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Entry version 190 (10 Apr 2019)
Sequence version 1 (01 Jul 1989)
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Protein

Anaphase-promoting complex subunit CDC16

Gene

CDC16

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

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.5 Publications

Miscellaneous

Present with 2753 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

<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 - 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

Biological processCell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31830-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00143

<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:
Anaphase-promoting complex subunit CDC16
Alternative name(s):
Cell division control protein 16
<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:CDC16
Ordered Locus Names:YKL022C
<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:YKL022C

Saccharomyces Genome Database

More...
SGDi
S000001505 CDC16

<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

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

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>Mutagenesisi44S → A: Abolishes phosphorylation; when associated with A-59; A-95; A-103; A-115 and A-406. 1 Publication1
Mutagenesisi59S → A: Abolishes phosphorylation; when associated with A-44; A-95; A-103; A-115 and A-406. 1 Publication1
Mutagenesisi95S → A: Abolishes phosphorylation; when associated with A-44; A-59; A-103; A-115 and A-406. 1 Publication1
Mutagenesisi103S → A: Abolishes phosphorylation; when associated with A-44; A-59; A-95; A-115 and A-406. 1 Publication1
Mutagenesisi115T → A: Abolishes phosphorylation; when associated with A-44; A-59; A-95; A-103 and A-406. 1 Publication1
Mutagenesisi406T → A: Abolishes phosphorylation; when associated with A-44; A-59; A-95; A-103 and A-115. 1 Publication1
Mutagenesisi482C → Y in CDC16-264; G2/M cell cycle arrest at 36 degrees Celsius. 1 Publication1
Mutagenesisi530S → P in CDC16-183; G2/M cell cycle arrest at 37 degrees Celsius. 1 Publication1
Mutagenesisi557S → F in CDC16-1; G2/M cell cycle arrest at 36 degrees Celsius. 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_00001062691 – 840Anaphase-promoting complex subunit CDC16Add BLAST840

<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

Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P09798

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

More...
PaxDbi
P09798

PRoteomics IDEntifications database

More...
PRIDEi
P09798

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P09798

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P09798

<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

The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. Interacts with AMA1.3 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

WithEntry#Exp.IntActNotes
DOC1P5306813EBI-4208,EBI-2603

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34109, 169 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-756 Anaphase-Promoting Complex variant 1
CPX-760 Anaphase-Promoting Complex variant 2
CPX-761 Anaphase-Promoting Complex variant 3
CPX-762 Anaphase-Promoting Complex variant 4

Database of interacting proteins

More...
DIPi
DIP-25N

Protein interaction database and analysis system

More...
IntActi
P09798, 30 interactors

Molecular INTeraction database

More...
MINTi
P09798

STRING: functional protein association networks

More...
STRINGi
4932.YKL022C

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P09798

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

More...
SMRi
P09798

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati229 – 260TPR 1Add BLAST32
Repeati263 – 288TPR 2Add BLAST26
Repeati296 – 319TPR 3Add BLAST24
Repeati357 – 388TPR 4Add BLAST32
Repeati393 – 416TPR 5Add BLAST24
Repeati426 – 454TPR 6Add BLAST29
Repeati464 – 492TPR 7Add BLAST29
Repeati499 – 526TPR 8Add BLAST28
Repeati531 – 560TPR 9Add BLAST30
Repeati565 – 593TPR 10Add BLAST29
Repeati600 – 628TPR 11Add BLAST29
Repeati633 – 665TPR 12Add BLAST33
Repeati671 – 703TPR 13Add BLAST33
Repeati708 – 737TPR 14Add BLAST30

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 biasi209 – 220Poly-ThrAdd BLAST12

<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

Belongs to the APC6/CDC16 family.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182950

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000160791

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P09798

KEGG Orthology (KO)

More...
KOi
K03353

Identification of Orthologs from Complete Genome Data

More...
OMAi
YIDQQQY

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR013105 TPR_2
IPR019734 TPR_repeat

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07719 TPR_2, 1 hit
PF13181 TPR_8, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00028 TPR, 8 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48452 SSF48452, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50005 TPR, 7 hits
PS50293 TPR_REGION, 2 hits

<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>.<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.

P09798-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKFCLYCCHC YIVICGKATH YYKSSKATSN LKSSNRVLMR NPMSPSEQHS
60 70 80 90 100
QHNSTLAASP FVSNVSAART QQSLPTDAQN DRLQQPWNRT NTATSPYQSL
110 120 130 140 150
ANSPLIQKLQ ANIMTPHQPS ANSNSNSNSI TGNVVNDNNL LASMSKNSMF
160 170 180 190 200
GSTIPSTLRK VSLQREYKDS VDGVVRDEDN DEDVHNNGDA AANANNDRES
210 220 230 240 250
KLGHNGPLTT TTLTTTTTAT QLDVSELSAI ERLRLWRFDA LMQHMYRTAE
260 270 280 290 300
YIADKVYNIS NDPDDAFWLG QVYYNNNQYV RAVELITRNN LDGVNILCRY
310 320 330 340 350
LLGLSFVKLQ RFDDALDVIG EYNPFSEDPS TTAANTMSNN GNNSNTSQPV
360 370 380 390 400
TDGGIKMESS LCFLRGKIYF AQNNFNKARD AFREAILVDI KNFEAFEMLL
410 420 430 440 450
SKNLLTPQEE WDLFDSLDFK EFGEDKEIMK NLYKINLSKY INTEDITKSN
460 470 480 490 500
EILAKDYKLA DNVDVVRSKV DICYTQCKFN ECLELCETVL ENDEFNTNIL
510 520 530 540 550
PAYIGCLYEL SNKNKLFLLS HRLAETFPKS AITWFSVATY YMSLDRISEA
560 570 580 590 600
QKYYSKSSIL DPSFAAAWLG FAHTYALEGE QDQALTAYST ASRFFPGMHL
610 620 630 640 650
PKLFLGMQFM AMNSLNLAES YFVLAYDICP NDPLVLNEMG VMYFKKNEFV
660 670 680 690 700
KAKKYLKKAL EVVKDLDPSS RTTISIQLNL GHTYRKLNEN EIAIKCFRCV
710 720 730 740 750
LEKNDKNSEI HCSLGYLYLK TKKLQKAIDH LHKSLYLKPN NSSATALLKN
760 770 780 790 800
ALELNVTLSL DASHPLIDKS NLMSQASKDK ASLNKKRSSL TYDPVNMAKR
810 820 830 840
LRTQKEIFDQ NNKALRKGGH DSKTGSNNAD DDFDADMELE
Length:840
Mass (Da):94,992
Last modified:July 1, 1989 - v1
<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:iA096B34441083488
GO

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
X06165 Genomic DNA Translation: CAA29521.1
Z28022 Genomic DNA Translation: CAA81857.1
BK006944 Genomic DNA Translation: DAA09133.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A27832

NCBI Reference Sequences

More...
RefSeqi
NP_012903.1, NM_001179588.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKL022C_mRNA; YKL022C_mRNA; YKL022C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853846

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKL022C

<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
X06165 Genomic DNA Translation: CAA29521.1
Z28022 Genomic DNA Translation: CAA81857.1
BK006944 Genomic DNA Translation: DAA09133.1
PIRiA27832
RefSeqiNP_012903.1, NM_001179588.1

3D structure databases

ProteinModelPortaliP09798
SMRiP09798
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34109, 169 interactors
ComplexPortaliCPX-756 Anaphase-Promoting Complex variant 1
CPX-760 Anaphase-Promoting Complex variant 2
CPX-761 Anaphase-Promoting Complex variant 3
CPX-762 Anaphase-Promoting Complex variant 4
DIPiDIP-25N
IntActiP09798, 30 interactors
MINTiP09798
STRINGi4932.YKL022C

PTM databases

iPTMnetiP09798

Proteomic databases

MaxQBiP09798
PaxDbiP09798
PRIDEiP09798
TopDownProteomicsiP09798

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL022C_mRNA; YKL022C_mRNA; YKL022C
GeneIDi853846
KEGGisce:YKL022C

Organism-specific databases

EuPathDBiFungiDB:YKL022C
SGDiS000001505 CDC16

Phylogenomic databases

GeneTreeiENSGT00950000182950
HOGENOMiHOG000160791
InParanoidiP09798
KOiK03353
OMAiYIDQQQY

Enzyme and pathway databases

UniPathwayi
UPA00143

BioCyciYEAST:G3O-31830-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P09798

Family and domain databases

InterProiView protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR013105 TPR_2
IPR019734 TPR_repeat
PfamiView protein in Pfam
PF07719 TPR_2, 1 hit
PF13181 TPR_8, 1 hit
SMARTiView protein in SMART
SM00028 TPR, 8 hits
SUPFAMiSSF48452 SSF48452, 2 hits
PROSITEiView protein in PROSITE
PS50005 TPR, 7 hits
PS50293 TPR_REGION, 2 hits

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 nameiCDC16_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: P09798
Secondary accession number(s): D6VXR3
<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: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 10, 2019
This is version 190 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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
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