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P25293 (NAP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleosome assembly protein
Gene names
Name:NAP1
Ordered Locus Names:YKR048C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6 Ref.11

Subunit structure

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). Ref.5 Ref.6 Ref.11 Ref.15

Subcellular location

Cytoplasm. Nucleus. Bud neck. Note: Phosphorylation by CK2 promotes the import into the nucleus. Ref.5 Ref.7 Ref.11

Domain

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

Post-translational modification

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

Disruption phenotype

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. Ref.11

Miscellaneous

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

Sequence similarities

Belongs to the nucleosome assembly protein (NAP) family.

Caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbudding cell bud growth

Inferred from mutant phenotype PubMed 13680156. Source: SGD

nucleosome assembly

Inferred from direct assay PubMed 1400414Ref.1. Source: SGD

nucleosome disassembly

Inferred from direct assay PubMed 16492771. Source: SGD

positive regulation of catalytic activity

Inferred from direct assay PubMed 22308335. Source: SGD

positive regulation of microtubule polymerization

Inferred from mutant phenotype PubMed 7622567. Source: SGD

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay PubMed 22308335. Source: SGD

protein import into nucleus

Inferred from mutant phenotype PubMed 12456659. Source: SGD

   Cellular_componentcellular bud neck

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.5. Source: UniProtKB

nucleus

Inferred from physical interaction PubMed 10767562. Source: SGD

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin binding

Inferred from physical interaction Ref.5. Source: UniProtKB

enzyme activator activity

Inferred from direct assay PubMed 22308335. Source: SGD

histone binding

Inferred from direct assay PubMed 17289584PubMed 21348863. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 11805826PubMed 18467557PubMed 18719252PubMed 21179020. Source: IntAct

protein binding

Inferred from physical interaction PubMed 10688190PubMed 11283351PubMed 11805826Ref.6PubMed 16429126PubMed 18467557PubMed 18719252PubMed 20489023PubMed 21179020PubMed 9214386PubMed 9813092. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Nucleosome assembly protein
PRO_0000185659

Regions

DNA binding330 – 35627H-T-H motif Potential
Region143 – 362220Interaction with NBA1
Compositional bias168 – 18013Asp/Glu-rich (acidic)
Compositional bias324 – 33613Asp/Glu-rich (acidic)
Compositional bias366 – 40338Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue201Phosphothreonine Ref.10 Ref.12 Ref.13
Modified residue241Phosphothreonine Ref.10 Ref.12 Ref.13
Modified residue271Phosphoserine Ref.10 Ref.12 Ref.13
Modified residue531Phosphothreonine Ref.13
Modified residue691Phosphoserine Ref.13
Modified residue761Phosphoserine Ref.9 Ref.10 Ref.12 Ref.13
Modified residue821Phosphoserine Ref.11 Ref.13
Modified residue981Phosphoserine Ref.11
Modified residue1041Phosphoserine Ref.11
Modified residue1401Phosphoserine Ref.11 Ref.12
Modified residue1591Phosphoserine; by CK2 Ref.11
Modified residue1771Phosphoserine; by CK2 Ref.10 Ref.11 Ref.12 Ref.13
Modified residue3971Phosphoserine; by CK2 Ref.11

Experimental info

Mutagenesis991L → S: Predominantly cytoplasmic; when associated with A-159, A-177 and S-397. Ref.11
Mutagenesis1591S → 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. Ref.11
Mutagenesis1591S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-177 and A-397. Ref.11
Mutagenesis1771S → 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. Ref.11
Mutagenesis1771S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-397. Ref.11
Mutagenesis3971S → 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. Ref.11
Mutagenesis3971S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-177. Ref.11
Sequence conflict21S → T in AAA34811. Ref.1
Sequence conflict103 – 1042QS → LC in AAA34811. Ref.1
Sequence conflict137 – 1382RI → TM in AAA34811. Ref.1
Sequence conflict3841E → D in AAA34811. Ref.1

Secondary structure

..................................................... 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25293 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: C0F97FBA1B9EEA83

FASTA41747,885
        10         20         30         40         50         60 
MSDPIRTKPK SSMQIDNAPT PHNTPASVLN PSYLKNGNPV RAQAQEQDDK IGTINEEDIL 

        70         80         90        100        110        120 
ANQPLLLQSI QDRLGSLVGQ DSGYVGGLPK NVKEKLLSLK TLQSELFEVE KEFQVEMFEL 

       130        140        150        160        170        180 
ENKFLQKYKP IWEQRSRIIS GQEQPKPEQI AKGQEIVESL NETELLVDEE EKAQNDSEEE 

       190        200        210        220        230        240 
QVKGIPSFWL TALENLPIVC DTITDRDAEV LEYLQDIGLE YLTDGRPGFK LLFRFDSSAN 

       250        260        270        280        290        300 
PFFTNDILCK TYFYQKELGY SGDFIYDHAE GCEISWKDNA HNVTVDLEMR KQRNKTTKQV 

       310        320        330        340        350        360 
RTIEKITPIE SFFNFFDPPK IQNEDQDEEL EEDLEERLAL DYSIGEQLKD KLIPRAVDWF 

       370        380        390        400        410 
TGAALEFEFE EDEEEADEDE DEEEDDDHGL EDDDGESAEE QDDFAGRPEQ APECKQS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"The structure of nucleosome assembly protein 1."
Park Y.-J., Luger K.
Proc. Natl. Acad. Sci. U.S.A. 103:1248-1253(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS38122.
RefSeqNP_012974.1. NM_001179838.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AYUX-ray3.00A1-417[»]
2Z2RX-ray3.20A/B74-365[»]
ProteinModelPortalP25293.
SMRP25293. Positions 82-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34179. 272 interactions.
DIPDIP-1380N.
IntActP25293. 77 interactions.
MINTMINT-397964.
STRING4932.YKR048C.

Proteomic databases

MaxQBP25293.
PaxDbP25293.
PeptideAtlasP25293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR048C; YKR048C; YKR048C.
GeneID853922.
KEGGsce:YKR048C.

Organism-specific databases

CYGDYKR048c.
SGDS000001756. NAP1.

Phylogenomic databases

eggNOGNOG285183.
GeneTreeENSGT00480000042668.
HOGENOMHOG000171827.
KOK11279.
OMAMIEDDDP.
OrthoDBEOG7PZS7F.

Enzyme and pathway databases

BioCycYEAST:G3O-32018-MONOMER.

Gene expression databases

GenevestigatorP25293.

Family and domain databases

InterProIPR002164. NAP_family.
[Graphical view]
PANTHERPTHR11875. PTHR11875. 1 hit.
PfamPF00956. NAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25293.
NextBio975273.
PROP25293.

Entry information

Entry nameNAP1_YEAST
AccessionPrimary (citable) accession number: P25293
Secondary accession number(s): D6VXA9, P87196
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 1, 1994
Last modified: June 11, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references