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Entry version 188 (08 May 2019)
Sequence version 2 (01 Jun 1994)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

Caution

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi330 – 356H-T-H motifSequence analysisAdd BLAST27

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-32018-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Nucleosome assembly protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NAP1
Ordered Locus Names:YKR048C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YKR048C

Saccharomyces Genome Database

More...
SGDi
S000001756 NAP1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001856591 – 417Nucleosome assembly proteinAdd BLAST417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei20PhosphothreonineCombined sources1
Modified residuei24PhosphothreonineCombined sources1
Modified residuei27PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P25293

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P25293

PRoteomics IDEntifications database

More...
PRIDEi
P25293

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P25293

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34179, 446 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1712 Gin4 complex

Database of interacting proteins

More...
DIPi
DIP-1380N

Protein interaction database and analysis system

More...
IntActi
P25293, 91 interactors

Molecular INTeraction database

More...
MINTi
P25293

STRING: functional protein association networks

More...
STRINGi
4932.YKR048C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P25293

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P25293

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni143 – 362Interaction with NBA11 PublicationAdd BLAST220

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi168 – 180Asp/Glu-rich (acidic)Add BLAST13
Compositional biasi324 – 336Asp/Glu-rich (acidic)Add BLAST13
Compositional biasi366 – 403Asp/Glu-rich (acidic)Add BLAST38

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000167738

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000171827

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25293

KEGG Orthology (KO)

More...
KOi
K11279

Identification of Orthologs from Complete Genome Data

More...
OMAi
CAPLYEK

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR037231 NAP-like_sf
IPR002164 NAP_family

The PANTHER Classification System

More...
PANTHERi
PTHR11875 PTHR11875, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00956 NAP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF143113 SSF143113, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC0F97FBA1B9EEA83
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S38122

NCBI Reference Sequences

More...
RefSeqi
NP_012974.1, NM_001179838.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKR048C_mRNA; YKR048C_mRNA; YKR048C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853922

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKR048C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
SMRiP25293
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34179, 446 interactors
ComplexPortaliCPX-1712 Gin4 complex
DIPiDIP-1380N
IntActiP25293, 91 interactors
MINTiP25293
STRINGi4932.YKR048C

PTM databases

iPTMnetiP25293

Proteomic databases

MaxQBiP25293
PaxDbiP25293
PRIDEiP25293

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR048C_mRNA; YKR048C_mRNA; YKR048C
GeneIDi853922
KEGGisce:YKR048C

Organism-specific databases

EuPathDBiFungiDB:YKR048C
SGDiS000001756 NAP1

Phylogenomic databases

GeneTreeiENSGT00940000167738
HOGENOMiHOG000171827
InParanoidiP25293
KOiK11279
OMAiCAPLYEK

Enzyme and pathway databases

BioCyciYEAST:G3O-32018-MONOMER

Miscellaneous databases

EvolutionaryTraceiP25293

Protein Ontology

More...
PROi
PR:P25293

Family and domain databases

InterProiView protein in InterPro
IPR037231 NAP-like_sf
IPR002164 NAP_family
PANTHERiPTHR11875 PTHR11875, 1 hit
PfamiView protein in Pfam
PF00956 NAP, 1 hit
SUPFAMiSSF143113 SSF143113, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNAP1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P25293
Secondary accession number(s): D6VXA9, P87196
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 1, 1994
Last modified: May 8, 2019
This is version 188 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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