CEBPB_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CEBPB_RAT
• UniProt AC: P21272
• Protein Name: CCAAT/enhancer-binding protein beta {ECO:0000312|RGD:2327}
• Gene Name: Cebpb {ECO:0000312|RGD:2327}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 297
• Subcellular Localization: Nucleus . Cytoplasm . Translocates to the nucleus when phosphorylated at Ser-288. In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (By similarity).
• Protein Description: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. [PubMed: 8336793 Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis]
• Protein Sequence: MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAAADFAAPAPAHHDFLSDLFADDYGAKPSKKPSDYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKAVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC

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	-
39	Acetylation	DCLAYGAKAARAAPR HHHHHHHHHHHHCCC	37.91	123027
39	Methylation	DCLAYGAKAARAAPR HHHHHHHHHHHHCCC	37.91	18647749
64	Phosphorylation	HERAIDFSPYLEPLA CCCCCCCCCCCCCCC	14.64	15314150
99	Acetylation	FADDYGAKPSKKPSD HCCCCCCCCCCCCCC	45.52	-
99	Methylation	FADDYGAKPSKKPSD HCCCCCCCCCCCCCC	45.52	21326902
102	Methylation	DYGAKPSKKPSDYGY CCCCCCCCCCCCCCC	76.78	21326902
102	Acetylation	DYGAKPSKKPSDYGY CCCCCCCCCCCCCCC	76.78	-
103	Acetylation	YGAKPSKKPSDYGYV CCCCCCCCCCCCCCC	54.84	-
105	Phosphorylation	AKPSKKPSDYGYVSL CCCCCCCCCCCCCCC	52.96	11684016
109	Phosphorylation	KKPSDYGYVSLGRAG CCCCCCCCCCCCCCC	4.80	20351173
111	Phosphorylation	PSDYGYVSLGRAGAK CCCCCCCCCCCCCCC	19.34	23984901
114	Methylation	YGYVSLGRAGAKAAP CCCCCCCCCCCCCCC	34.83	-
134	Methylation	PPPPAALKAEPGFEP CCCCHHHCCCCCCCH	46.08	21326902
145	Methylation	GFEPADCKRADDAPA CCCHHHCCCCCCCHH	51.69	21326902
164	Phosphorylation	FPFALRAYLGYQATP CCHHHHHHHCEECCC	8.33	23984901
167	Phosphorylation	ALRAYLGYQATPSGS HHHHHHCEECCCCCC	7.74	23984901
170	Phosphorylation	AYLGYQATPSGSSGS HHHCEECCCCCCCCC	11.49	23984901
172	Phosphorylation	LGYQATPSGSSGSLS HCEECCCCCCCCCCC	47.13	23984901
174	Phosphorylation	YQATPSGSSGSLSTS EECCCCCCCCCCCCC	35.54	23984901
175	Phosphorylation	QATPSGSSGSLSTSS ECCCCCCCCCCCCCC	35.61	23984901
177	Phosphorylation	TPSGSSGSLSTSSSS CCCCCCCCCCCCCCC	22.54	22673903
179	Phosphorylation	SGSSGSLSTSSSSSP CCCCCCCCCCCCCCC	28.13	23984901
180	Phosphorylation	GSSGSLSTSSSSSPP CCCCCCCCCCCCCCC	37.61	23984901
181	O-linked_Glycosylation	SSGSLSTSSSSSPPG CCCCCCCCCCCCCCC	25.50	-
181	Phosphorylation	SSGSLSTSSSSSPPG CCCCCCCCCCCCCCC	25.50	22673903
182	O-linked_Glycosylation	SGSLSTSSSSSPPGT CCCCCCCCCCCCCCC	34.04	-
182	Phosphorylation	SGSLSTSSSSSPPGT CCCCCCCCCCCCCCC	34.04	21630457
183	Phosphorylation	GSLSTSSSSSPPGTP CCCCCCCCCCCCCCC	34.30	23984901
184	Phosphorylation	SLSTSSSSSPPGTPS CCCCCCCCCCCCCCC	49.14	21630457
185	Phosphorylation	LSTSSSSSPPGTPSP CCCCCCCCCCCCCCH	36.74	21630457
189	Phosphorylation	SSSSPPGTPSPADAK CCCCCCCCCCHHHHH	26.77	29779826
191	Phosphorylation	SSPPGTPSPADAKAA CCCCCCCCHHHHHHC	32.34	23984901
212	Methylation	GPPAAPAKAKAKKAV CCCCCCHHHHHHHHH	49.73	21326902
216	Acetylation	APAKAKAKKAVDKLS CCHHHHHHHHHHHHH	40.33	60103
217	Acetylation	PAKAKAKKAVDKLSD CHHHHHHHHHHHHHH	59.51	60109
223	Phosphorylation	KKAVDKLSDEYKMRR HHHHHHHHHHHHHHH	33.85	-
240	Phosphorylation	NNIAVRKSRDKAKMR HCCCHHHHHHHHHHH	34.84	8200992
267	Methylation	AENERLQKKVEQLSR HHHHHHHHHHHHHHH	64.48	21326902
273	Phosphorylation	QKKVEQLSRELSTLR HHHHHHHHHHHHHHH	24.33	20351173
277	Phosphorylation	EQLSRELSTLRNLFK HHHHHHHHHHHHHHH	22.20	-
284	Methylation	STLRNLFKQLPEPLL HHHHHHHHHCCHHHH	54.84	21326902

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
64	S	Phosphorylation	Kinase	CDK2	P24941	PSP
64	S	Phosphorylation	Kinase	CDK1	P11440	PSP
105	S	Phosphorylation	Kinase	PKACA	P27791	PSP
105	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
105	S	Phosphorylation	Kinase	P90RSK	Q63531	PSP
105	S	Phosphorylation	Kinase	PRKCA	P05696	Uniprot
177	S	Phosphorylation	Kinase	GSK3B	P18266	GPS
180	T	Phosphorylation	Kinase	GSK3-BETA	P18266	Uniprot
181	S	Phosphorylation	Kinase	GSK3B	P18266	GPS
185	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
185	S	Phosphorylation	Kinase	GSK3-BETA	P18266	Uniprot
189	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
189	T	Phosphorylation	Kinase	MAPK	-	Uniprot
189	T	Phosphorylation	Kinase	CDK3	Q00526	PSP
189	T	Phosphorylation	Kinase	RPS6KA1	Q63531	Uniprot
189	T	Phosphorylation	Kinase	CDK2	Q63699	Uniprot
189	T	Phosphorylation	Kinase	CDK2	P24941	PSP
223	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
223	S	Phosphorylation	Kinase	CSNK2A1	Q60737	GPS
240	S	Phosphorylation	Kinase	PKCA	P05696	PSP
240	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
240	S	Phosphorylation	Kinase	PKACA	P27791	PSP
273	S	Phosphorylation	Kinase	RSK2	P18654	PSP
273	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
273	S	Phosphorylation	Kinase	RPS6KA2	Q9WUT3	GPS
277	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 inhibit transactivation activity.	-
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.	-
39	K	Methylation	Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2 inhibit transactivation activity.	-
105	S	Phosphorylation	Phosphorylation at Ser-105 enhances transactivation activity.	8336793
134	K	Sumoylation	In adipocytes, sumoylation at Lys-134 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation.	-
134	K	Sumoylation	Sumoylation at Lys-134 is required for inhibition of T-cells proliferation.	-
134	K	ubiquitylation	In adipocytes, sumoylation at Lys-134 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation.	-
180	T	Phosphorylation	Phosphorylated at Thr-189 by MAPK and CDK2, serves to prime phosphorylation at Thr-180 and Ser-185 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.	8336793
180	T	Phosphorylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
180	T	Glycosylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
181	S	Glycosylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
181	S	Phosphorylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
182	S	Glycosylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
182	S	Phosphorylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
185	S	Phosphorylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
185	S	Phosphorylation	Phosphorylated at Thr-189 by MAPK and CDK2, serves to prime phosphorylation at Thr-180 and Ser-185 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.	8336793
185	S	Glycosylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
189	T	Glycosylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
189	T	Methylation	Methylation is probably inhibited by phosphorylation at Thr-189.	-
189	T	Phosphorylation	MAPK and CDK2 act sequentially to maintain Thr-189 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation (By similarity).	8336793
189	T	Phosphorylation	Methylation is probably inhibited by phosphorylation at Thr-189.	-
189	T	Phosphorylation	O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.	-
189	T	Phosphorylation	Phosphorylated at Thr-189 by MAPK and CDK2, serves to prime phosphorylation at Thr-180 and Ser-185 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.	8336793
189	T	Phosphorylation	Phosphorylated at Thr-189 by RPS6KA1 (By similarity).	8336793
277	S	Phosphorylation	Phosphorylation at Ser-277 in response to calcium increases transactivation activity.	8336793

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TF2B_RAT	Gtf2b	physical	8972203
NOLC1_RAT	Nolc1	physical	8972203
SMCA2_HUMAN	SMARCA2	physical	22242598
SMCA4_HUMAN	SMARCA4	physical	22242598
SMRC1_HUMAN	SMARCC1	physical	22242598
SNF5_HUMAN	SMARCB1	physical	22242598
SMCA5_HUMAN	SMARCA5	physical	22242598
BAZ1A_HUMAN	BAZ1A	physical	22242598
CHRC1_HUMAN	CHRAC1	physical	22242598
DPOE3_HUMAN	POLE3	physical	22242598
INO80_HUMAN	INO80	physical	22242598
HLTF_HUMAN	HLTF	physical	22242598
PRKDC_HUMAN	PRKDC	physical	22242598
USF1_HUMAN	USF1	physical	22242598
TFAP4_HUMAN	TFAP4	physical	22242598
BEND3_HUMAN	BEND3	physical	22242598
TFCP2_HUMAN	TFCP2	physical	22242598
COT2_HUMAN	NR2F2	physical	22242598
JUNB_HUMAN	JUNB	physical	22242598
DNLI3_HUMAN	LIG3	physical	22242598
SKP1_HUMAN	SKP1	physical	22242598
PNKP_HUMAN	PNKP	physical	22242598
ATF7_HUMAN	ATF7	physical	22242598
XRCC1_HUMAN	XRCC1	physical	22242598
ERR1_HUMAN	ESRRA	physical	22242598
TE2IP_HUMAN	TERF2IP	physical	22242598
NR2C2_HUMAN	NR2C2	physical	22242598
RFXK_HUMAN	RFXANK	physical	22242598
RFC3_HUMAN	RFC3	physical	22242598
NP1L1_HUMAN	NAP1L1	physical	22242598
NFYC_HUMAN	NFYC	physical	22242598
MEIS1_HUMAN	MEIS1	physical	22242598
SSBP_HUMAN	SSBP1	physical	22242598
NFIC_HUMAN	NFIC	physical	22242598
RXRB_HUMAN	RXRB	physical	22242598
DDX49_HUMAN	DDX49	physical	22242598
RFX1_HUMAN	RFX1	physical	22242598
RHOA_HUMAN	RHOA	physical	22242598
HMGB2_HUMAN	HMGB2	physical	22242598
DEK_HUMAN	DEK	physical	22242598
RAD21_HUMAN	RAD21	physical	22242598
CDKA1_HUMAN	CDK2AP1	physical	22242598
RPAB5_HUMAN	POLR2L	physical	22242598
RBM7_HUMAN	RBM7	physical	22242598
RFA2_HUMAN	RPA2	physical	22242598
ZBT7A_HUMAN	ZBTB7A	physical	22242598
PAXI1_HUMAN	PAXIP1	physical	22242598
SHPRH_HUMAN	SHPRH	physical	22242598
SMAL1_HUMAN	SMARCAL1	physical	22242598

Drug and Disease Associations

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