FBRL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FBRL_HUMAN
• UniProt AC: P22087
• Protein Name: rRNA 2'-O-methyltransferase fibrillarin
• Gene Name: FBL
• Organism: Homo sapiens (Human).
• Sequence Length: 321
• Subcellular Localization: Nucleus, nucleolus . Fibrillar region of the nucleolus.
• Protein Description: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus. [PubMed: 24352239]
• Protein Sequence: MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGGGGGGGGGRGGGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN

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
6	Phosphorylation	--MKPGFSPRGGGFG --CCCCCCCCCCCCC	21.43	21712546
8	Methylation	MKPGFSPRGGGFGGR CCCCCCCCCCCCCCC	56.01	-
8	Asymmetric dimethylarginine	MKPGFSPRGGGFGGR CCCCCCCCCCCCCCC	56.01	-
15	Methylation	RGGGFGGRGGFGDRG CCCCCCCCCCCCCCC	42.30	-
15	Asymmetric dimethylarginine	RGGGFGGRGGFGDRG CCCCCCCCCCCCCCC	42.30	-
21	Methylation	GRGGFGDRGGRGGRG CCCCCCCCCCCCCCC	50.25	-
21	Asymmetric dimethylarginine	GRGGFGDRGGRGGRG CCCCCCCCCCCCCCC	50.25	-
24	Methylation	GFGDRGGRGGRGGFG CCCCCCCCCCCCCCC	47.41	-
24	Asymmetric dimethylarginine	GFGDRGGRGGRGGFG CCCCCCCCCCCCCCC	47.41	-
27	Asymmetric dimethylarginine	DRGGRGGRGGFGGGR CCCCCCCCCCCCCCC	44.90	-
27	Methylation	DRGGRGGRGGFGGGR CCCCCCCCCCCCCCC	44.90	-
34	Methylation	RGGFGGGRGRGGGFR CCCCCCCCCCCCCCC	34.60	-
36	Methylation	GFGGGRGRGGGFRGR CCCCCCCCCCCCCCC	38.94	-
45	Ubiquitination	GGFRGRGRGGGGGGG CCCCCCCCCCCCCCC	38.94	22817900
45	Methylation	GGFRGRGRGGGGGGG CCCCCCCCCCCCCCC	38.94	-
52	Ubiquitination	RGGGGGGGGGGGGGR CCCCCCCCCCCCCCC	34.54	23000965
59	Methylation	GGGGGGGRGGGGFHS CCCCCCCCCCCCCCC	43.81	-
64	Ubiquitination	GGRGGGGFHSGGNRG CCCCCCCCCCCCCCC	4.72	22817900
70	Methylation	GFHSGGNRGRGRGGK CCCCCCCCCCCCCCC	39.19	-
72	Methylation	HSGGNRGRGRGGKRG CCCCCCCCCCCCCCC	28.53	-
74	Ubiquitination	GGNRGRGRGGKRGNQ CCCCCCCCCCCCCCC	49.70	22817900
78	Methylation	GRGRGGKRGNQSGKN CCCCCCCCCCCCCCC	53.20	-
82	Phosphorylation	GGKRGNQSGKNVMVE CCCCCCCCCCCEEEC	56.59	29214152
84	Sumoylation	KRGNQSGKNVMVEPH CCCCCCCCCEEECCC	52.17	28112733
84	Ubiquitination	KRGNQSGKNVMVEPH CCCCCCCCCEEECCC	52.17	32015554
84	Acetylation	KRGNQSGKNVMVEPH CCCCCCCCCEEECCC	52.17	25953088
99	S-nitrosylation	RHEGVFICRGKEDAL CCCCEEEECCCCCEE	2.97	19483679
99	S-nitrosocysteine	RHEGVFICRGKEDAL CCCCEEEECCCCCEE	2.97	-
101	Ubiquitination	EGVFICRGKEDALVT CCEEEECCCCCEEEE	33.04	27667366
102	Sumoylation	GVFICRGKEDALVTK CEEEECCCCCEEEEC	32.82	-
102	Sumoylation	GVFICRGKEDALVTK CEEEECCCCCEEEEC	32.82	28112733
102	Ubiquitination	GVFICRGKEDALVTK CEEEECCCCCEEEEC	32.82	21906983
102	Acetylation	GVFICRGKEDALVTK CEEEECCCCCEEEEC	32.82	26051181
105	Ubiquitination	ICRGKEDALVTKNLV EECCCCCEEEECCCC	12.67	22817900
108	Ubiquitination	GKEDALVTKNLVPGE CCCCEEEECCCCCCC	18.31	23000965
109	Sumoylation	KEDALVTKNLVPGES CCCEEEECCCCCCCC	40.58	-
109	Sumoylation	KEDALVTKNLVPGES CCCEEEECCCCCCCC	40.58	28112733
109	Ubiquitination	KEDALVTKNLVPGES CCCEEEECCCCCCCC	40.58	23000965
109	Acetylation	KEDALVTKNLVPGES CCCEEEECCCCCCCC	40.58	25953088
116	Phosphorylation	KNLVPGESVYGEKRV CCCCCCCCCCCCCEE	26.93	23401153
118	Phosphorylation	LVPGESVYGEKRVSI CCCCCCCCCCCEEEE	28.93	28152594
120	Ubiquitination	PGESVYGEKRVSISE CCCCCCCCCEEEECC	21.72	22817900
121	Ubiquitination	GESVYGEKRVSISEG CCCCCCCCEEEECCC	54.45	21906983
121	Acetylation	GESVYGEKRVSISEG CCCCCCCCEEEECCC	54.45	30540930
121	2-Hydroxyisobutyrylation	GESVYGEKRVSISEG CCCCCCCCEEEECCC	54.45	-
124	Phosphorylation	VYGEKRVSISEGDDK CCCCCEEEECCCCCC	25.16	29255136
126	Phosphorylation	GEKRVSISEGDDKIE CCCEEEECCCCCCEE	28.20	30266825
130	Ubiquitination	VSISEGDDKIEYRAW EEECCCCCCEEEEEC	65.77	22817900
131	Ubiquitination	SISEGDDKIEYRAWN EECCCCCCEEEEECC	42.02	21906983
131	Acetylation	SISEGDDKIEYRAWN EECCCCCCEEEEECC	42.02	25953088
131	2-Hydroxyisobutyrylation	SISEGDDKIEYRAWN EECCCCCCEEEEECC	42.02	-
131	Sumoylation	SISEGDDKIEYRAWN EECCCCCCEEEEECC	42.02	28112733
134	Phosphorylation	EGDDKIEYRAWNPFR CCCCCEEEEECCHHH	14.76	23403867
142	O-linked_Glycosylation	RAWNPFRSKLAAAIL EECCHHHHHHHHHHH	32.19	23301498
143	Ubiquitination	AWNPFRSKLAAAILG ECCHHHHHHHHHHHC	37.58	32015554
143	Sumoylation	AWNPFRSKLAAAILG ECCHHHHHHHHHHHC	37.58	-
143	Sumoylation	AWNPFRSKLAAAILG ECCHHHHHHHHHHHC	37.58	28112733
143	Acetylation	AWNPFRSKLAAAILG ECCHHHHHHHHHHHC	37.58	25953088
148	Ubiquitination	RSKLAAAILGGVDQI HHHHHHHHHCCCCEE	2.93	22817900
149	Ubiquitination	SKLAAAILGGVDQIH HHHHHHHHCCCCEEE	4.13	22817900
157	Ubiquitination	GGVDQIHIKPGAKVL CCCCEEEECCCCEEE	6.51	21890473
158	Sumoylation	GVDQIHIKPGAKVLY CCCEEEECCCCEEEE	24.20	28112733
158	Acetylation	GVDQIHIKPGAKVLY CCCEEEECCCCEEEE	24.20	25953088
158	Sumoylation	GVDQIHIKPGAKVLY CCCEEEECCCCEEEE	24.20	-
158	Ubiquitination	GVDQIHIKPGAKVLY CCCEEEECCCCEEEE	24.20	21906983
161	Ubiquitination	QIHIKPGAKVLYLGA EEEECCCCEEEEEEC	13.81	22817900
162	Ubiquitination	IHIKPGAKVLYLGAA EEECCCCEEEEEECC	38.39	22817900
204	Ubiquitination	GRDLINLAKKRTNII CHHHHHHHHHHCCEE	15.73	22817900
205	Acetylation	RDLINLAKKRTNIIP HHHHHHHHHHCCEEC	46.05	30540930
205	Ubiquitination	RDLINLAKKRTNIIP HHHHHHHHHHCCEEC	46.05	30540930
205	2-Hydroxyisobutyrylation	RDLINLAKKRTNIIP HHHHHHHHHHCCEEC	46.05	-
206	Ubiquitination	DLINLAKKRTNIIPV HHHHHHHHHCCEECC	59.87	22817900
206	Acetylation	DLINLAKKRTNIIPV HHHHHHHHHCCEECC	59.87	25953088
208	Phosphorylation	INLAKKRTNIIPVIE HHHHHHHCCEECCCC	39.38	20068231
222	Ubiquitination	EDARHPHKYRMLIAM CCCCCHHHHHHHHHH	38.72	-
227	Ubiquitination	PHKYRMLIAMVDVIF HHHHHHHHHHHHEEE	1.37	22505724
235	Ubiquitination	AMVDVIFADVAQPDQ HHHHEEECCCCCCCC	10.15	21963094
261	Ubiquitination	LRNGGHFVISIKANC EEECCEEEEEEEECC	2.52	21890473
263	Phosphorylation	NGGHFVISIKANCID ECCEEEEEEEECCCC	16.85	24719451
283	Ubiquitination	EAVFASEVKKMQQEN HHHHHHHHHHHHHHC	7.18	22505724
284	Acetylation	AVFASEVKKMQQENM HHHHHHHHHHHHHCC	38.18	25953088
284	2-Hydroxyisobutyrylation	AVFASEVKKMQQENM HHHHHHHHHHHHHCC	38.18	-
284	Ubiquitination	AVFASEVKKMQQENM HHHHHHHHHHHHHCC	38.18	32015554
285	Ubiquitination	VFASEVKKMQQENMK HHHHHHHHHHHHCCC	47.30	-
286	Sulfoxidation	FASEVKKMQQENMKP HHHHHHHHHHHCCCH	4.05	28183972
291	Ubiquitination	KKMQQENMKPQEQLT HHHHHHCCCHHHHCC	7.06	21963094
291	Sulfoxidation	KKMQQENMKPQEQLT HHHHHHCCCHHHHCC	7.06	28183972
292	Ubiquitination	KMQQENMKPQEQLTL HHHHHCCCHHHHCCC	55.95	21963094
292	Acetylation	KMQQENMKPQEQLTL HHHHHCCCHHHHCCC	55.95	25953088
298	Phosphorylation	MKPQEQLTLEPYERD CCHHHHCCCCCCCCC	28.86	-
302	Phosphorylation	EQLTLEPYERDHAVV HHCCCCCCCCCCEEE	17.77	-
317	Ubiquitination	VGVYRPPPKVKN--- EEEECCCCCCCC---	57.67	21890473
318	Ubiquitination	GVYRPPPKVKN---- EEECCCCCCCC----	72.17	21890473
318	2-Hydroxyisobutyrylation	GVYRPPPKVKN---- EEECCCCCCCC----	72.17	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
105	Q	Acetylation	Acetylated by CREBBP/CBP, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me), without affecting rRNA methylation.	30540930
105	Q	Acetylation	Deacetylation by SIRT7 restores methylation of 'Gln-105' of histone H2A (H2AQ104me).	30540930
105	Q	Methylation	Acetylated by CREBBP/CBP, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me), without affecting rRNA methylation.	30540930
105	Q	Methylation	Deacetylation by SIRT7 restores methylation of 'Gln-105' of histone H2A (H2AQ104me).	30540930

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of FBRL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANM5_HUMAN	PRMT5	physical	14583623
ANM1_HUMAN	PRMT1	physical	14583623
C1QBP_HUMAN	C1QBP	physical	14583623
TBA3C_HUMAN	TUBA3C	physical	14583623
TBB1_HUMAN	TUBB1	physical	14583623
TBC17_HUMAN	TBC1D17	physical	16169070
SMN_HUMAN	SMN1	physical	11509230
GEMI2_HUMAN	GEMIN2	physical	11509230
DDX20_HUMAN	DDX20	physical	11509230
GEMI4_HUMAN	GEMIN4	physical	11509230
PIN4_HUMAN	PIN4	physical	11960984
NOP56_HUMAN	NOP56	physical	17636026
RL6_HUMAN	RPL6	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
NOP58_HUMAN	NOP58	physical	22939629
NOP56_HUMAN	NOP56	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
NH2L1_HUMAN	NHP2L1	physical	22939629
NOLC1_HUMAN	NOLC1	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL17_HUMAN	RPL17	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
GNL3_HUMAN	GNL3	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
IF6_HUMAN	EIF6	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RL1D1_HUMAN	RSL1D1	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
NSUN2_HUMAN	NSUN2	physical	22939629
SPB1_HUMAN	FTSJ3	physical	22939629
MK67I_HUMAN	NIFK	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
POP1_HUMAN	POP1	physical	22939629
MRT4_HUMAN	MRTO4	physical	22939629
PRPF3_HUMAN	PRPF3	physical	22939629
PNO1_HUMAN	PNO1	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
TAF9_HUMAN	TAF9	physical	22939629
NUCL_HUMAN	NCL	physical	18292223
BIG1_HUMAN	ARFGEF1	physical	18292223
LARP7_HUMAN	LARP7	physical	26186194
KNOP1_HUMAN	KNOP1	physical	26186194
NOLC1_HUMAN	NOLC1	physical	26186194
TROP_HUMAN	TRO	physical	26186194
ZFP91_HUMAN	ZFP91	physical	26186194
TF3C2_HUMAN	GTF3C2	physical	26186194
TE2IP_HUMAN	TERF2IP	physical	26186194
ZNF93_HUMAN	ZNF93	physical	26186194
ZN430_HUMAN	ZNF430	physical	26186194
ZN629_HUMAN	ZNF629	physical	26186194
Z324A_HUMAN	ZNF324	physical	26186194
C1QBP_HUMAN	C1QBP	physical	26186194
UTP18_HUMAN	UTP18	physical	26186194
TF3C3_HUMAN	GTF3C3	physical	26186194
RNBP6_HUMAN	RANBP6	physical	26186194
NOP56_HUMAN	NOP56	physical	26186194
RBM23_HUMAN	RBM23	physical	26186194
ZMYM4_HUMAN	ZMYM4	physical	26186194
TF3C5_HUMAN	GTF3C5	physical	26186194
BCORL_HUMAN	BCORL1	physical	26186194
PINX1_HUMAN	PINX1	physical	26186194
NOL11_HUMAN	NOL11	physical	26186194
NOL8_HUMAN	NOL8	physical	26186194
SRFB1_HUMAN	SRFBP1	physical	26186194
NH2L1_HUMAN	NHP2L1	physical	26186194
PRC2C_HUMAN	PRRC2C	physical	26186194
TGS1_HUMAN	TGS1	physical	26186194
TF3C1_HUMAN	GTF3C1	physical	26186194
NOM1_HUMAN	NOM1	physical	26186194
TERF2_HUMAN	TERF2	physical	26186194
NP1L2_HUMAN	NAP1L2	physical	26186194
NP1L3_HUMAN	NAP1L3	physical	26186194
RN19B_HUMAN	RNF19B	physical	26186194
TBB8_HUMAN	TUBB8	physical	26186194
NOP58_HUMAN	NOP58	physical	26186194
CCD86_HUMAN	CCDC86	physical	26186194
UTP15_HUMAN	UTP15	physical	26186194
U3IP2_HUMAN	RRP9	physical	26186194
WDR36_HUMAN	WDR36	physical	26186194
ZN496_HUMAN	ZNF496	physical	26186194
RRP5_HUMAN	PDCD11	physical	26186194
AHDC1_HUMAN	AHDC1	physical	26186194
WDR43_HUMAN	WDR43	physical	26186194
RIOK1_HUMAN	RIOK1	physical	26186194
RSPRY_HUMAN	RSPRY1	physical	26186194
UTP4_HUMAN	CIRH1A	physical	26186194
ARMX3_HUMAN	ARMCX3	physical	26186194
ZN318_HUMAN	ZNF318	physical	26186194
HASP_HUMAN	GSG2	physical	26186194
SAS10_HUMAN	UTP3	physical	26186194
PHAX_HUMAN	PHAX	physical	26186194
COPRS_HUMAN	COPRS	physical	26186194
ZNHI3_HUMAN	ZNHIT3	physical	26186194
ZN644_HUMAN	ZNF644	physical	26186194
ZN281_HUMAN	ZNF281	physical	26186194
CTCF_HUMAN	CTCF	physical	26186194
PWP2_HUMAN	PWP2	physical	26186194
WDR75_HUMAN	WDR75	physical	26186194
RECQ4_HUMAN	RECQL4	physical	26186194
GXLT2_HUMAN	GXYLT2	physical	26186194
YYAP1_HUMAN	YY1AP1	physical	26186194
ZN316_HUMAN	ZNF316	physical	26186194
LRC41_HUMAN	LRRC41	physical	26186194
BRX1_HUMAN	BRIX1	physical	26344197
DCA13_HUMAN	DCAF13	physical	26344197
DDX27_HUMAN	DDX27	physical	26344197
DDX56_HUMAN	DDX56	physical	26344197
DHX15_HUMAN	DHX15	physical	26344197
EBP2_HUMAN	EBNA1BP2	physical	26344197
IF2B_HUMAN	EIF2S2	physical	26344197
EXOS3_HUMAN	EXOSC3	physical	26344197
SPB1_HUMAN	FTSJ3	physical	26344197
GLYR1_HUMAN	GLYR1	physical	26344197
TF2B_HUMAN	GTF2B	physical	26344197
NOG1_HUMAN	GTPBP4	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
IMA5_HUMAN	KPNA1	physical	26344197
IMA6_HUMAN	KPNA5	physical	26344197
IMA7_HUMAN	KPNA6	physical	26344197
MPP10_HUMAN	MPHOSPH10	physical	26344197
NAA15_HUMAN	NAA15	physical	26344197
NHP2_HUMAN	NHP2	physical	26344197
MK67I_HUMAN	NIFK	physical	26344197
NOC2L_HUMAN	NOC2L	physical	26344197
NOC3L_HUMAN	NOC3L	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
NOLC1_HUMAN	NOLC1	physical	26344197
NOP2_HUMAN	NOP2	physical	26344197
NOP58_HUMAN	NOP58	physical	26344197
NSUN2_HUMAN	NSUN2	physical	26344197
PNO1_HUMAN	PNO1	physical	26344197
PRP31_HUMAN	PRPF31	physical	26344197
PUS7_HUMAN	PUS7	physical	26344197
RBM19_HUMAN	RBM19	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RRS1_HUMAN	RRS1	physical	26344197
RLP24_HUMAN	RSL24D1	physical	26344197
SDA1_HUMAN	SDAD1	physical	26344197
TBL3_HUMAN	TBL3	physical	26344197
UTP15_HUMAN	UTP15	physical	26344197
WDR36_HUMAN	WDR36	physical	26344197
TGS1_HUMAN	TGS1	physical	28514442
NP1L2_HUMAN	NAP1L2	physical	28514442
SRFB1_HUMAN	SRFBP1	physical	28514442
NP1L3_HUMAN	NAP1L3	physical	28514442
TF3C2_HUMAN	GTF3C2	physical	28514442
ZN430_HUMAN	ZNF430	physical	28514442
WDR43_HUMAN	WDR43	physical	28514442
TERF2_HUMAN	TERF2	physical	28514442
ZN316_HUMAN	ZNF316	physical	28514442
PINX1_HUMAN	PINX1	physical	28514442
COPRS_HUMAN	COPRS	physical	28514442
WDR36_HUMAN	WDR36	physical	28514442
U3IP2_HUMAN	RRP9	physical	28514442
ZN496_HUMAN	ZNF496	physical	28514442
YYAP1_HUMAN	YY1AP1	physical	28514442
NOL8_HUMAN	NOL8	physical	28514442
TROP_HUMAN	TRO	physical	28514442
NOP56_HUMAN	NOP56	physical	28514442
TF3C1_HUMAN	GTF3C1	physical	28514442
TE2IP_HUMAN	TERF2IP	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28514442
PHAX_HUMAN	PHAX	physical	28514442
Z324A_HUMAN	ZNF324	physical	28514442
ZNF93_HUMAN	ZNF93	physical	28514442
TF3C3_HUMAN	GTF3C3	physical	28514442
RIOK1_HUMAN	RIOK1	physical	28514442
AHDC1_HUMAN	AHDC1	physical	28514442
GXLT2_HUMAN	GXYLT2	physical	28514442
RSPRY_HUMAN	RSPRY1	physical	28514442
UTP15_HUMAN	UTP15	physical	28514442
WDR75_HUMAN	WDR75	physical	28514442
NOP58_HUMAN	NOP58	physical	28514442
NOM1_HUMAN	NOM1	physical	28514442
ZN644_HUMAN	ZNF644	physical	28514442
ZFP91_HUMAN	ZFP91	physical	28514442
RN19B_HUMAN	RNF19B	physical	28514442
PHF10_HUMAN	PHF10	physical	28514442
BCORL_HUMAN	BCORL1	physical	28514442
ARMX3_HUMAN	ARMCX3	physical	28514442
PWP2_HUMAN	PWP2	physical	28514442
RECQ4_HUMAN	RECQL4	physical	28514442
RNBP6_HUMAN	RANBP6	physical	28514442
SAS10_HUMAN	UTP3	physical	28514442
TF3C5_HUMAN	GTF3C5	physical	28514442
RBM23_HUMAN	RBM23	physical	28514442
ANM5_HUMAN	PRMT5	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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-205, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.
PubMed: 19007248