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Protein

NADPH--cytochrome P450 reductase 1

Gene

ATR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
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. Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and dichloroindophenol.UniRule annotation5 Publications

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotation1 PublicationNote: Binds 1 FAD per monomer.UniRule annotation
  • FMNUniRule annotation1 PublicationNote: Binds 1 FMN per monomer.UniRule annotation

Kineticsi

  1. KM=2.2 µM for NADPH (at pH 7.0 and 25 degrees Celsius)3 Publications
  2. KM=21.9 µM for NADPH (at pH 7.7 and 28 degrees Celsius)3 Publications
  3. KM=2.0 µM for NADPH (at pH 7.25 and 25 degrees Celsius)3 Publications
  4. KM=17 µM for cytochrome c (at pH 7.0 and 25 degrees Celsius)3 Publications
  5. KM=24.3 µM for cytochrome c (at pH 7.7 and 28 degrees Celsius)3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei219 – 2191FMNUniRule annotation
    Binding sitei310 – 3101NADPUniRule annotation
    Binding sitei551 – 5511NADPUniRule annotation
    Binding sitei654 – 6541NADPUniRule annotation
    Binding sitei692 – 6921FADUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi91 – 966FMNUniRule annotation
    Nucleotide bindingi146 – 1494FMNUniRule annotation
    Nucleotide bindingi184 – 19310FMNUniRule annotation
    Nucleotide bindingi470 – 4734FADUniRule annotation
    Nucleotide bindingi488 – 4903FADUniRule annotation
    Nucleotide bindingi504 – 5074FADUniRule annotation
    Nucleotide bindingi612 – 6132NADPUniRule annotation
    Nucleotide bindingi618 – 6225NADPUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    • phenylpropanoid metabolic process Source: TAIR
    • response to abscisic acid Source: TAIR
    • response to oxidative stress Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Phenylpropanoid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BioCyciARA:AT4G24520-MONOMER.
    ARA:GQT-1216-MONOMER.
    MetaCyc:MONOMER-2101.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductase 1UniRule annotation (EC:1.6.2.4UniRule annotation)
    Short name:
    CPR 1UniRule annotation
    Short name:
    P450R 1UniRule annotation
    Gene namesi
    Name:ATR1
    Synonyms:AR1
    Ordered Locus Names:At4g24520
    ORF Names:F22K18.280
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G24520.

    Subcellular locationi

    • Endoplasmic reticulum membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 2625LumenalUniRule annotationAdd
    BLAST
    Transmembranei27 – 4721HelicalUniRule annotationAdd
    BLAST
    Topological domaini48 – 692645CytoplasmicUniRule annotationAdd
    BLAST

    GO - Cellular componenti

    • cytosol Source: TAIR
    • endoplasmic reticulum Source: TAIR
    • endoplasmic reticulum membrane Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 692691NADPH--cytochrome P450 reductase 1PRO_0000416839Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineCombined sources
    Modified residuei249 – 2491PhosphoserineCombined sources

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9SB48.
    PRIDEiQ9SB48.

    PTM databases

    iPTMnetiQ9SB48.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, stems, flowers and siliques.1 Publication

    Gene expression databases

    ExpressionAtlasiQ9SB48. baseline and differential.
    GenevisibleiQ9SB48. AT.

    Interactioni

    Protein-protein interaction databases

    BioGridi13843. 2 interactions.
    STRINGi3702.AT4G24520.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SB48.
    SMRiQ9SB48. Positions 85-692.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini85 – 235151Flavodoxin-likeUniRule annotationAdd
    BLAST
    Domaini290 – 537248FAD-binding FR-typeUniRule annotationAdd
    BLAST

    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
    Contains 1 FAD-binding FR-type domain.UniRule annotation
    Contains 1 flavodoxin-like domain.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG1158. Eukaryota.
    COG0369. LUCA.
    HOGENOMiHOG000282027.
    InParanoidiQ9SB48.
    OMAiEIFPEND.
    PhylomeDBiQ9SB48.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    HAMAPiMF_03212. NCPR.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin-like.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like_dom.
    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.

    This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: Q9SB48-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MTSALYASDL FKQLKSIMGT DSLSDDVVLV IATTSLALVA GFVVLLWKKT
    60 70 80 90 100
    TADRSGELKP LMIPKSLMAK DEDDDLDLGS GKTRVSIFFG TQTGTAEGFA
    110 120 130 140 150
    KALSEEIKAR YEKAAVKVID LDDYAADDDQ YEEKLKKETL AFFCVATYGD
    160 170 180 190 200
    GEPTDNAARF YKWFTEENER DIKLQQLAYG VFALGNRQYE HFNKIGIVLD
    210 220 230 240 250
    EELCKKGAKR LIEVGLGDDD QSIEDDFNAW KESLWSELDK LLKDEDDKSV
    260 270 280 290 300
    ATPYTAVIPE YRVVTHDPRF TTQKSMESNV ANGNTTIDIH HPCRVDVAVQ
    310 320 330 340 350
    KELHTHESDR SCIHLEFDIS RTGITYETGD HVGVYAENHV EIVEEAGKLL
    360 370 380 390 400
    GHSLDLVFSI HADKEDGSPL ESAVPPPFPG PCTLGTGLAR YADLLNPPRK
    410 420 430 440 450
    SALVALAAYA TEPSEAEKLK HLTSPDGKDE YSQWIVASQR SLLEVMAAFP
    460 470 480 490 500
    SAKPPLGVFF AAIAPRLQPR YYSISSSPRL APSRVHVTSA LVYGPTPTGR
    510 520 530 540 550
    IHKGVCSTWM KNAVPAEKSH ECSGAPIFIR ASNFKLPSNP STPIVMVGPG
    560 570 580 590 600
    TGLAPFRGFL QERMALKEDG EELGSSLLFF GCRNRQMDFI YEDELNNFVD
    610 620 630 640 650
    QGVISELIMA FSREGAQKEY VQHKMMEKAA QVWDLIKEEG YLYVCGDAKG
    660 670 680 690
    MARDVHRTLH TIVQEQEGVS SSEAEAIVKK LQTEGRYLRD VW
    Length:692
    Mass (Da):76,766
    Last modified:May 1, 2000 - v1
    Checksum:i7DD77E418CCF2FA6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti161 – 1611Y → S in CAA46814 (PubMed:9235908).Curated
    Sequence conflicti477 – 4804SPRL → CQDW in CAA46814 (PubMed:9235908).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X66016 mRNA. Translation: CAA46814.1.
    AL035356 Genomic DNA. Translation: CAA23011.1.
    AL161561 Genomic DNA. Translation: CAB79362.1.
    CP002687 Genomic DNA. Translation: AEE84919.1.
    AY054688 mRNA. Translation: AAK96879.1.
    BT008426 mRNA. Translation: AAP37785.1.
    PIRiT05582.
    RefSeqiNP_194183.1. NM_118585.3. [Q9SB48-1]
    UniGeneiAt.144.
    At.70123.

    Genome annotation databases

    EnsemblPlantsiAT4G24520.1; AT4G24520.1; AT4G24520. [Q9SB48-1]
    GeneIDi828554.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X66016 mRNA. Translation: CAA46814.1.
    AL035356 Genomic DNA. Translation: CAA23011.1.
    AL161561 Genomic DNA. Translation: CAB79362.1.
    CP002687 Genomic DNA. Translation: AEE84919.1.
    AY054688 mRNA. Translation: AAK96879.1.
    BT008426 mRNA. Translation: AAP37785.1.
    PIRiT05582.
    RefSeqiNP_194183.1. NM_118585.3. [Q9SB48-1]
    UniGeneiAt.144.
    At.70123.

    3D structure databases

    ProteinModelPortaliQ9SB48.
    SMRiQ9SB48. Positions 85-692.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi13843. 2 interactions.
    STRINGi3702.AT4G24520.1.

    PTM databases

    iPTMnetiQ9SB48.

    Proteomic databases

    PaxDbiQ9SB48.
    PRIDEiQ9SB48.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G24520.1; AT4G24520.1; AT4G24520. [Q9SB48-1]
    GeneIDi828554.

    Organism-specific databases

    TAIRiAT4G24520.

    Phylogenomic databases

    eggNOGiKOG1158. Eukaryota.
    COG0369. LUCA.
    HOGENOMiHOG000282027.
    InParanoidiQ9SB48.
    OMAiEIFPEND.
    PhylomeDBiQ9SB48.

    Enzyme and pathway databases

    BioCyciARA:AT4G24520-MONOMER.
    ARA:GQT-1216-MONOMER.
    MetaCyc:MONOMER-2101.

    Miscellaneous databases

    PROiQ9SB48.

    Gene expression databases

    ExpressionAtlasiQ9SB48. baseline and differential.
    GenevisibleiQ9SB48. AT.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    HAMAPiMF_03212. NCPR.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin-like.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like_dom.
    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. "Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5."
      Urban P., Mignotte C., Kazmaier M., Delorme F., Pompon D.
      J. Biol. Chem. 272:19176-19186(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Strain: cv. Landsberg erecta.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Differential redox and electron-transfer properties of purified yeast, plant and human NADPH-cytochrome P-450 reductases highly modulate cytochrome P-450 activities."
      Louerat-Oriou B., Perret A., Pompon D.
      Eur. J. Biochem. 258:1040-1049(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    6. "Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation."
      Mizutani M., Ohta D.
      Plant Physiol. 116:357-367(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    7. "High yield purification and characterization of engineered human P450 1A2 and generation of immuno-inhibitor antibodies."
      Louerat-Oriou B., Flinois J.P., Beaune P.H., Pompon D.
      Pharmacogenetics 9:61-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Microsomal electron transfer in higher plants: cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis."
      Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.
      Plant Physiol. 119:353-361(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNCPR1_ARATH
    AccessioniPrimary (citable) accession number: Q9SB48
    Secondary accession number(s): Q39035
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2012
    Last sequence update: May 1, 2000
    Last modified: January 20, 2016
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    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.