dbPTM

CEBPB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CEBPB_HUMAN
UniProt AC	P17676
Protein Name	CCAAT/enhancer-binding protein beta {ECO:0000312\|HGNC:HGNC:1834}
Gene Name	CEBPB {ECO:0000312\|HGNC:HGNC:1834}
Organism	Homo sapiens (Human).
Sequence Length	345
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: 1741402]
Protein Sequence	MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSGHC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Dimethylation	-----MQRLVAWDPA -----CCCCCCCCCC	29.81	-
3	Methylation	-----MQRLVAWDPA -----CCCCCCCCCC	29.81	20111005
43	Acetylation	LAAAYGGKAAPAAPP HHHHHCCCCCCCCCC	36.69	-
43	Methylation	LAAAYGGKAAPAAPP HHHHHCCCCCCCCCC	36.69	-
62	Ubiquitination	GPRPPAGELGSIGDH CCCCCCCCCCCCCCC	52.65	21963094
64	Ubiquitination	RPPAGELGSIGDHER CCCCCCCCCCCCCCC	16.96	22817900
65	Phosphorylation	PPAGELGSIGDHERA CCCCCCCCCCCCCCC	35.70	25159151
66	Ubiquitination	PAGELGSIGDHERAI CCCCCCCCCCCCCCC	7.73	22817900
66	Acetylation	PAGELGSIGDHERAI CCCCCCCCCCCCCCC	7.73	12574125
67	Ubiquitination	AGELGSIGDHERAID CCCCCCCCCCCCCCC	31.74	22817900
67	Acetylation	AGELGSIGDHERAID CCCCCCCCCCCCCCC	31.74	12574125
76	Phosphorylation	HERAIDFSPYLEPLG CCCCCCCCCCCCCCC	14.64	22817900
77	Ubiquitination	ERAIDFSPYLEPLGA CCCCCCCCCCCCCCC	37.41	29967540
78	Phosphorylation	RAIDFSPYLEPLGAP CCCCCCCCCCCCCCC	23.62	19563810
104	Ubiquitination	FEAAPPAPAPAPASS CCCCCCCCCCCCCCC	44.54	33845483
106	Ubiquitination	AAPPAPAPAPASSGQ CCCCCCCCCCCCCCC	37.40	29967540
110	Ubiquitination	APAPAPASSGQHHDF CCCCCCCCCCCCCHH	33.66	33845483
117	Ubiquitination	SSGQHHDFLSDLFSD CCCCCCHHHHHHHCC	6.46	29967540
118	Ubiquitination	SGQHHDFLSDLFSDD CCCCCHHHHHHHCCC	4.92	33845483
126	Ubiquitination	SDLFSDDYGGKNCKK HHHHCCCCCCCCCCC	32.54	29967540
129	Ubiquitination	FSDDYGGKNCKKPAE HCCCCCCCCCCCCHH	55.60	29967540
129	Acetylation	FSDDYGGKNCKKPAE HCCCCCCCCCCCCHH	55.60	-
132	Acetylation	DYGGKNCKKPAEYGY CCCCCCCCCCHHHCC	71.79	-
133	Sumoylation	YGGKNCKKPAEYGYV CCCCCCCCCHHHCCE	52.22	28112733
133	Sumoylation	YGGKNCKKPAEYGYV CCCCCCCCCHHHCCE	52.22	-
133	Acetylation	YGGKNCKKPAEYGYV CCCCCCCCCHHHCCE	52.22	-
133	Ubiquitination	YGGKNCKKPAEYGYV CCCCCCCCCHHHCCE	52.22	33845483
134	Ubiquitination	GGKNCKKPAEYGYVS CCCCCCCCHHHCCEE	18.80	23000965
137	Phosphorylation	NCKKPAEYGYVSLGR CCCCCHHHCCEEHHH	18.83	19835603
139	Phosphorylation	KKPAEYGYVSLGRLG CCCHHHCCEEHHHHH	5.98	29978859
141	Phosphorylation	PAEYGYVSLGRLGAA CHHHCCEEHHHHHCC	19.34	25159151
149	Ubiquitination	LGRLGAAKGALHPGC HHHHHCCCCCCCCCC	44.15	29967540
162	Ubiquitination	GCFAPLHPPPPPPPP CCCCCCCCCCCCCCC	51.26	33845483
174	Sumoylation	PPPPAELKAEPGFEP CCCCHHHCCCCCCCH	42.06	12810706
174	Sumoylation	PPPPAELKAEPGFEP CCCCHHHCCCCCCCH	42.06	-
185	Ubiquitination	GFEPADCKRKEEAGA CCCHHHHCCHHHCCC	68.03	33845483
185	Sumoylation	GFEPADCKRKEEAGA CCCHHHHCCHHHCCC	68.03	28112733
187	Sumoylation	EPADCKRKEEAGAPG CHHHHCCHHHCCCCC	45.46	-
187	Sumoylation	EPADCKRKEEAGAPG CHHHHCCHHHCCCCC	45.46	28112733
205	Phosphorylation	GMAAGFPYALRAYLG HHHCCHHHHHHHHHC	18.92	21945579
210	Phosphorylation	FPYALRAYLGYQAVP HHHHHHHHHCCEECC	8.33	23663014
213	Phosphorylation	ALRAYLGYQAVPSGS HHHHHHCCEECCCCC	7.24	23663014
218	Phosphorylation	LGYQAVPSGSSGSLS HCCEECCCCCCCCCC	44.71	30278072
220	Phosphorylation	YQAVPSGSSGSLSTS CEECCCCCCCCCCCC	35.54	23927012
221	Phosphorylation	QAVPSGSSGSLSTSS EECCCCCCCCCCCCC	35.61	23927012
223	Phosphorylation	VPSGSSGSLSTSSSS CCCCCCCCCCCCCCC	22.54	30278072
225	Phosphorylation	SGSSGSLSTSSSSSP CCCCCCCCCCCCCCC	28.13	30278072
226	Phosphorylation	GSSGSLSTSSSSSPP CCCCCCCCCCCCCCC	37.61	30278072
227	O-linked_Glycosylation	SSGSLSTSSSSSPPG CCCCCCCCCCCCCCC	25.50	UniProtKB CARBOHYD
227	Phosphorylation	SSGSLSTSSSSSPPG CCCCCCCCCCCCCCC	25.50	30278072
228	O-linked_Glycosylation	SGSLSTSSSSSPPGT CCCCCCCCCCCCCCC	34.04	UniProtKB CARBOHYD
228	Phosphorylation	SGSLSTSSSSSPPGT CCCCCCCCCCCCCCC	34.04	23927012
229	Phosphorylation	GSLSTSSSSSPPGTP CCCCCCCCCCCCCCC	34.30	25159151
230	Phosphorylation	SLSTSSSSSPPGTPS CCCCCCCCCCCCCCC	49.14	23927012
231	Phosphorylation	LSTSSSSSPPGTPSP CCCCCCCCCCCCCCH	36.74	25159151
235	Phosphorylation	SSSSPPGTPSPADAK CCCCCCCCCCHHHCC	26.77	17540774
237	Ubiquitination	SSPPGTPSPADAKAP CCCCCCCCHHHCCCC	32.34	21963094
237	Phosphorylation	SSPPGTPSPADAKAP CCCCCCCCHHHCCCC	32.34	23927012
239	Ubiquitination	PPGTPSPADAKAPPT CCCCCCHHHCCCCCC	33.46	22817900
241	Ubiquitination	GTPSPADAKAPPTAC CCCCHHHCCCCCCCC	16.41	22817900
241	Acetylation	GTPSPADAKAPPTAC CCCCHHHCCCCCCCC	16.41	12574125
242	Ubiquitination	TPSPADAKAPPTACY CCCHHHCCCCCCCCC	63.07	22817900
242	Acetylation	TPSPADAKAPPTACY CCCHHHCCCCCCCCC	63.07	12574125
249	Phosphorylation	KAPPTACYAGAAPAP CCCCCCCCCCCCCCC	12.95	21945579
252	Ubiquitination	PTACYAGAAPAPSQV CCCCCCCCCCCCHHH	11.33	29967540
257	Phosphorylation	AGAAPAPSQVKSKAK CCCCCCCHHHHHHCC	50.11	25159151
260	Ubiquitination	APAPSQVKSKAKKTV CCCCHHHHHHCCHHH	38.30	21963094
260	Sumoylation	APAPSQVKSKAKKTV CCCCHHHHHHCCHHH	38.30	-
260	Sumoylation	APAPSQVKSKAKKTV CCCCHHHHHHCCHHH	38.30	28112733
262	Sumoylation	APSQVKSKAKKTVDK CCHHHHHHCCHHHHH	59.51	28112733
262	Ubiquitination	APSQVKSKAKKTVDK CCHHHHHHCCHHHHH	59.51	22817900
264	Acetylation	SQVKSKAKKTVDKHS HHHHHHCCHHHHHCC	53.35	60099
264	Ubiquitination	SQVKSKAKKTVDKHS HHHHHHCCHHHHHCC	53.35	22817900
265	Acetylation	QVKSKAKKTVDKHSD HHHHHCCHHHHHCCH	59.65	20167786
265	Ubiquitination	QVKSKAKKTVDKHSD HHHHHCCHHHHHCCH	59.65	22817900
266	Phosphorylation	VKSKAKKTVDKHSDE HHHHCCHHHHHCCHH	32.98	15738002
269	Acetylation	KAKKTVDKHSDEYKI HCCHHHHHCCHHHHH	40.44	20167786
275	Sumoylation	DKHSDEYKIRRERNN HHCCHHHHHHHHHHC	27.91	-
275	Sumoylation	DKHSDEYKIRRERNN HHCCHHHHHHHHHHC	27.91	-
275	Ubiquitination	DKHSDEYKIRRERNN HHCCHHHHHHHHHHC	27.91	29967540
279	Ubiquitination	DEYKIRRERNNIAVR HHHHHHHHHHCCCHH	50.33	33845483
288	Phosphorylation	NNIAVRKSRDKAKMR HCCCHHHHHHHHHHH	34.84	22817900
292	Ubiquitination	VRKSRDKAKMRNLET HHHHHHHHHHHCHHH	18.37	29967540
293	Ubiquitination	RKSRDKAKMRNLETQ HHHHHHHHHHCHHHH	44.10	33845483
302	Ubiquitination	RNLETQHKVLELTAE HCHHHHHHHHHHHHH	38.40	33845483
309	Ubiquitination	KVLELTAENERLQKK HHHHHHHHHHHHHHH	55.15	23000965
315	Ubiquitination	AENERLQKKVEQLSR HHHHHHHHHHHHHHH	64.48	29967540
316	Ubiquitination	ENERLQKKVEQLSRE HHHHHHHHHHHHHHH	37.73	33845483
325	Phosphorylation	EQLSRELSTLRNLFK HHHHHHHHHHHHHHH	22.20	1314426
332	Sumoylation	STLRNLFKQLPEPLL HHHHHHHHHCCHHHH	54.84	-
332	Ubiquitination	STLRNLFKQLPEPLL HHHHHHHHHCCHHHH	54.84	23000965
332	Sumoylation	STLRNLFKQLPEPLL HHHHHHHHHCCHHHH	54.84	28112733
341	Phosphorylation	LPEPLLASSGHC--- CCHHHHHCCCCC---	36.50	25159151
342	Phosphorylation	PEPLLASSGHC---- CHHHHHCCCCC----	27.27	25159151

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
76	S	Phosphorylation	Kinase	CDK2	P97377	PSP
76	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
78	Y	Phosphorylation	Kinase	ABL2	P42684	GPS
78	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
223	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
226	T	Phosphorylation	Kinase	GSK3-BETA	P49841	Uniprot
231	S	Phosphorylation	Kinase	GSK3-BETA	P49841	Uniprot
235	T	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
235	T	Phosphorylation	Kinase	MAPK	-	Uniprot
235	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
235	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
235	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
235	T	Phosphorylation	Kinase	RPS6KA1	Q15418	Uniprot
235	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
235	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
266	T	Phosphorylation	Kinase	KS6A1	Q15418	PhosphoELM
266	T	Phosphorylation	Kinase	PRKCA	P17252	Uniprot
288	S	Phosphorylation	Kinase	PRKCA	P17252	Uniprot
288	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
288	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
288	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
325	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
325	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
325	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
325	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	RNF41	Q9H4P4	PMID:22707723
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL9	Q9P2J3	PMID:25303533

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
3	R	Methylation	20111005
Methylation at Arg-3 by CARM1 and at Lys-43 by EHMT2 inhibit transactivation activity.
43	K	Acetylation	-
Acetylation at Lys-43 is an important and dynamic regulatory event that contributes to its ability to transactivate target genes, including those associated with adipogenesis and adipocyte function.
43	K	Methylation	18647749
Methylation at Arg-3 by CARM1 and at Lys-43 by EHMT2 inhibit transactivation activity.
174	K	Sumoylation	12810706
In adipocytes, sumoylation at Lys-174 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation.
174	K	Sumoylation	12810706
Sumoylation at Lys-174 is required for inhibition of T-cells proliferation.
174	K	ubiquitylation	12810706
In adipocytes, sumoylation at Lys-174 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation.
226	T	Phosphorylation	11684016
Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.
226	T	Phosphorylation	-
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
226	T	Glycosylation	-
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
227	S	Glycosylation	-
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
227	S	Phosphorylation	-
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
228	S	Glycosylation	-
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
228	S	Phosphorylation	-
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
231	S	Phosphorylation	11684016
Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.
231	S	Phosphorylation	-
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
231	S	Glycosylation	-
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
235	T	Glycosylation	11684016
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
235	T	Methylation	11684016
Methylation is probably inhibited by phosphorylation at Thr-235.
235	T	Phosphorylation	11684016
MAPK and CDK2 act sequentially to maintain Thr-235 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation.
235	T	Phosphorylation	11684016
Methylation is probably inhibited by phosphorylation at Thr-235.
235	T	Phosphorylation	11684016
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
235	T	Phosphorylation	11684016
Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis.
235	T	Phosphorylation	11684016
Phosphorylated at Thr-235 by RPS6KA1.
266	T	Phosphorylation	11684016
Phosphorylation at Thr-266 enhances transactivation activity.
325	S	Phosphorylation	11684016
Phosphorylation at Ser-325 in response to calcium increases transactivation activity.

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 CEBPB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MED23_HUMAN	MED23	physical	14759369
CREB1_HUMAN	CREB1	physical	12773552
TF65_HUMAN	RELA	physical	12707271
SP1_HUMAN	SP1	physical	12665574
HMGA1_HUMAN	HMGA1	physical	12665574
SMCA2_HUMAN	SMARCA2	physical	10619021
SMRC1_HUMAN	SMARCC1	physical	10619021
EP300_HUMAN	EP300	genetic	9343424
EP300_HUMAN	EP300	physical	9343424
DDIT3_HUMAN	DDIT3	physical	8662954
SPI1_HUMAN	SPI1	physical	7594592
GCR_HUMAN	NR3C1	physical	9817600
ANDR_HUMAN	AR	physical	9817600
ESR1_HUMAN	ESR1	physical	9817600
RARB_HUMAN	RARB	physical	9817600
NOLC1_HUMAN	NOLC1	genetic	9553145
CEBPG_HUMAN	CEBPG	physical	12177065
RB_HUMAN	RB1	physical	11596110
NFKB1_HUMAN	NFKB1	physical	1518839
CEBPD_HUMAN	CEBPD	physical	1840554
CEBPA_HUMAN	CEBPA	physical	1840554
RUNX1_HUMAN	RUNX1	physical	8622667
HDAC1_HUMAN	HDAC1	physical	19029947
ESR1_HUMAN	ESR1	physical	19652226
SP1_HUMAN	SP1	physical	16651265
SP3_HUMAN	SP3	physical	16651265
ESR1_HUMAN	ESR1	physical	16651265
EHMT2_HUMAN	EHMT2	physical	18647749
CBP_HUMAN	CREBBP	physical	12857754
NCOR2_HUMAN	NCOR2	physical	15870285
CEBPB_HUMAN	CEBPB	physical	12618752
STAT3_HUMAN	STAT3	physical	18203738
NRF1_HUMAN	NRF1	physical	15308669
KAT2A_HUMAN	KAT2A	physical	17301242
KAT2B_HUMAN	KAT2B	physical	17301242
HDAC9_HUMAN	HDAC9	physical	17301242
CARM1_HUMAN	CARM1	physical	20111005
GSK3B_HUMAN	GSK3B	physical	20110283
ATF3_HUMAN	ATF3	physical	20110283
CEBPB_HUMAN	CEBPB	physical	20110283
TAF9_HUMAN	TAF9	physical	10821850
SMCA2_HUMAN	SMARCA2	physical	22242598
SMCA4_HUMAN	SMARCA4	physical	22242598
SMRC1_HUMAN	SMARCC1	physical	22242598
SNF5_HUMAN	SMARCB1	physical	22242598
HDAC1_HUMAN	HDAC1	physical	21638299
SMCA2_HUMAN	SMARCA2	physical	21638299
CASP1_HUMAN	CASP1	physical	11684016
CASP8_HUMAN	CASP8	physical	11684016
DAXX_HUMAN	DAXX	physical	19690170
TF65_HUMAN	RELA	physical	16785565
RB_HUMAN	RB1	physical	8552662
EP300_HUMAN	EP300	physical	14630807
EGR1_HUMAN	EGR1	physical	22260630
KLF5_HUMAN	KLF5	physical	16054042
EP300_HUMAN	EP300	physical	12471036
ZC12A_HUMAN	ZC3H12A	physical	28328949

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
There are no disease associations of PTM sites.

Regulatory Network of CEBPB_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-231 AND THR-235, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"C/EBPbeta phosphorylation by RSK creates a functional XEXD caspaseinhibitory box critical for cell survival."; Buck M., Poli V., Hunter T., Chojkier M.; Mol. Cell 8:807-816(2001). Cited for: PHOSPHORYLATION AT THR-235.	11684016 [Abstract]
Sumoylation
Reference	PubMed
"Modification of CCAAT/enhancer-binding protein-beta by the smallubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3."; Eaton E.M., Sealy L.; J. Biol. Chem. 278:33416-33421(2003). Cited for: SUMOYLATION AT LYS-174.	12810706 [Abstract]

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