dbPTM

U2AF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	U2AF2_HUMAN
UniProt AC	P26368
Protein Name	Splicing factor U2AF 65 kDa subunit
Gene Name	U2AF2
Organism	Homo sapiens (Human).
Sequence Length	475
Subcellular Localization	Nucleus.
Protein Description	Plays a role in pre-mRNA splicing and 3'-end processing. [PubMed: 17024186 By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing]
Protein Sequence	MSDFDEFERQLNENKQERDKENRHRKRSHSRSRSRDRKRRSRSRDRRNRDQRSASRDRRRRSKPLTRGAKEEHGGLIRSPRHEKKKKVRKYWDVPPPGFEHITPMQYKAMQAAGQIPATALLPTMTPDGLAVTPTPVPVVGSQMTRQARRLYVGNIPFGITEEAMMDFFNAQMRLGGLTQAPGNPVLAVQINQDKNFAFLEFRSVDETTQAMAFDGIIFQGQSLKIRRPHDYQPLPGMSENPSVYVPGVVSTVVPDSAHKLFIGGLPNYLNDDQVKELLTSFGPLKAFNLVKDSATGLSKGYAFCEYVDINVTDQAIAGLNGMQLGDKKLLVQRASVGAKNATLVSPPSTINQTPVTLQVPGLMSSQVQMGGHPTEVLCLMNMVLPEELLDDEEYEEIVEDVRDECSKYGLVKSIEIPRPVDGVEVPGCGKIFVEFTSVFDCQKAMQGLTGRKFANRVVVTKYCDPDSYHRRDFW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDFDEFER ------CCCHHHHHH	47.16	29255136
2	Acetylation	------MSDFDEFER ------CCCHHHHHH	47.16	20068231
15	Sumoylation	ERQLNENKQERDKEN HHHHHHHHHHHHHHH	47.56	28112733
15	Ubiquitination	ERQLNENKQERDKEN HHHHHHHHHHHHHHH	47.56	33845483
15	Hydroxylation	ERQLNENKQERDKEN HHHHHHHHHHHHHHH	47.56	19574390
20	Ubiquitination	ENKQERDKENRHRKR HHHHHHHHHHHHHHH	64.21	24816145
28	Phosphorylation	ENRHRKRSHSRSRSR HHHHHHHHHHHHHHH	28.93	23882029
30	Phosphorylation	RHRKRSHSRSRSRDR HHHHHHHHHHHHHHH	32.95	23882029
32	Phosphorylation	RKRSHSRSRSRDRKR HHHHHHHHHHHHHHH	37.31	20068231
34	Phosphorylation	RSHSRSRSRDRKRRS HHHHHHHHHHHHHHH	39.52	20068231
41	Phosphorylation	SRDRKRRSRSRDRRN HHHHHHHHHHHHHHH	38.34	20068231
43	Phosphorylation	DRKRRSRSRDRRNRD HHHHHHHHHHHHHHH	39.52	20068231
53	Phosphorylation	RRNRDQRSASRDRRR HHHHHHHHHHHHHHH	25.59	20068231
55	Phosphorylation	NRDQRSASRDRRRRS HHHHHHHHHHHHHHH	35.64	20068231
61	Ubiquitination	ASRDRRRRSKPLTRG HHHHHHHHHCCCCCC	47.42	22053931
62	Phosphorylation	SRDRRRRSKPLTRGA HHHHHHHHCCCCCCC	36.49	20068231
66	Phosphorylation	RRRSKPLTRGAKEEH HHHHCCCCCCCHHHC	35.27	23312004
67	Methylation	RRSKPLTRGAKEEHG HHHCCCCCCCHHHCC	51.24	54560449
70	Ubiquitination	KPLTRGAKEEHGGLI CCCCCCCHHHCCCCC	67.47	33845483
70	2-Hydroxyisobutyrylation	KPLTRGAKEEHGGLI CCCCCCCHHHCCCCC	67.47	-
70	Sumoylation	KPLTRGAKEEHGGLI CCCCCCCHHHCCCCC	67.47	28112733
70	Acetylation	KPLTRGAKEEHGGLI CCCCCCCHHHCCCCC	67.47	19608861
70	Sumoylation	KPLTRGAKEEHGGLI CCCCCCCHHHCCCCC	67.47	-
79	Phosphorylation	EHGGLIRSPRHEKKK HCCCCCCCCCHHHCC	21.20	29255136
84	Ubiquitination	IRSPRHEKKKKVRKY CCCCCHHHCCCHHHH	64.86	24816145
119	Phosphorylation	AAGQIPATALLPTMT HCCCCCCCEECCEEC	16.69	25850435
121	Ubiquitination	GQIPATALLPTMTPD CCCCCCEECCEECCC	5.24	22053931
122	Ubiquitination	QIPATALLPTMTPDG CCCCCEECCEECCCC	2.84	21890473
124	Phosphorylation	PATALLPTMTPDGLA CCCEECCEECCCCCE	33.38	25850435
126	Phosphorylation	TALLPTMTPDGLAVT CEECCEECCCCCEEC	22.24	25106551
133	Phosphorylation	TPDGLAVTPTPVPVV CCCCCEECCCCCCCC	18.81	28176443
135	Phosphorylation	DGLAVTPTPVPVVGS CCCEECCCCCCCCCC	27.79	25850435
142	Phosphorylation	TPVPVVGSQMTRQAR CCCCCCCCHHHHHHH	12.74	25850435
145	Phosphorylation	PVVGSQMTRQARRLY CCCCCHHHHHHHHEE	16.40	25850435
182	Ubiquitination	LGGLTQAPGNPVLAV HCCCCCCCCCCEEEE	33.02	21890473
195	Methylation	AVQINQDKNFAFLEF EEEECCCCCEEEEEE	44.17	116265267
195	Ubiquitination	AVQINQDKNFAFLEF EEEECCCCCEEEEEE	44.17	33845483
225	Ubiquitination	IFQGQSLKIRRPHDY EECCCEEEECCCCCC	39.14	22053931
232	Phosphorylation	KIRRPHDYQPLPGMS EECCCCCCCCCCCCC	14.70	24144214
239	Phosphorylation	YQPLPGMSENPSVYV CCCCCCCCCCCCEEC	39.89	24144214
243	Phosphorylation	PGMSENPSVYVPGVV CCCCCCCCEECCCEE	37.35	24144214
245	Phosphorylation	MSENPSVYVPGVVST CCCCCCEECCCEEEE	12.79	27642862
251	Phosphorylation	VYVPGVVSTVVPDSA EECCCEEEEECCCCC	17.06	24144214
252	Phosphorylation	YVPGVVSTVVPDSAH ECCCEEEEECCCCCH	17.57	24144214
257	Phosphorylation	VSTVVPDSAHKLFIG EEEECCCCCHHHHCC	26.63	24144214
260	Ubiquitination	VVPDSAHKLFIGGLP ECCCCCHHHHCCCCC	44.82	29967540
267	Ubiquitination	KLFIGGLPNYLNDDQ HHHCCCCCCCCCHHH	30.60	21963094
269	Phosphorylation	FIGGLPNYLNDDQVK HCCCCCCCCCHHHHH	12.63	-
276	Hydroxylation	YLNDDQVKELLTSFG CCCHHHHHHHHHHCC	36.69	19574390
276	Ubiquitination	YLNDDQVKELLTSFG CCCHHHHHHHHHHCC	36.69	33845483
280	Phosphorylation	DQVKELLTSFGPLKA HHHHHHHHHCCCHHH	34.33	-
281	Phosphorylation	QVKELLTSFGPLKAF HHHHHHHHCCCHHHH	28.33	20068231
286 (in isoform 2)	Ubiquitination	-	54.81	21890473
286 (in isoform 1)	Ubiquitination	-	54.81	21890473
286	Ubiquitination	LTSFGPLKAFNLVKD HHHCCCHHHHHHHCC	54.81	22817900
292	Succinylation	LKAFNLVKDSATGLS HHHHHHHCCCCCCCC	49.48	23954790
292	Acetylation	LKAFNLVKDSATGLS HHHHHHHCCCCCCCC	49.48	26051181
292	2-Hydroxyisobutyrylation	LKAFNLVKDSATGLS HHHHHHHCCCCCCCC	49.48	-
292	Ubiquitination	LKAFNLVKDSATGLS HHHHHHHCCCCCCCC	49.48	32142685
294	Phosphorylation	AFNLVKDSATGLSKG HHHHHCCCCCCCCCC	23.24	25159151
296	Phosphorylation	NLVKDSATGLSKGYA HHHCCCCCCCCCCEE	42.48	23403867
298	Ubiquitination	VKDSATGLSKGYAFC HCCCCCCCCCCEEEE	4.09	23000965
299	Phosphorylation	KDSATGLSKGYAFCE CCCCCCCCCCEEEEE	25.94	23403867
327	Ubiquitination	LNGMQLGDKKLLVQR CCCCCCCCCEEEEEC	54.21	21963094
343	Phosphorylation	SVGAKNATLVSPPST CCCCCCCEEECCCCC	36.77	26074081
346	Phosphorylation	AKNATLVSPPSTINQ CCCCEEECCCCCCCC	33.92	26074081
349	Phosphorylation	ATLVSPPSTINQTPV CEEECCCCCCCCCCE	45.35	26074081
350	Phosphorylation	TLVSPPSTINQTPVT EEECCCCCCCCCCEE	29.71	26074081
354	Phosphorylation	PPSTINQTPVTLQVP CCCCCCCCCEEEECC	18.42	26074081
358	Ubiquitination	INQTPVTLQVPGLMS CCCCCEEEECCCCCC	5.00	23000965
404	Ubiquitination	EIVEDVRDECSKYGL HHHHHHHHHHHHHCC	62.19	32015554
408	Ubiquitination	DVRDECSKYGLVKSI HHHHHHHHHCCEEEE	55.80	32015554
408	2-Hydroxyisobutyrylation	DVRDECSKYGLVKSI HHHHHHHHHCCEEEE	55.80	-
409	Ubiquitination	VRDECSKYGLVKSIE HHHHHHHHCCEEEEE	10.21	32015554
413	Ubiquitination	CSKYGLVKSIEIPRP HHHHCCEEEEECCCC	51.24	32015554
413	Acetylation	CSKYGLVKSIEIPRP HHHHCCEEEEECCCC	51.24	25953088
413	2-Hydroxyisobutyrylation	CSKYGLVKSIEIPRP HHHHCCEEEEECCCC	51.24	-
414	Phosphorylation	SKYGLVKSIEIPRPV HHHCCEEEEECCCCC	20.27	21712546
427	Ubiquitination	PVDGVEVPGCGKIFV CCCCEECCCCCEEEE	20.89	21963094
429	Glutathionylation	DGVEVPGCGKIFVEF CCEECCCCCEEEEEE	4.03	22555962
431	Ubiquitination	VEVPGCGKIFVEFTS EECCCCCEEEEEEEE	36.73	21963094
437	Phosphorylation	GKIFVEFTSVFDCQK CEEEEEEEEHHHHHH	15.52	21712546
442	Glutathionylation	EFTSVFDCQKAMQGL EEEEHHHHHHHHCCC	2.80	22555962
450	Phosphorylation	QKAMQGLTGRKFANR HHHHCCCCCCCCCCE	41.59	20068231
457	Methylation	TGRKFANRVVVTKYC CCCCCCCEEEEEEEC	21.12	115919221
458	Acetylation	GRKFANRVVVTKYCD CCCCCCEEEEEEECC	3.99	19608861
458	Ubiquitination	GRKFANRVVVTKYCD CCCCCCEEEEEEECC	3.99	23000965
462	Ubiquitination	ANRVVVTKYCDPDSY CCEEEEEEECCCCCC	32.07	23000965
462	Acetylation	ANRVVVTKYCDPDSY CCEEEEEEECCCCCC	32.07	25825284
463	Phosphorylation	NRVVVTKYCDPDSYH CEEEEEEECCCCCCC	7.85	28152594
464	Glutathionylation	RVVVTKYCDPDSYHR EEEEEEECCCCCCCC	6.97	22555962
468	Phosphorylation	TKYCDPDSYHRRDFW EEECCCCCCCCCCCC	28.38	28152594
469	Phosphorylation	KYCDPDSYHRRDFW- EECCCCCCCCCCCC-	13.51	28152594

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
79	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
15	K	Hydroxylation	19574390
Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.
276	K	Hydroxylation	19574390
Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.

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 U2AF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CHIC2_HUMAN	CHIC2	physical	16189514
PUF60_HUMAN	PUF60	physical	16189514
LURA1_HUMAN	LURAP1	physical	16189514
BEND7_HUMAN	BEND7	physical	16189514
DPPA2_HUMAN	DPPA2	physical	16189514
THAP1_HUMAN	THAP1	physical	16189514
BLOM7_HUMAN	KIAA0907	physical	16189514
SRS11_HUMAN	SRSF11	physical	8816452
WT1_HUMAN	WT1	physical	9784496
PRP19_HUMAN	PRPF19	physical	21536736
CDC5L_HUMAN	CDC5L	physical	21536736
RPB1_HUMAN	POLR2A	physical	21536736
U520_HUMAN	SNRNP200	physical	22939629
ZCHC8_HUMAN	ZCCHC8	physical	22939629
VDAC2_HUMAN	VDAC2	physical	22939629
POC1A_HUMAN	POC1A	physical	22939629
SNRPA_HUMAN	SNRPA	physical	22365833
U2AF1_HUMAN	U2AF1	physical	22365833
CHERP_HUMAN	CHERP	physical	22365833
PUF60_HUMAN	PUF60	physical	22365833
CCAR1_HUMAN	CCAR1	physical	22365833
RBM10_HUMAN	RBM10	physical	22365833
SF01_HUMAN	SF1	physical	22365833
SUGP1_HUMAN	SUGP1	physical	22365833
RBM39_HUMAN	RBM39	physical	22365833
ROA0_HUMAN	HNRNPA0	physical	22365833
PRPF3_HUMAN	PRPF3	physical	22365833
DDX17_HUMAN	DDX17	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
S30BP_HUMAN	SAP30BP	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
HNRPD_HUMAN	HNRNPD	physical	22365833
QKI_HUMAN	QKI	physical	22365833
KHDR3_HUMAN	KHDRBS3	physical	22365833
KHDR1_HUMAN	KHDRBS1	physical	22365833
RFOX2_HUMAN	RBFOX2	physical	22365833
RBM5_HUMAN	RBM5	physical	22569250
IL7RA_HUMAN	IL7R	physical	23151878
TERF1_HUMAN	TERF1	physical	24389012
PUF60_HUMAN	PUF60	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
CHD8_HUMAN	CHD8	physical	26344197
HUWE1_HUMAN	HUWE1	physical	26344197
LC7L2_HUMAN	LUC7L2	physical	26344197
NONO_HUMAN	NONO	physical	26344197
PSPC1_HUMAN	PSPC1	physical	26344197
PUF60_HUMAN	PUF60	physical	26344197
RAGP1_HUMAN	RANGAP1	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
SNRPA_HUMAN	SNRPA	physical	21516116
U2AF1_HUMAN	U2AF1	physical	21516116
U2AF1_HUMAN	U2AF1	physical	26641092
SRSF1_HUMAN	SRSF1	physical	26641092
SRSF3_HUMAN	SRSF3	physical	26641092
TRA2B_HUMAN	TRA2B	physical	26641092
KHDR1_HUMAN	KHDRBS1	physical	26641092
ACINU_HUMAN	ACIN1	physical	26641092
AHNK_HUMAN	AHNAK	physical	26641092
KAD2_HUMAN	AK2	physical	26641092
AN32A_HUMAN	ANP32A	physical	26641092
ANXA1_HUMAN	ANXA1	physical	26641092
ANXA2_HUMAN	ANXA2	physical	26641092
ANXA5_HUMAN	ANXA5	physical	26641092
ANXA6_HUMAN	ANXA6	physical	26641092
APOA1_HUMAN	APOA1	physical	26641092
GDIR1_HUMAN	ARHGDIA	physical	26641092
GDIR2_HUMAN	ARHGDIB	physical	26641092
ARC1B_HUMAN	ARPC1B	physical	26641092
U520_HUMAN	SNRNP200	physical	26641092
PUR9_HUMAN	ATIC	physical	26641092
DX39B_HUMAN	DDX39B	physical	26641092
CHTOP_HUMAN	CHTOP	physical	26641092
CACO2_HUMAN	CALCOCO2	physical	26641092
CALR_HUMAN	CALR	physical	26641092
CALX_HUMAN	CANX	physical	26641092
CAP1_HUMAN	CAP1	physical	26641092
CAPZB_HUMAN	CAPZB	physical	26641092
CCAR1_HUMAN	CCAR1	physical	26641092
TCPB_HUMAN	CCT2	physical	26641092
TCPZ_HUMAN	CCT6A	physical	26641092
TCPQ_HUMAN	CCT8	physical	26641092
CDC37_HUMAN	CDC37	physical	26641092
CDC5L_HUMAN	CDC5L	physical	26641092
CDV3_HUMAN	CDV3	physical	26641092
COF1_HUMAN	CFL1	physical	26641092
CLIC1_HUMAN	CLIC1	physical	26641092
CLH1_HUMAN	CLTC	physical	26641092
CNN2_HUMAN	CNN2	physical	26641092
COR1A_HUMAN	CORO1A	physical	26641092
CPSF6_HUMAN	CPSF6	physical	26641092
SYDC_HUMAN	DARS	physical	26641092
DDX17_HUMAN	DDX17	physical	26641092
DDX21_HUMAN	DDX21	physical	26641092
DDX5_HUMAN	DDX5	physical	26641092
DHX15_HUMAN	DHX15	physical	26641092
DHX9_HUMAN	DHX9	physical	26641092
EF1A1_HUMAN	EEF1A1	physical	26641092
EF1D_HUMAN	EEF1D	physical	26641092
EF2_HUMAN	EEF2	physical	26641092
U5S1_HUMAN	EFTUD2	physical	26641092
EIF3A_HUMAN	EIF3A	physical	26641092
IF4A1_HUMAN	EIF4A1	physical	26641092
IF4A3_HUMAN	EIF4A3	physical	26641092
IF4H_HUMAN	EIF4H	physical	26641092
IF5A1_HUMAN	EIF5A	physical	26641092
ELAV1_HUMAN	ELAVL1	physical	26641092
SYEP_HUMAN	EPRS	physical	26641092
EVL_HUMAN	EVL	physical	26641092
EZRI_HUMAN	EZR	physical	26641092
FABP5_HUMAN	FABP5	physical	26641092
F107B_HUMAN	FAM107B	physical	26641092
ESYT1_HUMAN	ESYT1	physical	26641092
FBRL_HUMAN	FBL	physical	26641092
FLOT1_HUMAN	FLOT1	physical	26641092
FLOT2_HUMAN	FLOT2	physical	26641092
FUBP1_HUMAN	FUBP1	physical	26641092
SRS10_HUMAN	SRSF10	physical	26641092
GANAB_HUMAN	GANAB	physical	26641092
GBP1_HUMAN	GBP1	physical	26641092
GBP2_HUMAN	GBP2	physical	26641092
GDIB_HUMAN	GDI2	physical	26641092
DHE3_HUMAN	GLUD1	physical	26641092
GMFG_HUMAN	GMFG	physical	26641092
GNAI2_HUMAN	GNAI2	physical	26641092
RACK1_HUMAN	GNB2L1	physical	26641092
AATM_HUMAN	GOT2	physical	26641092
G6PI_HUMAN	GPI	physical	26641092
H2AJ_HUMAN	H2AFJ	physical	26641092
SARNP_HUMAN	SARNP	physical	26641092
HCLS1_HUMAN	HCLS1	physical	26641092
HDGF_HUMAN	HDGF	physical	26641092
HINT1_HUMAN	HINT1	physical	26641092
HXK1_HUMAN	HK1	physical	26641092
HMGB1_HUMAN	HMGB1	physical	26641092
HMGB2_HUMAN	HMGB2	physical	26641092
JUPI2_HUMAN	HN1L	physical	26641092
ROA0_HUMAN	HNRNPA0	physical	26641092
ROA1_HUMAN	HNRNPA1	physical	26641092
ROA2_HUMAN	HNRNPA2B1	physical	26641092
ROA3_HUMAN	HNRNPA3	physical	26641092
ROAA_HUMAN	HNRNPAB	physical	26641092
HNRPC_HUMAN	HNRNPC	physical	26641092
HNRPD_HUMAN	HNRNPD	physical	26641092
HNRPF_HUMAN	HNRNPF	physical	26641092
HNRH1_HUMAN	HNRNPH1	physical	26641092
HNRPK_HUMAN	HNRNPK	physical	26641092
HNRPL_HUMAN	HNRNPL	physical	26641092
HNRPM_HUMAN	HNRNPM	physical	26641092
HNRPR_HUMAN	HNRNPR	physical	26641092
HNRPU_HUMAN	HNRNPU	physical	26641092
HS90A_HUMAN	HSP90AA1	physical	26641092
HS90B_HUMAN	HSP90AB1	physical	26641092
ENPL_HUMAN	HSP90B1	physical	26641092
GRP78_HUMAN	HSPA5	physical	26641092
HSP7C_HUMAN	HSPA8	physical	26641092
GRP75_HUMAN	HSPA9	physical	26641092
CH60_HUMAN	HSPD1	physical	26641092
CH10_HUMAN	HSPE1	physical	26641092
HS105_HUMAN	HSPH1	physical	26641092
IF16_HUMAN	IFI16	physical	26641092
ILF2_HUMAN	ILF2	physical	26641092
ILF3_HUMAN	ILF3	physical	26641092
IMDH2_HUMAN	IMPDH2	physical	26641092
IQGA1_HUMAN	IQGAP1	physical	26641092
FUBP2_HUMAN	KHSRP	physical	26641092
VIR_HUMAN	KIAA1429	physical	26641092
KIFC1_HUMAN	KIFC1	physical	26641092
IMB1_HUMAN	KPNB1	physical	26641092
AMPL_HUMAN	LAP3	physical	26641092
LARP1_HUMAN	LARP1	physical	26641092
LASP1_HUMAN	LASP1	physical	26641092
PLSL_HUMAN	LCP1	physical	26641092
LEG1_HUMAN	LGALS1	physical	26641092
LRC59_HUMAN	LRRC59	physical	26641092
LRRF1_HUMAN	LRRFIP1	physical	26641092
LSP1_HUMAN	LSP1	physical	26641092
MARE1_HUMAN	MAPRE1	physical	26641092
MATR3_HUMAN	MATR3	physical	26641092
MDHM_HUMAN	MDH2	physical	26641092
MOES_HUMAN	MSN	physical	26641092
C1TC_HUMAN	MTHFD1	physical	26641092
MVP_HUMAN	MVP	physical	26641092
NAMPT_HUMAN	NAMPT	physical	26641092
NCBP1_HUMAN	NCBP1	physical	26641092
NUCL_HUMAN	NCL	physical	26641092
NCOA5_HUMAN	NCOA5	physical	26641092
NONO_HUMAN	NONO	physical	26641092
NPM_HUMAN	NPM1	physical	26641092
NUMA1_HUMAN	NUMA1	physical	26641092
NUSAP_HUMAN	NUSAP1	physical	26641092
PDIA1_HUMAN	P4HB	physical	26641092
PA2G4_HUMAN	PA2G4	physical	26641092
PABP1_HUMAN	PABPC1	physical	26641092
PABP4_HUMAN	PABPC4	physical	26641092
PABP2_HUMAN	PABPN1	physical	26641092
PUR6_HUMAN	PAICS	physical	26641092
PARK7_HUMAN	PARK7	physical	26641092
PCBP1_HUMAN	PCBP1	physical	26641092
PCNA_HUMAN	PCNA	physical	26641092
HAP28_HUMAN	PDAP1	physical	26641092
PDIA3_HUMAN	PDIA3	physical	26641092
PDIA6_HUMAN	PDIA6	physical	26641092
PGK1_HUMAN	PGK1	physical	26641092
PHB_HUMAN	PHB	physical	26641092
PHB2_HUMAN	PHB2	physical	26641092
KPYM_HUMAN	PKM	physical	26641092
PININ_HUMAN	PNN	physical	26641092
PDIP3_HUMAN	POLDIP3	physical	26641092
PPIA_HUMAN	PPIA	physical	26641092
PPIB_HUMAN	PPIB	physical	26641092
PRDX1_HUMAN	PRDX1	physical	26641092
PRDX2_HUMAN	PRDX2	physical	26641092
PRP19_HUMAN	PRPF19	physical	26641092
PRP8_HUMAN	PRPF8	physical	26641092
PSA4_HUMAN	PSMA4	physical	26641092
PSMD2_HUMAN	PSMD2	physical	26641092
PSME1_HUMAN	PSME1	physical	26641092
PSME2_HUMAN	PSME2	physical	26641092
PSPC1_HUMAN	PSPC1	physical	26641092
PTBP1_HUMAN	PTBP1	physical	26641092
PTPRC_HUMAN	PTPRC	physical	26641092
RAB7A_HUMAN	RAB7A	physical	26641092
RAC2_HUMAN	RAC2	physical	26641092
RALY_HUMAN	RALY	physical	26641092
RAN_HUMAN	RAN	physical	26641092
RBMX_HUMAN	RBMX	physical	26641092
RHOA_HUMAN	RHOA	physical	26641092
RNPS1_HUMAN	RNPS1	physical	26641092
RPN1_HUMAN	RPN1	physical	26641092
RUVB1_HUMAN	RUVBL1	physical	26641092
S10A6_HUMAN	S100A6	physical	26641092
SAMH1_HUMAN	SAMHD1	physical	26641092
SAP18_HUMAN	SAP18	physical	26641092
SEPT9_HUMAN	SEPT9	physical	26641092
PAIRB_HUMAN	SERBP1	physical	26641092
SF01_HUMAN	SF1	physical	26641092
SF3A1_HUMAN	SF3A1	physical	26641092
SF3B1_HUMAN	SF3B1	physical	26641092
SF3B2_HUMAN	SF3B2	physical	26641092
SF3B3_HUMAN	SF3B3	physical	26641092
SFPQ_HUMAN	SFPQ	physical	26641092
SRSF2_HUMAN	SRSF2	physical	26641092
SRSF4_HUMAN	SRSF4	physical	26641092
SRSF6_HUMAN	SRSF6	physical	26641092
SRSF7_HUMAN	SRSF7	physical	26641092
SRSF9_HUMAN	SRSF9	physical	26641092
GLYM_HUMAN	SHMT2	physical	26641092
ADT2_HUMAN	SLC25A5	physical	26641092
4F2_HUMAN	SLC3A2	physical	26641092
NHRF1_HUMAN	SLC9A3R1	physical	26641092
SND1_HUMAN	SND1	physical	26641092
RU17_HUMAN	SNRNP70	physical	26641092
RU2A_HUMAN	SNRPA1	physical	26641092
SMD1_HUMAN	SNRPD1	physical	26641092
SNW1_HUMAN	SNW1	physical	26641092
SON_HUMAN	SON	physical	26641092
SPTN1_HUMAN	SPTAN1	physical	26641092
SRRM1_HUMAN	SRRM1	physical	26641092
SRRM2_HUMAN	SRRM2	physical	26641092
F10A1_HUMAN	ST13	physical	26641092
STAT1_HUMAN	STAT1	physical	26641092
STIP1_HUMAN	STIP1	physical	26641092
HNRPQ_HUMAN	SYNCRIP	physical	26641092
TAGL2_HUMAN	TAGLN2	physical	26641092
TALDO_HUMAN	TALDO1	physical	26641092
THOC4_HUMAN	ALYREF	physical	26641092
TR150_HUMAN	THRAP3	physical	26641092
TKT_HUMAN	TKT	physical	26641092
TLN1_HUMAN	TLN1	physical	26641092
LAP2A_HUMAN	TMPO	physical	26641092
LAP2B_HUMAN	TMPO	physical	26641092
TPIS_HUMAN	TPI1	physical	26641092
TRA2A_HUMAN	TRA2A	physical	26641092
TIF1B_HUMAN	TRIM28	physical	26641092
EFTU_HUMAN	TUFM	physical	26641092
U2AF2_HUMAN	U2AF2	physical	26641092
UBA1_HUMAN	UBA1	physical	26641092
RENT1_HUMAN	UPF1	physical	26641092
TERA_HUMAN	VCP	physical	26641092
VDAC1_HUMAN	VDAC1	physical	26641092
SYWC_HUMAN	WARS	physical	26641092
WDR1_HUMAN	WDR1	physical	26641092
XRCC6_HUMAN	XRCC6	physical	26641092
YBOX1_HUMAN	YBX1	physical	26641092
1433E_HUMAN	YWHAE	physical	26641092
1433Z_HUMAN	YWHAZ	physical	26641092
ZC3HD_HUMAN	ZC3H13	physical	26641092
ZYX_HUMAN	ZYX	physical	26641092
SCAFB_HUMAN	SCAF11	physical	28514442
CLASR_HUMAN	CLASRP	physical	28514442
SRS12_HUMAN	SRSF12	physical	28514442
SRPK1_HUMAN	SRPK1	physical	28514442
GPTC8_HUMAN	GPATCH8	physical	28514442
SRPK2_HUMAN	SRPK2	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
SFR19_HUMAN	SCAF1	physical	28514442
PININ_HUMAN	PNN	physical	28514442
CLK3_HUMAN	CLK3	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
SRS10_HUMAN	SRSF10	physical	28514442
GPT11_HUMAN	GPATCH11	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28514442
SRSF1_HUMAN	SRSF1	physical	28514442
TRA2A_HUMAN	TRA2A	physical	28514442
CLK2_HUMAN	CLK2	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442
SR140_HUMAN	U2SURP	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
SF3B2_HUMAN	SF3B2	physical	28514442
BCLF1_HUMAN	BCLAF1	physical	28514442
SF3B1_HUMAN	SF3B1	physical	28514442
RT29_HUMAN	DAP3	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
TRA2B_HUMAN	TRA2B	physical	28514442
ZCHC3_HUMAN	ZCCHC3	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
RT09_HUMAN	MRPS9	physical	28514442
RL10A_HUMAN	RPL10A	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 U2AF2_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 LYS-70 AND LYS-462, AND MASSSPECTROMETRY.	19608861 [Abstract]
Hydroxylation
Reference	PubMed
"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associatedwith RNA splicing."; Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B.,Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M.,Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J.,Boettger A.; Science 325:90-93(2009). Cited for: FUNCTION, AND HYDROXYLATION AT LYS-15 AND LYS-276.	19574390 [Abstract]
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-79, AND MASSSPECTROMETRY.	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-79, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASSSPECTROMETRY.	18187866 [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 SER-79, AND MASSSPECTROMETRY.	17287340 [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 SER-79, AND MASSSPECTROMETRY.	17924679 [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 SER-2; SER-53; SER-55 ANDSER-79, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.	16097034 [Abstract]

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