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Protein Page:
Wee1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Wee1 a protein kinase of the WEE family. A nuclear protein which catalyzes the inhibitory tyrosine phosphorylation of CDC2/cyclin B kinase, and appears to coordinate the transition between DNA replication and mitosis by protecting the nucleus from cytoplasmically activated CDC2 kinase. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Protein kinase, Other; Protein kinase, Ser/Thr (non-receptor); EC 2.7.10.2; Other group; WEE family
Cellular Component: nucleoplasm; cytoplasm; nucleus
Molecular Function: protein serine/threonine kinase activity; protein binding; protein-tyrosine kinase activity; magnesium ion binding; non-membrane spanning protein tyrosine kinase activity; ATP binding
Biological Process: mitosis; peptidyl-tyrosine phosphorylation; regulation of cell cycle; microtubule cytoskeleton organization and biogenesis; establishment of cell polarity; cell division; mitotic cell cycle; blood coagulation; S phase of mitotic cell cycle; G2/M transition of mitotic cell cycle; cell cycle checkpoint; neurite morphogenesis; G1/S transition of mitotic cell cycle
Reference #:  P30291 (UniProtKB)
Alt. Names/Synonyms: DKFZp686I18166; FLJ16446; WEE1; WEE1 homolog (S. pombe); WEE1+ homolog; Wee1-like protein kinase; WEE1A; Wee1A kinase; WEE1hu
Gene Symbols: WEE1
Molecular weight: 71,597 Da
Basal Isoelectric point: 6.33  Predict pI for various phosphorylation states
CST Pathways:  Cell Cycle: G2/M DNA Damage Checkpoint  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Wee1
Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S53‑p, T239‑p
enzymatic activity, inhibited: S642‑p
intracellular localization: S642‑p
molecular association, regulation: S53‑p, S121‑p, S123‑p
phosphorylation: S123‑p
protein degradation: S53‑p, S121‑p, S123‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 7 C19 PRRAGAACTLRQKLI
0 1 S48-p EEEGSGHstGEDsAF
0 1 T49-p EEGSGHstGEDsAFQ
4 1 S53-p GHstGEDsAFQEPDS
0 2 S67-p SPLPPARsPtEPGPE
0 2 T69-p LPPARsPtEPGPERR
0 1 S85-p SPGPAPGsPGELEED
2 0 S121-p WEEEGFGsSsPVKsP
3 0 S123-p EEGFGsSsPVKsPAA
0 5 S127-p GsSsPVKsPAAPyFL
0 12 Y132-p VKsPAAPyFLGSSFs
1 15 S139-p yFLGSSFsPVRCGGP
0 4 S150-p CGGPGDAsPRGCGAR
0 12 S165-p RAGEGRRsPRPDHPG
0 9 H170 RRsPRPDHPGtPPHK
0 2 G172 sPRPDHPGtPPHKTF
0 11 T173-p PRPDHPGtPPHKTFR
0 4 T187-p RKLRLFDtPHtPKsL
0 8 T190-p RLFDtPHtPKsLLSK
0 1 S193-p DtPHtPKsLLSKARG
0 1 S211-p SSVKLRGssLFMDtE
0 1 S212-p SVKLRGssLFMDtEK
0 1 T217-p GssLFMDtEKSGKRE
1 0 T239-p QVNINPFtPDSLLLH
0 1 Y258-p CRRRKRTyWNDSCGE
0 1 S270-p CGEDMEAsDyELEDE
0 2 Y272-p EDMEAsDyELEDETR
0 1 S293-p ITESNMKsRYTTEFH
0 1 S307-p HELEKIGsGEFGsVF
0 1 S312-p IGsGEFGsVFKCVKR
0 1 K600 LLQKELKKAQMAKAA
0 1 K605 LKKAQMAKAAAEERA
4 2 S642-p KKMNRSVsLTIy___
0 1 Y646-p RSVsLTIy_______
4910 : Phospho-Wee1 (Ser642) (D47G5) Rabbit mAb
  mouse

 
Y19-p TRRVGAAySLRQKLI
S47 EEEGSGHSTGEDSAF
T48 EEGSGHSTGEDSAFQ
S52 GHSTGEDSAFQEPDS
S66 SPLPSARSPAEAEAE
A68 LPSARSPAEAEAERR
S85 SPGAEPSSPGELEDD
S121 WEEEGFGSSSPVKSP
S123 EEGFGSSSPVKSPST
S127 GSSSPVKSPSTAYFL
Y132 VKSPSTAYFLSSPFs
S139-p YFLSSPFsPVRCGGP
S150 CGGPGDASPQGCGAP
S165-p RAMDDPCsPQPDyPs
Y170-p PCsPQPDyPstPPHK
S172-p sPQPDyPstPPHKTF
T173-p PQPDyPstPPHKTFR
T187-p RKLRLFDtPHtPKSL
T190-p RLFDtPHtPKSLLSK
S193 DtPHtPKSLLSKARV
S211 GSVKLRGSSLFMDTE
S212 SVKLRGSSLFMDTEK
T217 GSSLFMDTEKSGKRE
T239 QVNINPFTPDPVLLH
Y258 CRGRKRAYFNDSSED
S269 SSEDMEASDYEFEDE
Y271 EDMEASDYEFEDETR
S292 ITESNMKSRYTTEFH
S306 HELEKIGSGEFGSVF
S311 IGSGEFGSVFKCVKR
K599 LLQKELKKAQMAAKV
K605 KKAQMAAKVAAEERA
S642-p KKMNRSVsLTIY___
Y646 RSVsLTIY_______
4910 : Phospho-Wee1 (Ser642) (D47G5) Rabbit mAb
  rat

 
C19 TRRAAAACSLRQKLI
S47 EEEGSGHSTGEDSAF
T48 EEGSGHSTGEDSAFQ
S52 GHSTGEDSAFQEPDS
S66 SPLPSARSPAEAEAE
A68 LPSARSPAEAEAERR
S85 SPGAEPSSPGELEED
S121 WEEEGFGSSSPVKSP
S123 EEGFGSSSPVKSPTT
S127 GSSSPVKSPTTAYFL
Y132 VKSPTTAYFLGSSFS
S139 YFLGSSFSPVRCGGP
S150 CGGPGDASPRGCGVP
S165 RAMDDPCSPQPDYPS
Y170 PCSPQPDYPSTPPHK
S172 SPQPDYPSTPPHKTF
T173 PQPDYPSTPPHKTFR
T187 RKLRLFDTPHTPKSL
T190 RLFDTPHTPKSLLSK
S193 DTPHTPKSLLSKARV
S211 SSVKLRGSSLFMDTE
S212 SVKLRGSSLFMDTEK
T217 GSSLFMDTEKSGKRE
T239 QVNINPFTPDPVMLH
Y258 CRGRKRAYFNDSSED
S269 SSEDMEASDYEFEDE
Y271 EDMEASDYEFEDETR
S292 ITESNMKSRYTTEFH
S306 HELEKIGSGEFGSVF
S311 IGSGEFGSVFKCVKR
K599-u LLQKELKkAQMAAkV
K605-u KkAQMAAkVAAEERA
S642 KKMNRSVSLTIY___
Y646 RSVSLTIY_______
4910 : Phospho-Wee1 (Ser642) (D47G5) Rabbit mAb
  frog

 
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
G85 SVGAECPGTPLHYST
T86 VGAECPGTPLHYSTW
T101 KKLKLCDTPYTPKSL
T104 KLCDTPYTPKSLLYK
S107 DTPYTPKSLLYKTLP
Q125 SRVHCRGQRLLRFVA
R126 RVHCRGQRLLRFVAG
V131 GQRLLRFVAGTGAEL
T150 LVNINPFTPESYRQT
P169 NGKRKERPEDDCRTD
Y181 RTDRQMKYAEKEHPA
E183 DRQMKYAEKEHPAVF
S204 LRETNMGSRYKTEFL
A218 LEIEKIGAGEFGSVF
S223 IGAGEFGSVFKCIKR
A510 MLERELKAAKLAQTS
T516 KAAKLAQTSGKDECS
S549-p AKNTRSLsFTCGGY_
Y555 LsFTCGGY_______
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