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Entry version 219 (29 Sep 2021)
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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

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-392154, Nitric oxide stimulates guanylate cyclase
R-SCE-5218920, VEGFR2 mediated vascular permeability
R-SCE-5578775, Ion homeostasis
R-SCE-9009391, Extra-nuclear 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

Saccharomyces Genome Database

More...
SGDi
S000001084, NCP1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YHR042W

<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

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 or proteolytic cleavage.<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, 71 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

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P16603, protein

<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

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

More...
SMRi
P16603

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1158, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156847

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001570_17_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16603

Identification of Orthologs from Complete Genome Data

More...
OMAi
QKRYQRD

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>. The information is filed in different subsections. The current subsections and their content are listed below:<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; 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:

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[»]
SMRiP16603
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36474, 71 interactors
DIPiDIP-8294N
IntActiP16603, 9 interactors
MINTiP16603
STRINGi4932.YHR042W

PTM databases

iPTMnetiP16603

Proteomic databases

MaxQBiP16603
PaxDbiP16603
PRIDEiP16603

Genome annotation databases

EnsemblFungiiYHR042W_mRNA; YHR042W; YHR042W
GeneIDi856438
KEGGisce:YHR042W

Organism-specific databases

SGDiS000001084, NCP1
VEuPathDBiFungiDB:YHR042W

Phylogenomic databases

eggNOGiKOG1158, Eukaryota
GeneTreeiENSGT00940000156847
HOGENOMiCLU_001570_17_3_1
InParanoidiP16603
OMAiQKRYQRD

Enzyme and pathway databases

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-392154, Nitric oxide stimulates guanylate cyclase
R-SCE-5218920, VEGFR2 mediated vascular permeability
R-SCE-5578775, Ion homeostasis
R-SCE-9009391, Extra-nuclear estrogen signaling
R-SCE-9033241, Peroxisomal protein import

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
CPR1, yeast
EvolutionaryTraceiP16603

Protein Ontology

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PROi
PR:P16603
RNActiP16603, protein

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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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: September 29, 2021
This is version 219 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, Direct protein sequencing, Reference proteome

Documents

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