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Protein

Wee1-like protein kinase

Gene

WEE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei328 – 3281ATPPROSITE-ProRule annotation
Active sitei426 – 4261Proton acceptorPROSITE-ProRule annotation
Metal bindingi431 – 4311Magnesium; via carbonyl oxygen1 Publication
Metal bindingi463 – 4631Magnesium; via carbonyl oxygen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi305 – 3139ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_1574. Cyclin E associated events during G1/S transition.
REACT_1846. G2/M DNA replication checkpoint.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP30291.

Names & Taxonomyi

Protein namesi
Recommended name:
Wee1-like protein kinase (EC:2.7.10.2)
Short name:
WEE1hu
Alternative name(s):
Wee1A kinase
Gene namesi
Name:WEE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:12761. WEE1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531S → 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 Publication
Mutagenesisi116 – 1172EE → AA: Impairs binding of the SCF(BTRC) complex. 1 Publication
Mutagenesisi123 – 1231S → 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 Publication
Mutagenesisi328 – 3281K → R: Abolishes activity. 1 Publication
Mutagenesisi642 – 6421S → A: Abolishes phosphorylation by BRSK1 and BRSK2. 1 Publication

Organism-specific databases

PharmGKBiPA366.

Polymorphism and mutation databases

BioMutaiWEE1.
DMDMi1351419.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 646646Wee1-like protein kinasePRO_0000086810Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531Phosphoserine; by PLK11 Publication
Modified residuei85 – 851Phosphoserine1 Publication
Modified residuei123 – 1231Phosphoserine; by CDK11 Publication
Modified residuei127 – 1271Phosphoserine1 Publication
Modified residuei139 – 1391Phosphoserine2 Publications
Modified residuei150 – 1501Phosphoserine1 Publication
Modified residuei190 – 1901Phosphothreonine1 Publication
Modified residuei239 – 2391Phosphothreonine1 Publication
Modified residuei312 – 3121Phosphoserine1 Publication
Modified residuei642 – 6421Phosphoserine; by BRSK1 and BRSK22 Publications

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

MaxQBiP30291.
PaxDbiP30291.
PRIDEiP30291.

PTM databases

PhosphoSiteiP30291.

Miscellaneous databases

PMAP-CutDBP30291.

Expressioni

Gene expression databases

BgeeiP30291.
CleanExiHS_WEE1.
ExpressionAtlasiP30291. baseline and differential.
GenevisibleiP30291. HS.

Organism-specific databases

HPAiCAB004619.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
BTRCQ9Y2972EBI-914695,EBI-307461
FBXW11Q9UKB13EBI-914695,EBI-355189
YWHAZP631043EBI-914695,EBI-347088

Protein-protein interaction databases

BioGridi113303. 25 interactions.
DIPiDIP-37969N.
IntActiP30291. 12 interactions.
MINTiMINT-129561.
STRINGi9606.ENSP00000402084.

Structurei

Secondary structure

1
646
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi294 – 2985Combined sources
Beta strandi299 – 30810Combined sources
Beta strandi311 – 3188Combined sources
Turni319 – 3213Combined sources
Beta strandi324 – 3318Combined sources
Beta strandi335 – 3373Combined sources
Helixi338 – 35215Combined sources
Beta strandi362 – 3687Combined sources
Beta strandi371 – 3777Combined sources
Helixi384 – 39411Combined sources
Helixi400 – 41920Combined sources
Helixi429 – 4313Combined sources
Beta strandi432 – 4354Combined sources
Beta strandi458 – 4614Combined sources
Helixi464 – 4663Combined sources
Helixi480 – 4823Combined sources
Helixi485 – 4884Combined sources
Helixi495 – 51016Combined sources
Beta strandi518 – 5203Combined sources
Helixi521 – 5277Combined sources
Helixi540 – 54910Combined sources
Helixi554 – 5563Combined sources
Helixi560 – 5645Combined sources
Helixi567 – 5693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00611.
ProteinModelPortaliP30291.
SMRiP30291. Positions 253-640.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30291.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini299 – 569271Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 124Poly-Pro
Compositional biasi34 – 4310Poly-Glu

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063230.
HOGENOMiHOG000004824.
HOVERGENiHBG005050.
InParanoidiP30291.
KOiK06632.
OMAiWNDSCGE.
OrthoDBiEOG7N63M9.
PhylomeDBiP30291.
TreeFamiTF101088.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR017164. Wee1-like_protein_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037281. Wee1-like_protein_kinase. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

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.

« 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
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.

Note: No experimental confirmation available.
Show »
Length:432
Mass (Da):49,072
Checksum:i48F8E9EC16E4184A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651A → E in CAA43979 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti210 – 2101G → C.1 Publication
Corresponds to variant rs34412975 [ dbSNP | Ensembl ].
VAR_041302
Natural varianti472 – 4721S → I.1 Publication
Corresponds to variant rs56411856 [ dbSNP | Ensembl ].
VAR_041303

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 214214Missing in isoform 2. 1 PublicationVSP_044959Add
BLAST

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]
UniGeneiHs.249441.

Genome annotation databases

EnsembliENST00000299613; ENSP00000299613; ENSG00000166483. [P30291-2]
ENST00000450114; ENSP00000402084; ENSG00000166483.
GeneIDi7465.
KEGGihsa:7465.
UCSCiuc001mhs.3. human. [P30291-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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]
UniGeneiHs.249441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00611.
ProteinModelPortaliP30291.
SMRiP30291. Positions 253-640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113303. 25 interactions.
DIPiDIP-37969N.
IntActiP30291. 12 interactions.
MINTiMINT-129561.
STRINGi9606.ENSP00000402084.

Chemistry

BindingDBiP30291.
ChEMBLiCHEMBL5491.
GuidetoPHARMACOLOGYi2278.

PTM databases

PhosphoSiteiP30291.

Polymorphism and mutation databases

BioMutaiWEE1.
DMDMi1351419.

Proteomic databases

MaxQBiP30291.
PaxDbiP30291.
PRIDEiP30291.

Protocols and materials databases

DNASUi7465.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299613; ENSP00000299613; ENSG00000166483. [P30291-2]
ENST00000450114; ENSP00000402084; ENSG00000166483.
GeneIDi7465.
KEGGihsa:7465.
UCSCiuc001mhs.3. human. [P30291-1]

Organism-specific databases

CTDi7465.
GeneCardsiGC11P009595.
HGNCiHGNC:12761. WEE1.
HPAiCAB004619.
MIMi193525. gene.
neXtProtiNX_P30291.
PharmGKBiPA366.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063230.
HOGENOMiHOG000004824.
HOVERGENiHBG005050.
InParanoidiP30291.
KOiK06632.
OMAiWNDSCGE.
OrthoDBiEOG7N63M9.
PhylomeDBiP30291.
TreeFamiTF101088.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_1574. Cyclin E associated events during G1/S transition.
REACT_1846. G2/M DNA replication checkpoint.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP30291.

Miscellaneous databases

ChiTaRSiWEE1. human.
EvolutionaryTraceiP30291.
GeneWikiiWee1-like_protein_kinase.
GenomeRNAii7465.
NextBioi29236.
PMAP-CutDBP30291.
PROiP30291.
SOURCEiSearch...

Gene expression databases

BgeeiP30291.
CleanExiHS_WEE1.
ExpressionAtlasiP30291. baseline and differential.
GenevisibleiP30291. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR017164. Wee1-like_protein_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037281. Wee1-like_protein_kinase. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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. 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-85; 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.
    , 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.

Entry informationi

Entry nameiWEE1_HUMAN
AccessioniPrimary (citable) accession number: P30291
Secondary accession number(s): B3KVE1, D3DQV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: July 22, 2015
This is version 169 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.