Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P30291 (WEE1_HUMAN)

Entry version 209 (17 Jun 2020)
Sequence version 2 (01 Feb 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Wee1-like protein kinase

Gene

WEE1

Organism
Homo sapiens (Human)
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

Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Synthesis is increased during S and G2 phases, presumably by an increase in transcription; activity is decreased by phosphorylation during m phase. Protein levels fall in M phase as a result of decreased synthesis combined with degradation. Activity seems to be negatively regulated by phosphorylation upon entry into mitosis, although N-terminal phosphorylation might also regulate the protein stability via protection from proteolysis or might regulate the subcellular location.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei328ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei426Proton acceptorPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi431Magnesium; via carbonyl oxygen1 Publication1
Metal bindingi463Magnesium; via carbonyl oxygen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi305 – 313ATPPROSITE-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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Transferase, Tyrosine-protein kinase
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.2 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-156711 Polo-like kinase mediated events
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69478 G2/M DNA replication checkpoint
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-75035 Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P30291

SIGNOR Signaling Network Open Resource

More...SIGNORi		P30291

<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%5Fand%5Ftaxonomy%5Fsection">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:
Wee1-like protein kinase (EC:2.7.10.2)
Short name:
WEE1hu
Alternative name(s):
Wee1A kinase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:WEE1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000166483.10

Human Gene Nomenclature Database

More...HGNCi		HGNC:12761 WEE1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		193525 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P30291

<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 Cytoskeleton Lysosome 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi53S → A: Abolishes phosphorylation by PLK1 and CDK1 and binding of the SCF(BTRC) complex, leading to stabilization of the protein; when associated with A-123. 1 Publication1
Mutagenesisi116 – 117EE → AA: Impairs binding of the SCF(BTRC) complex. 1 Publication2
Mutagenesisi123S → A: Abolishes phosphorylation by PLK1 and CDK1 and binding of the SCF(BTRC) complex, leading to stabilization of the protein; when associated with A-53. 1 Publication1
Mutagenesisi328K → R: Abolishes activity. 1 Publication1
Mutagenesisi642S → A: Abolishes phosphorylation by BRSK1 and BRSK2. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		7465

Open Targets

More...OpenTargetsi		ENSG00000166483

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA366

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P30291 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5491

Drug and drug target database

More...DrugBanki		DB07265 3-(9-HYDROXY-1,3-DIOXO-4-PHENYL-2,3-DIHYDROPYRROLO[3,4-C]CARBAZOL-6(1H)-YL)PROPANOIC ACID
DB07257 4-(2-chlorophenyl)-8-(2-hydroxyethyl)-6-methylpyrrolo[3,4-e]indole-1,3(2H,6H)-dione
DB08365 8-bromo-4-(2-chlorophenyl)-N-(2-hydroxyethyl)-6-methyl-1,3-dioxo-1,2,3,6-tetrahydropyrrolo[3,4-e]indole-7-carboxamide
DB04608 9-HYDROXY-4-PHENYL-6H-PYRROLO[3,4-C]CARBAZOLE-1,3-DIONE
DB07006 9-HYDROXY-6-(3-HYDROXYPROPYL)-4-(2-METHOXYPHENYL)PYRROLO[3,4-C]CARBAZOLE-1,3(2H,6H)-DIONE
DB12010 Fostamatinib
DB11740 MK-1775
DB07226 N-[4-(2-CHLOROPHENYL)-1,3-DIOXO-1,2,3,6-TETRAHYDROPYRROLO[3,4-C]CARBAZOL-9-YL]FORMAMIDE

DrugCentral

More...DrugCentrali		P30291

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2278

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		WEE1

Domain mapping of disease mutations (DMDM)

More...DMDMi		1351419

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000868101 – 646Wee1-like protein kinaseAdd BLAST646

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 residuei53Phosphoserine; by PLK11 Publication1
Modified residuei78PhosphoserineBy similarity1
Modified residuei85PhosphoserineCombined sources1
Modified residuei123Phosphoserine; by CDK11 Publication1
Modified residuei127PhosphoserineCombined sources1
Modified residuei137PhosphoserineCombined sources1
Modified residuei139PhosphoserineCombined sources1
Modified residuei150PhosphoserineCombined sources1
Modified residuei165PhosphoserineBy similarity1
Modified residuei187PhosphothreonineCombined sources1
Modified residuei190PhosphothreonineCombined sources1
Modified residuei239Phosphothreonine1 Publication1
Modified residuei270PhosphoserineCombined sources1
Modified residuei307PhosphoserineCombined sources1
Modified residuei312PhosphoserineCombined sources1
Modified residuei642Phosphoserine; by BRSK1 and BRSK22 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 during M and G1 phases. Also autophosphorylated. Phosphorylation at Ser-642 by BRSK1 and BRSK2 in post-mitotic neurons, leads to down-regulate WEE1 activity in polarized neurons. Phosphorylated at Ser-53 and Ser-123 by PLK1 and CDK1, respectively, generating an signal for degradation that can be recognized by the SCF(BTRC) complex, leading to its ubiquitination and degradation at the onset of G2/M phase.4 Publications
Dephosphorylated at Thr-239 by CTDP1.
Ubiquitinated and degraded at the onset of G2/M phase.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P30291

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P30291

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P30291

MaxQB - The MaxQuant DataBase

More...MaxQBi		P30291

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

More...PaxDbi		P30291

PeptideAtlas

More...PeptideAtlasi		P30291

PRoteomics IDEntifications database

More...PRIDEi		P30291

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		3755
54650 [P30291-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P30291

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P30291

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000166483 Expressed in female gonad and 202 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P30291 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P30291 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000166483 Low tissue specificity

<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%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		113303, 82 interactors

Database of interacting proteins

More...DIPi		DIP-37969N

Protein interaction database and analysis system

More...IntActi		P30291, 25 interactors

Molecular INTeraction database

More...MINTi		P30291

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000402084

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P30291

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P30291 protein

<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

1646
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

More...SMRi		P30291

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P30291

<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%5Fand%5Fdomains%5Fsection">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>Domaini299 – 569Protein kinasePROSITE-ProRule annotationAdd BLAST271

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 biasi9 – 12Poly-Pro4
Compositional biasi34 – 43Poly-Glu10

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0601 Eukaryota
ENOG410XS1M LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157939

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_25_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P30291

KEGG Orthology (KO)

More...KOi		K06632

Identification of Orthologs from Complete Genome Data

More...OMAi		RAHWNDS

Database for complete collections of gene phylogenies

More...PhylomeDBi		P30291

TreeFam database of animal gene trees

More...TreeFami		TF101088

Family and domain databases

Database of protein disorder

More...DisProti		DP00611

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
IPR017164 Wee1-like_protein_kinase

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF037281 Wee1-like_protein_kinase, 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

More...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%5Flength">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>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P30291-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSFLSRQQPP PPRRAGAACT LRQKLIFSPC SDCEEEEEEE EEEGSGHSTG 
        60         70         80         90        100
EDSAFQEPDS PLPPARSPTE PGPERRRSPG PAPGSPGELE EDLLLPGACP 
       110        120        130        140        150
GADEAGGGAE GDSWEEEGFG SSSPVKSPAA PYFLGSSFSP VRCGGPGDAS 
       160        170        180        190        200
PRGCGARRAG EGRRSPRPDH PGTPPHKTFR KLRLFDTPHT PKSLLSKARG 
       210        220        230        240        250
IDSSSVKLRG SSLFMDTEKS GKREFDVRQT PQVNINPFTP DSLLLHSSGQ 
       260        270        280        290        300
CRRRKRTYWN DSCGEDMEAS DYELEDETRP AKRITITESN MKSRYTTEFH 
       310        320        330        340        350
ELEKIGSGEF GSVFKCVKRL DGCIYAIKRS KKPLAGSVDE QNALREVYAH 
       360        370        380        390        400
AVLGQHSHVV RYFSAWAEDD HMLIQNEYCN GGSLADAISE NYRIMSYFKE 
       410        420        430        440        450
AELKDLLLQV GRGLRYIHSM SLVHMDIKPS NIFISRTSIP NAASEEGDED 
       460        470        480        490        500
DWASNKVMFK IGDLGHVTRI SSPQVEEGDS RFLANEVLQE NYTHLPKADI 
       510        520        530        540        550
FALALTVVCA AGAEPLPRNG DQWHEIRQGR LPRIPQVLSQ EFTELLKVMI 
       560        570        580        590        600
HPDPERRPSA MALVKHSVLL SASRKSAEQL RIELNAEKFK NSLLQKELKK 
       610        620        630        640 
AQMAKAAAEE RALFTDRMAT RSTTQSNRTS RLIGKKMNRS VSLTIY
Length:646
Mass (Da):71,597
Last modified:February 1, 1996 - 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:iDB00623D304562A0
GO
Isoform 2 (identifier: P30291-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-214: Missing.

Show »
Length:432
Mass (Da):49,072
Checksum:i48F8E9EC16E4184A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PRI3E9PRI3_HUMAN
Wee1-like protein kinase
WEE1
99Annotation score:

Annotation score:1 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>
E9PRU3E9PRU3_HUMAN
Wee1-like protein kinase
WEE1
214Annotation score:

Annotation score:1 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>
E9PQ51E9PQ51_HUMAN
Wee1-like protein kinase
WEE1
162Annotation score:

Annotation score:1 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>
H0YEJ2H0YEJ2_HUMAN
Wee1-like protein kinase
WEE1
145Annotation score:

Annotation score:1 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 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 conflicti65A → E in CAA43979 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_041302210G → C1 PublicationCorresponds to variant dbSNP:rs34412975Ensembl.1
Natural variantiVAR_041303472S → I1 PublicationCorresponds to variant dbSNP:rs56411856Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0449591 – 214Missing in isoform 2. 1 PublicationAdd BLAST214

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U10564 mRNA Translation: AAB60401.1
AJ277546 Genomic DNA Translation: CAC14173.1
AK122837 mRNA Translation: BAG53753.1
AC011979 Genomic DNA No translation available.
AC122179 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW68586.1
CH471064 Genomic DNA Translation: EAW68587.1
CH471064 Genomic DNA Translation: EAW68588.1
X62048 mRNA Translation: CAA43979.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS44536.1 [P30291-2]
CCDS7800.1 [P30291-1]

Protein sequence database of the Protein Information Resource

More...PIRi		S55048

NCBI Reference Sequences

More...RefSeqi		NP_001137448.1, NM_001143976.1 [P30291-2]
NP_003381.1, NM_003390.3 [P30291-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000299613; ENSP00000299613; ENSG00000166483 [P30291-2]
ENST00000450114; ENSP00000402084; ENSG00000166483 [P30291-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7465

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7465

UCSC genome browser

More...UCSCi		uc001mhs.4 human [P30291-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
U10564 mRNA Translation: AAB60401.1
AJ277546 Genomic DNA Translation: CAC14173.1
AK122837 mRNA Translation: BAG53753.1
AC011979 Genomic DNA No translation available.
AC122179 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW68586.1
CH471064 Genomic DNA Translation: EAW68587.1
CH471064 Genomic DNA Translation: EAW68588.1
X62048 mRNA Translation: CAA43979.1
CCDSiCCDS44536.1 [P30291-2]
CCDS7800.1 [P30291-1]
PIRiS55048
RefSeqiNP_001137448.1, NM_001143976.1 [P30291-2]
NP_003381.1, NM_003390.3 [P30291-1]

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
1X8BX-ray1.81A291-575[»]
2IN6X-ray1.90A291-575[»]
2IO6X-ray2.20A291-575[»]
2Z2WX-ray2.22A291-575[»]
3BI6X-ray2.20A291-575[»]
3BIZX-ray2.20A291-575[»]
3CQEX-ray2.50A291-575[»]
3CR0X-ray2.30A291-575[»]
5V5YX-ray1.90A291-575[»]
5VC3X-ray1.97A291-575[»]
5VC4X-ray2.10A291-575[»]
5VC5X-ray1.93A291-575[»]
5VC6X-ray2.00A291-575[»]
5VD2X-ray2.05A291-575[»]
5VD4X-ray2.02A291-575[»]
5VD5X-ray2.05A291-575[»]
5VD7X-ray2.08A291-575[»]
5VD8X-ray1.85A291-575[»]
5VD9X-ray1.87A291-575[»]
5VDAX-ray2.10A291-575[»]
SMRiP30291
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi113303, 82 interactors
DIPiDIP-37969N
IntActiP30291, 25 interactors
MINTiP30291
STRINGi9606.ENSP00000402084

Chemistry databases

BindingDBiP30291
ChEMBLiCHEMBL5491
DrugBankiDB07265 3-(9-HYDROXY-1,3-DIOXO-4-PHENYL-2,3-DIHYDROPYRROLO[3,4-C]CARBAZOL-6(1H)-YL)PROPANOIC ACID
DB07257 4-(2-chlorophenyl)-8-(2-hydroxyethyl)-6-methylpyrrolo[3,4-e]indole-1,3(2H,6H)-dione
DB08365 8-bromo-4-(2-chlorophenyl)-N-(2-hydroxyethyl)-6-methyl-1,3-dioxo-1,2,3,6-tetrahydropyrrolo[3,4-e]indole-7-carboxamide
DB04608 9-HYDROXY-4-PHENYL-6H-PYRROLO[3,4-C]CARBAZOLE-1,3-DIONE
DB07006 9-HYDROXY-6-(3-HYDROXYPROPYL)-4-(2-METHOXYPHENYL)PYRROLO[3,4-C]CARBAZOLE-1,3(2H,6H)-DIONE
DB12010 Fostamatinib
DB11740 MK-1775
DB07226 N-[4-(2-CHLOROPHENYL)-1,3-DIOXO-1,2,3,6-TETRAHYDROPYRROLO[3,4-C]CARBAZOL-9-YL]FORMAMIDE
DrugCentraliP30291
GuidetoPHARMACOLOGYi2278

PTM databases

iPTMnetiP30291
PhosphoSitePlusiP30291

Polymorphism and mutation databases

BioMutaiWEE1
DMDMi1351419

Proteomic databases

EPDiP30291
jPOSTiP30291
MassIVEiP30291
MaxQBiP30291
PaxDbiP30291
PeptideAtlasiP30291
PRIDEiP30291
ProteomicsDBi3755
54650 [P30291-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3903 628 antibodies

The DNASU plasmid repository

More...DNASUi		7465

Genome annotation databases

EnsembliENST00000299613; ENSP00000299613; ENSG00000166483 [P30291-2]
ENST00000450114; ENSP00000402084; ENSG00000166483 [P30291-1]
GeneIDi7465
KEGGihsa:7465
UCSCiuc001mhs.4 human [P30291-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7465
DisGeNETi7465
EuPathDBiHostDB:ENSG00000166483.10

GeneCards: human genes, protein and diseases

More...GeneCardsi		WEE1
HGNCiHGNC:12761 WEE1
HPAiENSG00000166483 Low tissue specificity
MIMi193525 gene
neXtProtiNX_P30291
OpenTargetsiENSG00000166483
PharmGKBiPA366

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0601 Eukaryota
ENOG410XS1M LUCA
GeneTreeiENSGT00940000157939
HOGENOMiCLU_000288_25_1_1
InParanoidiP30291
KOiK06632
OMAiRAHWNDS
PhylomeDBiP30291
TreeFamiTF101088

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-156711 Polo-like kinase mediated events
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69478 G2/M DNA replication checkpoint
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-75035 Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SignaLinkiP30291
SIGNORiP30291

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		7465 754 hits in 819 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		WEE1 human
EvolutionaryTraceiP30291

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Wee1-like_protein_kinase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		7465
PharosiP30291 Tchem

Protein Ontology

More...PROi		PR:P30291
RNActiP30291 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000166483 Expressed in female gonad and 202 other tissues
ExpressionAtlasiP30291 baseline and differential
GenevisibleiP30291 HS

Family and domain databases

DisProtiDP00611
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR017164 Wee1-like_protein_kinase
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PIRSFiPIRSF037281 Wee1-like_protein_kinase, 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

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiWEE1_HUMAN
<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: P30291
Secondary accession number(s): B3KVE1, D3DQV0
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: June 17, 2020
This is version 209 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 programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, 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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again