dbPTM

RUNX2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RUNX2_HUMAN
UniProt AC	Q13950
Protein Name	Runt-related transcription factor 2
Gene Name	RUNX2
Organism	Homo sapiens (Human).
Sequence Length	521
Subcellular Localization	Nucleus .
Protein Description	Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. [PubMed: 28505335]
Protein Sequence	MASNSLFSTVTPCQQNFFWDPSTSRRFSPPSSSLQPGKMSDVSPVVAAQQQQQQQQQQQQQQQQQQQQQQQEAAAAAAAAAAAAAAAAAVPRLRPPHDNRTMVEIIADHPAELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKVTVDGPREPRRHRQKLDDSKPSLFSDRLSDLGRIPHPSMRVGVPPQNPRPSLNSAPSPFNPQGQSQITDPRQAQSSPPWSYDQSYPSYLSQMTSPSIHSTTPLSSTRGTGLPAITDVPRRISDDDTATSDFCLWPSTLSKKSQAGASELGPFSDPRQFPSISSLTESRFSNPRMHYPATFTYTPPVTSGMSLGMSATTHYHTYLPPPYPGSSQSQSGPFQTSSTPYLYYGTSSGSYQFPMVPGGDRSPSRMLPPCTTTSNGSTLLNPNLPNQNDGVDADGSHSSSPTVLNSSGRMDESVWRPY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14 (in isoform 2)	Phosphorylation	-	42.32	25849741
24	Phosphorylation	FFWDPSTSRRFSPPS CCCCCCCCCCCCCCC	26.29	19801668
28	Phosphorylation	PSTSRRFSPPSSSLQ CCCCCCCCCCCCCCC	33.80	19264160
31	Phosphorylation	SRRFSPPSSSLQPGK CCCCCCCCCCCCCCC	35.62	28450419
32	O-linked_Glycosylation	RRFSPPSSSLQPGKM CCCCCCCCCCCCCCC	40.62	17707335
32	Phosphorylation	RRFSPPSSSLQPGKM CCCCCCCCCCCCCCC	40.62	22199227
33	Phosphorylation	RFSPPSSSLQPGKMS CCCCCCCCCCCCCCC	35.05	28450419
33	O-linked_Glycosylation	RFSPPSSSLQPGKMS CCCCCCCCCCCCCCC	35.05	17707335
43	Phosphorylation	PGKMSDVSPVVAAQQ CCCCCCCHHHHHHHH	19.57	19801668
116	Phosphorylation	HPAELVRTDSPNFLC CHHHHEECCCCCCCE	33.09	28450419
118	Phosphorylation	AELVRTDSPNFLCSV HHHEECCCCCCCEEE	22.56	22247071
162 (in isoform 2)	Ubiquitination	-	63.17	21906983
176	Ubiquitination	RNASAVMKNQVARFN HCHHHHHHHHHHHHC	37.31	2190698
176 (in isoform 1)	Ubiquitination	-	37.31	21906983
196	Phosphorylation	GRSGRGKSFTLTITV ECCCCCCEEEEEEEE	26.70	55456607
198	Phosphorylation	SGRGKSFTLTITVFT CCCCCEEEEEEEEEC	30.04	55456609
200	Phosphorylation	RGKSFTLTITVFTNP CCCEEEEEEEEECCC	16.14	55456605
202	Phosphorylation	KSFTLTITVFTNPPQ CEEEEEEEEECCCCC	12.34	-
220	Phosphorylation	YHRAIKVTVDGPREP EEEEEEEECCCCCCC	14.10	111142801
233	Ubiquitination	EPRRHRQKLDDSKPS CCCHHHHCCCCCCCC	54.57	-
237	Phosphorylation	HRQKLDDSKPSLFSD HHHCCCCCCCCHHHH	46.24	44523801
238	Ubiquitination	RQKLDDSKPSLFSDR HHCCCCCCCCHHHHH	45.69	-
238	Sumoylation	RQKLDDSKPSLFSDR HHCCCCCCCCHHHHH	45.69	28112733
238	Acetylation	RQKLDDSKPSLFSDR HHCCCCCCCCHHHHH	45.69	26822725
240	Phosphorylation	KLDDSKPSLFSDRLS CCCCCCCCHHHHHHH	45.87	27080861
243	Phosphorylation	DSKPSLFSDRLSDLG CCCCCHHHHHHHHHC	27.41	27080861
244 (in isoform 3)	Ubiquitination	-	48.48	21906983
247	Phosphorylation	SLFSDRLSDLGRIPH CHHHHHHHHHCCCCC	31.51	29496963
258	Methylation	RIPHPSMRVGVPPQN CCCCCHHCCCCCCCC	26.78	-
267	Methylation	GVPPQNPRPSLNSAP CCCCCCCCCCCCCCC	40.77	-
267	Asymmetric dimethylarginine	GVPPQNPRPSLNSAP CCCCCCCCCCCCCCC	40.77	-
269	Phosphorylation	PPQNPRPSLNSAPSP CCCCCCCCCCCCCCC	41.27	23312004
272	Phosphorylation	NPRPSLNSAPSPFNP CCCCCCCCCCCCCCC	47.02	23312004
275	Phosphorylation	PSLNSAPSPFNPQGQ CCCCCCCCCCCCCCC	41.67	25850435
283	Phosphorylation	PFNPQGQSQITDPRQ CCCCCCCCCCCCHHH	30.30	23312004
286	Phosphorylation	PQGQSQITDPRQAQS CCCCCCCCCHHHHHC	32.11	23312004
293	Phosphorylation	TDPRQAQSSPPWSYD CCHHHHHCCCCCCCC	48.07	23401153
294	Phosphorylation	DPRQAQSSPPWSYDQ CHHHHHCCCCCCCCC	23.93	29496963
298	Phosphorylation	AQSSPPWSYDQSYPS HHCCCCCCCCCCCCH	25.30	27080861
299	Phosphorylation	QSSPPWSYDQSYPSY HCCCCCCCCCCCCHH	17.71	27080861
302	Phosphorylation	PPWSYDQSYPSYLSQ CCCCCCCCCCHHHHH	35.79	27080861
303	Phosphorylation	PWSYDQSYPSYLSQM CCCCCCCCCHHHHHC	7.20	27080861
305	Phosphorylation	SYDQSYPSYLSQMTS CCCCCCCHHHHHCCC	30.39	27080861
306	Phosphorylation	YDQSYPSYLSQMTSP CCCCCCHHHHHCCCC	13.08	27080861
308	Phosphorylation	QSYPSYLSQMTSPSI CCCCHHHHHCCCCCC	15.07	27080861
311	Phosphorylation	PSYLSQMTSPSIHST CHHHHHCCCCCCCCC	29.83	27080861
312	Phosphorylation	SYLSQMTSPSIHSTT HHHHHCCCCCCCCCC	16.00	28450419
314	Phosphorylation	LSQMTSPSIHSTTPL HHHCCCCCCCCCCCC	32.47	28450419
317	Phosphorylation	MTSPSIHSTTPLSST CCCCCCCCCCCCCCC	32.10	27080861
318	Phosphorylation	TSPSIHSTTPLSSTR CCCCCCCCCCCCCCC	20.47	27080861
319	Phosphorylation	SPSIHSTTPLSSTRG CCCCCCCCCCCCCCC	25.83	27080861
322	Phosphorylation	IHSTTPLSSTRGTGL CCCCCCCCCCCCCCC	30.76	27080861
323	Phosphorylation	HSTTPLSSTRGTGLP CCCCCCCCCCCCCCC	29.79	27080861
324	Phosphorylation	STTPLSSTRGTGLPA CCCCCCCCCCCCCCC	29.73	27080861
340 (in isoform 3)	Phosphorylation	-	32.92	22617229
340	Phosphorylation	TDVPRRISDDDTATS CCCCCCCCCCCCCCC	32.92	19264160
343 (in isoform 3)	Phosphorylation	-	43.14	28450419
344	Phosphorylation	RRISDDDTATSDFCL CCCCCCCCCCCCEEE	38.54	26657352
346	Phosphorylation	ISDDDTATSDFCLWP CCCCCCCCCCEEECH	30.81	28450419
347	Phosphorylation	SDDDTATSDFCLWPS CCCCCCCCCEEECHH	26.65	28450419
349 (in isoform 3)	Phosphorylation	-	3.55	28102081
358	Ubiquitination	LWPSTLSKKSQAGAS ECHHHCCHHHCCCCH	60.60	-
359	Ubiquitination	WPSTLSKKSQAGASE CHHHCCHHHCCCCHH	44.41	-
371	O-linked_Glycosylation	ASELGPFSDPRQFPS CHHCCCCCCCCCCCC	50.25	17707335
378	Phosphorylation	SDPRQFPSISSLTES CCCCCCCCHHHHCCC	36.07	-
386	Dimethylation	ISSLTESRFSNPRMH HHHHCCCCCCCCCCC	32.55	-
386	Methylation	ISSLTESRFSNPRMH HHHHCCCCCCCCCCC	32.55	-
388	Phosphorylation	SLTESRFSNPRMHYP HHCCCCCCCCCCCCC	44.83	44523803
451	Phosphorylation	YLYYGTSSGSYQFPM EEEEECCCCCEECCC	31.43	11857736
465	Phosphorylation	MVPGGDRSPSRMLPP CCCCCCCCCCCCCCC	31.78	16407259
499	Phosphorylation	DGVDADGSHSSSPTV CCCCCCCCCCCCCEE	22.27	12231506
501	Phosphorylation	VDADGSHSSSPTVLN CCCCCCCCCCCEEEC	33.92	27080861
502	Phosphorylation	DADGSHSSSPTVLNS CCCCCCCCCCEEECC	34.61	27080861
503	Phosphorylation	ADGSHSSSPTVLNSS CCCCCCCCCEEECCC	27.83	19801668
505	Phosphorylation	GSHSSSPTVLNSSGR CCCCCCCEEECCCCC	39.30	27080861
521	Phosphorylation	DESVWRPY------- CCCCCCCC-------	23.71	20090780

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
24	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
28	S	Phosphorylation	Kinase	AKT1	P31749	PSP
28	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
43	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
118	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
118	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
196	S	Phosphorylation	Kinase	AKT1	P31749	PSP
198	T	Phosphorylation	Kinase	AKT1	P31749	PSP
200	T	Phosphorylation	Kinase	AKT1	P31749	PSP
275	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
294	S	Phosphorylation	Kinase	ERK-SUBFAMILY	-	GPS
294	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
312	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
314	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
340	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
451	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
465	S	Phosphorylation	Kinase	CDK4	P11802	PSP
465	S	Phosphorylation	Kinase	CDK1	P06493	PSP
503	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:18541707
-	K	Ubiquitination	E3 ubiquitin ligase	WWP1	Q9H0M0	PMID:17966382
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:12738770
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF2	Q9HAU4	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
340	S	Phosphorylation	18220336
Isoform 3 is phosphorylated on Ser-340.
451	S	Phosphorylation	16407259
Phosphorylation at Ser-451 by CDK1 promotes endothelial cell proliferation required for tumor angiogenesis probably by facilitating cell cycle progression.

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 RUNX2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC3_HUMAN	HDAC3	physical	15292260
SMAD1_HUMAN	SMAD1	physical	10962029
JUN_HUMAN	JUN	physical	11274169
FOS_HUMAN	FOS	physical	11274169
JUN_HUMAN	JUN	physical	11641401
FOS_HUMAN	FOS	physical	11641401
MSX2_HUMAN	MSX2	physical	11683913
CHIP_HUMAN	STUB1	physical	18541707
TLE1_HUMAN	TLE1	physical	20160071
HDAC4_HUMAN	HDAC4	physical	20097749
HDAC4_HUMAN	HDAC4	physical	16613856
HDAC5_HUMAN	HDAC5	physical	16613856
HDAC1_HUMAN	HDAC1	physical	16728531
EP300_HUMAN	EP300	physical	16613856
BMR1A_HUMAN	BMPR1A	physical	16613856
HES1_HUMAN	HES1	physical	16195230
HDAC5_HUMAN	HDAC5	physical	15990875
HDAC4_HUMAN	HDAC4	physical	15537544
HDAC3_HUMAN	HDAC3	physical	18321663
CBP_HUMAN	CREBBP	physical	18321663
HDAC7_HUMAN	HDAC7	physical	17997710
SMAD1_HUMAN	SMAD1	physical	20851880
SOX9_HUMAN	SOX9	physical	20593410
RBM14_HUMAN	RBM14	physical	19585539
SMAD3_HUMAN	SMAD3	physical	21986102
HDAC1_HUMAN	HDAC1	physical	21972143
SUV91_HUMAN	SUV39H1	physical	22537242
HDAC1_HUMAN	HDAC1	physical	22393235
UBF1_HUMAN	UBTF	physical	22393235
ZEP3_HUMAN	HIVEP3	physical	16728642
WWP1_HUMAN	WWP1	physical	16728642
SMAD1_HUMAN	SMAD1	physical	17215250
SMUF1_HUMAN	SMURF1	physical	17215250
HIF1A_HUMAN	HIF1A	physical	22351759
RB_HUMAN	RB1	physical	15583032
P53_HUMAN	TP53	physical	23618908
HDAC6_HUMAN	HDAC6	physical	23618908
STA5A_HUMAN	STAT5A	physical	23533197
SKP2_HUMAN	SKP2	physical	26778333

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
119600	Cleidocranial dysplasia (CLCD)
156510	Metaphyseal dysplasia with maxillary hypoplasia with or without brachydactyly (MDMHB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RUNX2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Cell cycle-dependent phosphorylation of the RUNX2 transcriptionfactor by cdc2 regulates endothelial cell proliferation."; Qiao M., Shapiro P., Fosbrink M., Rus H., Kumar R., Passaniti A.; J. Biol. Chem. 281:7118-7128(2006). Cited for: INTERACTION WITH CCNB1, PHOSPHORYLATION AT SER-451 BY CDK1, ANDMUTAGENESIS OF SER-451.	16407259 [Abstract]

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