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P25293

- NAP1_YEAST

UniProt

P25293 - NAP1_YEAST

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Protein

Nucleosome assembly protein

Gene
NAP1, YKR048C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 motif Reviewed predictionAdd
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
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

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

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.

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → T in AAA34811. 1 Publication
Sequence conflicti103 – 1042QS → LC in AAA34811. 1 Publication
Sequence conflicti137 – 1382RI → TM in AAA34811. 1 Publication
Sequence conflicti384 – 3841E → D in AAA34811. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 145 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.

Caution

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

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

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