WEE1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: WEE1_MOUSE
• UniProt AC: P47810
• Protein Name: Wee1-like protein kinase
• Gene Name: Wee1
• Organism: Mus musculus (Mouse).
• Sequence Length: 646
• Subcellular Localization: Nucleus.
• Protein Description: 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 (By similarity)..
• Protein Sequence: MSFLSRQQPPPTRRVGAAYSLRQKLIFSPGSDCEEEEEEEEEGSGHSTGEDSAFQEPDSPLPSARSPAEAEAERRRRSPGAEPSSPGELEDDLLLQGGGGGAQAAGGGAEGDSWEEEGFGSSSPVKSPSTAYFLSSPFSPVRCGGPGDASPQGCGAPRAMDDPCSPQPDYPSTPPHKTFRKLRLFDTPHTPKSLLSKARVIDSGSVKLRGSSLFMDTEKSGKREFDTRQTPQVNINPFTPDPVLLHSSGRCRGRKRAYFNDSSEDMEASDYEFEDETRPAKRITITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRVMSYLTEVELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVSEEGDEDDWISNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGEQWHEIRQGRLPRIPQVLSQEVTELLRVMIHPDPERRPSAMELVKHSVLLSASRKSAEQLRIELNAEKFKNSLLQKELKKAQMAAKVAAEERALFTDRMATRSTTQSNRTSRLIGKKMNRSVSLTIY

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSFLSRQQP ------CCCCCCCCC	34.59	26239621
5	Phosphorylation	---MSFLSRQQPPPT ---CCCCCCCCCCCC	26.49	26239621
19	Phosphorylation	TRRVGAAYSLRQKLI CCCCCHHHHHHHHHC	14.01	22499769
20	Phosphorylation	RRVGAAYSLRQKLIF CCCCHHHHHHHHHCC	16.61	22499769
52	Phosphorylation	GHSTGEDSAFQEPDS CCCCCCCCCCCCCCC	27.04	-
66	Phosphorylation	SPLPSARSPAEAEAE CCCCCCCCHHHHHHH	28.33	28066266
78	Phosphorylation	EAERRRRSPGAEPSS HHHHHHCCCCCCCCC	26.35	-
85	Phosphorylation	SPGAEPSSPGELEDD CCCCCCCCCCCCCCC	47.87	-
123	Phosphorylation	EEGFGSSSPVKSPST CCCCCCCCCCCCCCC	35.10	27149854
127	Phosphorylation	GSSSPVKSPSTAYFL CCCCCCCCCCCEEEC	25.07	26643407
129	Phosphorylation	SSPVKSPSTAYFLSS CCCCCCCCCEEECCC	32.53	28066266
130	Phosphorylation	SPVKSPSTAYFLSSP CCCCCCCCEEECCCC	28.85	26643407
135	Phosphorylation	PSTAYFLSSPFSPVR CCCEEECCCCCCCCC	26.51	28066266
136	Phosphorylation	STAYFLSSPFSPVRC CCEEECCCCCCCCCC	31.92	28066266
139	Phosphorylation	YFLSSPFSPVRCGGP EECCCCCCCCCCCCC	26.35	26745281
150	Phosphorylation	CGGPGDASPQGCGAP CCCCCCCCCCCCCCC	23.61	24453211
165	Phosphorylation	RAMDDPCSPQPDYPS CCCCCCCCCCCCCCC	31.77	21082442
170	Phosphorylation	PCSPQPDYPSTPPHK CCCCCCCCCCCCCCC	13.03	22499769
172	Phosphorylation	SPQPDYPSTPPHKTF CCCCCCCCCCCCCCC	47.52	22499769
173	Phosphorylation	PQPDYPSTPPHKTFR CCCCCCCCCCCCCCC	36.01	22499769
187	Phosphorylation	RKLRLFDTPHTPKSL CCEECCCCCCCCHHH	15.05	22817900
190	Phosphorylation	RLFDTPHTPKSLLSK ECCCCCCCCHHHHHC	33.35	26824392
193	Phosphorylation	DTPHTPKSLLSKARV CCCCCCHHHHHCCEE	35.43	26370283
203	Phosphorylation	SKARVIDSGSVKLRG HCCEEECCCCEEEEC	23.11	28066266
205	Phosphorylation	ARVIDSGSVKLRGSS CEEECCCCEEEECCC	21.74	28066266
239	Phosphorylation	QVNINPFTPDPVLLH CCCCCCCCCCCEEEC	28.21	-
262	Phosphorylation	KRAYFNDSSEDMEAS CCCCCCCCCHHHHHC	36.41	26643407
263	Phosphorylation	RAYFNDSSEDMEASD CCCCCCCCHHHHHCC	40.24	26643407
269	Phosphorylation	SSEDMEASDYEFEDE CCHHHHHCCCCCCCC	27.67	26643407
306	Phosphorylation	HELEKIGSGEFGSVF EEEEECCCCCCCHHH	38.33	-
311	Phosphorylation	IGSGEFGSVFKCVKR CCCCCCCHHHHHHHH	29.69	-
640	Phosphorylation	IGKKMNRSVSLTIY- HHHCCCCCEEEEEC-	15.85	28066266
642	Phosphorylation	KKMNRSVSLTIY--- HCCCCCEEEEEC---	22.50	26643407
644	Phosphorylation	MNRSVSLTIY----- CCCCEEEEEC-----	15.66	28066266

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
52	S	Phosphorylation	Kinase	PLK1	Q07832	Uniprot
123	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
642	S	Phosphorylation	Kinase	BRSK1	Q5RJI5	Uniprot
642	S	Phosphorylation	Kinase	BRSK2	Q69Z98	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
52	S	Phosphorylation	Dephosphorylated at Ser-52 and Ser-123 by the serine/threonine-protein phosphatase 2A preventing its ubiquitin-mediated degradation (By similarity).	-
52	S	Phosphorylation	Phosphorylated at Ser-52 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 (By similarity).	-
52	S	ubiquitylation	Dephosphorylated at Ser-52 and Ser-123 by the serine/threonine-protein phosphatase 2A preventing its ubiquitin-mediated degradation (By similarity).	-
52	S	ubiquitylation	Phosphorylated at Ser-52 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 (By similarity).	-
123	S	Phosphorylation	Dephosphorylated at Ser-52 and Ser-123 by the serine/threonine-protein phosphatase 2A preventing its ubiquitin-mediated degradation (By similarity).	-
123	S	Phosphorylation	Phosphorylated at Ser-52 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 (By similarity).	-
123	S	ubiquitylation	Dephosphorylated at Ser-52 and Ser-123 by the serine/threonine-protein phosphatase 2A preventing its ubiquitin-mediated degradation (By similarity).	-
123	S	ubiquitylation	Phosphorylated at Ser-52 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 (By similarity).	-
239	T	Phosphorylation	Dephosphorylated at Thr-239 by CTDP1 (By similarity).	-
642	S	Phosphorylation	Phosphorylation at Ser-642 by BRSK1 and BRSK2 in post-mitotic neurons, leads to down-regulate WEE1 activity in polarized neurons.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of WEE1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of WEE1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.