dbPTM

GSK3B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GSK3B_HUMAN
UniProt AC	P49841
Protein Name	Glycogen synthase kinase-3 beta
Gene Name	GSK3B
Organism	Homo sapiens (Human).
Sequence Length	420
Subcellular Localization	Cytoplasm . Nucleus. Cell membrane. The phosphorylated form shows localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane.
Protein Description	Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2, leading to inhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates SFPQ at 'Thr-687' upon T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1, CLOCK and PER2. Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation. [PubMed: 24391509]
Protein Sequence	MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGRPRTTS ------CCCCCCCCC	43.43	19413330
2	Phosphorylation	------MSGRPRTTS ------CCCCCCCCC	43.43	26074081
7	Phosphorylation	-MSGRPRTTSFAESC -CCCCCCCCCHHHHC	29.49	23927012
8	Phosphorylation	MSGRPRTTSFAESCK CCCCCCCCCHHHHCC	24.11	22322096
9	Phosphorylation	SGRPRTTSFAESCKP CCCCCCCCHHHHCCC	23.11	16940331
13	Phosphorylation	RTTSFAESCKPVQQP CCCCHHHHCCCCCCC	24.82	22322096
15 (in isoform 2)	Ubiquitination	-	58.46	-
15	Acetylation	TSFAESCKPVQQPSA CCHHHHCCCCCCCCC	58.46	25953088
15	Ubiquitination	TSFAESCKPVQQPSA CCHHHHCCCCCCCCC	58.46	-
21	Phosphorylation	CKPVQQPSAFGSMKV CCCCCCCCCCCCEEE	31.71	23927012
25	Phosphorylation	QQPSAFGSMKVSRDK CCCCCCCCEEEEECC	14.69	23401153
27	Ubiquitination	PSAFGSMKVSRDKDG CCCCCCEEEEECCCC	38.46	-
27	Methylation	PSAFGSMKVSRDKDG CCCCCCEEEEECCCC	38.46	-
29	Phosphorylation	AFGSMKVSRDKDGSK CCCCEEEEECCCCCE	29.28	26074081
35	Phosphorylation	VSRDKDGSKVTTVVA EEECCCCCEEEEEEE	33.80	21601212
36	Ubiquitination	SRDKDGSKVTTVVAT EECCCCCEEEEEEEC	49.48	-
38	O-linked_Glycosylation	DKDGSKVTTVVATPG CCCCCEEEEEEECCC	20.01	28510447
39	O-linked_Glycosylation	KDGSKVTTVVATPGQ CCCCEEEEEEECCCC	18.90	28510447
43	Phosphorylation	KVTTVVATPGQGPDR EEEEEEECCCCCCCC	19.15	16039586
43	O-linked_Glycosylation	KVTTVVATPGQGPDR EEEEEEECCCCCCCC	19.15	28510447
55	Phosphorylation	PDRPQEVSYTDTKVI CCCCCEEEEEEEEEE	22.89	29496907
56	Phosphorylation	DRPQEVSYTDTKVIG CCCCEEEEEEEEEEC	17.51	29438985
59	Phosphorylation	QEVSYTDTKVIGNGS CEEEEEEEEEECCCC	21.29	21601212
66	Phosphorylation	TKVIGNGSFGVVYQA EEEECCCCCEEEEEE	23.87	28348404
71	Phosphorylation	NGSFGVVYQAKLCDS CCCCEEEEEEEECCC	10.59	25147952
78	Phosphorylation	YQAKLCDSGELVAIK EEEEECCCCCEEEHH	32.92	30622161
85	Ubiquitination	SGELVAIKKVLQDKR CCCEEEHHHHHHCCC	27.39	-
86	Ubiquitination	GELVAIKKVLQDKRF CCEEEHHHHHHCCCC	41.90	-
86 (in isoform 2)	Ubiquitination	-	41.90	-
103	Ubiquitination	RELQIMRKLDHCNIV HHHHHHHHCCCCCEE	40.67	-
114	Phosphorylation	CNIVRLRYFFYSSGE CCEEEEEEEEECCCC	11.57	-
117	Phosphorylation	VRLRYFFYSSGEKKD EEEEEEEECCCCCCC	7.63	-
147	Phosphorylation	YRVARHYSRAKQTLP HHHHHHHHHHHCCCH	21.45	-
183 (in isoform 2)	Ubiquitination	-	44.85	-
183	Ubiquitination	GICHRDIKPQNLLLD CEECCCCCCHHEECC	44.85	-
197 (in isoform 2)	Ubiquitination	-	40.23	-
197	Ubiquitination	DPDTAVLKLCDFGSA CCCCHHHHHCCCCCH	40.23	-
203	Phosphorylation	LKLCDFGSAKQLVRG HHHCCCCCHHHHHCC	32.08	-
205	Ubiquitination	LCDFGSAKQLVRGEP HCCCCCHHHHHCCCC	45.95	-
205 (in isoform 2)	Ubiquitination	-	45.95	-
205	Acetylation	LCDFGSAKQLVRGEP HCCCCCHHHHHCCCC	45.95	55837983
215	Phosphorylation	VRGEPNVSYICSRYY HCCCCCHHHHHCCCC	18.54	29255136
216	Phosphorylation	RGEPNVSYICSRYYR CCCCCHHHHHCCCCC	11.15	19664994
219	Phosphorylation	PNVSYICSRYYRAPE CCHHHHHCCCCCCCC	17.48	23927012
221	Phosphorylation	VSYICSRYYRAPELI HHHHHCCCCCCCCHH	4.88	28152594
222	Phosphorylation	SYICSRYYRAPELIF HHHHCCCCCCCCHHC	10.13	28152594
275	Phosphorylation	EIIKVLGTPTREQIR HHHHHHCCCCHHHHH	19.82	17192257
277	Phosphorylation	IKVLGTPTREQIREM HHHHCCCCHHHHHHH	46.83	17192257
288	Phosphorylation	IREMNPNYTEFKFPQ HHHHCCCCCCCCCCC	14.65	27642862
292	Sumoylation	NPNYTEFKFPQIKAH CCCCCCCCCCCCCCC	50.32	-
292 (in isoform 2)	Ubiquitination	-	50.32	21890473
292 (in isoform 1)	Ubiquitination	-	50.32	21890473
292	Ubiquitination	NPNYTEFKFPQIKAH CCCCCCCCCCCCCCC	50.32	2189047
292	Sumoylation	NPNYTEFKFPQIKAH CCCCCCCCCCCCCCC	50.32	-
297	Ubiquitination	EFKFPQIKAHPWTKV CCCCCCCCCCCCCCC	35.08	-
297 (in isoform 2)	Ubiquitination	-	35.08	21890473
297 (in isoform 1)	Ubiquitination	-	35.08	21890473
317	S-nitrosylation	PPEAIALCSRLLEYT CHHHHHHHHHHHHHC	1.32	2212679
323	Phosphorylation	LCSRLLEYTPTARLT HHHHHHHHCCCCCCC	20.28	28102081
324	Phosphorylation	CSRLLEYTPTARLTP HHHHHHHCCCCCCCH	12.56	28102081
349	Ubiquitination	ELRDPNVKLPNGRDT HHCCCCCCCCCCCCC	65.94	-
362 (in isoform 2)	Ubiquitination	-	6.48	-
368	Phosphorylation	NFTTQELSSNPPLAT EECHHHHHCCCCCEE	27.58	21601212
369	Phosphorylation	FTTQELSSNPPLATI ECHHHHHCCCCCEEE	67.01	21601212
389	Phosphorylation	ARIQAAASTPTNATA HHHHHHHCCCCCCCC	30.14	25159151
390	Phosphorylation	RIQAAASTPTNATAA HHHHHHCCCCCCCCC	29.43	25159151
392	Phosphorylation	QAAASTPTNATAASD HHHHCCCCCCCCCCC	37.26	25159151
395	Phosphorylation	ASTPTNATAASDANT HCCCCCCCCCCCCCC	25.48	21712546
398	Phosphorylation	PTNATAASDANTGDR CCCCCCCCCCCCCCC	34.49	21601212
402	Phosphorylation	TAASDANTGDRGQTN CCCCCCCCCCCCCCC	42.03	21712546
403	Phosphorylation	AASDANTGDRGQTNN CCCCCCCCCCCCCCC	23.56	24719451
405	Phosphorylation	SDANTGDRGQTNNAA CCCCCCCCCCCCCCH	40.23	-
408	Phosphorylation	NTGDRGQTNNAASAS CCCCCCCCCCCHHHH	33.01	30177828
413	Phosphorylation	GQTNNAASASASNST CCCCCCHHHHCCCCC	21.98	18691976
415	Phosphorylation	TNNAASASASNST-- CCCCHHHHCCCCC--	29.72	18691976
417	Phosphorylation	NAASASASNST---- CCHHHHCCCCC----	28.90	19060867
419	Phosphorylation	ASASASNST------ HHHHCCCCC------	32.76	18691976
420	Phosphorylation	SASASNST------- HHHCCCCC-------	47.05	25262027
426	Phosphorylation	ST------------- CC-------------		-
428	Phosphorylation	--------------- ---------------		-
432	Phosphorylation	------------------- -------------------		-

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
9	S	Phosphorylation	Kinase	AURKA	O14965	GPS
9	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
9	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
9	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
9	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
9	S	Phosphorylation	Kinase	SGK3	Q96BR1	Uniprot
9	S	Phosphorylation	Kinase	MAP4K5	Q9Y4K4	GPS
9	S	Phosphorylation	Kinase	RPS6KB2	Q9UBS0	GPS
9	S	Phosphorylation	Kinase	P70S6K ISO2	P23443-2	PSP
9	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
9	S	Phosphorylation	Kinase	RSK2	P51812	PSP
9	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
9	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
9	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
9	S	Phosphorylation	Kinase	PRKCG	P05129	GPS
9	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
9	S	Phosphorylation	Kinase	PKCB ISO2	P05771-2	PSP
9	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
9	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
9	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
9	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
21	S	Phosphorylation	Kinase	SGK_GROUP	-	PhosphoELM
21	S	Phosphorylation	Kinase	SGK-FAMILY	-	GPS
43	T	Phosphorylation	Kinase	P38A	Q16539	PSP
43	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
43	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
56	Y	Phosphorylation	Kinase	MET	P08581	PSP
147	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
216	Y	Phosphorylation	Kinase	MAP2K1	Q02750	GPS
216	Y	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
216	Y	Phosphorylation	Kinase	GSK3B	P49841-2	GPS
216	Y	Phosphorylation	Kinase	GSK3B	P49841	PSP
389	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
390	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24451375
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF2	Q9HAU4	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
9	S	Phosphorylation		7980435
Inactivated by phosphorylation at Ser-9 (Probable).

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of GSK3B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GEMI4_HUMAN	GEMIN4	physical	17353931
SMYD2_HUMAN	SMYD2	physical	17353931
DDX20_HUMAN	DDX20	physical	17353931
GSKIP_HUMAN	GSKIP	physical	17353931
XPO6_HUMAN	XPO6	physical	17353931
DHX36_HUMAN	DHX36	physical	17353931
RPF2_HUMAN	RPF2	physical	17353931
IF2B1_HUMAN	IGF2BP1	physical	17353931
RU17_HUMAN	SNRNP70	physical	17353931
EWS_HUMAN	EWSR1	physical	17353931
ACLY_HUMAN	ACLY	physical	17353931
STRAP_HUMAN	STRAP	physical	17353931
SF3B1_HUMAN	SF3B1	physical	17353931
AXIN1_HUMAN	AXIN1	physical	9734785
ANDR_HUMAN	AR	physical	15178691
MUC1_HUMAN	MUC1	physical	9819408
APC_HUMAN	APC	physical	11251183
CCNE1_HUMAN	CCNE1	physical	14536078
NOTC2_HUMAN	NOTCH2	physical	12794074
AKA11_HUMAN	AKAP11	physical	12147701
KAP2_HUMAN	PRKAR2A	physical	12147701
AKT2_HUMAN	AKT2	physical	12434148
P53_HUMAN	TP53	physical	12048243
NFKB1_HUMAN	NFKB1	physical	11425860
FAK1_HUMAN	PTK2	physical	11809746
TSC1_HUMAN	TSC1	physical	12511557
TSC2_HUMAN	TSC2	physical	16959574
TSC2_HUMAN	TSC2	physical	12511557
NOTC1_HUMAN	NOTCH1	physical	12123574
CTNB1_HUMAN	CTNNB1	physical	10330181
AXIN1_RAT	Axin1	physical	10330181
NIN_HUMAN	NIN	physical	11004522
PRGC1_HUMAN	PPARGC1A	physical	18198341
SMAD3_HUMAN	SMAD3	physical	18172167
PSN1_HUMAN	PSEN1	physical	17360711
PHLP1_HUMAN	PHLPP1	physical	19797085
SNCAP_HUMAN	SNCAIP	physical	16174773
EPM2A_HUMAN	EPM2A	physical	16115820
SNAI1_HUMAN	SNAI1	physical	15448698
MYC_HUMAN	MYC	physical	14563837
DVL1_MOUSE	Dvl1	genetic	9271238
GSK3B_HUMAN	GSK3B	physical	11835406
CTNB1_HUMAN	CTNNB1	physical	11835406
C2TA_HUMAN	CIITA	physical	17991736
FBW1A_HUMAN	BTRC	physical	10228155
AXIN1_HUMAN	AXIN1	physical	10228155
CTNB1_HUMAN	CTNNB1	physical	10228155
ATF3_HUMAN	ATF3	physical	20110283
CEBPB_HUMAN	CEBPB	physical	20110283
SMUF2_HUMAN	SMURF2	physical	19481076
CTNB1_HUMAN	CTNNB1	physical	10074433
CTNB1_HUMAN	CTNNB1	physical	19061640
SRBP1_HUMAN	SREBF1	physical	19126544
UBR5_HUMAN	UBR5	physical	21118991
BCL3_HUMAN	BCL3	physical	15469820
KLF5_HUMAN	KLF5	physical	20484041
YBOX1_HUMAN	YBX1	physical	16198352
YBOX3_HUMAN	YBX3	physical	16198352
STRAP_HUMAN	STRAP	physical	21502811
AXIN1_HUMAN	AXIN1	physical	21502811
NOTC3_HUMAN	NOTCH3	physical	21502811
NAT9_HUMAN	NAT9	physical	21900206
ATX3_HUMAN	ATXN3	physical	21900206
TMM44_HUMAN	TMEM44	physical	21900206
MTOR_HUMAN	MTOR	physical	21900206
ENTP6_HUMAN	ENTPD6	physical	21900206
RXRA_HUMAN	RXRA	physical	21900206
P53_HUMAN	TP53	physical	21900206
ADIRF_HUMAN	ADIRF	physical	21900206
CSAD_HUMAN	CSAD	physical	21900206
CYTM_HUMAN	CST6	physical	21900206
GIPC1_HUMAN	GIPC1	physical	21900206
SYNE4_HUMAN	SYNE4	physical	21900206
BRX1_HUMAN	BRIX1	physical	21900206
EF1G_HUMAN	EEF1G	physical	21900206
GBB2_HUMAN	GNB2	physical	21900206
DJC13_HUMAN	DNAJC13	physical	21900206
ERG28_HUMAN	C14orf1	physical	21900206
APR_HUMAN	PMAIP1	physical	21900206
UBR1_HUMAN	UBR1	physical	21900206
LMO4_HUMAN	LMO4	physical	21900206
NSF1C_HUMAN	NSFL1C	physical	21900206
GBP2_HUMAN	GBP2	physical	21900206
BAG6_HUMAN	BAG6	physical	21900206
UB2D1_HUMAN	UBE2D1	physical	21900206
DNMT1_HUMAN	DNMT1	physical	21900206
FEN1_HUMAN	FEN1	physical	21900206
CAMP3_HUMAN	CAMSAP3	physical	21900206
G3P_HUMAN	GAPDH	physical	21900206
TBA1A_HUMAN	TUBA1A	physical	21900206
MICA1_HUMAN	MICAL1	physical	21900206
VIME_HUMAN	VIM	physical	21900206
ZN227_HUMAN	ZNF227	physical	21900206
RSU1_HUMAN	RSU1	physical	21900206
S30BP_HUMAN	SAP30BP	physical	21900206
SPTN4_HUMAN	SPTBN4	physical	21900206
M1IP1_HUMAN	MID1IP1	physical	21900206
CHD3_HUMAN	CHD3	physical	21900206
TONSL_HUMAN	TONSL	physical	21900206
4EBP1_HUMAN	EIF4EBP1	physical	21900206
MAP4_HUMAN	MAP4	physical	21900206
CEBPZ_HUMAN	CEBPZ	physical	21900206
RLA1_HUMAN	RPLP1	physical	21900206
TLE1_HUMAN	TLE1	physical	21900206
XPP1_HUMAN	XPNPEP1	physical	21900206
MTF2_HUMAN	MTF2	physical	21900206
CXB5_HUMAN	GJB5	physical	21900206
MASP1_HUMAN	MASP1	physical	21900206
PTN_HUMAN	PTN	physical	21900206
DCTN3_HUMAN	DCTN3	physical	21900206
RS2_HUMAN	RPS2	physical	21900206
DNM3L_HUMAN	DNMT3L	physical	21900206
WSB1_HUMAN	WSB1	physical	21900206
IGS21_HUMAN	IGSF21	physical	21900206
CENPB_HUMAN	CENPB	physical	21900206
RAI1_HUMAN	RAI1	physical	21900206
SLAP1_HUMAN	SLA	physical	21900206
BZW2_HUMAN	BZW2	physical	21900206
EF1A1_HUMAN	EEF1A1	physical	21900206
FBN3_HUMAN	FBN3	physical	21900206
KINH_HUMAN	KIF5B	physical	21900206
VPS51_HUMAN	VPS51	physical	21900206
ACBG1_HUMAN	ACSBG1	physical	21900206
ADAP1_HUMAN	ADAP1	physical	21900206
IQCG_HUMAN	IQCG	physical	21900206
ZN746_HUMAN	ZNF746	physical	21900206
U5S1_HUMAN	EFTUD2	physical	21900206
OGA_HUMAN	MGEA5	physical	21900206
MED24_HUMAN	MED24	physical	21900206
FIBP_HUMAN	FIBP	physical	21900206
FKB14_HUMAN	FKBP14	physical	21900206
LC7L2_HUMAN	LUC7L2	physical	21900206
P33MX_HUMAN	KIAA1191	physical	21900206
F264_HUMAN	PFKFB4	physical	21900206
ATIF1_HUMAN	ATPIF1	physical	21900206
ACL6B_HUMAN	ACTL6B	physical	21900206
ASGL1_HUMAN	ASRGL1	physical	21900206
RL36L_HUMAN	RPL36AL	physical	21900206
UBXN6_HUMAN	UBXN6	physical	21900206
EM55_HUMAN	MPP1	physical	21900206
DHX34_HUMAN	DHX34	physical	21900206
BEX1_HUMAN	BEX1	physical	21900206
UFM1_HUMAN	UFM1	physical	21900206
DEF1_HUMAN	DEFA1	physical	21900206
ZHX1_HUMAN	ZHX1	physical	21900206
SYQ_HUMAN	QARS	physical	21900206
ACBP_HUMAN	DBI	physical	21900206
FA83D_HUMAN	FAM83D	physical	21900206
ZN135_HUMAN	ZNF135	physical	21900206
FUBP2_HUMAN	KHSRP	physical	21900206
GPR39_HUMAN	GPR39	physical	21900206
SUH_HUMAN	RBPJ	physical	21900206
PIM2_HUMAN	PIM2	physical	21900206
NRBP_HUMAN	NRBP1	physical	21900206
TETN_HUMAN	CLEC3B	physical	21900206
FZD5_HUMAN	FZD5	physical	21900206
ARRB1_HUMAN	ARRB1	physical	10347142
TAU_HUMAN	MAPT	physical	14612456
NCOA3_HUMAN	NCOA3	physical	15383283
SMAD3_HUMAN	SMAD3	physical	21310903
A4_HUMAN	APP	physical	22613765
AXIN1_HUMAN	AXIN1	physical	22613765
TAZ_HUMAN	TAZ	physical	22692215
NF2L2_HUMAN	NFE2L2	physical	22751928
PDE4D_HUMAN	PDE4D	physical	20647544
MDM2_HUMAN	MDM2	physical	16055726
CTNB1_MOUSE	Ctnnb1	physical	12417018
HSP74_HUMAN	HSPA4	physical	22824801
HS90A_HUMAN	HSP90AA1	physical	22824801
2A5D_HUMAN	PPP2R5D	physical	22893788
ATX3_HUMAN	ATXN3	physical	17434145
CREB1_HUMAN	CREB1	physical	14635195
M3K1_HUMAN	MAP3K1	physical	12584189
AXIN1_HUMAN	AXIN1	physical	12584189
XIAP_HUMAN	XIAP	physical	19698783
BIRC2_HUMAN	BIRC2	physical	19698783
BIRC3_HUMAN	BIRC3	physical	19698783
TAU_HUMAN	MAPT	physical	9771888
TAU_HUMAN	MAPT	physical	22965877
NUB1_HUMAN	NUB1	physical	22965877
TAU_HUMAN	MAPT	physical	10090741
SNAI2_HUMAN	SNAI2	physical	23011797
TAU_HUMAN	MAPT	physical	21985244
GYS1_HUMAN	GYS1	physical	21985244
GSK3B_HUMAN	GSK3B	physical	21985244
SYUA_HUMAN	SNCA	physical	21985244
HSP74_HUMAN	HSPA4	physical	21985244
CTNB1_HUMAN	CTNNB1	physical	16039586
MK01_HUMAN	MAPK1	physical	16039586
TAU_HUMAN	MAPT	physical	9546672
KAPCA_HUMAN	PRKACA	physical	11035810
A4_HUMAN	APP	physical	21832049
PTN11_HUMAN	PTPN11	physical	22939629
TAU_HUMAN	MAPT	physical	17512525
TAU_HUMAN	MAPT	physical	12387894
SNAI1_HUMAN	SNAI1	physical	19411070
DDIT4_HUMAN	DDIT4	physical	19557001
RELB_HUMAN	RELB	physical	21217772
TF65_HUMAN	RELA	physical	21217772
DEAF1_HUMAN	DEAF1	physical	20368287
SPICE_HUMAN	SPICE1	physical	20368287
VTA1_HUMAN	VTA1	physical	20368287
NBR1_MOUSE	Nbr1	physical	20368287
SPICE_MOUSE	Spice1	physical	20368287
DEAF1_MOUSE	Deaf1	physical	20368287
KRBA1_MOUSE	Krba1	physical	20368287
LZTS2_MOUSE	Lzts2	physical	20368287
M3K11_MOUSE	Map3k11	physical	20368287
NONO_MOUSE	Nono	physical	20368287
PROX2_MOUSE	Prox2	physical	20368287
PRUN1_MOUSE	Prune	physical	20368287
VTA1_MOUSE	Vta1	physical	20368287
ZBED3_MOUSE	Zbed3	physical	20368287
M3K11_HUMAN	MAP3K11	physical	20368287
ARHGB_HUMAN	ARHGEF11	physical	20368287
KRBA1_HUMAN	KRBA1	physical	20368287
AXIN1_MOUSE	Axin1	physical	20368287
HA2B_MOUSE	H2-Aa	physical	20368287
F193B_HUMAN	FAM193B	physical	20368287
SMAD1_HUMAN	SMAD1	physical	18045539
KLF2_HUMAN	KLF2	physical	23507969
NF2L1_HUMAN	NFE2L1	physical	23623971
CSF3R_HUMAN	CSF3R	physical	23820376
CTNB1_HUMAN	CTNNB1	physical	19107203
LRP6_HUMAN	LRP6	physical	19107203
FOG1_HUMAN	ZFPM1	physical	21988832
SGK3_HUMAN	SGK3	physical	21988832
GSK3B_HUMAN	GSK3B	physical	23602568
AXIN1_HUMAN	AXIN1	physical	23602568
AXIN2_HUMAN	AXIN2	physical	23602568
GSKIP_HUMAN	GSKIP	physical	23602568
AKA11_HUMAN	AKAP11	physical	23602568
KAP0_HUMAN	PRKAR1A	physical	23602568
IPP2_HUMAN	PPP1R2	physical	23602568
KAPCA_HUMAN	PRKACA	physical	23602568
APC_HUMAN	APC	physical	23602568
CTNB1_HUMAN	CTNNB1	physical	23602568
FRAT1_HUMAN	FRAT1	physical	23602568
CTNB1_HUMAN	CTNNB1	physical	24451375
AXIN1_HUMAN	AXIN1	physical	24451375
FBW1A_HUMAN	BTRC	physical	24451375
AXIN1_HUMAN	AXIN1	physical	23455922
CLAP2_HUMAN	CLASP2	physical	23455922
FRAT2_HUMAN	FRAT2	physical	23455922
IPP2_HUMAN	PPP1R2	physical	23455922
PP1A_HUMAN	PPP1CA	physical	23455922
DYL1_HUMAN	DYNLL1	physical	23455922
PRUN1_HUMAN	PRUNE	physical	23455922
FRAT1_HUMAN	FRAT1	physical	23455922
GSKIP_HUMAN	GSKIP	physical	23455922
E41L3_HUMAN	EPB41L3	physical	23455922
AXIN2_HUMAN	AXIN2	physical	23455922
EYA1_HUMAN	EYA1	physical	24752894
NBR1_HUMAN	NBR1	physical	24879152
AURKA_HUMAN	AURKA	physical	23204235
SNAI2_HUMAN	SNAI2	physical	23851495
HDAC4_HUMAN	HDAC4	physical	21118993
JUN_HUMAN	JUN	physical	17215518
TAU_HUMAN	MAPT	physical	19014373
M3K4_HUMAN	MAP3K4	physical	17726008
RICTR_HUMAN	RICTOR	physical	21343617
TAU_HUMAN	MAPT	physical	19527721
KLF5_HUMAN	KLF5	physical	20388706
TAU_HUMAN	MAPT	physical	17078951
TAU_HUMAN	MAPT	physical	12048243
RICTR_HUMAN	RICTOR	physical	25897075
CTNB1_HUMAN	CTNNB1	physical	25897075
SP7_HUMAN	SP7	physical	25728276
ILKAP_HUMAN	ILKAP	physical	26344197
CTNB1_HUMAN	CTNNB1	physical	25241761
AXIN1_HUMAN	AXIN1	physical	25241761
CADH1_HUMAN	CDH1	physical	25241761
NEMO_HUMAN	IKBKG	physical	25241761
CCND1_HUMAN	CCND1	physical	25241761
FOXO1_HUMAN	FOXO1	physical	25241761
JUN_HUMAN	JUN	physical	25241761
NF2L3_HUMAN	NFE2L3	physical	26306035
CR3L3_HUMAN	CREB3L3	physical	26108621
PIAS1_HUMAN	PIAS1	physical	26157031
PCAT1_HUMAN	LPCAT1	physical	21068446
SOX10_HUMAN	SOX10	physical	26461473
M3K2_HUMAN	MAP3K2	physical	26884171
TBK1_HUMAN	TBK1	physical	26915459
UBE3A_HUMAN	UBE3A	physical	27902311
SOX9_HUMAN	SOX9	physical	27566146
NEMO_HUMAN	IKBKG	physical	27929056
CTND1_HUMAN	CTNND1	physical	28069439
B2CL1_HUMAN	BCL2L1	physical	22617334
DISC1_HUMAN	DISC1	physical	28727686

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01356	Lithium

Regulatory Network of GSK3B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; SER-9; SER-25;SER-215; TYR-216; SER-219; THR-275; THR-277; SER-389; THR-390;THR-392; SER-398; SER-413; SER-415; SER-417 AND SER-419, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-216; SER-219;THR-275; THR-277; THR-390 AND THR-392, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-216 AND THR-390,AND MASS SPECTROMETRY.	17192257 [Abstract]
"Human serum and glucocorticoid-inducible kinase-like kinase (SGKL)phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction."; Dai F., Yu L., He H., Chen Y., Yu J., Yang Y., Xu Y., Ling W.,Zhao S.; Biochem. Biophys. Res. Commun. 293:1191-1196(2002). Cited for: PHOSPHORYLATION AT SER-9 BY SGK3, AND INTERACTION WITH SGK3.	12054501 [Abstract]
"Inactivation of glycogen synthase kinase-3 beta by phosphorylation:new kinase connections in insulin and growth-factor signalling."; Sutherland C., Leighton I.A., Cohen P.; Biochem. J. 296:15-19(1993). Cited for: PHOSPHORYLATION AT SER-9.	8250835 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND THR-390, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Structural basis for recruitment of glycogen synthase kinase 3beta tothe axin-APC scaffold complex."; Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V.,Dale T.C., Pearl L.H.; EMBO J. 22:494-501(2003). Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 35-384 IN COMPLEX WITH AXIN1,INTERACTION WITH AXIN1 AND FRAT1, FUNCTION, ENZYME REGULATION, ANDPHOSPHORYLATION AT TYR-216.	12554650 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.	18083107 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.	15951569 [Abstract]

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