EBP2_HUMAN - dbPTM
EBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
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 Orthologous
Protein Cluster
1Acetylation-------MDTPPLSD
-------CCCCCCCC
13.4522814378
3Phosphorylation-----MDTPPLSDSE
-----CCCCCCCCCC
26.0517081983
7Phosphorylation-MDTPPLSDSESESD
-CCCCCCCCCCCCCC
44.8817081983
9PhosphorylationDTPPLSDSESESDES
CCCCCCCCCCCCCHH
39.3817081983
11PhosphorylationPPLSDSESESDESLV
CCCCCCCCCCCHHCC
46.4817081983
13PhosphorylationLSDSESESDESLVTD
CCCCCCCCCHHCCCH
56.8320068231
16PhosphorylationSESESDESLVTDREL
CCCCCCHHCCCHHHH
32.8817081983
19PhosphorylationESDESLVTDRELQDA
CCCHHCCCHHHHHHH
34.3320068231
28PhosphorylationRELQDAFSRGLLKPG
HHHHHHHHCCCCCCC
27.4530177828
33UbiquitinationAFSRGLLKPGLNVVL
HHHCCCCCCCCEEEE
41.9221890473
33AcetylationAFSRGLLKPGLNVVL
HHHCCCCCCCCEEEE
41.9225953088
44AcetylationNVVLEGPKKAVNDVN
EEEEECCHHHHHCCC
65.3126051181
452-HydroxyisobutyrylationVVLEGPKKAVNDVNG
EEEECCHHHHHCCCH
61.78-
45AcetylationVVLEGPKKAVNDVNG
EEEECCHHHHHCCCH
61.7826051181
54AcetylationVNDVNGLKQCLAEFK
HHCCCHHHHHHHHHH
40.1226051181
542-HydroxyisobutyrylationVNDVNGLKQCLAEFK
HHCCCHHHHHHHHHH
40.12-
61AcetylationKQCLAEFKRDLEWVE
HHHHHHHHHHHHHHH
36.1925825284
612-HydroxyisobutyrylationKQCLAEFKRDLEWVE
HHHHHHHHHHHHHHH
36.19-
64PhosphorylationLAEFKRDLEWVERLD
HHHHHHHHHHHHHCC
6.9217081983
66PhosphorylationEFKRDLEWVERLDVT
HHHHHHHHHHHCCCE
12.4517081983
68PhosphorylationKRDLEWVERLDVTLG
HHHHHHHHHCCCEEC
48.9117081983
71PhosphorylationLEWVERLDVTLGPVP
HHHHHHCCCEECCCC
37.2617081983
73PhosphorylationWVERLDVTLGPVPEI
HHHHCCCEECCCCCC
26.18-
74PhosphorylationVERLDVTLGPVPEIG
HHHCCCEECCCCCCC
7.9817081983
83PhosphorylationPVPEIGGSEAPAPQN
CCCCCCCCCCCCCCC
25.9320068231
88UbiquitinationGGSEAPAPQNKDQKA
CCCCCCCCCCCCCCC
36.90-
91AcetylationEAPAPQNKDQKAVDP
CCCCCCCCCCCCCCC
57.1826051181
94UbiquitinationAPQNKDQKAVDPEDD
CCCCCCCCCCCCCHH
61.5821890473
94SumoylationAPQNKDQKAVDPEDD
CCCCCCCCCCCCCHH
61.5828112733
94AcetylationAPQNKDQKAVDPEDD
CCCCCCCCCCCCCHH
61.5826051181
109UbiquitinationFQREMSFYRQAQAAV
HHHHHHHHHHHHHHH
8.43-
116AcetylationYRQAQAAVLAVLPRL
HHHHHHHHHHHHHHH
3.85-
127AcetylationLPRLHQLKVPTKRPT
HHHHHHCCCCCCCCC
39.3325953088
131AcetylationHQLKVPTKRPTDYFA
HHCCCCCCCCCHHHH
50.7625953088
134PhosphorylationKVPTKRPTDYFAEMA
CCCCCCCCHHHHHHH
47.5720860994
136PhosphorylationPTKRPTDYFAEMAKS
CCCCCCHHHHHHHHH
13.73-
143PhosphorylationYFAEMAKSDLQMQKI
HHHHHHHHHHHHHHH
33.7321712546
149AcetylationKSDLQMQKIRQKLQT
HHHHHHHHHHHHHHH
34.2226051181
149UbiquitinationKSDLQMQKIRQKLQT
HHHHHHHHHHHHHHH
34.22-
157UbiquitinationIRQKLQTKQAAMERS
HHHHHHHHHHHHHHH
25.61-
1572-HydroxyisobutyrylationIRQKLQTKQAAMERS
HHHHHHHHHHHHHHH
25.61-
166AcetylationAAMERSEKAKQLRAL
HHHHHHHHHHHHHHH
63.2318603147
168AcetylationMERSEKAKQLRALRK
HHHHHHHHHHHHHHH
62.0218603157
175AcetylationKQLRALRKYGKKVQT
HHHHHHHHHHHHHHH
60.247825407
179SumoylationALRKYGKKVQTEVLQ
HHHHHHHHHHHHHHH
34.9028112733
179AcetylationALRKYGKKVQTEVLQ
HHHHHHHHHHHHHHH
34.907369625
182PhosphorylationKYGKKVQTEVLQKRQ
HHHHHHHHHHHHHHH
30.9228555341
186UbiquitinationKVQTEVLQKRQQEKA
HHHHHHHHHHHHHHH
44.02-
187UbiquitinationVQTEVLQKRQQEKAH
HHHHHHHHHHHHHHH
48.27-
187AcetylationVQTEVLQKRQQEKAH
HHHHHHHHHHHHHHH
48.2726051181
1872-HydroxyisobutyrylationVQTEVLQKRQQEKAH
HHHHHHHHHHHHHHH
48.27-
191PhosphorylationVLQKRQQEKAHMMNA
HHHHHHHHHHHHHHH
43.82-
198PhosphorylationEKAHMMNAIKKYQKG
HHHHHHHHHHHHHCC
9.33-
2002-HydroxyisobutyrylationAHMMNAIKKYQKGFS
HHHHHHHHHHHCCCC
42.91-
204UbiquitinationNAIKKYQKGFSDKLD
HHHHHHHCCCCCHHH
59.85-
207PhosphorylationKKYQKGFSDKLDFLE
HHHHCCCCCHHHHHC
42.3725159151
209UbiquitinationYQKGFSDKLDFLEGD
HHCCCCCHHHHHCCC
49.0821890473
2092-HydroxyisobutyrylationYQKGFSDKLDFLEGD
HHCCCCCHHHHHCCC
49.08-
209AcetylationYQKGFSDKLDFLEGD
HHCCCCCHHHHHCCC
49.0823749302
212UbiquitinationGFSDKLDFLEGDQKP
CCCCHHHHHCCCCCH
10.96-
218SumoylationDFLEGDQKPLAQRKK
HHHCCCCCHHHHHHH
46.90-
218AcetylationDFLEGDQKPLAQRKK
HHHCCCCCHHHHHHH
46.9026051181
218SumoylationDFLEGDQKPLAQRKK
HHHCCCCCHHHHHHH
46.9028112733
218UbiquitinationDFLEGDQKPLAQRKK
HHHCCCCCHHHHHHH
46.90-
224MethylationQKPLAQRKKAGAKGQ
CCHHHHHHHHCHHHH
34.59-
229AcetylationQRKKAGAKGQQMRKG
HHHHHCHHHHHHCCC
57.2326051181
234UbiquitinationGAKGQQMRKGPSAKR
CHHHHHHCCCCCHHH
36.12-
235AcetylationAKGQQMRKGPSAKRR
HHHHHHCCCCCHHHH
70.597296959
237PhosphorylationGQQMRKGPSAKRRYK
HHHHCCCCCHHHHHC
33.86-
242UbiquitinationKGPSAKRRYKNQKFG
CCCCHHHHHCCCCCC
46.18-
247AcetylationKRRYKNQKFGFGGKK
HHHHCCCCCCCCCCC
57.7726051181
247UbiquitinationKRRYKNQKFGFGGKK
HHHHCCCCCCCCCCC
57.77-
253AcetylationQKFGFGGKKKGSKWN
CCCCCCCCCCCCCCC
52.2525953088
256UbiquitinationGFGGKKKGSKWNTRE
CCCCCCCCCCCCCCC
43.25-
258AcetylationGGKKKGSKWNTRESY
CCCCCCCCCCCCCCC
53.8025953088
261PhosphorylationKKGSKWNTRESYDDV
CCCCCCCCCCCCCCH
34.4022199227
262PhosphorylationKGSKWNTRESYDDVS
CCCCCCCCCCCCCHH
27.87-
264AcetylationSKWNTRESYDDVSSF
CCCCCCCCCCCHHHH
30.48-
264UbiquitinationSKWNTRESYDDVSSF
CCCCCCCCCCCHHHH
30.48-
264PhosphorylationSKWNTRESYDDVSSF
CCCCCCCCCCCHHHH
30.4825159151
265PhosphorylationKWNTRESYDDVSSFR
CCCCCCCCCCHHHHH
16.0619691289
269PhosphorylationRESYDDVSSFRAKTA
CCCCCCHHHHHHHCC
30.6525627689
270PhosphorylationESYDDVSSFRAKTAH
CCCCCHHHHHHHCCC
20.7125159151
273SumoylationDDVSSFRAKTAHGRG
CCHHHHHHHCCCCCC
16.13-
273UbiquitinationDDVSSFRAKTAHGRG
CCHHHHHHHCCCCCC
16.13-
279MethylationRAKTAHGRGLKRPGK
HHHCCCCCCCCCCCC
37.09-
302UbiquitinationKRTREKMKNRTH---
HHHHHHHHHCCC---
55.11-
313UbiquitinationH--------------
C--------------
-
319Phosphorylation--------------------
--------------------
24719451
320Phosphorylation---------------------
---------------------
27642862
325Phosphorylation--------------------------
--------------------------
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
182TPhosphorylationKinaseCHEK1O14757
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
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 Domain-Domain Interactions
FGF3_HUMANFGF3physical
11438656
EBNA1_EBVB9BKRF1physical
22345443
FBXW7_HUMANFBXW7physical
21220517
GNL3_HUMANGNL3physical
22939629
NOP58_HUMANNOP58physical
22939629
RS6_HUMANRPS6physical
22939629
NOP56_HUMANNOP56physical
22939629
FBRL_HUMANFBLphysical
22939629
RL7_HUMANRPL7physical
22939629
RL31_HUMANRPL31physical
22939629
RL5_HUMANRPL5physical
22939629
IF6_HUMANEIF6physical
22939629
NOP2_HUMANNOP2physical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
SPB1_HUMANFTSJ3physical
22939629
RRS1_HUMANRRS1physical
22939629
SAP18_HUMANSAP18physical
22939629
NXF1_HUMANNXF1physical
22939629
EI2BD_HUMANEIF2B4physical
22939629
RED1_HUMANADARB1physical
24778252
ZN622_HUMANZNF622physical
24778252
FAM9B_HUMANFAM9Bphysical
25416956
RL34_HUMANRPL34physical
26186194
RL3_HUMANRPL3physical
26186194
HSP7C_HUMANHSPA8physical
26186194
RL6_HUMANRPL6physical
26186194
H11_HUMANHIST1H1Aphysical
26186194
H14_HUMANHIST1H1Ephysical
26186194
NPM_HUMANNPM1physical
26186194
RL8_HUMANRPL8physical
26186194
DDX21_HUMANDDX21physical
26186194
RL27_HUMANRPL27physical
26186194
RS8_HUMANRPS8physical
26186194
BRX1_HUMANBRIX1physical
26186194
TPM2_HUMANTPM2physical
26186194
RL13_HUMANRPL13physical
26186194
RL14_HUMANRPL14physical
26186194
RL27A_HUMANRPL27Aphysical
26186194
AATF_HUMANAATFphysical
26344197
BRX1_HUMANBRIX1physical
26344197
DDX24_HUMANDDX24physical
26344197
DDX56_HUMANDDX56physical
26344197
IF6_HUMANEIF6physical
26344197
MPP10_HUMANMPHOSPH10physical
26344197
MRT4_HUMANMRTO4physical
26344197
MK67I_HUMANNIFKphysical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
NOC3L_HUMANNOC3Lphysical
26344197
NOL6_HUMANNOL6physical
26344197
NSA2_HUMANNSA2physical
26344197
PESC_HUMANPES1physical
26344197
RPAC1_HUMANPOLR1Cphysical
26344197
RBM34_HUMANRBM34physical
26344197
RPF2_HUMANRPF2physical
26344197
RL11_HUMANRPL11physical
26344197
SURF6_HUMANSURF6physical
26344197
H11_HUMANHIST1H1Aphysical
28514442
TPM2_HUMANTPM2physical
28514442
RL18_HUMANRPL18physical
28514442
RL8_HUMANRPL8physical
28514442
RL30_HUMANRPL30physical
28514442
RS8_HUMANRPS8physical
28514442
RL3_HUMANRPL3physical
28514442
BRX1_HUMANBRIX1physical
28514442
RL7A_HUMANRPL7Aphysical
28514442
H14_HUMANHIST1H1Ephysical
28514442
NPM_HUMANNPM1physical
28514442
NUCL_HUMANNCLphysical
28514442
RL18A_HUMANRPL18Aphysical
28514442
RS9_HUMANRPS9physical
28514442
RL27A_HUMANRPL27Aphysical
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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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