dbPTM

RUNX3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RUNX3_HUMAN
UniProt AC	Q13761
Protein Name	Runt-related transcription factor 3
Gene Name	RUNX3
Organism	Homo sapiens (Human).
Sequence Length	415
Subcellular Localization	Nucleus . Cytoplasm . The tyrosine phosphorylated form localizes to the cytoplasm. Translocates from the cytoplasm to the nucleus following TGF-beta stimulation.
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 (By similarity). May be involved in the control of cellular proliferation and/or differentiation. In association with ZFHX3, upregulates CDKN1A promoter activity following TGF-beta stimulation. [PubMed: 20599712 CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity]
Protein Sequence	MRIPVDPSTSRRFTPPSPAFPCGGGGGKMGENSGALSAQAAVGPGGRARPEVRSMVDVLADHAGELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGDVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPTQVATYHRAIKVTVDGPREPRRHRQKLEDQTKPFPDRFGDLERLRMRVTPSTPSPRGSLSTTSHFSSQPQTPIQGTSELNPFSDPRQFDRSFPTLPTLTESRFPDPRMHYPGAMSAAFPYSATPSGTSISSLSVAGMPATSRFHHTYLPPPYPGAPQNQSGPFQANPSPYHLYYGTSSGSYQFSMVAGSSSGGDRSPTRMLASCTSSAASVAAGNLMNPSLGGQSDGVEADGSHSNSPTALSTPGRMDEAVWRPY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12 (in isoform 2)	Phosphorylation	-	39.29	25850435
13 (in isoform 2)	Phosphorylation	-	13.46	25850435
14 (in isoform 2)	Phosphorylation	-	32.26	25850435
14	Phosphorylation	PSTSRRFTPPSPAFP CCCCCCCCCCCCCCC	32.26	23401153
16 (in isoform 2)	Phosphorylation	-	50.30	25850435
17	Phosphorylation	SRRFTPPSPAFPCGG CCCCCCCCCCCCCCC	30.02	23401153
28	Phosphorylation	PCGGGGGKMGENSGA CCCCCCCCCCCCCCC	47.18	24719451
28	Acetylation	PCGGGGGKMGENSGA CCCCCCCCCCCCCCC	47.18	25953088
31	Phosphorylation	GGGGKMGENSGALSA CCCCCCCCCCCCCCC	44.73	24719451
37	Phosphorylation	GENSGALSAQAAVGP CCCCCCCCCEEEECC	20.15	23879269
54	Phosphorylation	RARPEVRSMVDVLAD CCCHHHHHHHHHHHH	28.47	30108239
69	Phosphorylation	HAGELVRTDSPNFLC HCCCEEECCCCCCEE	33.09	28450419
71	Phosphorylation	GELVRTDSPNFLCSV CCEEECCCCCCEEEE	22.56	28450419
94	Acetylation	KTLPVAFKVVALGDV CCCCEEEEEEEECCC	26.51	115352803
94	Ubiquitination	KTLPVAFKVVALGDV CCCCEEEEEEEECCC	26.51	19808967
129	Acetylation	RNASAVMKNQVARFN HCHHHHHHHHHHHHC	37.31	25953088
129 (in isoform 1)	Ubiquitination	-	37.31	21906983
129	Ubiquitination	RNASAVMKNQVARFN HCHHHHHHHHHHHHC	37.31	21906983
143 (in isoform 2)	Ubiquitination	-	30.54	21906983
144	Phosphorylation	DLRFVGRSGRGKSFT CEEEEECCCCCCEEE	27.24	25954137
148	Acetylation	VGRSGRGKSFTLTIT EECCCCCCEEEEEEE	40.82	15138260
148	Ubiquitination	VGRSGRGKSFTLTIT EECCCCCCEEEEEEE	40.82	1980896
149	Phosphorylation	GRSGRGKSFTLTITV ECCCCCCEEEEEEEE	26.70	18767071
151	Phosphorylation	SGRGKSFTLTITVFT CCCCCEEEEEEEEEC	30.04	18767071
153	Phosphorylation	RGKSFTLTITVFTNP CCCEEEEEEEEECCC	16.14	18767071
155	Phosphorylation	KSFTLTITVFTNPTQ CEEEEEEEEECCCCC	12.34	18767071
166	Phosphorylation	NPTQVATYHRAIKVT CCCCEEEEEEEEEEE	4.60	25954137
171	Acetylation	ATYHRAIKVTVDGPR EEEEEEEEEECCCCC	30.76	115352801
173	Phosphorylation	YHRAIKVTVDGPREP EEEEEEEECCCCCCC	14.10	111142801
186	Ubiquitination	EPRRHRQKLEDQTKP CCHHHHHHHHHCCCC	54.52	15138260
186	Acetylation	EPRRHRQKLEDQTKP CCHHHHHHHHHCCCC	54.52	15138260
192	Sumoylation	QKLEDQTKPFPDRFG HHHHHCCCCCCCCCC	38.74	-
192	Sumoylation	QKLEDQTKPFPDRFG HHHHHCCCCCCCCCC	38.74	28112733
192	Acetylation	QKLEDQTKPFPDRFG HHHHHCCCCCCCCCC	38.74	23749302
192	Ubiquitination	QKLEDQTKPFPDRFG HHHHHCCCCCCCCCC	38.74	15138260
209	Phosphorylation	ERLRMRVTPSTPSPR HHHEEEECCCCCCCC	10.93	28450419
211	Phosphorylation	LRMRVTPSTPSPRGS HEEEECCCCCCCCCC	43.51	28450419
212	O-linked_Glycosylation	RMRVTPSTPSPRGSL EEEECCCCCCCCCCC	29.05	29351928
212	Phosphorylation	RMRVTPSTPSPRGSL EEEECCCCCCCCCCC	29.05	29255136
214	Phosphorylation	RVTPSTPSPRGSLST EECCCCCCCCCCCCC	27.58	29255136
216	Methylation	TPSTPSPRGSLSTTS CCCCCCCCCCCCCCC	52.23	-
218	Phosphorylation	STPSPRGSLSTTSHF CCCCCCCCCCCCCCC	22.04	28450419
220	Phosphorylation	PSPRGSLSTTSHFSS CCCCCCCCCCCCCCC	31.19	28450419
221	Phosphorylation	SPRGSLSTTSHFSSQ CCCCCCCCCCCCCCC	37.30	27251275
222	Phosphorylation	PRGSLSTTSHFSSQP CCCCCCCCCCCCCCC	19.48	28450419
223	Phosphorylation	RGSLSTTSHFSSQPQ CCCCCCCCCCCCCCC	23.71	28450419
225	Phosphorylation	SLSTTSHFSSQPQTP CCCCCCCCCCCCCCC	8.23	24719451
226	Phosphorylation	LSTTSHFSSQPQTPI CCCCCCCCCCCCCCC	23.73	26714015
227	Phosphorylation	STTSHFSSQPQTPIQ CCCCCCCCCCCCCCC	44.96	28450419
228	Phosphorylation	TTSHFSSQPQTPIQG CCCCCCCCCCCCCCC	32.68	24719451
231	Phosphorylation	HFSSQPQTPIQGTSE CCCCCCCCCCCCCCC	29.10	23401153
236	Phosphorylation	PQTPIQGTSELNPFS CCCCCCCCCCCCCCC	11.58	27251275
237	Phosphorylation	QTPIQGTSELNPFSD CCCCCCCCCCCCCCC	47.08	27251275
237	O-linked_Glycosylation	QTPIQGTSELNPFSD CCCCCCCCCCCCCCC	47.08	29351928
243	Phosphorylation	TSELNPFSDPRQFDR CCCCCCCCCHHHCCC	48.22	28112733
245	Phosphorylation	ELNPFSDPRQFDRSF CCCCCCCHHHCCCCC	30.67	24719451
251	Phosphorylation	DPRQFDRSFPTLPTL CHHHCCCCCCCCCCC	37.11	30108239
254	Phosphorylation	QFDRSFPTLPTLTES HCCCCCCCCCCCCCC	43.27	50564955
261	O-linked_Glycosylation	TLPTLTESRFPDPRM CCCCCCCCCCCCCCC	33.70	29351928
261	Phosphorylation	TLPTLTESRFPDPRM CCCCCCCCCCCCCCC	33.70	50564961
262	Dimethylation	LPTLTESRFPDPRMH CCCCCCCCCCCCCCC	40.67	-
262	Methylation	LPTLTESRFPDPRMH CCCCCCCCCCCCCCC	40.67	-
265	Phosphorylation	LTESRFPDPRMHYPG CCCCCCCCCCCCCCC	40.50	24719451
267	Methylation	ESRFPDPRMHYPGAM CCCCCCCCCCCCCCC	31.71	-
281	O-linked_Glycosylation	MSAAFPYSATPSGTS CCCCCCCCCCCCCCC	26.38	29351928
283	O-linked_Glycosylation	AAFPYSATPSGTSIS CCCCCCCCCCCCCCC	16.43	29351928
285	O-linked_Glycosylation	FPYSATPSGTSISSL CCCCCCCCCCCCCCE	50.80	29351928
288	O-linked_Glycosylation	SATPSGTSISSLSVA CCCCCCCCCCCEEEC	24.81	29351928
291	Phosphorylation	PSGTSISSLSVAGMP CCCCCCCCEEECCCC	24.00	22210691
293	O-linked_Glycosylation	GTSISSLSVAGMPAT CCCCCCEEECCCCCC	16.33	29351928
301	Phosphorylation	VAGMPATSRFHHTYL ECCCCCCCCCCCCCC	34.75	22210691
301	O-linked_Glycosylation	VAGMPATSRFHHTYL ECCCCCCCCCCCCCC	34.75	29351928
302	Methylation	AGMPATSRFHHTYLP CCCCCCCCCCCCCCC	30.48	-
320	O-linked_Glycosylation	PGAPQNQSGPFQANP CCCCCCCCCCCCCCC	56.85	29351928
328	O-linked_Glycosylation	GPFQANPSPYHLYYG CCCCCCCCCCEEEEE	37.59	29351928
356	Phosphorylation	SSSGGDRSPTRMLAS CCCCCCCCHHHHHHH	35.05	26074081
358	Phosphorylation	SGGDRSPTRMLASCT CCCCCCHHHHHHHCC	29.92	26074081
363	Phosphorylation	SPTRMLASCTSSAAS CHHHHHHHCCCCHHH	17.61	27080861
365	Phosphorylation	TRMLASCTSSAASVA HHHHHHCCCCHHHHH	24.18	27080861
366	Phosphorylation	RMLASCTSSAASVAA HHHHHCCCCHHHHHH	23.47	27080861
367	Phosphorylation	MLASCTSSAASVAAG HHHHCCCCHHHHHHH	15.09	27080861
370	Phosphorylation	SCTSSAASVAAGNLM HCCCCHHHHHHHCCC	16.41	27080861
380	Phosphorylation	AGNLMNPSLGGQSDG HHCCCCHHHCCCCCC	34.34	27080861
385	Phosphorylation	NPSLGGQSDGVEADG CHHHCCCCCCCCCCC	39.34	27080861
393	Phosphorylation	DGVEADGSHSNSPTA CCCCCCCCCCCCCCC	25.04	27080861
395	Phosphorylation	VEADGSHSNSPTALS CCCCCCCCCCCCCCC	40.47	30108239
397	Phosphorylation	ADGSHSNSPTALSTP CCCCCCCCCCCCCCC	27.00	30108239
399	Phosphorylation	GSHSNSPTALSTPGR CCCCCCCCCCCCCCC	39.80	30108239
402	Phosphorylation	SNSPTALSTPGRMDE CCCCCCCCCCCCCCC	30.05	27080861
403	Phosphorylation	NSPTALSTPGRMDEA CCCCCCCCCCCCCCC	30.52	27080861
409	Phosphorylation	STPGRMDEAVWRPY- CCCCCCCCCCCCCC-	35.46	27251275
411	Phosphorylation	PGRMDEAVWRPY--- CCCCCCCCCCCC---	4.13	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
14	T	Phosphorylation	Kinase	AURKA	O14965	GPS
14	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
149	S	Phosphorylation	Kinase	PIM1	P11309	PSP
151	T	Phosphorylation	Kinase	PIM1	P11309	PSP
153	T	Phosphorylation	Kinase	PIM1	P11309	PSP
155	T	Phosphorylation	Kinase	PIM1	P11309	PSP
173	T	Phosphorylation	Kinase	AURKA	O14965	GPS
173	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
209	T	Phosphorylation	Kinase	PAK1	Q13153	PSP
356	S	Phosphorylation	Kinase	CDK4	P11802	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RUNX3_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 RUNX3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TLE1_HUMAN	TLE1	physical	9751710
SP110_HUMAN	SP110	physical	20211142
EP300_HUMAN	EP300	physical	15138260
PEBB_HUMAN	CBFB	physical	15138260
SMAD3_HUMAN	SMAD3	physical	15138260
SMUF1_HUMAN	SMURF1	physical	15138260
SMUF2_HUMAN	SMURF2	physical	15138260
VDR_RAT	Vdr	physical	20236534
EZH2_HUMAN	EZH2	physical	20714105
MDM2_HUMAN	MDM2	physical	19808967
SIR2_HUMAN	SIRT2	physical	21511279
NOTC1_HUMAN	NOTCH1	physical	19800882
SUH_HUMAN	RBPJ	physical	19800882
HDAC5_HUMAN	HDAC5	physical	15138260
HDAC1_HUMAN	HDAC1	physical	15138260
FACD2_HUMAN	FANCD2	physical	25066130
FANCI_HUMAN	FANCI	physical	25066130
PEBB_MOUSE	Cbfb	physical	25066130

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 RUNX3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-243, AND MASSSPECTROMETRY.	18220336 [Abstract]