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Entry version 181 (18 Sep 2019)
Sequence version 1 (01 Oct 1993)
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Protein

Mitosis inhibitor protein kinase SWE1

Gene

SWE1

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

Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylating and inhibiting the mitosis-promoting cyclin B-bound CDC28 at 'Tyr-19'. SWE1-mediated inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to delay mitosis in response to defects in growth, actin organization or bud formation. Inhibits the activity of B-type cyclins in replication initiation strongly for CLB2, moderately for CLB3 and CLB4, and there is no apparent inhibition for CLB5 and CLB6, correlating with the normal expression timing of those cyclins. Hyperphosphorylation and degradation of SWE1 when all checkpoint requirement are met releases CLB2-CDC28 from inhibition and allows for progression through the cell cycle. SWE1-dependent CDC28 phosphorylation is also required for pachytene arrest upon activation of the recombination checkpoint during meiosis. Also involved in the regulation of nitrogen starvation- and short chain alcohol-induced filamentous growth, or filamentous differentiation in response to slowed DNA synthesis. Can act both on serines and on tyrosines.18 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei473ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei579Proton acceptorPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi584Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi597Magnesium; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi450 – 458ATPPROSITE-ProRule annotation9

<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 functionKinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
Biological processCell cycle, Cell division, Meiosis, Mitosis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31620-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-156711 Polo-like kinase mediated events

<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:
Mitosis inhibitor protein kinase SWE1 (EC:2.7.11.1)
Alternative name(s):
Wee1 homolog
<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:SWE1
Ordered Locus Names:YJL187C
ORF Names:J0406
<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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YJL187C

Saccharomyces Genome Database

More...
SGDi
S000003723 SWE1

<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>Mutagenesisi318 – 328Missing : Impairs interaction with HSL7 and prevents bud neck localization and degradation. 1 PublicationAdd BLAST11
Mutagenesisi320L → P or Q: Prevents degradation. 1 Publication1
Mutagenesisi324L → S: Prevents degradation. 1 Publication1
Mutagenesisi327F → S: Prevents degradation. 1 Publication1
Mutagenesisi328K → E: Prevents degradation. 1 Publication1
Mutagenesisi331L → I: Prevents degradation. 1 Publication1
Mutagenesisi332Y → C: Prevents degradation. 1 Publication1
Mutagenesisi473K → A or P: Loss of catalytic activity. 1 Publication1
Mutagenesisi797E → K, V or G: Prevents degradation. 1 Publication1
Mutagenesisi806I → T, A or N: Prevents degradation. 1 Publication1
Mutagenesisi807Q → R or E: Prevents degradation. 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_00000867271 – 819Mitosis inhibitor protein kinase SWE1Add BLAST819

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 residuei36Phosphoserine; by CDC52 Publications1
Modified residuei45Phosphothreonine; by CDC281 Publication1
Modified residuei56Phosphoserine; by CDC281 Publication1
Modified residuei63Phosphoserine; by CDC281 Publication1
Modified residuei70Phosphoserine1 Publication1
Modified residuei74Phosphothreonine; by CDC281 Publication1
Modified residuei102Phosphoserine; by CDC51 Publication1
Modified residuei105Phosphoserine; by CDC281 Publication1
Modified residuei111Phosphoserine; by CDC5, CDC28 and CLA42 Publications1
Modified residuei118Phosphoserine; by CDC52 Publications1
Modified residuei121Phosphothreonine; by CDC281 Publication1
Modified residuei124Phosphothreonine; by CDC281 Publication1
Modified residuei127Phosphoserine; by CDC281 Publication1
Modified residuei131Phosphothreonine; by CDC51 Publication1
Modified residuei133Phosphoserine; by CDC281 Publication1
Modified residuei136Phosphoserine; by CDC28 and CLA42 Publications1
Modified residuei156Phosphoserine; by CDC51 Publication1
Modified residuei169Phosphoserine; by CDC51 Publication1
Modified residuei196Phosphothreonine; by CDC281 Publication1
Modified residuei201Phosphoserine; by CDC281 Publication1
Modified residuei225Phosphoserine; by CDC51 Publication1
Modified residuei254Phosphoserine; by CDC51 Publication1
Modified residuei262Phosphoserine1 Publication1
Modified residuei263Phosphoserine; by CDC281 Publication1
Modified residuei266Phosphoserine; by CDC281 Publication1
Modified residuei280Phosphothreonine; by CDC51 Publication1
Modified residuei284Phosphoserine1 Publication1
Modified residuei294Phosphoserine1 Publication1
Modified residuei312Phosphoserine; by CLA41 Publication1
Modified residuei345Phosphoserine1 Publication1
Modified residuei367Phosphothreonine; by CDC281 Publication1
Modified residuei373Phosphothreonine; by CDC281 Publication1
Modified residuei379Phosphoserine; by CDC5 and CLA4Combined sources2 Publications1
Modified residuei384Phosphothreonine; by CDC281 Publication1
Modified residuei395Phosphoserine; by CDC5 and CLA41 Publication1
Modified residuei438Phosphoserine; by CDC5 and CLA41 Publication1
Modified residuei610Phosphoserine; by CDC52 Publications1
Modified residuei629Phosphothreonine; by CDC51 Publication1
Modified residuei688Phosphothreonine; by CDC5 and CLA41 Publication1
Modified residuei692Phosphothreonine1 Publication1
<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-linki741Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

<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 progressively by CLA4, CLB2-CDC28 and CDC5. CLA4-dependent phosphorylation occurs in late S phase, followed by phosphorylation by CLB2-CDC28 in early G2, when the levels of mitotic CLB2 increases. This phosphorylation is critical for triggering subsequent SWE1-CDC5 interaction and CDC5-dependent phosphorylation. The resulting cumulative hyperphosphorylation down-regulates SWE1 by targeting it for ubiquitin-mediated degradation. This stepwise phosphorylation is thought to be a mechanism to integrate the different checkpoint requirements before entry into mitosis.7 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32944

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

More...
PaxDbi
P32944

PRoteomics IDEntifications database

More...
PRIDEi
P32944

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32944

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expressed periodically during the cell cycle, with a peak in late G1. Transcriptional repression requires ZDS1. Protein accumulation is also periodic, peaking during S/G2 and declining prior to and during nuclear division of the unperturbed cell cycle. Stabilized during a checkpoint response in G2. Induced during meiosis. Induced by ethanol (at protein level).5 Publications

<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

Interacts with CLB2-CDC28. Partial hyperphosphorylation of SWE1 by CLB2-CDC28 stabilizes the ternary complex of SWE1 and CLB2-CDC28 and stimulates kinase activity of SWE1 in a positive feedback loop, maintaining CLB2-CDC28 in the tyrosine-phosphorylated state. Fully hyperphosphorylated SWE1 dissociates from CLB2-CDC28.

Interacts with HSL7, KCC4 and MET30.

7 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33575, 457 interactors

Database of interacting proteins

More...
DIPi
DIP-2410N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P32944

Protein interaction database and analysis system

More...
IntActi
P32944, 35 interactors

Molecular INTeraction database

More...
MINTi
P32944

STRING: functional protein association networks

More...
STRINGi
4932.YJL187C

<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

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

More...
SMRi
P32944

Database of comparative protein structure models

More...
ModBasei
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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini444 – 794Protein kinasePROSITE-ProRule annotationAdd BLAST351

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 biasi88 – 96Poly-Glu9

<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 protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.PROSITE-ProRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000057137

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P32944

KEGG Orthology (KO)

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KOi
K03114

Identification of Orthologs from Complete Genome Data

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OMAi
DWRIWKI

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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.

P32944-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSLDEDEED FEMLDTENLQ FMGKKMFGKQ AGEDESDDFA IGGSTPTNKL
60 70 80 90 100
KFYPYSNNKL TRSTGTLNLS LSNTALSEAN SKFLGKIEEE EEEEEEGKDE
110 120 130 140 150
ESVDSRIKRW SPFHENESVT TPITKRSAEK TNSPISLKQW NQRWFPKNDA
160 170 180 190 200
RTENTSSSSS YSVAKPNQSA FTSSGLVSKM SMDTSLYPAK LRIPETPVKK
210 220 230 240 250
SPLVEGRDHK HVHLSSSKNA SSSLSVSPLN FVEDNNLQED LLFSDSPSSK
260 270 280 290 300
ALPSIHVPTI DSSPLSEAKY HAHDRHNNQT NILSPTNSLV TNSSPQTLHS
310 320 330 340 350
NKFKKIKRAR NSVILKNREL TNSLQQFKDD LYGTDENFPP PIIISSHHST
360 370 380 390 400
RKNPQPYQFR GRYDNDTDEE ISTPTRRKSI IGATSQTHRE SRPLSLSSAI
410 420 430 440 450
VTNTTSAETH SISSTDSSPL NSKRRLISSN KLSANPDSHL FEKFTNVHSI
460 470 480 490 500
GKGQFSTVYQ VTFAQTNKKY AIKAIKPNKY NSLKRILLEI KILNEVTNQI
510 520 530 540 550
TMDQEGKEYI IDYISSWKFQ NSYYIMTELC ENGNLDGFLQ EQVIAKKKRL
560 570 580 590 600
EDWRIWKIIV ELSLALRFIH DSCHIVHLDL KPANVMITFE GNLKLGDFGM
610 620 630 640 650
ATHLPLEDKS FENEGDREYI APEIISDCTY DYKADIFSLG LMIVEIAANV
660 670 680 690 700
VLPDNGNAWH KLRSGDLSDA GRLSSTDIHS ESLFSDITKV DTNDLFDFER
710 720 730 740 750
DNISGNSNNA GTSTVHNNSN INNPNMNNGN DNNNVNTAAT KNRLILHKSS
760 770 780 790 800
KIPAWVPKFL IDGESLERIV RWMIEPNYER RPTANQILQT EECLYVEMTR
810
NAGAIIQEDD FGPKPKFFI
Length:819
Mass (Da):92,468
Last modified:October 1, 1993 - 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:iF49FE73937958A02
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X73966 Genomic DNA Translation: CAA52150.1
Z49462 Genomic DNA Translation: CAA89482.1
BK006943 Genomic DNA Translation: DAA08619.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S40400

NCBI Reference Sequences

More...
RefSeqi
NP_012348.1, NM_001181620.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJL187C_mRNA; YJL187C; YJL187C

Database of genes from NCBI RefSeq genomes

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GeneIDi
853252

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJL187C

<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
X73966 Genomic DNA Translation: CAA52150.1
Z49462 Genomic DNA Translation: CAA89482.1
BK006943 Genomic DNA Translation: DAA08619.1
PIRiS40400
RefSeqiNP_012348.1, NM_001181620.1

3D structure databases

SMRiP32944
ModBaseiSearch...

Protein-protein interaction databases

BioGridi33575, 457 interactors
DIPiDIP-2410N
ELMiP32944
IntActiP32944, 35 interactors
MINTiP32944
STRINGi4932.YJL187C

PTM databases

iPTMnetiP32944

Proteomic databases

MaxQBiP32944
PaxDbiP32944
PRIDEiP32944

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL187C_mRNA; YJL187C; YJL187C
GeneIDi853252
KEGGisce:YJL187C

Organism-specific databases

EuPathDBiFungiDB:YJL187C
SGDiS000003723 SWE1

Phylogenomic databases

HOGENOMiHOG000057137
InParanoidiP32944
KOiK03114
OMAiDWRIWKI

Enzyme and pathway databases

BioCyciYEAST:G3O-31620-MONOMER
ReactomeiR-SCE-156711 Polo-like kinase mediated events

Miscellaneous databases

Protein Ontology

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PROi
PR:P32944

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiSWE1_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: P32944
Secondary accession number(s): D6VW03
<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: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 18, 2019
This is version 181 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
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