dbPTM

RUNX1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RUNX1_HUMAN
UniProt AC	Q01196
Protein Name	Runt-related transcription factor 1
Gene Name	RUNX1
Organism	Homo sapiens (Human).
Sequence Length	453
Subcellular Localization	Nucleus.
Protein Description	Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis. [PubMed: 17431401 Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter]
Protein Sequence	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPPYPGSSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNSPTNMAPSARLEEAVWRPY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3 (in isoform 8)	Phosphorylation	-	3.63	26552605
5 (in isoform 8)	Phosphorylation	-	10.00	26552605
8	Phosphorylation	MRIPVDASTSRRFTP CCCCCCCCCCCCCCC	23.58	26074081
9	Phosphorylation	RIPVDASTSRRFTPP CCCCCCCCCCCCCCC	28.15	26074081
9 (in isoform 8)	Phosphorylation	-	28.15	26552605
10	Phosphorylation	IPVDASTSRRFTPPS CCCCCCCCCCCCCCC	20.97	26074081
12 (in isoform 8)	Phosphorylation	-	39.29	26552605
13 (in isoform 8)	Phosphorylation	-	13.46	26552605
14	Phosphorylation	ASTSRRFTPPSTALS CCCCCCCCCCCCCCC	32.26	29255136
17	Phosphorylation	SRRFTPPSTALSPGK CCCCCCCCCCCCCCC	27.76	23401153
17 (in isoform 9)	Phosphorylation	-	27.76	15302935
18	Phosphorylation	RRFTPPSTALSPGKM CCCCCCCCCCCCCCH	37.07	23401153
19	Ubiquitination	RFTPPSTALSPGKMS CCCCCCCCCCCCCHH	15.47	21890473
21	Phosphorylation	TPPSTALSPGKMSEA CCCCCCCCCCCHHCC	29.19	29255136
24	Acetylation	STALSPGKMSEALPL CCCCCCCCHHCCCCC	42.51	19608861
24	Ubiquitination	STALSPGKMSEALPL CCCCCCCCHHCCCCC	42.51	19608861
26	Phosphorylation	ALSPGKMSEALPLGA CCCCCCHHCCCCCCC	24.17	28787133
41 (in isoform 8)	Phosphorylation	-	14.35	15302935
43	Acetylation	AGAALAGKLRSGDRS HHHHHHHHCCCCCCC	34.81	19608861
43	Ubiquitination	AGAALAGKLRSGDRS HHHHHHHHCCCCCCC	34.81	23000965
43 (in isoform 1)	Ubiquitination	-	34.81	21890473
43 (in isoform 2)	Ubiquitination	-	34.81	21890473
43 (in isoform 3)	Ubiquitination	-	34.81	21890473
43 (in isoform 4)	Ubiquitination	-	34.81	21890473
43 (in isoform 5)	Ubiquitination	-	34.81	21890473
43 (in isoform 6)	Ubiquitination	-	34.81	21890473
46	Phosphorylation	ALAGKLRSGDRSMVE HHHHHCCCCCCCCEE	56.32	30576142
46 (in isoform 7)	Ubiquitination	-	56.32	21890473
46 (in isoform 9)	Ubiquitination	-	56.32	21890473
50	Phosphorylation	KLRSGDRSMVEVLAD HCCCCCCCCEEHHHC	31.74	30576142
51	Acetylation	LRSGDRSMVEVLADH CCCCCCCCEEHHHCC	2.87	19608861
51	Sulfoxidation	LRSGDRSMVEVLADH CCCCCCCCEEHHHCC	2.87	21406390
51	Ubiquitination	LRSGDRSMVEVLADH CCCCCCCCEEHHHCC	2.87	19608861
51 (in isoform 8)	Ubiquitination	-	2.87	-
57	Ubiquitination	SMVEVLADHPGELVR CCEEHHHCCCCCEEE	44.33	21890473
58	Ubiquitination	MVEVLADHPGELVRT CEEHHHCCCCCEEEC	27.02	21890473
58 (in isoform 10)	Ubiquitination	-	27.02	21890473
65	Phosphorylation	HPGELVRTDSPNFLC CCCCEEECCCCCCEE	33.09	28450419
67	Phosphorylation	GELVRTDSPNFLCSV CCEEECCCCCCEEEE	22.56	28450419
70	Ubiquitination	VRTDSPNFLCSVLPT EECCCCCCEEEECCC	9.15	21890473
70	Acetylation	VRTDSPNFLCSVLPT EECCCCCCEEEECCC	9.15	19608861
70	Ubiquitination	VRTDSPNFLCSVLPT EECCCCCCEEEECCC	9.15	23000965
70 (in isoform 8)	Ubiquitination	-	9.15	21890473
83	Ubiquitination	PTHWRCNKTLPIAFK CCCCCCCCCCCEEEE	55.88	29967540
83 (in isoform 11)	Ubiquitination	-	55.88	21890473
84	Phosphorylation	THWRCNKTLPIAFKV CCCCCCCCCCEEEEE	24.63	28555341
90	Ubiquitination	KTLPIAFKVVALGDV CCCCEEEEEEEECCC	27.12	-
101	Ubiquitination	LGDVPDGTLVTVMAG ECCCCCCCEEEEEEC	25.99	23000965
110	Ubiquitination	VTVMAGNDENYSAEL EEEEECCCCCHHHHH	44.60	29967540
110 (in isoform 8)	Ubiquitination	-	44.60	-
125	Acetylation	RNATAAMKNQVARFN HHHHHHHHHHHHHHC	39.23	25953088
125	Ubiquitination	RNATAAMKNQVARFN HHHHHHHHHHHHHHC	39.23	23000965
139	Ubiquitination	NDLRFVGRSGRGKSF CCEEEECCCCCCCEE	30.54	23000965
140	Ubiquitination	DLRFVGRSGRGKSFT CEEEECCCCCCCEEE	27.24	23000965
144	Acetylation	VGRSGRGKSFTLTIT ECCCCCCCEEEEEEE	40.82	15138260
144	Ubiquitination	VGRSGRGKSFTLTIT ECCCCCCCEEEEEEE	40.82	-
145	O-linked_Glycosylation	GRSGRGKSFTLTITV CCCCCCCEEEEEEEE	26.70	27655845
145	Phosphorylation	GRSGRGKSFTLTITV CCCCCCCEEEEEEEE	26.70	55456607
147	Phosphorylation	SGRGKSFTLTITVFT CCCCCEEEEEEEEEC	30.04	55456609
149	Phosphorylation	RGKSFTLTITVFTNP CCCEEEEEEEEECCC	16.14	55456605
151	Phosphorylation	KSFTLTITVFTNPPQ CEEEEEEEEECCCCC	12.34	-
152	Ubiquitination	SFTLTITVFTNPPQV EEEEEEEEECCCCCC	5.01	23000965
152 (in isoform 8)	Ubiquitination	-	5.01	-
158	Ubiquitination	TVFTNPPQVATYHRA EEECCCCCCEEEEEE	38.44	23000965
158 (in isoform 7)	Ubiquitination	-	38.44	21890473
164	Ubiquitination	PQVATYHRAIKITVD CCCEEEEEEEEEECC	27.82	21890473
167	Ubiquitination	ATYHRAIKITVDGPR EEEEEEEEEECCCCC	31.19	-
169	Phosphorylation	YHRAIKITVDGPREP EEEEEEEECCCCCCC	13.93	24043423
182	Acetylation	EPRRHRQKLDDQTKP CCCCCHHHCCCCCCC	54.57	25953088
182	Ubiquitination	EPRRHRQKLDDQTKP CCCCCHHHCCCCCCC	54.57	23000965
187	Phosphorylation	RQKLDDQTKPGSLSF HHHCCCCCCCCCCCH	46.32	23186163
188	Acetylation	QKLDDQTKPGSLSFS HHCCCCCCCCCCCHH	41.57	23749302
188	Ubiquitination	QKLDDQTKPGSLSFS HHCCCCCCCCCCCHH	41.57	23000965
188 (in isoform 1)	Ubiquitination	-	41.57	21890473
188 (in isoform 2)	Ubiquitination	-	41.57	21890473
188 (in isoform 3)	Ubiquitination	-	41.57	21890473
188 (in isoform 4)	Ubiquitination	-	41.57	21890473
191	Phosphorylation	DDQTKPGSLSFSERL CCCCCCCCCCHHHHH	29.39	23401153
191 (in isoform 9)	Ubiquitination	-	29.39	21890473
193	Phosphorylation	QTKPGSLSFSERLSE CCCCCCCCHHHHHHH	28.55	23401153
194 (in isoform 8)	Ubiquitination	-	12.18	-
195	Phosphorylation	KPGSLSFSERLSELE CCCCCCHHHHHHHHH	20.59	30576142
196	Ubiquitination	PGSLSFSERLSELEQ CCCCCHHHHHHHHHH	56.48	23000965
197	Ubiquitination	GSLSFSERLSELEQL CCCCHHHHHHHHHHH	42.17	23000965
199	Phosphorylation	LSFSERLSELEQLRR CCHHHHHHHHHHHHH	46.48	4114501
202	Ubiquitination	SERLSELEQLRRTAM HHHHHHHHHHHHHHH	43.44	21890473
203	Ubiquitination	ERLSELEQLRRTAMR HHHHHHHHHHHHHHH	53.55	21890473
203 (in isoform 10)	Ubiquitination	-	53.55	21890473
206	Methylation	SELEQLRRTAMRVSP HHHHHHHHHHHHHCC	35.11	-
207	Phosphorylation	ELEQLRRTAMRVSPH HHHHHHHHHHHHCCC	20.55	23927012
209	Ubiquitination	EQLRRTAMRVSPHHP HHHHHHHHHHCCCCC	4.26	23000965
209 (in isoform 8)	Ubiquitination	-	4.26	-
210	Methylation	QLRRTAMRVSPHHPA HHHHHHHHHCCCCCC	24.25	-
212	Phosphorylation	RRTAMRVSPHHPAPT HHHHHHHCCCCCCCC	14.25	23401153
215	Ubiquitination	AMRVSPHHPAPTPNP HHHHCCCCCCCCCCC	24.49	21890473
215	Ubiquitination	AMRVSPHHPAPTPNP HHHHCCCCCCCCCCC	24.49	21890473
215 (in isoform 8)	Ubiquitination	-	24.49	21890473
219	Phosphorylation	SPHHPAPTPNPRASL CCCCCCCCCCCCCCC	37.49	23927012
223	Methylation	PAPTPNPRASLNHST CCCCCCCCCCCCCCC	43.37	-
225	Phosphorylation	PTPNPRASLNHSTAF CCCCCCCCCCCCCCC	30.86	28450419
229	Phosphorylation	PRASLNHSTAFNPQP CCCCCCCCCCCCCCC	21.98	24260401
230	Phosphorylation	RASLNHSTAFNPQPQ CCCCCCCCCCCCCCC	27.93	28450419
238	Phosphorylation	AFNPQPQSQMQDTRQ CCCCCCCHHCCCCCC	34.01	23312004
238 (in isoform 3)	Phosphorylation	-	34.01	26714015
239	Phosphorylation	FNPQPQSQMQDTRQI CCCCCCHHCCCCCCC	28.45	32645325
249	Phosphorylation	DTRQIQPSPPWSYDQ CCCCCCCCCCCCCCC	27.50	22115753
253	Phosphorylation	IQPSPPWSYDQSYQY CCCCCCCCCCCCCCC	25.30	22115753
254	Phosphorylation	QPSPPWSYDQSYQYL CCCCCCCCCCCCCCC	17.71	19690332
257	Phosphorylation	PPWSYDQSYQYLGSI CCCCCCCCCCCCCCC	16.00	28464451
258	Phosphorylation	PWSYDQSYQYLGSIA CCCCCCCCCCCCCCC	8.78	28464451
260	Phosphorylation	SYDQSYQYLGSIASP CCCCCCCCCCCCCCC	12.56	28796482
263	Phosphorylation	QSYQYLGSIASPSVH CCCCCCCCCCCCCCC	16.64	28796482
266	Phosphorylation	QYLGSIASPSVHPAT CCCCCCCCCCCCCCC	18.94	22115753
268	Phosphorylation	LGSIASPSVHPATPI CCCCCCCCCCCCCCC	30.48	23401153
273	Phosphorylation	SPSVHPATPISPGRA CCCCCCCCCCCCCCC	26.13	22115753
276	Phosphorylation	VHPATPISPGRASGM CCCCCCCCCCCCCCC	23.62	23401153
281	Phosphorylation	PISPGRASGMTTLSA CCCCCCCCCCCHHHH	27.95	26074081
284	Phosphorylation	PGRASGMTTLSAELS CCCCCCCCHHHHHHH	28.27	20068231
285	Phosphorylation	GRASGMTTLSAELSS CCCCCCCHHHHHHHH	15.15	20068231
287	Phosphorylation	ASGMTTLSAELSSRL CCCCCHHHHHHHHHC	20.01	26074081
291	Phosphorylation	TTLSAELSSRLSTAP CHHHHHHHHHCCCCC	12.62	20068231
292	Phosphorylation	TLSAELSSRLSTAPD HHHHHHHHHCCCCCC	50.28	20068231
295	Phosphorylation	AELSSRLSTAPDLTA HHHHHHCCCCCCCCC	22.78	29255136
296	Phosphorylation	ELSSRLSTAPDLTAF HHHHHCCCCCCCCCC	46.96	29255136
304	Phosphorylation	APDLTAFSDPRQFPA CCCCCCCCCCCCCCC	44.21	21815630
319	Dimethylation	LPSISDPRMHYPGAF CCCCCCCCCCCCCCE	29.51	-
319	Methylation	LPSISDPRMHYPGAF CCCCCCCCCCCCCCE	29.51	-
322	Phosphorylation	ISDPRMHYPGAFTYS CCCCCCCCCCCEECC	8.26	28122231
327	Phosphorylation	MHYPGAFTYSPTPVT CCCCCCEECCCCCCC	23.66	26074081
328	Phosphorylation	HYPGAFTYSPTPVTS CCCCCEECCCCCCCC	13.24	26074081
329	Phosphorylation	YPGAFTYSPTPVTSG CCCCEECCCCCCCCC	21.17	46162909
331	Phosphorylation	GAFTYSPTPVTSGIG CCEECCCCCCCCCCE	25.17	46162933
334	Phosphorylation	TYSPTPVTSGIGIGM ECCCCCCCCCCEECC	23.57	26074081
335	Phosphorylation	YSPTPVTSGIGIGMS CCCCCCCCCCEECCC	28.75	26074081
346	Phosphorylation	IGMSAMGSATRYHTY ECCCCCCCCCEECCC	17.24	27251275
361	O-linked_Glycosylation	LPPPYPGSSQAQGGP CCCCCCCCCCCCCCC	18.12	27655845
361	Phosphorylation	LPPPYPGSSQAQGGP CCCCCCCCCCCCCCC	18.12	27251275
362	O-linked_Glycosylation	PPPYPGSSQAQGGPF CCCCCCCCCCCCCCC	35.14	27655845
362	Phosphorylation	PPPYPGSSQAQGGPF CCCCCCCCCCCCCCC	35.14	27251275
372	Phosphorylation	QGGPFQASSPSYHLY CCCCCCCCCCCEEEE	31.81	27251275
373	Phosphorylation	GGPFQASSPSYHLYY CCCCCCCCCCEEEEE	22.38	27251275
375	Phosphorylation	PFQASSPSYHLYYGA CCCCCCCCEEEEEEC	27.42	27251275
376	Phosphorylation	FQASSPSYHLYYGAS CCCCCCCEEEEEECC	10.14	27251275
383	Phosphorylation	YHLYYGASAGSYQFS EEEEEECCCCCEEEE	28.88	27251275
386	Phosphorylation	YYGASAGSYQFSMVG EEECCCCCEEEEECC	18.58	27251275
390	Phosphorylation	SAGSYQFSMVGGERS CCCCEEEEECCCCCC	9.31	26074081
397	Phosphorylation	SMVGGERSPPRILPP EECCCCCCCCCCCCC	34.65	26074081
406	Phosphorylation	PRILPPCTNASTGSA CCCCCCCCCCCCCCH	39.32	26552605
409	Phosphorylation	LPPCTNASTGSALLN CCCCCCCCCCCHHCC	35.06	26552605
410	Phosphorylation	PPCTNASTGSALLNP CCCCCCCCCCHHCCC	32.51	26552605
412	Phosphorylation	CTNASTGSALLNPSL CCCCCCCCHHCCCCC	18.81	26552605
418	Phosphorylation	GSALLNPSLPNQSDV CCHHCCCCCCCCCCC	56.22	26552605
423	Phosphorylation	NPSLPNQSDVVEAEG CCCCCCCCCCEECCC	38.73	30576142
431	Phosphorylation	DVVEAEGSHSNSPTN CCEECCCCCCCCCCC	18.43	30576142
433	Phosphorylation	VEAEGSHSNSPTNMA EECCCCCCCCCCCCC	40.47	30576142
435	Phosphorylation	AEGSHSNSPTNMAPS CCCCCCCCCCCCCCC	35.80	7835892
437	Phosphorylation	GSHSNSPTNMAPSAR CCCCCCCCCCCCCHH	37.13	30576142
442	Phosphorylation	SPTNMAPSARLEEAV CCCCCCCCHHHHHHH	19.24	26552605
453	Phosphorylation	EEAVWRPY------- HHHHCCCC-------	23.71	26074081
458 (in isoform 2)	Phosphorylation	-		20068231
460 (in isoform 2)	Phosphorylation	-		20068231

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
48	S	Phosphorylation	Kinase	CDK1	P06493	PSP
48	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
207	T	Phosphorylation	Kinase	PAK4	O96013	PSP
249	S	Phosphorylation	Kinase	ERK-SUBFAMILY	-	GPS
249	S	Phosphorylation	Kinase	MAPK3	P21708	GPS
249	S	Phosphorylation	Kinase	MAPK1	P63086	GPS
249	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
266	S	Phosphorylation	Kinase	ERK-SUBFAMILY	-	GPS
266	S	Phosphorylation	Kinase	MAPK3	P21708	GPS
266	S	Phosphorylation	Kinase	MAPK1	P63086	GPS
273	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
276	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
276	S	Phosphorylation	Kinase	CDK1	P06493	PSP
276	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
276	S	Phosphorylation	Kinase	CDK2	P24941	PSP
276	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
276	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
293	S	Phosphorylation	Kinase	CDK2	P24941	PSP
293	S	Phosphorylation	Kinase	CDK1	P06493	PSP
293	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
293	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
293	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
300	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
300	T	Phosphorylation	Kinase	CDK2	P24941	PSP
300	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
300	T	Phosphorylation	Kinase	CDK1	P06493	PSP
300	T	Phosphorylation	Kinase	CDK6	Q00534	PSP
303	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
303	S	Phosphorylation	Kinase	CDK2	P24941	PSP
303	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
303	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
303	S	Phosphorylation	Kinase	CDK1	P06493	PSP
424	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
424	S	Phosphorylation	Kinase	CDK1	P06493	PSP
462	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
462	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	CDC20	Q12834	PMID:17015473
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:19524548
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:17015473

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
249	S	Phosphorylation	18695000
Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA.
273	T	Phosphorylation	18695000
Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA.
276	S	Phosphorylation	18695000
Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA.

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 RUNX1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PEBB_HUMAN	CBFB	physical	10856244
AES_HUMAN	AES	physical	10825294
JUN_HUMAN	JUN	physical	11274169
FOS_HUMAN	FOS	physical	11274169
VDR_HUMAN	VDR	physical	12460926
JUN_HUMAN	JUN	physical	11641401
FOS_HUMAN	FOS	physical	11641401
ELF4_HUMAN	ELF4	physical	10207087
ELF2_HUMAN	ELF2	physical	10207087
TLE1_HUMAN	TLE1	physical	9751710
MTG8R_HUMAN	CBFA2T2	physical	9447981
HIPK2_HUMAN	HIPK2	physical	16917507
EP300_HUMAN	EP300	physical	16917507
KAT6A_HUMAN	KAT6A	physical	11742995
PEBB_HUMAN	CBFB	physical	11742995
HTF4_HUMAN	TCF12	physical	15333839
TFE2_HUMAN	TCF3	physical	15333839
MTG8_HUMAN	RUNX1T1	physical	10882117
RUNX1_HUMAN	RUNX1	physical	18073335
SIAH1_HUMAN	SIAH1	physical	18073335
PML_HUMAN	PML	physical	18073335
RARA_HUMAN	RARA	physical	18073335
HDAC2_HUMAN	HDAC2	physical	18073335
SIN3A_HUMAN	SIN3A	physical	14729951
PEBB_HUMAN	CBFB	physical	14729951
NR4A2_HUMAN	NR4A2	physical	21468021
CHIP_HUMAN	STUB1	physical	19524548
VDR_RAT	Vdr	physical	20236534
SMCA4_HUMAN	SMARCA4	physical	20506188
SNF5_HUMAN	SMARCB1	physical	20506188
SMRC1_HUMAN	SMARCC1	physical	20506188
HDAC1_HUMAN	HDAC1	physical	21059642
HDAC3_HUMAN	HDAC3	physical	21059642
KMT2A_HUMAN	KMT2A	physical	22012064
RBM14_HUMAN	RBM14	physical	19585539
MTG8_HUMAN	RUNX1T1	physical	22498736
MTG8R_HUMAN	CBFA2T2	physical	22498736
MTG16_HUMAN	CBFA2T3	physical	22498736
PEBB_HUMAN	CBFB	physical	22498736
HDAC1_HUMAN	HDAC1	physical	22498736
HDAC2_HUMAN	HDAC2	physical	22498736
ANM1_HUMAN	PRMT1	physical	22498736
KAT6A_HUMAN	KAT6A	physical	15331439
CBP_HUMAN	CREBBP	physical	15331439
PML_HUMAN	PML	physical	15331439
PEBB_HUMAN	CBFB	physical	15331439
UXT_HUMAN	UXT	physical	17635584
CTBP2_HUMAN	CTBP2	physical	17635584
NCOR2_HUMAN	NCOR2	physical	17560331
FOXP3_HUMAN	FOXP3	physical	17377532
RUNX1_HUMAN	RUNX1	physical	15897867
YAP1_HUMAN	YAP1	physical	18280240
PEBB_HUMAN	CBFB	physical	14752096
RAG1_HUMAN	RAG1	physical	25135298
SPI1_HUMAN	SPI1	physical	10207087
ELF1_HUMAN	ELF1	physical	10207087
PEBB_HUMAN	CBFB	physical	26598521
FACD2_HUMAN	FANCD2	physical	25066130
PEBB_MOUSE	Cbfb	physical	25066130

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
	Note=A chromosomal aberration involving RUNX1/AML1 is a cause of M2 type acute myeloid leukemia (AML-M2). Translocation t(8
	21)(q22
	q22) with RUNX1T1.
601399
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RUNX1_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-24 AND LYS-43, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-14; SER-21; SER-249;SER-266; SER-268 AND SER-276, AND MASS SPECTROMETRY.	19690332 [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 THR-14 AND SER-21, AND MASSSPECTROMETRY.	18669648 [Abstract]
"PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 byHIPK2: implications for leukemogenesis."; Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.; Blood 112:3777-3787(2008). Cited for: PHOSPHORYLATION AT SER-249; THR-273 AND SER-276 BY HIPK2, VARIANTGLN-174, AND MUTAGENESIS OF SER-67; LYS-83; GLY-108; SER-249; THR-273AND SER-276.	18695000 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND SER-21, AND MASSSPECTROMETRY.	15302935 [Abstract]

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