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P30291 (WEE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Wee1-like protein kinase

Short name=WEE1hu
EC=2.7.10.2
Alternative name(s):
Wee1A kinase
Gene names
Name:WEE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length646 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactor

Binds 2 magnesium ions per subunit.

Enzyme regulation

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.

Subcellular location

Nucleus.

Post-translational modification

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. Ref.9 Ref.10 Ref.14 Ref.16

Dephosphorylated at Thr-239 by CTDP1. Ref.9 Ref.10 Ref.14 Ref.16

Ubiquitinated and degraded at the onset of G2/M phase. Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

establishment of cell polarity

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement PubMed 8348613. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.10PubMed 15161933. Source: IntAct

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

protein tyrosine kinase activity

Traceable author statement PubMed 7774574. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30291-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P30291-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-214: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 646646Wee1-like protein kinase
PRO_0000086810

Regions

Domain299 – 569271Protein kinase
Nucleotide binding305 – 3139ATP By similarity
Compositional bias9 – 124Poly-Pro
Compositional bias34 – 4310Poly-Glu

Sites

Active site4261Proton acceptor By similarity
Metal binding4311Magnesium; via carbonyl oxygen
Metal binding4631Magnesium; via carbonyl oxygen
Binding site3281ATP By similarity

Amino acid modifications

Modified residue531Phosphoserine; by PLK1 Ref.10
Modified residue1231Phosphoserine; by CDK1 Ref.10
Modified residue1271Phosphoserine Ref.15
Modified residue1391Phosphoserine Ref.13 Ref.15
Modified residue1501Phosphoserine Ref.12
Modified residue1901Phosphothreonine Ref.12
Modified residue2391Phosphothreonine Ref.16
Modified residue3121Phosphoserine Ref.12
Modified residue6421Phosphoserine; by BRSK1 and BRSK2 Ref.9 Ref.14

Natural variations

Alternative sequence1 – 214214Missing in isoform 2.
VSP_044959
Natural variant2101G → C. Ref.18
Corresponds to variant rs34412975 [ dbSNP | Ensembl ].
VAR_041302
Natural variant4721S → I. Ref.18
Corresponds to variant rs56411856 [ dbSNP | Ensembl ].
VAR_041303

Experimental info

Mutagenesis531S → 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. Ref.10
Mutagenesis116 – 1172EE → AA: Impairs binding of the SCF(BTRC) complex.
Mutagenesis1231S → 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. Ref.10
Mutagenesis3281K → R: Abolishes activity. Ref.8
Mutagenesis6421S → A: Abolishes phosphorylation by BRSK1 and BRSK2. Ref.14
Sequence conflict651A → E in CAA43979. Ref.6

Secondary structure

............................................ 646
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: DB00623D304562A0

FASTA64671,597
        10         20         30         40         50         60 
MSFLSRQQPP PPRRAGAACT LRQKLIFSPC SDCEEEEEEE EEEGSGHSTG EDSAFQEPDS 

        70         80         90        100        110        120 
PLPPARSPTE PGPERRRSPG PAPGSPGELE EDLLLPGACP GADEAGGGAE GDSWEEEGFG 

       130        140        150        160        170        180 
SSSPVKSPAA PYFLGSSFSP VRCGGPGDAS PRGCGARRAG EGRRSPRPDH PGTPPHKTFR 

       190        200        210        220        230        240 
KLRLFDTPHT PKSLLSKARG IDSSSVKLRG SSLFMDTEKS GKREFDVRQT PQVNINPFTP 

       250        260        270        280        290        300 
DSLLLHSSGQ CRRRKRTYWN DSCGEDMEAS DYELEDETRP AKRITITESN MKSRYTTEFH 

       310        320        330        340        350        360 
ELEKIGSGEF GSVFKCVKRL DGCIYAIKRS KKPLAGSVDE QNALREVYAH AVLGQHSHVV 

       370        380        390        400        410        420 
RYFSAWAEDD HMLIQNEYCN GGSLADAISE NYRIMSYFKE AELKDLLLQV GRGLRYIHSM 

       430        440        450        460        470        480 
SLVHMDIKPS NIFISRTSIP NAASEEGDED DWASNKVMFK IGDLGHVTRI SSPQVEEGDS 

       490        500        510        520        530        540 
RFLANEVLQE NYTHLPKADI FALALTVVCA AGAEPLPRNG DQWHEIRQGR LPRIPQVLSQ 

       550        560        570        580        590        600 
EFTELLKVMI HPDPERRPSA MALVKHSVLL SASRKSAEQL RIELNAEKFK NSLLQKELKK 

       610        620        630        640 
AQMAKAAAEE RALFTDRMAT RSTTQSNRTS RLIGKKMNRS VSLTIY 

« Hide

Isoform 2 [UniParc].

Checksum: 48F8E9EC16E4184A
Show »

FASTA43249,072

References

« Hide 'large scale' references
[1]"Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle."
Watanabe N., Broome M., Hunter T.
EMBO J. 14:1878-1891(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
[2]"Comparative architectural aspects of regions of conserved synteny on human chromosome 11p15.3 and mouse chromosome 7 (including genes WEE1 and LMO1)."
Cichutek A., Brueckmann T., Seipel B., Hauser H., Schlaubitz S., Prawitt D., Hankeln T., Schmidt E.R., Winterpacht A., Zabel B.U.
Cytogenet. Cell Genet. 93:277-283(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Amygdala.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Igarashi M.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-214 (ISOFORM 1).
[7]"Wee1(+)-like gene in human cells."
Igarashi M., Nagata A., Jinno S., Suto K., Okayama H.
Nature 353:80-83(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 215-646 (ISOFORM 1).
[8]"Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15."
McGowan C.H., Russell P.
EMBO J. 12:75-85(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-328.
[9]"Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function."
Lu R., Niida H., Nakanishi M.
J. Biol. Chem. 279:31164-31170(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-642.
Tissue: Testis.
[10]"M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP."
Watanabe N., Arai H., Nishihara Y., Taniguchi M., Watanabe N., Hunter T., Osada H.
Proc. Natl. Acad. Sci. U.S.A. 101:4419-4424(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-53 AND SER-123, UBIQUITINATION, MUTAGENESIS OF SER-53; 116-GLU-GLU-117 AND SER-123.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; THR-190 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and SadB-deficient neurons disrupts neuronal polarity."
Muller M., Lutter D., Puschel A.W.
J. Cell Sci. 123:286-294(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-642, MUTAGENESIS OF SER-642.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit."
Visconti R., Palazzo L., Della Monica R., Grieco D.
Nat. Commun. 3:894-894(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-239, DEPHOSPHORYLATION.
[17]"Structure and inhibition of the human cell cycle checkpoint kinase, Wee1A kinase: an atypical tyrosine kinase with a key role in CDK1 regulation."
Squire C.J., Dickson J.M., Ivanovic I., Baker E.N.
Structure 13:541-550(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 291-575 IN COMPLEX WITH MAGNESIUM AND AN INHIBITOR.
[18]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-210 AND ILE-472.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44536.1. [P30291-2]
CCDS7800.1. [P30291-1]
PIRS55048.
RefSeqNP_001137448.1. NM_001143976.1. [P30291-2]
NP_003381.1. NM_003390.3. [P30291-1]
UniGeneHs.249441.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00611.
ProteinModelPortalP30291.
SMRP30291. Positions 253-640.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113303. 21 interactions.
DIPDIP-37969N.
IntActP30291. 8 interactions.
MINTMINT-129561.
STRING9606.ENSP00000402084.

Chemistry

BindingDBP30291.
ChEMBLCHEMBL5491.
GuidetoPHARMACOLOGY2278.

PTM databases

PhosphoSiteP30291.

Polymorphism databases

DMDM1351419.

Proteomic databases

MaxQBP30291.
PaxDbP30291.
PRIDEP30291.

Protocols and materials databases

DNASU7465.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299613; ENSP00000299613; ENSG00000166483. [P30291-2]
ENST00000450114; ENSP00000402084; ENSG00000166483. [P30291-1]
GeneID7465.
KEGGhsa:7465.
UCSCuc001mhs.3. human. [P30291-1]

Organism-specific databases

CTD7465.
GeneCardsGC11P009595.
HGNCHGNC:12761. WEE1.
HPACAB004619.
MIM193525. gene.
neXtProtNX_P30291.
PharmGKBPA366.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000004824.
HOVERGENHBG005050.
InParanoidP30291.
KOK06632.
OMARTYWNDS.
OrthoDBEOG7N63M9.
PhylomeDBP30291.
TreeFamTF101088.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_115566. Cell Cycle.
REACT_604. Hemostasis.
SignaLinkP30291.

Gene expression databases

ArrayExpressP30291.
BgeeP30291.
CleanExHS_WEE1.
GenevestigatorP30291.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR017164. Wee1-like_protein_kinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037281. Wee1-like_protein_kinase. 1 hit.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30291.
GeneWikiWee1-like_protein_kinase.
GenomeRNAi7465.
NextBio29236.
PMAP-CutDBP30291.
PROP30291.
SOURCESearch...

Entry information

Entry nameWEE1_HUMAN
AccessionPrimary (citable) accession number: P30291
Secondary accession number(s): B3KVE1, D3DQV0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM