dbPTM

EBP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EBP2_HUMAN
UniProt AC	Q99848
Protein Name	Probable rRNA-processing protein EBP2
Gene Name	EBNA1BP2
Organism	Homo sapiens (Human).
Sequence Length	306
Subcellular Localization	Nucleus, nucleolus . Associated with the nucleolus in an RNA-dependent manner.
Protein Description	Required for the processing of the 27S pre-rRNA..
Protein Sequence	MDTPPLSDSESESDESLVTDRELQDAFSRGLLKPGLNVVLEGPKKAVNDVNGLKQCLAEFKRDLEWVERLDVTLGPVPEIGGSEAPAPQNKDQKAVDPEDDFQREMSFYRQAQAAVLAVLPRLHQLKVPTKRPTDYFAEMAKSDLQMQKIRQKLQTKQAAMERSEKAKQLRALRKYGKKVQTEVLQKRQQEKAHMMNAIKKYQKGFSDKLDFLEGDQKPLAQRKKAGAKGQQMRKGPSAKRRYKNQKFGFGGKKKGSKWNTRESYDDVSSFRAKTAHGRGLKRPGKKGSNKRPGKRTREKMKNRTH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDTPPLSD -------CCCCCCCC	13.45	22814378
3	Phosphorylation	-----MDTPPLSDSE -----CCCCCCCCCC	26.05	17081983
7	Phosphorylation	-MDTPPLSDSESESD -CCCCCCCCCCCCCC	44.88	17081983
9	Phosphorylation	DTPPLSDSESESDES CCCCCCCCCCCCCHH	39.38	17081983
11	Phosphorylation	PPLSDSESESDESLV CCCCCCCCCCCHHCC	46.48	17081983
13	Phosphorylation	LSDSESESDESLVTD CCCCCCCCCHHCCCH	56.83	20068231
16	Phosphorylation	SESESDESLVTDREL CCCCCCHHCCCHHHH	32.88	17081983
19	Phosphorylation	ESDESLVTDRELQDA CCCHHCCCHHHHHHH	34.33	20068231
28	Phosphorylation	RELQDAFSRGLLKPG HHHHHHHHCCCCCCC	27.45	30177828
33	Ubiquitination	AFSRGLLKPGLNVVL HHHCCCCCCCCEEEE	41.92	21890473
33	Acetylation	AFSRGLLKPGLNVVL HHHCCCCCCCCEEEE	41.92	25953088
44	Acetylation	NVVLEGPKKAVNDVN EEEEECCHHHHHCCC	65.31	26051181
45	2-Hydroxyisobutyrylation	VVLEGPKKAVNDVNG EEEECCHHHHHCCCH	61.78	-
45	Acetylation	VVLEGPKKAVNDVNG EEEECCHHHHHCCCH	61.78	26051181
54	Acetylation	VNDVNGLKQCLAEFK HHCCCHHHHHHHHHH	40.12	26051181
54	2-Hydroxyisobutyrylation	VNDVNGLKQCLAEFK HHCCCHHHHHHHHHH	40.12	-
61	Acetylation	KQCLAEFKRDLEWVE HHHHHHHHHHHHHHH	36.19	25825284
61	2-Hydroxyisobutyrylation	KQCLAEFKRDLEWVE HHHHHHHHHHHHHHH	36.19	-
64	Phosphorylation	LAEFKRDLEWVERLD HHHHHHHHHHHHHCC	6.92	17081983
66	Phosphorylation	EFKRDLEWVERLDVT HHHHHHHHHHHCCCE	12.45	17081983
68	Phosphorylation	KRDLEWVERLDVTLG HHHHHHHHHCCCEEC	48.91	17081983
71	Phosphorylation	LEWVERLDVTLGPVP HHHHHHCCCEECCCC	37.26	17081983
73	Phosphorylation	WVERLDVTLGPVPEI HHHHCCCEECCCCCC	26.18	-
74	Phosphorylation	VERLDVTLGPVPEIG HHHCCCEECCCCCCC	7.98	17081983
83	Phosphorylation	PVPEIGGSEAPAPQN CCCCCCCCCCCCCCC	25.93	20068231
88	Ubiquitination	GGSEAPAPQNKDQKA CCCCCCCCCCCCCCC	36.90	-
91	Acetylation	EAPAPQNKDQKAVDP CCCCCCCCCCCCCCC	57.18	26051181
94	Ubiquitination	APQNKDQKAVDPEDD CCCCCCCCCCCCCHH	61.58	21890473
94	Sumoylation	APQNKDQKAVDPEDD CCCCCCCCCCCCCHH	61.58	28112733
94	Acetylation	APQNKDQKAVDPEDD CCCCCCCCCCCCCHH	61.58	26051181
109	Ubiquitination	FQREMSFYRQAQAAV HHHHHHHHHHHHHHH	8.43	-
116	Acetylation	YRQAQAAVLAVLPRL HHHHHHHHHHHHHHH	3.85	-
127	Acetylation	LPRLHQLKVPTKRPT HHHHHHCCCCCCCCC	39.33	25953088
131	Acetylation	HQLKVPTKRPTDYFA HHCCCCCCCCCHHHH	50.76	25953088
134	Phosphorylation	KVPTKRPTDYFAEMA CCCCCCCCHHHHHHH	47.57	20860994
136	Phosphorylation	PTKRPTDYFAEMAKS CCCCCCHHHHHHHHH	13.73	-
143	Phosphorylation	YFAEMAKSDLQMQKI HHHHHHHHHHHHHHH	33.73	21712546
149	Acetylation	KSDLQMQKIRQKLQT HHHHHHHHHHHHHHH	34.22	26051181
149	Ubiquitination	KSDLQMQKIRQKLQT HHHHHHHHHHHHHHH	34.22	-
157	Ubiquitination	IRQKLQTKQAAMERS HHHHHHHHHHHHHHH	25.61	-
157	2-Hydroxyisobutyrylation	IRQKLQTKQAAMERS HHHHHHHHHHHHHHH	25.61	-
166	Acetylation	AAMERSEKAKQLRAL HHHHHHHHHHHHHHH	63.23	18603147
168	Acetylation	MERSEKAKQLRALRK HHHHHHHHHHHHHHH	62.02	18603157
175	Acetylation	KQLRALRKYGKKVQT HHHHHHHHHHHHHHH	60.24	7825407
179	Sumoylation	ALRKYGKKVQTEVLQ HHHHHHHHHHHHHHH	34.90	28112733
179	Acetylation	ALRKYGKKVQTEVLQ HHHHHHHHHHHHHHH	34.90	7369625
182	Phosphorylation	KYGKKVQTEVLQKRQ HHHHHHHHHHHHHHH	30.92	28555341
186	Ubiquitination	KVQTEVLQKRQQEKA HHHHHHHHHHHHHHH	44.02	-
187	Ubiquitination	VQTEVLQKRQQEKAH HHHHHHHHHHHHHHH	48.27	-
187	Acetylation	VQTEVLQKRQQEKAH HHHHHHHHHHHHHHH	48.27	26051181
187	2-Hydroxyisobutyrylation	VQTEVLQKRQQEKAH HHHHHHHHHHHHHHH	48.27	-
191	Phosphorylation	VLQKRQQEKAHMMNA HHHHHHHHHHHHHHH	43.82	-
198	Phosphorylation	EKAHMMNAIKKYQKG HHHHHHHHHHHHHCC	9.33	-
200	2-Hydroxyisobutyrylation	AHMMNAIKKYQKGFS HHHHHHHHHHHCCCC	42.91	-
204	Ubiquitination	NAIKKYQKGFSDKLD HHHHHHHCCCCCHHH	59.85	-
207	Phosphorylation	KKYQKGFSDKLDFLE HHHHCCCCCHHHHHC	42.37	25159151
209	Ubiquitination	YQKGFSDKLDFLEGD HHCCCCCHHHHHCCC	49.08	21890473
209	2-Hydroxyisobutyrylation	YQKGFSDKLDFLEGD HHCCCCCHHHHHCCC	49.08	-
209	Acetylation	YQKGFSDKLDFLEGD HHCCCCCHHHHHCCC	49.08	23749302
212	Ubiquitination	GFSDKLDFLEGDQKP CCCCHHHHHCCCCCH	10.96	-
218	Sumoylation	DFLEGDQKPLAQRKK HHHCCCCCHHHHHHH	46.90	-
218	Acetylation	DFLEGDQKPLAQRKK HHHCCCCCHHHHHHH	46.90	26051181
218	Sumoylation	DFLEGDQKPLAQRKK HHHCCCCCHHHHHHH	46.90	28112733
218	Ubiquitination	DFLEGDQKPLAQRKK HHHCCCCCHHHHHHH	46.90	-
224	Methylation	QKPLAQRKKAGAKGQ CCHHHHHHHHCHHHH	34.59	-
229	Acetylation	QRKKAGAKGQQMRKG HHHHHCHHHHHHCCC	57.23	26051181
234	Ubiquitination	GAKGQQMRKGPSAKR CHHHHHHCCCCCHHH	36.12	-
235	Acetylation	AKGQQMRKGPSAKRR HHHHHHCCCCCHHHH	70.59	7296959
237	Phosphorylation	GQQMRKGPSAKRRYK HHHHCCCCCHHHHHC	33.86	-
242	Ubiquitination	KGPSAKRRYKNQKFG CCCCHHHHHCCCCCC	46.18	-
247	Acetylation	KRRYKNQKFGFGGKK HHHHCCCCCCCCCCC	57.77	26051181
247	Ubiquitination	KRRYKNQKFGFGGKK HHHHCCCCCCCCCCC	57.77	-
253	Acetylation	QKFGFGGKKKGSKWN CCCCCCCCCCCCCCC	52.25	25953088
256	Ubiquitination	GFGGKKKGSKWNTRE CCCCCCCCCCCCCCC	43.25	-
258	Acetylation	GGKKKGSKWNTRESY CCCCCCCCCCCCCCC	53.80	25953088
261	Phosphorylation	KKGSKWNTRESYDDV CCCCCCCCCCCCCCH	34.40	22199227
262	Phosphorylation	KGSKWNTRESYDDVS CCCCCCCCCCCCCHH	27.87	-
264	Acetylation	SKWNTRESYDDVSSF CCCCCCCCCCCHHHH	30.48	-
264	Ubiquitination	SKWNTRESYDDVSSF CCCCCCCCCCCHHHH	30.48	-
264	Phosphorylation	SKWNTRESYDDVSSF CCCCCCCCCCCHHHH	30.48	25159151
265	Phosphorylation	KWNTRESYDDVSSFR CCCCCCCCCCHHHHH	16.06	19691289
269	Phosphorylation	RESYDDVSSFRAKTA CCCCCCHHHHHHHCC	30.65	25627689
270	Phosphorylation	ESYDDVSSFRAKTAH CCCCCHHHHHHHCCC	20.71	25159151
273	Sumoylation	DDVSSFRAKTAHGRG CCHHHHHHHCCCCCC	16.13	-
273	Ubiquitination	DDVSSFRAKTAHGRG CCHHHHHHHCCCCCC	16.13	-
279	Methylation	RAKTAHGRGLKRPGK HHHCCCCCCCCCCCC	37.09	-
302	Ubiquitination	KRTREKMKNRTH--- HHHHHHHHHCCC---	55.11	-
313	Ubiquitination	H-------------- C--------------		-
319	Phosphorylation	-------------------- --------------------		24719451
320	Phosphorylation	--------------------- ---------------------		27642862
325	Phosphorylation	-------------------------- --------------------------		18669648

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
182	T	Phosphorylation	Kinase	CHEK1	O14757	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:21220517

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EBP2_HUMAN !!

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 EBP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FGF3_HUMAN	FGF3	physical	11438656
EBNA1_EBVB9	BKRF1	physical	22345443
FBXW7_HUMAN	FBXW7	physical	21220517
GNL3_HUMAN	GNL3	physical	22939629
NOP58_HUMAN	NOP58	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
NOP56_HUMAN	NOP56	physical	22939629
FBRL_HUMAN	FBL	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
IF6_HUMAN	EIF6	physical	22939629
NOP2_HUMAN	NOP2	physical	22939629
RRP7A_HUMAN	RRP7A	physical	22939629
SPB1_HUMAN	FTSJ3	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
SAP18_HUMAN	SAP18	physical	22939629
NXF1_HUMAN	NXF1	physical	22939629
EI2BD_HUMAN	EIF2B4	physical	22939629
RED1_HUMAN	ADARB1	physical	24778252
ZN622_HUMAN	ZNF622	physical	24778252
FAM9B_HUMAN	FAM9B	physical	25416956
RL34_HUMAN	RPL34	physical	26186194
RL3_HUMAN	RPL3	physical	26186194
HSP7C_HUMAN	HSPA8	physical	26186194
RL6_HUMAN	RPL6	physical	26186194
H11_HUMAN	HIST1H1A	physical	26186194
H14_HUMAN	HIST1H1E	physical	26186194
NPM_HUMAN	NPM1	physical	26186194
RL8_HUMAN	RPL8	physical	26186194
DDX21_HUMAN	DDX21	physical	26186194
RL27_HUMAN	RPL27	physical	26186194
RS8_HUMAN	RPS8	physical	26186194
BRX1_HUMAN	BRIX1	physical	26186194
TPM2_HUMAN	TPM2	physical	26186194
RL13_HUMAN	RPL13	physical	26186194
RL14_HUMAN	RPL14	physical	26186194
RL27A_HUMAN	RPL27A	physical	26186194
AATF_HUMAN	AATF	physical	26344197
BRX1_HUMAN	BRIX1	physical	26344197
DDX24_HUMAN	DDX24	physical	26344197
DDX56_HUMAN	DDX56	physical	26344197
IF6_HUMAN	EIF6	physical	26344197
MPP10_HUMAN	MPHOSPH10	physical	26344197
MRT4_HUMAN	MRTO4	physical	26344197
MK67I_HUMAN	NIFK	physical	26344197
NOC2L_HUMAN	NOC2L	physical	26344197
NOC3L_HUMAN	NOC3L	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
NSA2_HUMAN	NSA2	physical	26344197
PESC_HUMAN	PES1	physical	26344197
RPAC1_HUMAN	POLR1C	physical	26344197
RBM34_HUMAN	RBM34	physical	26344197
RPF2_HUMAN	RPF2	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
SURF6_HUMAN	SURF6	physical	26344197
H11_HUMAN	HIST1H1A	physical	28514442
TPM2_HUMAN	TPM2	physical	28514442
RL18_HUMAN	RPL18	physical	28514442
RL8_HUMAN	RPL8	physical	28514442
RL30_HUMAN	RPL30	physical	28514442
RS8_HUMAN	RPS8	physical	28514442
RL3_HUMAN	RPL3	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
RL7A_HUMAN	RPL7A	physical	28514442
H14_HUMAN	HIST1H1E	physical	28514442
NPM_HUMAN	NPM1	physical	28514442
NUCL_HUMAN	NCL	physical	28514442
RL18A_HUMAN	RPL18A	physical	28514442
RS9_HUMAN	RPS9	physical	28514442
RL27A_HUMAN	RPL27A	physical	28514442

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 EBP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-270, AND MASSSPECTROMETRY.	18669648 [Abstract]