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Entry version 206 (08 May 2019)
Sequence version 3 (23 Jan 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.UniRule annotation4 Publications

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

The Vmax of the reaction is 721 pmol/min/pmol enzyme towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.1 Publication
  1. KM=1.59 µM for cytochrome c1 Publication
  2. KM=1.46 µM for NADPH1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei78FMN; alternate1 Publication1
    Binding sitei187FMNUniRule annotation1
    Binding sitei187FMN; alternate1 Publication1
    Binding sitei285NADPUniRule annotation1 Publication1
    Binding sitei543NADPUniRule annotation1 Publication1
    Binding sitei646NADP1 Publication1
    Binding sitei691FADUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi67 – 72FMNUniRule annotation2 Publications6
    Nucleotide bindingi116 – 119FMNUniRule annotation2 Publications4
    Nucleotide bindingi152 – 161FMNUniRule annotation2 Publications10
    Nucleotide bindingi439 – 442FADUniRule annotation1 Publication4
    Nucleotide bindingi457 – 459FADUniRule annotation1 Publication3
    Nucleotide bindingi476 – 479FADUniRule annotation1 Publication4
    Nucleotide bindingi610 – 611NADPUniRule annotation1 Publication2
    Nucleotide bindingi617 – 621NADPUniRule annotation1 Publication5

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    • ergosterol biosynthetic process Source: SGD

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
    LigandFAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:YHR042W-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.6.2.4 984

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-1222556 ROS and RNS production in phagocytes
    R-SCE-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
    R-SCE-203615 eNOS activation
    R-SCE-203641 NOSTRIN mediated eNOS trafficking
    R-SCE-392154 Nitric oxide stimulates guanylate cyclase
    R-SCE-5218920 VEGFR2 mediated vascular permeability
    R-SCE-5578775 Ion homeostasis
    R-SCE-9009391 Non-genomic estrogen signaling
    R-SCE-9033241 Peroxisomal protein import

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductaseUniRule annotation (EC:1.6.2.4UniRule annotation)
    Short name:
    CPRUniRule annotation
    Short name:
    P450RUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:NCP1UniRule annotation
    Synonyms:CPR1, NCPR1, PRD1
    Ordered Locus Names:YHR042WImported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VIII

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YHR042W

    Saccharomyces Genome Database

    More...
    SGDi
    S000001084 NCP1

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 7LumenalCurated6
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei8 – 24HelicalSequence analysisAdd BLAST17
    Topological domaini25 – 691CytoplasmicCuratedAdd BLAST667

    Keywords - Cellular componenti

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

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Accumulates 20% of ergosterol of wild type.1 Publication

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001676082 – 691NADPH--cytochrome P450 reductaseAdd BLAST690

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki666Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P16603

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P16603

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P16603

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P16603

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with PCL1.2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    36474, 68 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-8294N

    Protein interaction database and analysis system

    More...
    IntActi
    P16603, 9 interactors

    Molecular INTeraction database

    More...
    MINTi
    P16603

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YHR042W

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1691
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2BF4X-ray3.00A/B47-691[»]
    2BN4X-ray2.91A/B47-691[»]
    2BPOX-ray2.90A/B47-691[»]
    3FJOX-ray2.50A44-211[»]

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P16603

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P16603

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini61 – 204Flavodoxin-likeUniRule annotationAdd BLAST144
    Domaini266 – 529FAD-binding FR-typeUniRule annotationAdd BLAST264

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the NADPH--cytochrome P450 reductase family.UniRule annotation
    In the N-terminal section; belongs to the flavodoxin family.UniRule annotation
    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000156847

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000282027

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P16603

    KEGG Orthology (KO)

    More...
    KOi
    K00327

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    TKMDVAF

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.20.990.10, 1 hit
    3.40.50.360, 1 hit
    3.40.50.80, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_03212 NCPR, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003097 CysJ-like_FAD-binding
    IPR017927 FAD-bd_FR_type
    IPR001094 Flavdoxin-like
    IPR008254 Flavodoxin/NO_synth
    IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
    IPR029039 Flavoprotein-like_sf
    IPR039261 FNR_nucleotide-bd
    IPR023173 NADPH_Cyt_P450_Rdtase_alpha
    IPR001433 OxRdtase_FAD/NAD-bd
    IPR023208 P450R
    IPR017938 Riboflavin_synthase-like_b-brl

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00667 FAD_binding_1, 1 hit
    PF00258 Flavodoxin_1, 1 hit
    PF00175 NAD_binding_1, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000208 P450R, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00369 FLAVODOXIN
    PR00371 FPNCR

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52218 SSF52218, 1 hit
    SSF52343 SSF52343, 1 hit
    SSF63380 SSF63380, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51384 FAD_FR, 1 hit
    PS50902 FLAVODOXIN_LIKE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i82BB847701E5438B
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti423T → N in BAA02936 (PubMed:3139648).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti474V → G. 1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S46735

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_011908.1, NM_001179172.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YHR042W_mRNA; YHR042W_mRNA; YHR042W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    856438

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YHR042W

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2BF4X-ray3.00A/B47-691[»]
    2BN4X-ray2.91A/B47-691[»]
    2BPOX-ray2.90A/B47-691[»]
    3FJOX-ray2.50A44-211[»]
    SMRiP16603
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36474, 68 interactors
    DIPiDIP-8294N
    IntActiP16603, 9 interactors
    MINTiP16603
    STRINGi4932.YHR042W

    PTM databases

    iPTMnetiP16603

    Proteomic databases

    MaxQBiP16603
    PaxDbiP16603
    PRIDEiP16603

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYHR042W_mRNA; YHR042W_mRNA; YHR042W
    GeneIDi856438
    KEGGisce:YHR042W

    Organism-specific databases

    EuPathDBiFungiDB:YHR042W
    SGDiS000001084 NCP1

    Phylogenomic databases

    GeneTreeiENSGT00940000156847
    HOGENOMiHOG000282027
    InParanoidiP16603
    KOiK00327
    OMAiTKMDVAF

    Enzyme and pathway databases

    BioCyciYEAST:YHR042W-MONOMER
    BRENDAi1.6.2.4 984
    ReactomeiR-SCE-1222556 ROS and RNS production in phagocytes
    R-SCE-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
    R-SCE-203615 eNOS activation
    R-SCE-203641 NOSTRIN mediated eNOS trafficking
    R-SCE-392154 Nitric oxide stimulates guanylate cyclase
    R-SCE-5218920 VEGFR2 mediated vascular permeability
    R-SCE-5578775 Ion homeostasis
    R-SCE-9009391 Non-genomic estrogen signaling
    R-SCE-9033241 Peroxisomal protein import

    Miscellaneous databases

    EvolutionaryTraceiP16603

    Protein Ontology

    More...
    PROi
    PR:P16603

    Family and domain databases

    Gene3Di1.20.990.10, 1 hit
    3.40.50.360, 1 hit
    3.40.50.80, 1 hit
    HAMAPiMF_03212 NCPR, 1 hit
    InterProiView protein in InterPro
    IPR003097 CysJ-like_FAD-binding
    IPR017927 FAD-bd_FR_type
    IPR001094 Flavdoxin-like
    IPR008254 Flavodoxin/NO_synth
    IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
    IPR029039 Flavoprotein-like_sf
    IPR039261 FNR_nucleotide-bd
    IPR023173 NADPH_Cyt_P450_Rdtase_alpha
    IPR001433 OxRdtase_FAD/NAD-bd
    IPR023208 P450R
    IPR017938 Riboflavin_synthase-like_b-brl
    PfamiView protein in Pfam
    PF00667 FAD_binding_1, 1 hit
    PF00258 Flavodoxin_1, 1 hit
    PF00175 NAD_binding_1, 1 hit
    PIRSFiPIRSF000208 P450R, 1 hit
    PRINTSiPR00369 FLAVODOXIN
    PR00371 FPNCR
    SUPFAMiSSF52218 SSF52218, 1 hit
    SSF52343 SSF52343, 1 hit
    SSF63380 SSF63380, 1 hit
    PROSITEiView protein in PROSITE
    PS51384 FAD_FR, 1 hit
    PS50902 FLAVODOXIN_LIKE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNCPR_YEAST
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16603
    Secondary accession number(s): D3DKZ0
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: May 8, 2019
    This is version 206 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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