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Protein

Nucleosome assembly protein

Gene

NAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
DNA bindingi330 – 356H-T-H motifSequence analysisAdd BLAST27

GO - Molecular functioni

  • cyclin binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • enzyme activator activity Source: SGD
  • histone binding Source: SGD

GO - Biological processi

  • budding cell bud growth Source: SGD
  • nucleosome assembly Source: SGD
  • nucleosome disassembly Source: SGD
  • positive regulation of catalytic activity Source: SGD
  • positive regulation of histone H3-K9 acetylation Source: CACAO
  • positive regulation of microtubule polymerization Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR048C.
SGDiS000001756. NAP1.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
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)DescriptionActionsGraphical viewLength
Mutagenesisi99L → S: Predominantly cytoplasmic; when associated with A-159, A-177 and S-397. 1 Publication1
Mutagenesisi159S → 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 Publication1
Mutagenesisi159S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-177 and A-397. 1 Publication1
Mutagenesisi177S → 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 Publication1
Mutagenesisi177S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-397. 1 Publication1
Mutagenesisi397S → 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 Publication1
Mutagenesisi397S → D: Leads to a prolonged S phase and a shortened passage through G1; when associated with A-159 and A-177. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001856591 – 417Nucleosome assembly proteinAdd BLAST417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei20PhosphothreonineCombined sources1
Modified residuei24PhosphothreonineCombined sources1
Modified residuei27PhosphoserineCombined sources1
Cross-linki50Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei53PhosphothreonineCombined sources1
Modified residuei69PhosphoserineCombined sources1
Modified residuei76PhosphoserineCombined sources1
Modified residuei82PhosphoserineCombined sources1 Publication1
Modified residuei98Phosphoserine1 Publication1
Modified residuei104Phosphoserine1 Publication1
Modified residuei140PhosphoserineCombined sources1 Publication1
Modified residuei159Phosphoserine; by CK21 Publication1
Modified residuei177Phosphoserine; by CK2Combined sources1 Publication1
Modified residuei397Phosphoserine; by CK21 Publication1

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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25293.
PRIDEiP25293.

PTM databases

iPTMnetiP25293.

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
AIM44Q992994EBI-11850,EBI-29423
CKI1P204855EBI-11850,EBI-9699
GIN4Q1226312EBI-11850,EBI-7595
KCC4P253896EBI-11850,EBI-9607
NIS1P539397EBI-11850,EBI-28760
RIM11P386158EBI-11850,EBI-10642
TCO89Q089212EBI-11850,EBI-37395

GO - Molecular functioni

  • cyclin binding Source: UniProtKB
  • histone binding Source: SGD

Protein-protein interaction databases

BioGridi34179. 279 interactors.
DIPiDIP-1380N.
IntActiP25293. 81 interactors.
MINTiMINT-397964.

Structurei

Secondary structure

1417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni73 – 75Combined sources3
Helixi77 – 87Combined sources11
Helixi90 – 140Combined sources51
Beta strandi141 – 143Combined sources3
Helixi147 – 159Combined sources13
Helixi163 – 165Combined sources3
Helixi188 – 194Combined sources7
Helixi199 – 201Combined sources3
Helixi205 – 208Combined sources4
Helixi210 – 213Combined sources4
Beta strandi214 – 218Combined sources5
Beta strandi224 – 226Combined sources3
Beta strandi228 – 235Combined sources8
Turni237 – 239Combined sources3
Beta strandi241 – 243Combined sources3
Beta strandi246 – 257Combined sources12
Beta strandi260 – 263Combined sources4
Beta strandi265 – 271Combined sources7
Turni279 – 281Combined sources3
Beta strandi285 – 289Combined sources5
Turni295 – 297Combined sources3
Beta strandi304 – 308Combined sources5
Helixi312 – 316Combined sources5
Beta strandi327 – 329Combined sources3
Helixi332 – 350Combined sources19
Turni351 – 355Combined sources5
Helixi356 – 361Combined sources6
Helixi363 – 369Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AYUX-ray3.00A1-417[»]
2Z2RX-ray3.20A/B74-365[»]
5G2EX-ray6.70A/B/E/F/I/J/M/N/Q/R/U/V74-372[»]
ProteinModelPortaliP25293.
SMRiP25293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25293.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni143 – 362Interaction with NBA11 PublicationAdd BLAST220

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi168 – 180Asp/Glu-rich (acidic)Add BLAST13
Compositional biasi324 – 336Asp/Glu-rich (acidic)Add BLAST13
Compositional biasi366 – 403Asp/Glu-rich (acidic)Add BLAST38

Domaini

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

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00480000042668.
HOGENOMiHOG000171827.
InParanoidiP25293.
KOiK11279.
OMAiMIVEADY.
OrthoDBiEOG092C3XI2.

Family and domain databases

InterProiIPR002164. NAP_family.
[Graphical view]
PANTHERiPTHR11875. PTHR11875. 2 hits.
PfamiPF00956. NAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDPIRTKPK SSMQIDNAPT PHNTPASVLN PSYLKNGNPV RAQAQEQDDK
60 70 80 90 100
IGTINEEDIL ANQPLLLQSI QDRLGSLVGQ DSGYVGGLPK NVKEKLLSLK
110 120 130 140 150
TLQSELFEVE KEFQVEMFEL ENKFLQKYKP IWEQRSRIIS GQEQPKPEQI
160 170 180 190 200
AKGQEIVESL NETELLVDEE EKAQNDSEEE QVKGIPSFWL TALENLPIVC
210 220 230 240 250
DTITDRDAEV LEYLQDIGLE YLTDGRPGFK LLFRFDSSAN PFFTNDILCK
260 270 280 290 300
TYFYQKELGY SGDFIYDHAE GCEISWKDNA HNVTVDLEMR KQRNKTTKQV
310 320 330 340 350
RTIEKITPIE SFFNFFDPPK IQNEDQDEEL EEDLEERLAL DYSIGEQLKD
360 370 380 390 400
KLIPRAVDWF TGAALEFEFE EDEEEADEDE DEEEDDDHGL EDDDGESAEE
410
QDDFAGRPEQ APECKQS
Length:417
Mass (Da):47,885
Last modified:June 1, 1994 - v2
Checksum:iC0F97FBA1B9EEA83
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2S → T in AAA34811 (PubMed:2016313).Curated1
Sequence conflicti103 – 104QS → LC in AAA34811 (PubMed:2016313).Curated2
Sequence conflicti137 – 138RI → TM in AAA34811 (PubMed:2016313).Curated2
Sequence conflicti384E → D in AAA34811 (PubMed:2016313).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AYUX-ray3.00A1-417[»]
2Z2RX-ray3.20A/B74-365[»]
5G2EX-ray6.70A/B/E/F/I/J/M/N/Q/R/U/V74-372[»]
ProteinModelPortaliP25293.
SMRiP25293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34179. 279 interactors.
DIPiDIP-1380N.
IntActiP25293. 81 interactors.
MINTiMINT-397964.

PTM databases

iPTMnetiP25293.

Proteomic databases

MaxQBiP25293.
PRIDEiP25293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YKR048C.
SGDiS000001756. NAP1.

Phylogenomic databases

GeneTreeiENSGT00480000042668.
HOGENOMiHOG000171827.
InParanoidiP25293.
KOiK11279.
OMAiMIVEADY.
OrthoDBiEOG092C3XI2.

Enzyme and pathway databases

BioCyciYEAST:G3O-32018-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25293.
PROiP25293.

Family and domain databases

InterProiIPR002164. NAP_family.
[Graphical view]
PANTHERiPTHR11875. PTHR11875. 2 hits.
PfamiPF00956. NAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 166 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

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.