publication
  • FMN1 PublicationNote: Binds 1 FMN per monomer.1 Publication

Kineticsi

The Vmax of the reaction is 721 pmol/min/pmol enzyme towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.

  1. KM=1.59 µM for cytochrome c1 Publication
  2. KM=1.46 µM for NADPH1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei67 – 671FMN1 Publication
    Binding sitei187 – 1871FMN; alternate1 Publication
    Binding sitei441 – 4411FAD1 Publication
    Binding sitei478 – 4781FAD1 Publication
    Binding sitei646 – 6461NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi71 – 788FMN; alternatePROSITE-ProRule annotation1 Publication
    Nucleotide bindingi116 – 1194FMNPROSITE-ProRule annotation1 Publication
    Nucleotide bindingi610 – 62112NADP1 PublicationAdd
    BLAST

    GO - Molecular functioni

    • electron carrier activity Source: SGD
    • FMN binding Source: InterPro
    • iron ion binding Source: InterPro
    • NADPH-hemoprotein reductase activity Source: SGD

    GO - Biological processi

    • ergosterol biosynthetic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BioCyciYEAST:YHR042W-MONOMER.
    BRENDAi1.6.2.4. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductase (EC:1.6.2.4)
    Short name:
    CPR
    Short name:
    P450R
    Gene namesi
    Name:NCP1
    Synonyms:CPR1, NCPR1, PRD1
    Ordered Locus Names:YHR042W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome VIII

    Organism-specific databases

    EuPathDBiFungiDB:YHR042W.
    SGDiS000001084. NCP1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2417HelicalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Disruption phenotypei

    Accumulates 20% of ergosterol of wild type.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 691690NADPH--cytochrome P450 reductasePRO_0000167608Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki666 – 666Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Phosphorylated by the cyclin-CDK PCL1-PHO85.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP16603.
    PaxDbiP16603.
    PeptideAtlasiP16603.

    Expressioni

    Inductioni

    By galactose and on the plasma membrane by iron or copper deficiency. Repressed by glucose.1 Publication

    Interactioni

    Subunit structurei

    Interacts with PCL1.2 Publications

    Protein-protein interaction databases

    BioGridi36474. 63 interactions.
    DIPiDIP-8294N.
    IntActiP16603. 8 interactions.
    MINTiMINT-2782506.
    STRINGi4932.YHR042W.

    Structurei

    Secondary structure

    1
    691
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi50 – 567Combined sources
    Beta strandi60 – 667Combined sources
    Beta strandi68 – 703Combined sources
    Helixi71 – 8717Combined sources
    Beta strandi91 – 955Combined sources
    Helixi96 – 983Combined sources
    Helixi104 – 1063Combined sources
    Beta strandi109 – 1168Combined sources
    Beta strandi119 – 1213Combined sources
    Helixi125 – 1273Combined sources
    Helixi128 – 1369Combined sources
    Turni139 – 1446Combined sources
    Beta strandi146 – 1538Combined sources
    Beta strandi157 – 1593Combined sources
    Helixi162 – 17312Combined sources
    Beta strandi183 – 1864Combined sources
    Turni187 – 1904Combined sources
    Helixi192 – 21019Combined sources
    Beta strandi223 – 2264Combined sources
    Beta strandi234 – 2396Combined sources
    Helixi243 – 2453Combined sources
    Beta strandi271 – 2788Combined sources
    Beta strandi287 – 2937Combined sources
    Beta strandi306 – 3094Combined sources
    Helixi315 – 32511Combined sources
    Beta strandi332 – 3343Combined sources
    Beta strandi337 – 3393Combined sources
    Beta strandi348 – 3514Combined sources
    Helixi352 – 3587Combined sources
    Helixi368 – 3747Combined sources
    Helixi375 – 3773Combined sources
    Helixi381 – 39010Combined sources
    Helixi394 – 4007Combined sources
    Helixi402 – 4043Combined sources
    Helixi408 – 4169Combined sources
    Helixi426 – 4327Combined sources
    Beta strandi439 – 4435Combined sources
    Turni447 – 4493Combined sources
    Beta strandi453 – 4597Combined sources
    Beta strandi469 – 4713Combined sources
    Helixi477 – 48913Combined sources
    Turni494 – 4963Combined sources
    Helixi508 – 5103Combined sources
    Turni511 – 5155Combined sources
    Beta strandi519 – 5224Combined sources
    Beta strandi536 – 5416Combined sources
    Helixi542 – 5454Combined sources
    Helixi546 – 56015Combined sources
    Turni564 – 5663Combined sources
    Beta strandi574 – 58512Combined sources
    Turni587 – 5915Combined sources
    Helixi592 – 5998Combined sources
    Helixi600 – 6023Combined sources
    Beta strandi603 – 6108Combined sources
    Helixi620 – 6267Combined sources
    Helixi628 – 6358Combined sources
    Turni636 – 6383Combined sources
    Beta strandi640 – 6456Combined sources
    Helixi650 – 66516Combined sources
    Helixi670 – 68213Combined sources
    Beta strandi685 – 6906Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BF4X-ray3.00A/B47-691[»]
    2BN4X-ray2.91A/B47-691[»]
    2BPOX-ray2.90A/B47-691[»]
    3FJOX-ray2.50A44-211[»]
    ProteinModelPortaliP16603.
    SMRiP16603. Positions 47-691.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16603.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 204144Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini266 – 529264FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0369.
    GeneTreeiENSGT00780000122041.
    HOGENOMiHOG000282027.
    InParanoidiP16603.
    KOiK00327.
    OMAiISHICNT.
    OrthoDBiEOG744TKC.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR023208. P450R.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000208. P450R. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16603-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI
    60 70 80 90 100
    AQVVTENNKN YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD
    110 120 130 140 150
    FESLNDVPVI VSIFISTYGE GDFPDGAVNF EDFICNAEAG ALSNLRYNMF
    160 170 180 190 200
    GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG KLGEADDGAG TTDEDYMAWK
    210 220 230 240 250
    DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE PSAHYLPSHQ
    260 270 280 290 300
    LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK
    310 320 330 340 350
    YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT
    360 370 380 390 400
    TIGAAIKHYL EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE
    410 420 430 440 450
    ITSKYFNIAD ALKYLSDGAK WDTVPMQFLV ESVPQMTPRY YSISSSSLSE
    460 470 480 490 500
    KQTVHVTSIV ENFPNPELPD APPVVGVTTN LLRNIQLAQN NVNIAETNLP
    510 520 530 540 550
    VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG PGTGVAPFRG
    560 570 580 590 600
    FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD
    610 620 630 640 650
    GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM
    660 670 680 690
    AKGVSTALVG ILSRGKSITT DEATELIKML KTSGRYQEDV W
    Length:691
    Mass (Da):76,772
    Last modified:January 23, 2007 - v3
    Checksum:i82BB847701E5438B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti423 – 4231T → N in BAA02936 (PubMed:3139648).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti474 – 4741V → G.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D13788 Genomic DNA. Translation: BAA02936.1.
    U00062 Genomic DNA. Translation: AAB68904.1.
    AY693091 Genomic DNA. Translation: AAT93110.1.
    BK006934 Genomic DNA. Translation: DAA06734.1.
    PIRiS46735.
    RefSeqiNP_011908.1. NM_001179172.1.

    Genome annotation databases

    EnsemblFungiiYHR042W; YHR042W; YHR042W.
    GeneIDi856438.
    KEGGisce:YHR042W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D13788 Genomic DNA. Translation: BAA02936.1.
    U00062 Genomic DNA. Translation: AAB68904.1.
    AY693091 Genomic DNA. Translation: AAT93110.1.
    BK006934 Genomic DNA. Translation: DAA06734.1.
    PIRiS46735.
    RefSeqiNP_011908.1. NM_001179172.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BF4X-ray3.00A/B47-691[»]
    2BN4X-ray2.91A/B47-691[»]
    2BPOX-ray2.90A/B47-691[»]
    3FJOX-ray2.50A44-211[»]
    ProteinModelPortaliP16603.
    SMRiP16603. Positions 47-691.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36474. 63 interactions.
    DIPiDIP-8294N.
    IntActiP16603. 8 interactions.
    MINTiMINT-2782506.
    STRINGi4932.YHR042W.

    Proteomic databases

    MaxQBiP16603.
    PaxDbiP16603.
    PeptideAtlasiP16603.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYHR042W; YHR042W; YHR042W.
    GeneIDi856438.
    KEGGisce:YHR042W.

    Organism-specific databases

    EuPathDBiFungiDB:YHR042W.
    SGDiS000001084. NCP1.

    Phylogenomic databases

    eggNOGiCOG0369.
    GeneTreeiENSGT00780000122041.
    HOGENOMiHOG000282027.
    InParanoidiP16603.
    KOiK00327.
    OMAiISHICNT.
    OrthoDBiEOG744TKC.

    Enzyme and pathway databases

    BioCyciYEAST:YHR042W-MONOMER.
    BRENDAi1.6.2.4. 984.

    Miscellaneous databases

    EvolutionaryTraceiP16603.
    NextBioi982042.
    PROiP16603.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR023208. P450R.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000208. P450R. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene."
      Yabusaki Y., Murakami H., Ohkawa H.
      J. Biochem. 103:1004-1010(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13 AND 45-62.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Multiple regulatory elements control expression of the gene encoding the Saccharomyces cerevisiae cytochrome P450, lanosterol 14 alpha-demethylase (ERG11)."
      Turi T.G., Loper J.C.
      J. Biol. Chem. 267:2046-2056(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Cytochrome P-450 reductase is responsible for the ferrireductase activity associated with isolated plasma membranes of Saccharomyces cerevisiae."
      Lesuisse E., Casteras-Simon M., Labbe P.
      FEMS Microbiol. Lett. 156:147-152(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
    7. "The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity."
      Venkateswarlu K., Lamb D.C., Kelly D.E., Manning N.J., Kelly S.L.
      J. Biol. Chem. 273:4492-4496(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    8. "Activities and kinetic mechanisms of native and soluble NADPH-cytochrome P450 reductase."
      Lamb D.C., Warrilow A.G., Venkateswarlu K., Kelly D.E., Kelly S.L.
      Biochem. Biophys. Res. Commun. 286:48-54(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
      Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. "The identification of Pcl1-interacting proteins that genetically interact with Cla4 may indicate a link between G1 progression and mitotic exit."
      Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.
      Genetics 166:1177-1186(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH PCL1.
    13. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
      Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
      J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    14. "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
      Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
      Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific."
      Ivanov A.S., Gnedenko O.V., Molnar A.A., Archakov A.I., Podust L.M.
      ACS Chem. Biol. 5:767-776(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FMN-BINDING AND FAD-BINDING.
    16. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases."
      Lamb D.C., Kim Y., Yermalitskaya L.V., Yermalitsky V.N., Lepesheva G.I., Kelly S.L., Waterman M.R., Podust L.M.
      Structure 14:51-61(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 34-691 IN COMPLEX WITH FAD; FMN AND NADP.

    Entry informationi

    Entry nameiNCPR_YEAST
    AccessioniPrimary (citable) accession number: P16603
    Secondary accession number(s): D3DKZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 169 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 46600 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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 VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    External Data

    Dasty 3

    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 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.