dbPTM

RUVB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RUVB2_HUMAN
UniProt AC	Q9Y230
Protein Name	RuvB-like 2
Gene Name	RUVBL2
Organism	Homo sapiens (Human).
Sequence Length	463
Subcellular Localization	Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm. Membrane. Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol. Although it is also present in the cytoplasm and associated with the cell membranes.
Protein Description	Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.; Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.; Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional activity of ATF2.; Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes..
Protein Sequence	MATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIESLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTTPYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATVTATTK ------CCEEEECCC	15.69	25944712
3	Phosphorylation	-----MATVTATTKV -----CCEEEECCCC	19.66	20068231
5	Phosphorylation	---MATVTATTKVPE ---CCEEEECCCCCC	17.58	28857561
7	Phosphorylation	-MATVTATTKVPEIR -CCEEEECCCCCCHH	20.13	20860994
8	Phosphorylation	MATVTATTKVPEIRD CCEEEECCCCCCHHC	27.81	30622161
9	Ubiquitination	ATVTATTKVPEIRDV CEEEECCCCCCHHCC	51.98	21890473
9	Acetylation	ATVTATTKVPEIRDV CEEEECCCCCCHHCC	51.98	25953088
9	Sumoylation	ATVTATTKVPEIRDV CEEEECCCCCCHHCC	51.98	28112733
9	Ubiquitination	ATVTATTKVPEIRDV CEEEECCCCCCHHCC	51.98	21890473
26	Phosphorylation	IERIGAHSHIRGLGL EEEECCCCCCCCCCC	21.78	20068231
29	Methylation	IGAHSHIRGLGLDDA ECCCCCCCCCCCCCC	28.94	115493015
46	Sulfoxidation	PRQASQGMVGQLAAR HHHHCCHHHHHHHHH	2.07	21406390
67	Methylation	LEMIREGKIAGRAVL HHHHHCCCCCCEEEE	25.32	20603076
81	Phosphorylation	LIAGQPGTGKTAIAM EEECCCCCCHHHHHH	42.03	21406692
110	Phosphorylation	IAGSEIFSLEMSKTE ECCCEEEEEECCHHH	29.13	-
115	Ubiquitination	IFSLEMSKTEALTQA EEEEECCHHHHHHHH	49.42	-
119	Ubiquitination	EMSKTEALTQAFRRS ECCHHHHHHHHHHHH	2.72	-
132	Ubiquitination	RSIGVRIKEETEIIE HHHCCEECCCEEEEE	38.64	-
139	Ubiquitination	KEETEIIEGEVVEIQ CCCEEEEECEEEEEE	55.77	-
141	Ubiquitination	ETEIIEGEVVEIQID CEEEEECEEEEEEEE	30.51	-
152	Ubiquitination	IQIDRPATGTGSKVG EEEECCCCCCCCCCE	37.65	-
157	2-Hydroxyisobutyrylation	PATGTGSKVGKLTLK CCCCCCCCCEEEEEE	57.25	-
160	Acetylation	GTGSKVGKLTLKTTE CCCCCCEEEEEEECC	41.09	26051181
160	Ubiquitination	GTGSKVGKLTLKTTE CCCCCCEEEEEEECC	41.09	-
162	Phosphorylation	GSKVGKLTLKTTEME CCCCEEEEEEECCCE	29.69	24719451
164	Ubiquitination	KVGKLTLKTTEMETI CCEEEEEEECCCEEH	48.44	21906983
168	Sulfoxidation	LTLKTTEMETIYDLG EEEEECCCEEHHHHC	5.31	28183972
170	Phosphorylation	LKTTEMETIYDLGTK EEECCCEEHHHHCHH	24.43	29978859
172	Phosphorylation	TTEMETIYDLGTKMI ECCCEEHHHHCHHHH	16.73	28796482
176	Phosphorylation	ETIYDLGTKMIESLT EEHHHHCHHHHHHHC	25.41	28796482
177	Ubiquitination	TIYDLGTKMIESLTK EHHHHCHHHHHHHCC	35.76	-
178	Ubiquitination	IYDLGTKMIESLTKD HHHHCHHHHHHHCCC	4.06	-
181	Phosphorylation	LGTKMIESLTKDKVQ HCHHHHHHHCCCCCC	30.34	26074081
183	Phosphorylation	TKMIESLTKDKVQAG HHHHHHHCCCCCCCC	46.61	26074081
184	2-Hydroxyisobutyrylation	KMIESLTKDKVQAGD HHHHHHCCCCCCCCC	61.93	-
184	Ubiquitination	KMIESLTKDKVQAGD HHHHHHCCCCCCCCC	61.93	21906983
186	2-Hydroxyisobutyrylation	IESLTKDKVQAGDVI HHHHCCCCCCCCCEE	37.49	-
186	Acetylation	IESLTKDKVQAGDVI HHHHCCCCCCCCCEE	37.49	25953088
186	Ubiquitination	IESLTKDKVQAGDVI HHHHCCCCCCCCCEE	37.49	21906983
189	Ubiquitination	LTKDKVQAGDVITID HCCCCCCCCCEEEEE	21.09	-
191	Ubiquitination	KDKVQAGDVITIDKA CCCCCCCCEEEEECC	31.49	-
197	Ubiquitination	GDVITIDKATGKISK CCEEEEECCCCCCHH	43.95	21890473
197	2-Hydroxyisobutyrylation	GDVITIDKATGKISK CCEEEEECCCCCCHH	43.95	-
197	Acetylation	GDVITIDKATGKISK CCEEEEECCCCCCHH	43.95	25953088
197	Ubiquitination	GDVITIDKATGKISK CCEEEEECCCCCCHH	43.95	21890473
199	O-linked_Glycosylation	VITIDKATGKISKLG EEEEECCCCCCHHHC	44.76	30379171
208	Phosphorylation	KISKLGRSFTRARDY CCHHHCCCCCCCCCC	29.22	28555341
215	Phosphorylation	SFTRARDYDAMGSQT CCCCCCCCCCCCCCC	10.47	28796482
218	Sulfoxidation	RARDYDAMGSQTKFV CCCCCCCCCCCCEEE	4.92	30846556
220	Phosphorylation	RDYDAMGSQTKFVQC CCCCCCCCCCEEEEC	22.92	17525332
222	Phosphorylation	YDAMGSQTKFVQCPD CCCCCCCCEEEECCC	28.31	21815630
223	Acetylation	DAMGSQTKFVQCPDG CCCCCCCEEEECCCC	35.58	25953088
223	Ubiquitination	DAMGSQTKFVQCPDG CCCCCCCEEEECCCC	35.58	-
224	Ubiquitination	AMGSQTKFVQCPDGE CCCCCCEEEECCCCH	5.35	-
234	Ubiquitination	CPDGELQKRKEVVHT CCCCHHHHCCEEEEE	77.41	-
234	2-Hydroxyisobutyrylation	CPDGELQKRKEVVHT CCCCHHHHCCEEEEE	77.41	-
234	Acetylation	CPDGELQKRKEVVHT CCCCHHHHCCEEEEE	77.41	25953088
234	Ubiquitination	CPDGELQKRKEVVHT CCCCHHHHCCEEEEE	77.41	21906983
236	2-Hydroxyisobutyrylation	DGELQKRKEVVHTVS CCHHHHCCEEEEEEE	62.99	-
236	Ubiquitination	DGELQKRKEVVHTVS CCHHHHCCEEEEEEE	62.99	-
241	Phosphorylation	KRKEVVHTVSLHEID HCCEEEEEEEHHHEE	10.53	30622161
243	Phosphorylation	KEVVHTVSLHEIDVI CEEEEEEEHHHEEEE	25.76	30622161
252	Phosphorylation	HEIDVINSRTQGFLA HHEEEEECCCCCEEE	26.11	30622161
254	Phosphorylation	IDVINSRTQGFLALF EEEEECCCCCEEEEE	32.63	21712546
262	Phosphorylation	QGFLALFSGDTGEIK CCEEEEECCCCCCCC	36.29	19651622
265	Phosphorylation	LALFSGDTGEIKSEV EEEECCCCCCCCHHH	39.99	19651622
269	Sumoylation	SGDTGEIKSEVREQI CCCCCCCCHHHHHHH	35.94	-
269	Ubiquitination	SGDTGEIKSEVREQI CCCCCCCCHHHHHHH	35.94	21906983
279	2-Hydroxyisobutyrylation	VREQINAKVAEWREE HHHHHHHHHHHHHHH	37.17	-
279	Acetylation	VREQINAKVAEWREE HHHHHHHHHHHHHHH	37.17	25038526
279	Ubiquitination	VREQINAKVAEWREE HHHHHHHHHHHHHHH	37.17	21906983
318	Phosphorylation	FLNRALESDMAPVLI HHHHHHHCCCCCEEE	33.27	-
320	Acetylation	NRALESDMAPVLIMA HHHHHCCCCCEEEEE	6.72	-
320	Ubiquitination	NRALESDMAPVLIMA HHHHHCCCCCEEEEE	6.72	-
320	Sulfoxidation	NRALESDMAPVLIMA HHHHHCCCCCEEEEE	6.72	21406390
323	Ubiquitination	LESDMAPVLIMATNR HHCCCCCEEEEEECC	4.03	-
326	Sulfoxidation	DMAPVLIMATNRGIT CCCCEEEEEECCCCE	3.09	30846556
328	Phosphorylation	APVLIMATNRGITRI CCEEEEEECCCCEEE	14.20	20068231
336	Methylation	NRGITRIRGTSYQSP CCCCEEEECCCCCCC	38.76	115493023
338	Phosphorylation	GITRIRGTSYQSPHG CCEEEECCCCCCCCC	17.89	28152594
339	Phosphorylation	ITRIRGTSYQSPHGI CEEEECCCCCCCCCC	24.81	28152594
340	Phosphorylation	TRIRGTSYQSPHGIP EEEECCCCCCCCCCC	16.91	28152594
342	Phosphorylation	IRGTSYQSPHGIPID EECCCCCCCCCCCHH	15.61	28152594
353	Methylation	IPIDLLDRLLIVSTT CCHHHHCCEEEEECC	31.22	115493007
358	Phosphorylation	LDRLLIVSTTPYSEK HCCEEEEECCCCCCC	21.41	28152594
359	Phosphorylation	DRLLIVSTTPYSEKD CCEEEEECCCCCCCC	22.39	28152594
360	Phosphorylation	RLLIVSTTPYSEKDT CEEEEECCCCCCCCH	16.84	21815630
362	Phosphorylation	LIVSTTPYSEKDTKQ EEEECCCCCCCCHHH	27.63	28152594
363	Phosphorylation	IVSTTPYSEKDTKQI EEECCCCCCCCHHHH	39.10	28152594
365	2-Hydroxyisobutyrylation	STTPYSEKDTKQILR ECCCCCCCCHHHHEE	65.83	-
365	Acetylation	STTPYSEKDTKQILR ECCCCCCCCHHHHEE	65.83	23954790
365	Malonylation	STTPYSEKDTKQILR ECCCCCCCCHHHHEE	65.83	26320211
365	Ubiquitination	STTPYSEKDTKQILR ECCCCCCCCHHHHEE	65.83	21906983
367	Phosphorylation	TPYSEKDTKQILRIR CCCCCCCHHHHEEEE	35.60	23312004
368	2-Hydroxyisobutyrylation	PYSEKDTKQILRIRC CCCCCCHHHHEEEEE	45.54	-
368	Acetylation	PYSEKDTKQILRIRC CCCCCCHHHHEEEEE	45.54	25953088
368	Malonylation	PYSEKDTKQILRIRC CCCCCCHHHHEEEEE	45.54	26320211
368	Ubiquitination	PYSEKDTKQILRIRC CCCCCCHHHHEEEEE	45.54	-
372	Ubiquitination	KDTKQILRIRCEEED CCHHHHEEEEECHHH	18.88	-
382	Acetylation	CEEEDVEMSEDAYTV ECHHHCCCCCCHHHH	5.51	-
382	Ubiquitination	CEEEDVEMSEDAYTV ECHHHCCCCCCHHHH	5.51	-
399	Ubiquitination	RIGLETSLRYAIQLI HHCHHHHHHHHHHHH	6.74	-
411	Ubiquitination	QLITAASLVCRKRKG HHHHHHHHHHHHCCC	3.46	-
415	Methylation	AASLVCRKRKGTEVQ HHHHHHHHCCCCEEE	54.02	20137074
417	Acetylation	SLVCRKRKGTEVQVD HHHHHHCCCCEEEHH	73.54	71283
417	Ubiquitination	SLVCRKRKGTEVQVD HHHHHHCCCCEEEHH	73.54	21906983
419	Phosphorylation	VCRKRKGTEVQVDDI HHHHCCCCEEEHHHH	35.70	29255136
427	Ubiquitination	EVQVDDIKRVYSLFL EEEHHHHHHHHHHHH	42.69	21890473
427	2-Hydroxyisobutyrylation	EVQVDDIKRVYSLFL EEEHHHHHHHHHHHH	42.69	-
427	Acetylation	EVQVDDIKRVYSLFL EEEHHHHHHHHHHHH	42.69	23954790
427	Malonylation	EVQVDDIKRVYSLFL EEEHHHHHHHHHHHH	42.69	26320211
427	Ubiquitination	EVQVDDIKRVYSLFL EEEHHHHHHHHHHHH	42.69	21890473
430	Nitration	VDDIKRVYSLFLDES HHHHHHHHHHHHCCH	12.04	-
430	Phosphorylation	VDDIKRVYSLFLDES HHHHHHHHHHHHCCH	12.04	20090780
431	Phosphorylation	DDIKRVYSLFLDESR HHHHHHHHHHHCCHH	15.13	28152594
437	Phosphorylation	YSLFLDESRSTQYMK HHHHHCCHHCHHHHH	31.06	28112733
440	Phosphorylation	FLDESRSTQYMKEYQ HHCCHHCHHHHHHHH	23.70	21601212
444	Sumoylation	SRSTQYMKEYQDAFL HHCHHHHHHHHHHHH	48.62	28112733
444	Ubiquitination	SRSTQYMKEYQDAFL HHCHHHHHHHHHHHH	48.62	21906983
446	Phosphorylation	STQYMKEYQDAFLFN CHHHHHHHHHHHHHH	13.23	20068231
456	Sumoylation	AFLFNELKGETMDTS HHHHHHHCCCCCCCC	48.82	-
456	Sumoylation	AFLFNELKGETMDTS HHHHHHHCCCCCCCC	48.82	28112733
456	Ubiquitination	AFLFNELKGETMDTS HHHHHHHCCCCCCCC	48.82	2190698
459	Phosphorylation	FNELKGETMDTS--- HHHHCCCCCCCC---	29.08	21712546
460	Sulfoxidation	NELKGETMDTS---- HHHCCCCCCCC----	4.62	30846556
462	Phosphorylation	LKGETMDTS------ HCCCCCCCC------	26.05	27251275
463	Phosphorylation	KGETMDTS------- CCCCCCCC-------	33.68	27251275

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
Oops, there are no upstream regulatory protein records of RUVB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RUVB2_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 RUVB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPCD_HUMAN	DPCD	physical	16189514
WDCP_HUMAN	C2orf44	physical	17353931
PLOD2_HUMAN	PLOD2	physical	17353931
RUVB1_HUMAN	RUVBL1	physical	17353931
UBP7_HUMAN	USP7	physical	17353931
RS11_HUMAN	RPS11	physical	17353931
DPCD_HUMAN	DPCD	physical	17353931
ATF2_HUMAN	ATF2	physical	11713276
FDFT_HUMAN	FDFT1	physical	16169070
CCD87_HUMAN	CCDC87	physical	17643375
DDX42_HUMAN	DDX42	physical	17643375
RPAP3_HUMAN	RPAP3	physical	17643375
TTI1_HUMAN	TTI1	physical	17643375
CCAR2_HUMAN	CCAR2	physical	17643375
MATR3_HUMAN	MATR3	physical	17643375
PIHD1_HUMAN	PIH1D1	physical	17643375
PCBP2_HUMAN	PCBP2	physical	17643375
RPB2_HUMAN	POLR2B	physical	17643375
RFC4_HUMAN	RFC4	physical	17643375
DPCD_HUMAN	DPCD	physical	17643375
RUVB1_HUMAN	RUVBL1	physical	17643375
SRCAP_HUMAN	SRCAP	physical	17643375
UXT_HUMAN	UXT	physical	17643375
ACTB_HUMAN	ACTB	physical	17643375
ACTG_HUMAN	ACTG1	physical	17643375
RMP_HUMAN	URI1	physical	17643375
YETS4_HUMAN	YEATS4	physical	17643375
U5S1_HUMAN	EFTUD2	physical	17643375
NTPCR_HUMAN	NTPCR	physical	17643375
ZNHI2_HUMAN	ZNHIT2	physical	17643375
PFD6_HUMAN	PFDN6	physical	17643375
PDRG1_HUMAN	PDRG1	physical	17643375
RPAB1_HUMAN	POLR2E	physical	17643375
IMB1_HUMAN	KPNB1	physical	17643375
GRP78_HUMAN	HSPA5	physical	17643375
PP1A_HUMAN	PPP1CA	physical	17643375
HNRPU_HUMAN	HNRNPU	physical	17643375
RFC5_HUMAN	RFC5	physical	17643375
CL045_HUMAN	C12orf45	physical	17643375
RS4X_HUMAN	RPS4X	physical	17643375
TTI2_HUMAN	TTI2	physical	17643375
RPAB3_HUMAN	POLR2H	physical	17643375
PCBP1_HUMAN	PCBP1	physical	17643375
ACL6A_HUMAN	ACTL6A	physical	17643375
TIF1B_HUMAN	TRIM28	physical	17643375
CNOT9_HUMAN	RQCD1	physical	17643375
DYN2_HUMAN	DNM2	physical	17643375
ARP6_HUMAN	ACTR6	physical	17643375
NOP58_HUMAN	NOP58	physical	17643375
NFRKB_HUMAN	NFRKB	physical	17643375
TFPT_HUMAN	TFPT	physical	17643375
DMAP1_HUMAN	DMAP1	physical	17643375
IN80E_HUMAN	INO80E	physical	17643375
UCHL5_HUMAN	UCHL5	physical	17643375
TELO2_HUMAN	TELO2	physical	17643375
RL38_HUMAN	RPL38	physical	17643375
ARP5_HUMAN	ACTR5	physical	17643375
PCBP3_HUMAN	PCBP3	physical	17643375
ARF6_HUMAN	ARF6	physical	17643375
RS2_HUMAN	RPS2	physical	17643375
ARP8_HUMAN	ACTR8	physical	17643375
HS71L_HUMAN	HSPA1L	physical	17643375
RPAP3_HUMAN	RPAP3	physical	19180575
RUVB1_HUMAN	RUVBL1	physical	17157868
SENP6_HUMAN	SENP6	physical	16699503
CTNB1_HUMAN	CTNNB1	physical	16699503
HDAC1_HUMAN	HDAC1	physical	16699503
DP13A_HUMAN	APPL1	physical	19433865
DP13B_HUMAN	APPL2	physical	19433865
CNBP1_HUMAN	CTNNBIP1	physical	19433865
HDAC1_HUMAN	HDAC1	physical	19433865
HDAC2_HUMAN	HDAC2	physical	19433865
TYY1_HUMAN	YY1	physical	18026119
FBRL_HUMAN	FBL	physical	17636026
TAF9_HUMAN	TAF9	physical	17636026
EHMT2_HUMAN	EHMT2	physical	20603076
SENP6_HUMAN	SENP6	physical	20603076
CTNB1_HUMAN	CTNNB1	physical	20603076
SENP1_HUMAN	SENP1	physical	20603076
HDAC1_HUMAN	HDAC1	physical	20603076
RUVB1_HUMAN	RUVBL1	physical	20603076
SUV91_HUMAN	SUV39H1	physical	20603076
RUVB1_HUMAN	RUVBL1	physical	17721549
ACL6A_HUMAN	ACTL6A	physical	17721549
IN80C_HUMAN	INO80C	physical	17721549
TYY1_HUMAN	YY1	physical	17721549
INO80_HUMAN	INO80	physical	17721549
NFRKB_HUMAN	NFRKB	physical	17721549
TFPT_HUMAN	TFPT	physical	17721549
ARP8_HUMAN	ACTR8	physical	17721549
IN80B_HUMAN	INO80B	physical	17721549
IN80E_HUMAN	INO80E	physical	17721549
UCHL5_HUMAN	UCHL5	physical	17721549
IN80D_HUMAN	INO80D	physical	17721549
MCRS1_HUMAN	MCRS1	physical	17721549
BCL3_HUMAN	BCL3	physical	15829968
A4_HUMAN	APP	physical	21832049
SRCAP_HUMAN	SRCAP	physical	22939629
VPS72_HUMAN	VPS72	physical	22939629
SMCA5_HUMAN	SMARCA5	physical	22939629
HINT1_HUMAN	HINT1	physical	16014379
TERT_HUMAN	TERT	physical	18358808
DKC1_HUMAN	DKC1	physical	18358808
RUVB1_HUMAN	RUVBL1	physical	18358808
RUVB2_HUMAN	RUVBL2	physical	11080158
RUVB1_HUMAN	RUVBL1	physical	11080158
CTNB1_HUMAN	CTNNB1	physical	11080158
TBP_HUMAN	TBP	physical	11080158
RUVB2_HUMAN	RUVBL2	physical	21988832
ASNA_HUMAN	ASNA1	physical	22863883
PP6R3_HUMAN	PPP6R3	physical	22863883
RUVB1_HUMAN	RUVBL1	physical	22863883
DPCD_HUMAN	DPCD	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
CC103_HUMAN	CCDC103	physical	25416956
BRD2_HUMAN	BRD2	physical	26344197
DYHC1_HUMAN	DYNC1H1	physical	26344197
DYHC2_HUMAN	DYNC2H1	physical	26344197
IF6_HUMAN	EIF6	physical	26344197
IPO4_HUMAN	IPO4	physical	26344197
SSA27_HUMAN	SSSCA1	physical	26344197
SNUT2_HUMAN	USP39	physical	26344197
DPCD_HUMAN	DPCD	physical	28514442
INO80_HUMAN	INO80	physical	28514442
IN80D_HUMAN	INO80D	physical	28514442
ARP5_HUMAN	ACTR5	physical	28514442
IN80B_HUMAN	INO80B	physical	28514442
NFRKB_HUMAN	NFRKB	physical	28514442
IN80C_HUMAN	INO80C	physical	28514442
ZNHI1_HUMAN	ZNHIT1	physical	28514442
WDCP_HUMAN	C2orf44	physical	28514442
EPC2_HUMAN	EPC2	physical	28514442
EPC1_HUMAN	EPC1	physical	28514442
EP400_HUMAN	EP400	physical	28514442
MBTD1_HUMAN	MBTD1	physical	28514442
ING3_HUMAN	ING3	physical	28514442
SRCAP_HUMAN	SRCAP	physical	28514442
TYY1_HUMAN	YY1	physical	28514442
IN80E_HUMAN	INO80E	physical	28514442
KAT5_HUMAN	KAT5	physical	28514442
VPS72_HUMAN	VPS72	physical	28514442
TFPT_HUMAN	TFPT	physical	28514442
BRD8_HUMAN	BRD8	physical	28514442
DMAP1_HUMAN	DMAP1	physical	28514442
ZNHI2_HUMAN	ZNHIT2	physical	28514442
KCD15_HUMAN	KCTD15	physical	28514442
MCRS1_HUMAN	MCRS1	physical	28514442
YETS4_HUMAN	YEATS4	physical	28514442
TRRAP_HUMAN	TRRAP	physical	28514442
ACL6B_HUMAN	ACTL6B	physical	28514442
RMP_HUMAN	URI1	physical	28514442
RPC1_HUMAN	POLR3A	physical	28514442
AAR2_HUMAN	AAR2	physical	28561026
CL045_HUMAN	C12orf45	physical	28561026
WDCP_HUMAN	C2orf44	physical	28561026
DKC1_HUMAN	DKC1	physical	28561026
DPCD_HUMAN	DPCD	physical	28561026
U5S1_HUMAN	EFTUD2	physical	28561026
MAP1B_HUMAN	MAP1B	physical	28561026
NOP58_HUMAN	NOP58	physical	28561026
PFD2_HUMAN	PFDN2	physical	28561026
PIHD1_HUMAN	PIH1D1	physical	28561026
RPB1_HUMAN	POLR2A	physical	28561026
RPB2_HUMAN	POLR2B	physical	28561026
RPC1_HUMAN	POLR3A	physical	28561026
PRP8_HUMAN	PRPF8	physical	28561026
RICTR_HUMAN	RICTOR	physical	28561026
RPAP3_HUMAN	RPAP3	physical	28561026
RUVB1_HUMAN	RUVBL1	physical	28561026
RUVB2_HUMAN	RUVBL2	physical	28561026
SHQ1_HUMAN	SHQ1	physical	28561026
S7A6O_HUMAN	SLC7A6OS	physical	28561026
U520_HUMAN	SNRNP200	physical	28561026
TNG6_HUMAN	TANGO6	physical	28561026
TSSC4_HUMAN	TSSC4	physical	28561026
TTI1_HUMAN	TTI1	physical	28561026
TTI2_HUMAN	TTI2	physical	28561026
RENT1_HUMAN	UPF1	physical	28561026
RMP_HUMAN	URI1	physical	28561026
WDR92_HUMAN	WDR92	physical	28561026
ZNHI2_HUMAN	ZNHIT2	physical	28561026
ACL6A_HUMAN	ACTL6A	physical	28561026
BRD8_HUMAN	BRD8	physical	28561026
CHD4_HUMAN	CHD4	physical	28561026
DMAP1_HUMAN	DMAP1	physical	28561026
EP400_HUMAN	EP400	physical	28561026
INO80_HUMAN	INO80	physical	28561026
IWS1_HUMAN	IWS1	physical	28561026
SRCAP_HUMAN	SRCAP	physical	28561026
SUGP2_HUMAN	SUGP2	physical	28561026
TRRAP_HUMAN	TRRAP	physical	28561026
WAPL_HUMAN	WAPAL	physical	28561026

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 RUVB2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASSSPECTROMETRY.	17525332 [Abstract]