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YEAST:NAP1

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) NAP1
Protein Name(s) Nucleosome assembly protein
External Links
UniProt P25293
EMBL M63555
AY692777
Z28272
Z28273
BK006944
PIR S38122
RefSeq NP_012974.1
PDB 2AYU
2Z2R
PDBsum 2AYU
2Z2R
ProteinModelPortal P25293
SMR P25293
BioGrid 34179
DIP DIP-1380N
IntAct P25293
MINT MINT-397964
STRING 4932.YKR048C
MaxQB P25293
PaxDb P25293
PeptideAtlas P25293
EnsemblFungi [example_ID YKR048C]
GeneID 853922
KEGG sce:YKR048C
CYGD YKR048c
SGD S000001756
eggNOG NOG285183
GeneTree ENSGT00480000042668
HOGENOM HOG000171827
InParanoid P25293
KO K11279
OMA IGTINEE
OrthoDB EOG7PZS7F
BioCyc YEAST:G3O-32018-MONOMER
EvolutionaryTrace P25293
NextBio 975273
PRO PR:P25293
Proteomes UP000002311
Genevestigator P25293
GO GO:0005935
GO:0005737
GO:0005634
GO:0030332
GO:0003677
GO:0008047
GO:0042393
GO:0042802
GO:0007117
GO:0006334
GO:0006337
GO:0043085
GO:0031116
GO:0032968
GO:0006606
InterPro IPR002164
PANTHER PTHR11875
Pfam PF00956

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:2000617

positive regulation of histone H3-K9 acetylation

PMID:23401858[1]

ECO:0000315

P

Figures 1 and 4 describe the role of Nap1 in transcription and should be considered when analyzing Figure 7. Figure 7 shows that Nap1 regulates histone acetylation.

complete
CACAO 7232

involved_in

GO:2000617

positive regulation of histone H3-K9 acetylation

PMID:23401858[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043085

positive regulation of catalytic activity

PMID:22308335[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042393

histone binding

PMID:21348863[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042393

histone binding

PMID:17289584[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0032968

positive regulation of transcription elongation from RNA polymerase II promoter

PMID:22308335[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0031116

positive regulation of microtubule polymerization

PMID:7622567[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0030332

cyclin binding

PMID:7622566[6]

ECO:0000353

physical interaction evidence used in manual assertion

SGD:S000006323

F

Seeded From UniProt

complete

enables

GO:0008047

enzyme activator activity

PMID:22308335[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0007117

budding cell bud growth

PMID:13680156[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006606

protein import into nucleus

PMID:12456659[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006337

nucleosome disassembly

PMID:16492771[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006334

nucleosome assembly

PMID:2016313[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006334

nucleosome assembly

PMID:1400414[11]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:7622566[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0030332

cyclin binding

PMID:7622566[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P24869

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:7622566[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21179020[12]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25293

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18719252[13]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25293

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18467557[14]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25293

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16432217[15]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25293

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002164

C

Seeded From UniProt

complete

involved_in

GO:0006334

nucleosome assembly

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002164

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005935

cellular bud neck

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0029

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Xue, YM et al. (2013) Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation. Mol. Cell. Biol. 33 1645-56 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 Kuryan, BG et al. (2012) Histone density is maintained during transcription mediated by the chromatin remodeler RSC and histone chaperone NAP1 in vitro. Proc. Natl. Acad. Sci. U.S.A. 109 1931-6 PubMed GONUTS page
  3. ↑ Noda, M et al. (2011) Assembly states of the nucleosome assembly protein 1 (NAP-1) revealed by sedimentation velocity and non-denaturing MS. Biochem. J. 436 101-12 PubMed GONUTS page
  4. ↑ Luk, E et al. (2007) Chz1, a nuclear chaperone for histone H2AZ. Mol. Cell 25 357-68 PubMed GONUTS page
  5. ↑ Kellogg, DR & Murray, AW (1995) NAP1 acts with Clb1 to perform mitotic functions and to suppress polar bud growth in budding yeast. J. Cell Biol. 130 675-85 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 6.3 Kellogg, DR et al. (1995) Members of the NAP/SET family of proteins interact specifically with B-type cyclins. J. Cell Biol. 130 661-73 PubMed GONUTS page
  7. ↑ Shields, CM et al. (2003) Saccharomyces cerevisiae Ats1p interacts with Nap1p, a cytoplasmic protein that controls bud morphogenesis. Curr. Genet. 44 184-94 PubMed GONUTS page
  8. ↑ Mosammaparast, N et al. (2002) A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B. EMBO J. 21 6527-38 PubMed GONUTS page
  9. ↑ Lorch, Y et al. (2006) Chromatin remodeling by nucleosome disassembly in vitro. Proc. Natl. Acad. Sci. U.S.A. 103 3090-3 PubMed GONUTS page
  10. ↑ Ishimi, Y & Kikuchi, A (1991) Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro. J. Biol. Chem. 266 7025-9 PubMed GONUTS page
  11. ↑ Fujii-Nakata, T et al. (1992) Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity. J. Biol. Chem. 267 20980-6 PubMed GONUTS page
  12. ↑ Lambert, JP et al. (2010) Defining the budding yeast chromatin-associated interactome. Mol. Syst. Biol. 6 448 PubMed GONUTS page
  13. ↑ Yu, H et al. (2008) High-quality binary protein interaction map of the yeast interactome network. Science 322 104-10 PubMed GONUTS page
  14. ↑ Tarassov, K et al. (2008) An in vivo map of the yeast protein interactome. Science 320 1465-70 PubMed GONUTS page
  15. ↑ Park, YJ & Luger, K (2006) The structure of nucleosome assembly protein 1. Proc. Natl. Acad. Sci. U.S.A. 103 1248-53 PubMed GONUTS page
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