dbPTM

NONO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NONO_HUMAN
UniProt AC	Q15233
Protein Name	Non-POU domain-containing octamer-binding protein
Gene Name	NONO
Organism	Homo sapiens (Human).
Sequence Length	471
Subcellular Localization	Nucleus. Nucleus, nucleolus. Nucleus speckle. Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.
Protein Description	DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double-stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. Together with PSPC1, required for the formation of nuclear paraspeckles. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Important for the functional organization of GABAergic synapses. Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. [PubMed: 28712728]
Protein Sequence	MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MQSNKTFN -------CCCCCCCC	9.95	-
3	Phosphorylation	-----MQSNKTFNLE -----CCCCCCCCHH	38.71	29083192
5	Methylation	---MQSNKTFNLEKQ ---CCCCCCCCHHHC	60.79	22638387
5	Acetylation	---MQSNKTFNLEKQ ---CCCCCCCCHHHC	60.79	19608861
5	Sumoylation	---MQSNKTFNLEKQ ---CCCCCCCCHHHC	60.79	-
5	Ubiquitination	---MQSNKTFNLEKQ ---CCCCCCCCHHHC	60.79	21890473
5	Sumoylation	---MQSNKTFNLEKQ ---CCCCCCCCHHHC	60.79	28112733
5	Malonylation	---MQSNKTFNLEKQ ---CCCCCCCCHHHC	60.79	26320211
5	Ubiquitination	---MQSNKTFNLEKQ ---CCCCCCCCHHHC	60.79	21890473
6	Phosphorylation	--MQSNKTFNLEKQN --CCCCCCCCHHHCC	23.23	28857561
11	Acetylation	NKTFNLEKQNHTPRK CCCCCHHHCCCCCCH	60.61	19608861
11	Sumoylation	NKTFNLEKQNHTPRK CCCCCHHHCCCCCCH	60.61	-
11	Ubiquitination	NKTFNLEKQNHTPRK CCCCCHHHCCCCCCH	60.61	19608861
11	Sumoylation	NKTFNLEKQNHTPRK CCCCCHHHCCCCCCH	60.61	19608861
15	Phosphorylation	NLEKQNHTPRKHHQH CHHHCCCCCCHHHHH	32.13	30266825
18	Acetylation	KQNHTPRKHHQHHHQ HCCCCCCHHHHHHHH	46.79	19608861
18	Ubiquitination	KQNHTPRKHHQHHHQ HCCCCCCHHHHHHHH	46.79	19608861
50	Phosphorylation	ANGQQASSQNEGLTI CCCCCCCCCCCCCEE	39.79	22817901
60	Sumoylation	EGLTIDLKNFRKPGE CCCEEECCCCCCCCC	50.74	28112733
60	Ubiquitination	EGLTIDLKNFRKPGE CCCEEECCCCCCCCC	50.74	-
64	Acetylation	IDLKNFRKPGEKTFT EECCCCCCCCCCCEE	53.92	19608861
64	Ubiquitination	IDLKNFRKPGEKTFT EECCCCCCCCCCCEE	53.92	21906983
64	Sumoylation	IDLKNFRKPGEKTFT EECCCCCCCCCCCEE	53.92	19608861
68	Acetylation	NFRKPGEKTFTQRSR CCCCCCCCCEECCHH	55.65	25825284
68	Sumoylation	NFRKPGEKTFTQRSR CCCCCCCCCEECCHH	55.65	-
68	Ubiquitination	NFRKPGEKTFTQRSR CCCCCCCCCEECCHH	55.65	-
68	Sumoylation	NFRKPGEKTFTQRSR CCCCCCCCCEECCHH	55.65	-
86	Phosphorylation	GNLPPDITEEEMRKL CCCCCCCCHHHHHHH	44.73	-
92	Ubiquitination	ITEEEMRKLFEKYGK CCHHHHHHHHHHHCC	57.10	-
96	Acetylation	EMRKLFEKYGKAGEV HHHHHHHHHCCCCCE	52.55	25825284
96	Sumoylation	EMRKLFEKYGKAGEV HHHHHHHHHCCCCCE	52.55	-
96	Ubiquitination	EMRKLFEKYGKAGEV HHHHHHHHHCCCCCE	52.55	19608861
96	Sumoylation	EMRKLFEKYGKAGEV HHHHHHHHHCCCCCE	52.55	28112733
97	Phosphorylation	MRKLFEKYGKAGEVF HHHHHHHHCCCCCEE	19.36	29496907
99	Sumoylation	KLFEKYGKAGEVFIH HHHHHHCCCCCEEEE	50.56	-
99	Ubiquitination	KLFEKYGKAGEVFIH HHHHHHCCCCCEEEE	50.56	-
99	Sumoylation	KLFEKYGKAGEVFIH HHHHHHCCCCCEEEE	50.56	28112733
99	Malonylation	KLFEKYGKAGEVFIH HHHHHHCCCCCEEEE	50.56	26320211
99	Acetylation	KLFEKYGKAGEVFIH HHHHHHCCCCCEEEE	50.56	26051181
107	Acetylation	AGEVFIHKDKGFGFI CCCEEEECCCCCCEE	57.21	23749302
107	Sumoylation	AGEVFIHKDKGFGFI CCCEEEECCCCCCEE	57.21	-
107	Ubiquitination	AGEVFIHKDKGFGFI CCCEEEECCCCCCEE	57.21	19608861
107	Sumoylation	AGEVFIHKDKGFGFI CCCEEEECCCCCCEE	57.21	19608861
107	Malonylation	AGEVFIHKDKGFGFI CCCEEEECCCCCCEE	57.21	26320211
109	Acetylation	EVFIHKDKGFGFIRL CEEEECCCCCCEEEE	62.03	23749302
109	Sumoylation	EVFIHKDKGFGFIRL CEEEECCCCCCEEEE	62.03	-
109	Ubiquitination	EVFIHKDKGFGFIRL CEEEECCCCCCEEEE	62.03	21890473
109	Sumoylation	EVFIHKDKGFGFIRL CEEEECCCCCCEEEE	62.03	-
109	Malonylation	EVFIHKDKGFGFIRL CEEEECCCCCCEEEE	62.03	26320211
109	Ubiquitination	EVFIHKDKGFGFIRL CEEEECCCCCCEEEE	62.03	21890473
115	Methylation	DKGFGFIRLETRTLA CCCCCEEEEEECCHH	24.98	115485349
118	Phosphorylation	FGFIRLETRTLAEIA CCEEEEEECCHHHHH	33.28	24117733
120	Phosphorylation	FIRLETRTLAEIAKV EEEEEECCHHHHHCE	37.43	24117733
126	Acetylation	RTLAEIAKVELDNMP CCHHHHHCEEHHCCC	41.73	25825284
126	Sumoylation	RTLAEIAKVELDNMP CCHHHHHCEEHHCCC	41.73	-
126	Ubiquitination	RTLAEIAKVELDNMP CCHHHHHCEEHHCCC	41.73	21906983
126	Sumoylation	RTLAEIAKVELDNMP CCHHHHHCEEHHCCC	41.73	28112733
126	Ubiquitination	RTLAEIAKVELDNMP CCHHHHHCEEHHCCC	41.73	21890473
132	Sulfoxidation	AKVELDNMPLRGKQL HCEEHHCCCCCCCEE	3.10	21406390
145	S-nitrosocysteine	QLRVRFACHSASLTV EEEEEEEECCCCCEE	2.10	-
145	Glutathionylation	QLRVRFACHSASLTV EEEEEEEECCCCCEE	2.10	22555962
145	S-nitrosylation	QLRVRFACHSASLTV EEEEEEEECCCCCEE	2.10	22178444
145	S-palmitoylation	QLRVRFACHSASLTV EEEEEEEECCCCCEE	2.10	29575903
147	Phosphorylation	RVRFACHSASLTVRN EEEEEECCCCCEECC	21.31	30266825
149	Phosphorylation	RFACHSASLTVRNLP EEEECCCCCEECCCC	27.82	30266825
151	Phosphorylation	ACHSASLTVRNLPQY EECCCCCEECCCCHH	18.22	28348404
184	Methylation	AVVIVDDRGRPSGKG EEEEECCCCCCCCCC	38.26	-
186	Methylation	VIVDDRGRPSGKGIV EEECCCCCCCCCCEE	24.09	115485333
188	Phosphorylation	VDDRGRPSGKGIVEF ECCCCCCCCCCEEEE	52.34	20068231
190	Methylation	DRGRPSGKGIVEFSG CCCCCCCCCEEEECC	50.21	18526801
190	Acetylation	DRGRPSGKGIVEFSG CCCCCCCCCEEEECC	50.21	26051181
190	Sumoylation	DRGRPSGKGIVEFSG CCCCCCCCCEEEECC	50.21	-
190	Ubiquitination	DRGRPSGKGIVEFSG CCCCCCCCCEEEECC	50.21	1906983
190	Sumoylation	DRGRPSGKGIVEFSG CCCCCCCCCEEEECC	50.21	28112733
196	Phosphorylation	GKGIVEFSGKPAARK CCCEEEECCCHHHHH	32.19	28674419
198	Acetylation	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	19608861
198	Sumoylation	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	-
198	Ubiquitination	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	21890473
198	Sumoylation	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	28112733
198	Malonylation	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	26320211
198	Ubiquitination	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	21890473
208	Glutathionylation	ARKALDRCSEGSFLL HHHHHHHHCCCCEEE	4.30	22555962
208	S-palmitoylation	ARKALDRCSEGSFLL HHHHHHHHCCCCEEE	4.30	29575903
209	Phosphorylation	RKALDRCSEGSFLLT HHHHHHHCCCCEEEE	45.98	20873877
212	Phosphorylation	LDRCSEGSFLLTTFP HHHHCCCCEEEEECC	14.52	20873877
227	Sulfoxidation	RPVTVEPMDQLDDEE CCEEECCCCCCCCCC	3.03	21406390
239	Ubiquitination	DEEGLPEKLVIKNQQ CCCCCCHHHEEECHH	46.22	-
239	Sumoylation	DEEGLPEKLVIKNQQ CCCCCCHHHEEECHH	46.22	-
243	Acetylation	LPEKLVIKNQQFHKE CCHHHEEECHHHHCC	41.02	25825284
243	Sumoylation	LPEKLVIKNQQFHKE CCHHHEEECHHHHCC	41.02	-
243	Ubiquitination	LPEKLVIKNQQFHKE CCHHHEEECHHHHCC	41.02	-
243	Sumoylation	LPEKLVIKNQQFHKE CCHHHEEECHHHHCC	41.02	28112733
243	Malonylation	LPEKLVIKNQQFHKE CCHHHEEECHHHHCC	41.02	26320211
249	Ubiquitination	IKNQQFHKEREQPPR EECHHHHCCCCCCCC	60.81	-
249	Succinylation	IKNQQFHKEREQPPR EECHHHHCCCCCCCC	60.81	23954790
249	Sumoylation	IKNQQFHKEREQPPR EECHHHHCCCCCCCC	60.81	28112733
256	Methylation	KEREQPPRFAQPGSF CCCCCCCCCCCCCCC	46.33	18601075
262	Phosphorylation	PRFAQPGSFEYEYAM CCCCCCCCCHHHHHH	22.91	21945579
265	Phosphorylation	AQPGSFEYEYAMRWK CCCCCCHHHHHHHHH	16.54	21945579
267	Phosphorylation	PGSFEYEYAMRWKAL CCCCHHHHHHHHHHH	12.56	21945579
272	Sumoylation	YEYAMRWKALIEMEK HHHHHHHHHHHHHHH	23.97	-
272	Ubiquitination	YEYAMRWKALIEMEK HHHHHHHHHHHHHHH	23.97	-
272	Sumoylation	YEYAMRWKALIEMEK HHHHHHHHHHHHHHH	23.97	-
277	Sulfoxidation	RWKALIEMEKQQQDQ HHHHHHHHHHHHHHH	6.55	28183972
279	Ubiquitination	KALIEMEKQQQDQVD HHHHHHHHHHHHHHH	52.69	21906983
279	Sumoylation	KALIEMEKQQQDQVD HHHHHHHHHHHHHHH	52.69	-
279	Ubiquitination	KALIEMEKQQQDQVD HHHHHHHHHHHHHHH	52.69	21890473
279	Acetylation	KALIEMEKQQQDQVD HHHHHHHHHHHHHHH	52.69	26051181
287	Methylation	QQQDQVDRNIKEARE HHHHHHHHHHHHHHH	48.17	115485365
290	Sumoylation	DQVDRNIKEAREKLE HHHHHHHHHHHHHHH	49.20	-
290	Sumoylation	DQVDRNIKEAREKLE HHHHHHHHHHHHHHH	49.20	-
290	Ubiquitination	DQVDRNIKEAREKLE HHHHHHHHHHHHHHH	49.20	-
290	Succinylation	DQVDRNIKEAREKLE HHHHHHHHHHHHHHH	49.20	23954790
295	Acetylation	NIKEAREKLEMEMEA HHHHHHHHHHHHHHH	44.16	25953088
295	Sumoylation	NIKEAREKLEMEMEA HHHHHHHHHHHHHHH	44.16	-
295	Ubiquitination	NIKEAREKLEMEMEA HHHHHHHHHHHHHHH	44.16	-
295	Sumoylation	NIKEAREKLEMEMEA HHHHHHHHHHHHHHH	44.16	-
298	Sulfoxidation	EAREKLEMEMEAARH HHHHHHHHHHHHHHH	9.59	21406390
304	Methylation	EMEMEAARHEHQVML HHHHHHHHHHHHHHH	42.65	116195867
325	Methylation	RRQEELRRMEELHNQ HHHHHHHHHHHHHHH	49.87	115485373
326	Sulfoxidation	RQEELRRMEELHNQE HHHHHHHHHHHHHHH	3.66	21406390
336	Ubiquitination	LHNQEVQKRKQLELR HHHHHHHHHHHHHHH	67.73	21906983
336	Acetylation	LHNQEVQKRKQLELR HHHHHHHHHHHHHHH	67.73	23236377
338	Ubiquitination	NQEVQKRKQLELRQE HHHHHHHHHHHHHHH	67.29	-
343	Methylation	KRKQLELRQEEERRR HHHHHHHHHHHHHHH	32.27	115485357
364	Methylation	RQQEEMMRRQQEGFK HHHHHHHHHHHHCCC	31.76	115485381
371	Acetylation	RRQQEGFKGTFPDAR HHHHHCCCCCCCCHH	68.82	23749302
371	Sumoylation	RRQQEGFKGTFPDAR HHHHHCCCCCCCCHH	68.82	-
371	Ubiquitination	RRQQEGFKGTFPDAR HHHHHCCCCCCCCHH	68.82	21906983
371	Sumoylation	RRQQEGFKGTFPDAR HHHHHCCCCCCCCHH	68.82	28112733
373	Phosphorylation	QQEGFKGTFPDAREQ HHHCCCCCCCCHHHH	32.36	29214152
378	Acetylation	KGTFPDAREQEIRMG CCCCCCHHHHHHHHH	54.21	19608861
378	Ubiquitination	KGTFPDAREQEIRMG CCCCCCHHHHHHHHH	54.21	19608861
384	Sulfoxidation	AREQEIRMGQMAMGG HHHHHHHHHCCHHCC	5.55	28465586
387	Sulfoxidation	QEIRMGQMAMGGAMG HHHHHHCCHHCCCCC	1.99	28465586
393	Sulfoxidation	QMAMGGAMGINNRGA CCHHCCCCCCCCCCC	6.65	28465586
410	Phosphorylation	PAPVPAGTPAPPGPA CCCCCCCCCCCCCCC	20.55	29255136
418	Phosphorylation	PAPPGPATMMPDGTL CCCCCCCCCCCCCCC	19.69	29255136
424	Phosphorylation	ATMMPDGTLGLTPPT CCCCCCCCCCCCCCC	25.65	29255136
428	Phosphorylation	PDGTLGLTPPTTERF CCCCCCCCCCCCHHH	25.98	29255136
431	Phosphorylation	TLGLTPPTTERFGQA CCCCCCCCCHHHCCC	42.36	29255136
432	Phosphorylation	LGLTPPTTERFGQAA CCCCCCCCHHHCCCC	30.82	29255136
440	Phosphorylation	ERFGQAATMEGIGAI HHHCCCCEECCCCCC	20.83	29255136
441	Sulfoxidation	RFGQAATMEGIGAIG HHCCCCEECCCCCCC	3.68	21406390
450	Phosphorylation	GIGAIGGTPPAFNRA CCCCCCCCCCCCCCC	22.38	29255136
456	Methylation	GTPPAFNRAAPGAEF CCCCCCCCCCCCCCC	26.18	24129315
467	Methylation	GAEFAPNKRRRY--- CCCCCCCCCCCC---	46.34	19608861
467	Acetylation	GAEFAPNKRRRY--- CCCCCCCCCCCC---	46.34	23954790
467	Sumoylation	GAEFAPNKRRRY--- CCCCCCCCCCCC---	46.34	-
467	Ubiquitination	GAEFAPNKRRRY--- CCCCCCCCCCCC---	46.34	19608861
467	Sumoylation	GAEFAPNKRRRY--- CCCCCCCCCCCC---	46.34	28112733
467	Succinylation	GAEFAPNKRRRY--- CCCCCCCCCCCC---	46.34	23954790
471	Phosphorylation	APNKRRRY------- CCCCCCCC-------	22.54	-
471	Acetylation	APNKRRRY------- CCCCCCCC-------	22.54	19608861

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
15	T	Phosphorylation	Kinase	CDK1	P06493	GPS
410	T	Phosphorylation	Kinase	CDK1	P06493	GPS
428	T	Phosphorylation	Kinase	CDK1	P06493	GPS
450	T	Phosphorylation	Kinase	CDK1	P06493	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MD1L1_HUMAN	MAD1L1	physical	16189514
PKHF2_HUMAN	PLEKHF2	physical	16189514
RPA12_HUMAN	ZNRD1	physical	16189514
NONO_HUMAN	NONO	physical	16189514
FXR2_HUMAN	FXR2	physical	16189514
PIN1_HUMAN	PIN1	physical	16189514
SPI1_HUMAN	SPI1	physical	8626664
SMCA4_HUMAN	SMARCA4	physical	18042045
SNF5_HUMAN	SMARCB1	physical	18042045
SMRC1_HUMAN	SMARCC1	physical	18042045
SMRD1_HUMAN	SMARCD1	physical	18042045
SFPQ_HUMAN	SFPQ	physical	18042045
PP1A_HUMAN	PPP1CA	physical	21566083
SIN3A_HUMAN	SIN3A	physical	21566083
HDAC1_HUMAN	HDAC1	physical	21566083
SNRPA_HUMAN	SNRPA	physical	21566083
U2AF2_HUMAN	U2AF2	physical	21566083
PARK7_HUMAN	PARK7	physical	18439917
HDAC1_HUMAN	HDAC1	physical	18439917
HDAC2_HUMAN	HDAC2	physical	18439917
HDAC3_HUMAN	HDAC3	physical	18439917
SFPQ_HUMAN	SFPQ	physical	22939629
SCO2_HUMAN	SCO2	physical	22939629
SPEB_HUMAN	AGMAT	physical	22939629
SCRB2_HUMAN	SCARB2	physical	22939629
SON_HUMAN	SON	physical	22939629
STRN4_HUMAN	STRN4	physical	22939629
TMED9_HUMAN	TMED9	physical	22939629
SLK_HUMAN	SLK	physical	22939629
RALB_HUMAN	RALB	physical	22939629
P5CS_HUMAN	ALDH18A1	physical	22939629
TIF1A_HUMAN	TRIM24	physical	22939629
RM39_HUMAN	MRPL39	physical	22939629
NU133_HUMAN	NUP133	physical	22939629
POP1_HUMAN	POP1	physical	22939629
SQOR_HUMAN	SQRDL	physical	22939629
TPM2_HUMAN	TPM2	physical	22939629
RALA_HUMAN	RALA	physical	22939629
ZC11A_HUMAN	ZC3H11A	physical	22939629
RM41_HUMAN	MRPL41	physical	22939629
RIR2_HUMAN	RRM2	physical	22939629
VPP1_HUMAN	ATP6V0A1	physical	22939629
SUGP2_HUMAN	SUGP2	physical	22939629
RL36_HUMAN	RPL36	physical	22939629
UBAC2_HUMAN	UBAC2	physical	22939629
SRC8_HUMAN	CTTN	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
NONO_HUMAN	NONO	physical	21988832
ORC5_HUMAN	ORC5	physical	21988832
SFPQ_HUMAN	SFPQ	physical	21988832
SYNPO_HUMAN	SYNPO	physical	21988832
YLPM1_HUMAN	YLPM1	physical	21988832
PTBP1_HUMAN	PTBP1	physical	17507659
SFPQ_HUMAN	SFPQ	physical	17507659
NONO_HUMAN	NONO	physical	25416956
PIN1_HUMAN	PIN1	physical	25416956
AAPK2_HUMAN	PRKAA2	physical	25416956
LMO4_HUMAN	LMO4	physical	25416956
PSPC1_HUMAN	PSPC1	physical	25416956
CK068_HUMAN	C11orf68	physical	25416956
NONO_HUMAN	NONO	physical	23555304
COX5A_HUMAN	COX5A	physical	26344197
CSTF2_HUMAN	CSTF2	physical	26344197
DYHC2_HUMAN	DYNC2H1	physical	26344197
HABP4_HUMAN	HABP4	physical	26344197
ROA3_HUMAN	HNRNPA3	physical	26344197
CAF17_HUMAN	IBA57	physical	26344197
NDUS3_HUMAN	NDUFS3	physical	26344197
PO210_HUMAN	NUP210	physical	26344197
NONO_HUMAN	NONO	physical	21516116
TET2_HUMAN	TET2	physical	28514442
PRSR1_HUMAN	PROSER1	physical	28514442
SFPQ_HUMAN	SFPQ	physical	28514442
GLYG2_HUMAN	GYG2	physical	28514442
PSPC1_HUMAN	PSPC1	physical	28514442
SPB7_HUMAN	SERPINB7	physical	28514442
CATH_HUMAN	CTSH	physical	28514442
TGM1_HUMAN	TGM1	physical	28514442
CYTM_HUMAN	CST6	physical	28514442
FBXW7_HUMAN	FBXW7	physical	29150959

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 NONO_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 MET-1; LYS-5; LYS-11; LYS-96;LYS-198 AND LYS-467, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-147 AND THR-450, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND THR-450, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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 THR-428 AND THR-450, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND MASSSPECTROMETRY.	17693683 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND MASSSPECTROMETRY.	17081983 [Abstract]