CEBPB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CEBPB_MOUSE
• UniProt AC: P28033
• Protein Name: CCAAT/enhancer-binding protein beta {ECO:0000312|MGI:MGI:88373}
• Gene Name: Cebpb {ECO:0000312|MGI:MGI:88373}
• Organism: Mus musculus (Mouse).
• Sequence Length: 296
• Subcellular Localization: Nucleus . Cytoplasm . In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (PubMed:16585579). Translocates to the nucleus when phosphorylated at Ser-288 (By similarity).
• Protein Description: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. [PubMed: 16585579]
• Protein Sequence: MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAADFAAPAPAHHDFLSDLFADDYGAKPSKKPADYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKTVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC

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
3	Methylation	-----MHRLLAWDAA -----CCCCCCCCHH	30.05	20111005
39	Acetylation	DCLAYGAKAARAAPR HHHHHHHHHHHHCCC	37.91	18486321
39	Methylation	DCLAYGAKAARAAPR HHHHHHHHHHHHCCC	37.91	18647749
64	Phosphorylation	HERAIDFSPYLEPLA CCCCCCCCCCCCCCC	14.64	26643407
66	Phosphorylation	RAIDFSPYLEPLAPA CCCCCCCCCCCCCCC	23.62	26643407
98	Acetylation	FADDYGAKPSKKPAD HCCCCCCCCCCCCCC	45.52	17301242
101	Acetylation	DYGAKPSKKPADYGY CCCCCCCCCCCCCCC	71.89	17301242
102	Acetylation	YGAKPSKKPADYGYV CCCCCCCCCCCCCCE	50.18	17301242
106	Phosphorylation	PSKKPADYGYVSLGR CCCCCCCCCCEECCC	16.68	25159016
108	Phosphorylation	KKPADYGYVSLGRAG CCCCCCCCEECCCCC	4.80	25159016
110	Phosphorylation	PADYGYVSLGRAGAK CCCCCCEECCCCCCC	19.34	25159016
117	Acetylation	SLGRAGAKAAPPACF ECCCCCCCCCCCCCC	44.13	17110376
133	Ubiquitination	PPPPAALKAEPGFEP CCCCHHHCCCCCCCH	46.08	16585579
133	Sumoylation	PPPPAALKAEPGFEP CCCCHHHCCCCCCCH	46.08	16585579
163	Phosphorylation	FPFALRAYLGYQATP CCHHHHHHHCEECCC	8.33	25159016
166	Phosphorylation	ALRAYLGYQATPSGS HHHHHHCEECCCCCC	7.74	25159016
169	Phosphorylation	AYLGYQATPSGSSGS HHHCEECCCCCCCCC	11.49	25159016
171	Phosphorylation	LGYQATPSGSSGSLS HCEECCCCCCCCCCC	47.13	26239621
173	Phosphorylation	YQATPSGSSGSLSTS EECCCCCCCCCCCCC	35.54	24453211
174	Phosphorylation	QATPSGSSGSLSTSS ECCCCCCCCCCCCCC	35.61	25159016
176	Phosphorylation	TPSGSSGSLSTSSSS CCCCCCCCCCCCCCC	22.54	25159016
178	Phosphorylation	SGSSGSLSTSSSSSP CCCCCCCCCCCCCCC	28.13	25159016
179	Phosphorylation	GSSGSLSTSSSSSPP CCCCCCCCCCCCCCC	37.61	17264204
180	Phosphorylation	SSGSLSTSSSSSPPG CCCCCCCCCCCCCCC	25.50	25159016
180	O-linked_Glycosylation	SSGSLSTSSSSSPPG CCCCCCCCCCCCCCC	25.50	28135057
181	Phosphorylation	SGSLSTSSSSSPPGT CCCCCCCCCCCCCCC	34.04	25521595
181	O-linked_Glycosylation	SGSLSTSSSSSPPGT CCCCCCCCCCCCCCC	34.04	28135057
182	Phosphorylation	GSLSTSSSSSPPGTP CCCCCCCCCCCCCCC	34.30	25159016
183	Phosphorylation	SLSTSSSSSPPGTPS CCCCCCCCCCCCCCC	49.14	25168779
184	Phosphorylation	LSTSSSSSPPGTPSP CCCCCCCCCCCCCCH	36.74	25521595
188	Phosphorylation	SSSSPPGTPSPADAK CCCCCCCCCCHHHHH	26.77	25521595
190	Phosphorylation	SSPPGTPSPADAKAA CCCCCCCCHHHHHHC	32.34	25159016
215	Acetylation	APAKAKAKKTVDKLS CCCHHHHHHHHHHHH	48.55	17110376
216	Acetylation	PAKAKAKKTVDKLSD CCHHHHHHHHHHHHH	59.65	17110376
217	Phosphorylation	AKAKAKKTVDKLSDE CHHHHHHHHHHHHHH	32.98	11684016
222	Phosphorylation	KKTVDKLSDEYKMRR HHHHHHHHHHHHHHH	33.85	-
239	Phosphorylation	NNIAVRKSRDKAKMR HCCCHHHHHHHHHHH	34.84	-
272	Phosphorylation	QKKVEQLSRELSTLR HHHHHHHHHHHHHHH	24.33	-
276	Phosphorylation	EQLSRELSTLRNLFK HHHHHHHHHHHHHHH	22.20	16585579

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
179	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
179	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
179	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
179	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
184	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
184	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
184	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
184	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
188	T	Phosphorylation	Kinase	MAPK	-	Uniprot
188	T	Phosphorylation	Kinase	MAPK3	Q63844	GPS
188	T	Phosphorylation	Kinase	ERK1	P27361	PSP
188	T	Phosphorylation	Kinase	MK01	P63085	PhosphoELM
188	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
188	T	Phosphorylation	Kinase	P38A	P47811	PSP
188	T	Phosphorylation	Kinase	RPS6KA1	P18653	Uniprot
188	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
188	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
188	T	Phosphorylation	Kinase	CDK2	P97377	Uniprot
217	T	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
217	T	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
217	T	Phosphorylation	Kinase	P90RSK	P18653	PSP
217	T	Phosphorylation	Kinase	PRKCA	P20444	Uniprot
222	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
239	S	Phosphorylation	Kinase	PRKCA	P20444	Uniprot
276	S	Phosphorylation	Kinase	CAMK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
3	R	Methylation	Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2, inhibits transactivation activity.	20111005
39	K	Acetylation	Acetylation at Lys-39 is an important and dynamic regulatory event that contributes to its ability to transactivate target genes, including those associated with adipogenesis and adipocyte function.	18647749
39	K	Methylation	Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2, inhibits transactivation activity.	18647749
133	K	Sumoylation	In adipocytes, sumoylation at Lys-133 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation.	16585579
133	K	Sumoylation	Sumoylation at Lys-133 is required for inhibition of T-cells proliferation.	16585579
133	K	ubiquitylation	In adipocytes, sumoylation at Lys-133 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation.	16585579
179	T	Phosphorylation	Phosphorylated at Thr-188 by MAPK and CDK2, serves to prime phosphorylation at Thr-179 and Ser-184 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.	15985551
179	T	Phosphorylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	15985551
179	T	Glycosylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	15985551
180	S	Glycosylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	19478079
180	S	Phosphorylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	19478079
181	S	Glycosylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	19478079
181	S	Phosphorylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	19478079
184	S	Phosphorylation	Phosphorylated at Thr-188 by MAPK and CDK2, serves to prime phosphorylation at Thr-179 and Ser-184 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.	15985551
184	S	Phosphorylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	15985551
184	S	Glycosylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	15985551
188	T	Glycosylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	15985551
188	T	Methylation	Methylation is probably inhibited by phosphorylation at Thr-188.	15985551
188	T	Phosphorylation	MAPK and CDK2 act sequentially to maintain Thr-188 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation.	15985551
188	T	Phosphorylation	Methylation is probably inhibited by phosphorylation at Thr-188.	15985551
188	T	Phosphorylation	O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.	15985551
188	T	Phosphorylation	Phosphorylated at Thr-188 by MAPK and CDK2, serves to prime phosphorylation at Thr-179 and Ser-184 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.	15985551
188	T	Phosphorylation	Phosphorylated at Thr-188 by RPS6KA1 (By similarity).	15985551
217	T	Phosphorylation	Phosphorylation at Thr-217 enhances transactivation activity.	10635333
276	S	Phosphorylation	Phosphorylation at Ser-276 in response to calcium increases transactivation activity.	1314426

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_MOUSE	Hdac1	physical	16431920
MED1_MOUSE	Med1	physical	18339625
HMGA1_MOUSE	Hmga1	physical	11259597
BHE40_MOUSE	Bhlhe40	physical	22610404
RNF41_MOUSE	Rnf41	physical	22707723
RB_MOUSE	Rb1	physical	8946919
MDM2_MOUSE	Mdm2	physical	25720496
PGES2_MOUSE	Ptges2	physical	15879117

Drug and Disease Associations

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