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P25293

- NAP1_YEAST

UniProt

P25293 - NAP1_YEAST

Protein

Nucleosome assembly protein

Gene

NAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi330 – 35627H-T-H motifSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. cyclin binding Source: UniProtKB
    2. DNA binding Source: UniProtKB-KW
    3. enzyme activator activity Source: SGD
    4. histone binding Source: SGD
    5. identical protein binding Source: IntAct
    6. protein binding Source: IntAct

    GO - Biological processi

    1. budding cell bud growth Source: SGD
    2. nucleosome assembly Source: SGD
    3. nucleosome disassembly Source: SGD
    4. positive regulation of catalytic activity Source: SGD
    5. positive regulation of microtubule polymerization Source: SGD
    6. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
    7. protein import into nucleus Source: SGD

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32018-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleosome assembly protein
    Gene namesi
    Name:NAP1
    Ordered Locus Names:YKR048C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKR048c.
    SGDiS000001756. NAP1.

    Subcellular locationi

    Cytoplasm. Nucleus. Bud neck
    Note: Phosphorylation by CK2 promotes the import into the nucleus.

    GO - Cellular componenti

    1. cellular bud neck Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Exhibits a large proportion of multinucleate cells. Elongated buds. The percentage of elongated buds is significantly increased when GIN4 or CKI1 is also deleted. Small decrease in the percentage of cells with elongated buds is observed in NAP1 and CKA2 double mutant. NAP1 and CKI1 double mutant exhibits increased sensitivity to benomyl. Increased resistance to benomyl in NAP1 and CKA2 double mutant.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi99 – 991L → S: Predominantly cytoplasmic; when associated with A-159, A-177 and S-397. 1 Publication
    Mutagenesisi159 – 1591S → A: Significant reduction in phosphorylation; when associated with A-397. Complete inhibition of phosphorylation; when associated with A-177 and A-397. Leads to a prolonged S phase and a shortened passage through G1; when associated with A-177 and A-397. Predominantly cytoplasmic; when associated with S-99, A-177 and A-397. 1 Publication
    Mutagenesisi159 – 1591S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-177 and A-397. 1 Publication
    Mutagenesisi177 – 1771S → A: Significant reduction in phosphorylation; when associated with A-397. Complete inhibition of phosphorylation; when associated with A-159 and A-397. Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-397. Predominantly cytoplasmic; when associated with S-99, A-159 and A-397. 1 Publication
    Mutagenesisi177 – 1771S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-397. 1 Publication
    Mutagenesisi397 – 3971S → A: Significant reduction in phosphorylation; when associated with either A-159 or A-177. Complete inhibition of phosphorylation; when associated with A-159 and A-177. Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-177. Predominantly cytoplasmic; when associated with S-99; A-159 and A-177. 1 Publication
    Mutagenesisi397 – 3971S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-177. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 417417Nucleosome assembly proteinPRO_0000185659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201Phosphothreonine3 Publications
    Modified residuei24 – 241Phosphothreonine3 Publications
    Modified residuei27 – 271Phosphoserine3 Publications
    Modified residuei53 – 531Phosphothreonine1 Publication
    Modified residuei69 – 691Phosphoserine1 Publication
    Modified residuei76 – 761Phosphoserine4 Publications
    Modified residuei82 – 821Phosphoserine2 Publications
    Modified residuei98 – 981Phosphoserine1 Publication
    Modified residuei104 – 1041Phosphoserine1 Publication
    Modified residuei140 – 1401Phosphoserine2 Publications
    Modified residuei159 – 1591Phosphoserine; by CK21 Publication
    Modified residuei177 – 1771Phosphoserine; by CK24 Publications
    Modified residuei397 – 3971Phosphoserine; by CK21 Publication

    Post-translational modificationi

    Phosphorylation by CK2 is required for normal progression through S phase. CK2 phosphorylation is not required for correct bud formation nor histone binding.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP25293.
    PaxDbiP25293.
    PeptideAtlasiP25293.

    Expressioni

    Gene expression databases

    GenevestigatoriP25293.

    Interactioni

    Subunit structurei

    Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1 which forms a ring at the bud neck. Interacts with the B-type cyclin CLB2. Interacts with 60S ribosomal protein L18 (RPL18A or RPL18B), CKA2, CKI1, eukaryotic elongation factor 1 complex eEF1A (TEF1 or TEF2), FOL1, HSC82, HTA2, HTB2, HTZ1, KAP114, KCC4, NIS1, SSA1, SSA2, SSB1, SSC1, SHM1, SIP5 and TCO89. Interacts with NBA1. Homodimer (in-vitro).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-11850,EBI-11850
    CKI1P204855EBI-11850,EBI-9699
    GIN4Q1226312EBI-11850,EBI-7595
    KCC4P253896EBI-11850,EBI-9607
    NIS1P539396EBI-11850,EBI-28760
    RIM11P386158EBI-11850,EBI-10642
    TCO89Q089212EBI-11850,EBI-37395

    Protein-protein interaction databases

    BioGridi34179. 273 interactions.
    DIPiDIP-1380N.
    IntActiP25293. 77 interactions.
    MINTiMINT-397964.
    STRINGi4932.YKR048C.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni73 – 753
    Helixi77 – 8711
    Helixi90 – 14051
    Beta strandi141 – 1433
    Helixi147 – 15913
    Helixi163 – 1653
    Helixi188 – 1947
    Helixi199 – 2013
    Helixi205 – 2084
    Helixi210 – 2134
    Beta strandi214 – 2185
    Beta strandi224 – 2263
    Beta strandi228 – 2358
    Turni237 – 2393
    Beta strandi241 – 2433
    Beta strandi246 – 25712
    Beta strandi260 – 2634
    Beta strandi265 – 2717
    Turni279 – 2813
    Beta strandi285 – 2895
    Turni295 – 2973
    Beta strandi304 – 3085
    Helixi312 – 3165
    Beta strandi327 – 3293
    Helixi332 – 35019
    Turni351 – 3555
    Helixi356 – 3616
    Helixi363 – 3697

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AYUX-ray3.00A1-417[»]
    2Z2RX-ray3.20A/B74-365[»]
    ProteinModelPortaliP25293.
    SMRiP25293. Positions 82-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25293.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni143 – 362220Interaction with NBA1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi168 – 18013Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi324 – 33613Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi366 – 40338Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    The acidic domains are probably involved in the interaction with histones.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG285183.
    GeneTreeiENSGT00480000042668.
    HOGENOMiHOG000171827.
    KOiK11279.
    OMAiMIEDDDP.
    OrthoDBiEOG7PZS7F.

    Family and domain databases

    InterProiIPR002164. NAP_family.
    [Graphical view]
    PANTHERiPTHR11875. PTHR11875. 1 hit.
    PfamiPF00956. NAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25293-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDPIRTKPK SSMQIDNAPT PHNTPASVLN PSYLKNGNPV RAQAQEQDDK    50
    IGTINEEDIL ANQPLLLQSI QDRLGSLVGQ DSGYVGGLPK NVKEKLLSLK 100
    TLQSELFEVE KEFQVEMFEL ENKFLQKYKP IWEQRSRIIS GQEQPKPEQI 150
    AKGQEIVESL NETELLVDEE EKAQNDSEEE QVKGIPSFWL TALENLPIVC 200
    DTITDRDAEV LEYLQDIGLE YLTDGRPGFK LLFRFDSSAN PFFTNDILCK 250
    TYFYQKELGY SGDFIYDHAE GCEISWKDNA HNVTVDLEMR KQRNKTTKQV 300
    RTIEKITPIE SFFNFFDPPK IQNEDQDEEL EEDLEERLAL DYSIGEQLKD 350
    KLIPRAVDWF TGAALEFEFE EDEEEADEDE DEEEDDDHGL EDDDGESAEE 400
    QDDFAGRPEQ APECKQS 417
    Length:417
    Mass (Da):47,885
    Last modified:June 1, 1994 - v2
    Checksum:iC0F97FBA1B9EEA83
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21S → T in AAA34811. (PubMed:2016313)Curated
    Sequence conflicti103 – 1042QS → LC in AAA34811. (PubMed:2016313)Curated
    Sequence conflicti137 – 1382RI → TM in AAA34811. (PubMed:2016313)Curated
    Sequence conflicti384 – 3841E → D in AAA34811. (PubMed:2016313)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63555 Genomic DNA. Translation: AAA34811.1.
    AY692777 Genomic DNA. Translation: AAT92796.1.
    Z28272 Genomic DNA. Translation: CAA82124.2.
    Z28273 Genomic DNA. Translation: CAA82125.1.
    BK006944 Genomic DNA. Translation: DAA09199.1.
    PIRiS38122.
    RefSeqiNP_012974.1. NM_001179838.1.

    Genome annotation databases

    EnsemblFungiiYKR048C; YKR048C; YKR048C.
    GeneIDi853922.
    KEGGisce:YKR048C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63555 Genomic DNA. Translation: AAA34811.1 .
    AY692777 Genomic DNA. Translation: AAT92796.1 .
    Z28272 Genomic DNA. Translation: CAA82124.2 .
    Z28273 Genomic DNA. Translation: CAA82125.1 .
    BK006944 Genomic DNA. Translation: DAA09199.1 .
    PIRi S38122.
    RefSeqi NP_012974.1. NM_001179838.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AYU X-ray 3.00 A 1-417 [» ]
    2Z2R X-ray 3.20 A/B 74-365 [» ]
    ProteinModelPortali P25293.
    SMRi P25293. Positions 82-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34179. 273 interactions.
    DIPi DIP-1380N.
    IntActi P25293. 77 interactions.
    MINTi MINT-397964.
    STRINGi 4932.YKR048C.

    Proteomic databases

    MaxQBi P25293.
    PaxDbi P25293.
    PeptideAtlasi P25293.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKR048C ; YKR048C ; YKR048C .
    GeneIDi 853922.
    KEGGi sce:YKR048C.

    Organism-specific databases

    CYGDi YKR048c.
    SGDi S000001756. NAP1.

    Phylogenomic databases

    eggNOGi NOG285183.
    GeneTreei ENSGT00480000042668.
    HOGENOMi HOG000171827.
    KOi K11279.
    OMAi MIEDDDP.
    OrthoDBi EOG7PZS7F.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32018-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P25293.
    NextBioi 975273.
    PROi P25293.

    Gene expression databases

    Genevestigatori P25293.

    Family and domain databases

    InterProi IPR002164. NAP_family.
    [Graphical view ]
    PANTHERi PTHR11875. PTHR11875. 1 hit.
    Pfami PF00956. NAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro."
      Ishimi Y., Kikuchi A.
      J. Biol. Chem. 266:7025-7029(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Members of the NAP/SET family of proteins interact specifically with B-type cyclins."
      Kellogg D.R., Kikuchi A., Fujii-Nakata T., Turck C.W., Murray A.W.
      J. Cell Biol. 130:661-673(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 251-256, FUNCTION, INTERACTION WITH CLB2, SUBCELLULAR LOCATION.
    6. "Cell cycle-dependent assembly of a Gin4-septin complex."
      Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R.
      Mol. Biol. Cell 13:2091-2105(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE GIN4 COMPLEX.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; THR-24; SER-27; SER-76 AND SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
      Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
      Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RPL18A OR RPL18B; CKA2; CKI1; TEF1 OR TEF2; FOL1; HSC82; HTA2; HTB2; HTZ1; KAP114; KCC4; NIS1; SSA1; SSA2; SSB1; SSC1; SHM1; SIP5; TCO89 AND NBA1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-82; SER-98; SER-104 AND SER-140, PHOSPHORYLATION AT SER-159; SER-177 AND SER-397 BY CK2, MUTAGENESIS OF LEU-99; SER-159; SER-177 AND SER-397, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; THR-24; SER-27; SER-76; SER-140 AND SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; THR-24; SER-27; THR-53; SER-69; SER-76; SER-82 AND SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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].
    15. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiNAP1_YEAST
    AccessioniPrimary (citable) accession number: P25293
    Secondary accession number(s): D6VXA9, P87196
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8070 molecules/cell in log phase SD medium.1 Publication

    Caution

    NAP-I was previously referred to as AP-I.Curated

    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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3