RUNX2_MOUSE - dbPTM
RUNX2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RUNX2_MOUSE
UniProt AC Q08775
Protein Name Runt-related transcription factor 2
Gene Name Runx2
Organism Mus musculus (Mouse).
Sequence Length 607
Subcellular Localization Nucleus .
Protein Description Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. Inhibits KAT6B-dependent transcriptional activation (By similarity). In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE)..
Protein Sequence MLHSPHKQPQNHKCGANFLQEDCKKALAFKWLISAGHYQPPRPTESVSALTTVHAGIFKAASSIYNRGHKFYLEKKGGTMASNSLFSAVTPCQQSFFWDPSTSRRFSPPSSSLQPGKMSDVSPVVAAQQQQQQQQQQQQQQQQQQQQQQQQQQQQQEAAAAAAAAAAAAAAAAAAVPRLRPPHDNRTMVEIIADHPAELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKVTVDGPREPRRHRQKLDDSKPSLFSDRLSDLGRIPHPSMRVGVPPQNPRPSLNSAPSPFNPQGQSQITDPRQAQSSPPWSYDQSYPSYLSQMTSPSIHSTTPLSSTRGTGLPAITDVPRRISDDDTATSDFCLWPSSLSKKSQAGASELGPFSDPRQFPSISSLTESRFSNPRMHYPATFTYTPPVTSGMSLGMSATTHYHTYLPPPYPGSSQSQSGPFQTSSTPYLYYGTSSASYQFPMVPGGDRSPSRMVPPCTTTSNGSTLLNPNLPNQNDGVDADGSHSSSPTVLNSSGRMDESVWRPY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
14 (in isoform 3)Phosphorylation-4.9129514104
14 (in isoform 4)Phosphorylation-4.9129514104
79PhosphorylationYLEKKGGTMASNSLF
EEEECCCCCCCCCHH		20.4522871156
87PhosphorylationMASNSLFSAVTPCQQ
CCCCCHHHCCCCCCC		27.4226643407
90PhosphorylationNSLFSAVTPCQQSFF
CCHHHCCCCCCCCCC		20.3326643407
95PhosphorylationAVTPCQQSFFWDPST
CCCCCCCCCCCCCCC		9.1326643407
101PhosphorylationQSFFWDPSTSRRFSP
CCCCCCCCCCCCCCC		36.2226643407
102PhosphorylationSFFWDPSTSRRFSPP
CCCCCCCCCCCCCCC		31.4726643407
103PhosphorylationFFWDPSTSRRFSPPS
CCCCCCCCCCCCCCC		26.2926643407
107PhosphorylationPSTSRRFSPPSSSLQ
CCCCCCCCCCCCCCC		33.8026824392
110PhosphorylationSRRFSPPSSSLQPGK
CCCCCCCCCCCCCCC		35.6226745281
111PhosphorylationRRFSPPSSSLQPGKM
CCCCCCCCCCCCCCC		40.6226745281
112PhosphorylationRFSPPSSSLQPGKMS
CCCCCCCCCCCCCCC		35.0526745281
204PhosphorylationAELVRTDSPNFLCSV
HHHEECCCCCCCCEE		22.5612231506
326PhosphorylationKLDDSKPSLFSDRLS
CCCCCCCCHHHHHHH		45.8765943
353MethylationGVPPQNPRPSLNSAP
CCCCCCCCCCCCCCC		40.7724129315
353Asymmetric dimethylarginineGVPPQNPRPSLNSAP
CCCCCCCCCCCCCCC		40.77-
358 (in isoform 9)Phosphorylation-47.0225168779
358PhosphorylationNPRPSLNSAPSPFNP
CCCCCCCCCCCCCCC		47.0226160508
361 (in isoform 9)Phosphorylation-41.6725168779
361PhosphorylationPSLNSAPSPFNPQGQ
CCCCCCCCCCCCCCC		41.6720007706
362 (in isoform 9)Phosphorylation-31.7925168779
365 (in isoform 9)Phosphorylation-39.8125168779
366 (in isoform 9)Phosphorylation-64.7625168779
367 (in isoform 9)Phosphorylation-30.2925168779
379PhosphorylationTDPRQAQSSPPWSYD
CCHHHHHCCCCCCCC		48.0726160508
380PhosphorylationDPRQAQSSPPWSYDQ
CHHHHHCCCCCCCCC		23.9320007706
380 (in isoform 9)Phosphorylation-23.9325168779
383 (in isoform 9)Phosphorylation-16.9525168779
384PhosphorylationAQSSPPWSYDQSYPS
HHCCCCCCCCCCCCH		25.3026160508
385PhosphorylationQSSPPWSYDQSYPSY
HCCCCCCCCCCCCHH		17.7126160508
385 (in isoform 9)Phosphorylation-17.7125168779
386 (in isoform 9)Phosphorylation-25.9825168779
388PhosphorylationPPWSYDQSYPSYLSQ
CCCCCCCCCCHHHHH		35.7926160508
389PhosphorylationPWSYDQSYPSYLSQM
CCCCCCCCCHHHHHC		7.2026160508
391PhosphorylationSYDQSYPSYLSQMTS
CCCCCCCHHHHHCCC		30.3926160508
392PhosphorylationYDQSYPSYLSQMTSP
CCCCCCHHHHHCCCC		13.0826160508
394PhosphorylationQSYPSYLSQMTSPSI
CCCCHHHHHCCCCCC		15.0726160508
397PhosphorylationPSYLSQMTSPSIHST
CHHHHHCCCCCCCCC		29.8325777480
398PhosphorylationSYLSQMTSPSIHSTT
HHHHHCCCCCCCCCC		16.0020007706
400PhosphorylationLSQMTSPSIHSTTPL
HHHCCCCCCCCCCCC		32.4725777480
403PhosphorylationMTSPSIHSTTPLSST
CCCCCCCCCCCCCCC		32.1025777480
404PhosphorylationTSPSIHSTTPLSSTR
CCCCCCCCCCCCCCC		20.4725777480
405PhosphorylationSPSIHSTTPLSSTRG
CCCCCCCCCCCCCCC		25.8325777480
408PhosphorylationIHSTTPLSSTRGTGL
CCCCCCCCCCCCCCC		30.7625777480
409PhosphorylationHSTTPLSSTRGTGLP
CCCCCCCCCCCCCCC		29.7925777480
410PhosphorylationSTTPLSSTRGTGLPA
CCCCCCCCCCCCCCC		29.7325777480
416 (in isoform 8)Phosphorylation-23.9825168779
419 (in isoform 8)Phosphorylation-32.8125168779
420 (in isoform 8)Phosphorylation-42.1625168779
423 (in isoform 8)Phosphorylation-48.7025168779
424 (in isoform 8)Phosphorylation-27.0525168779
425 (in isoform 8)Phosphorylation-5.8225168779
426PhosphorylationTDVPRRISDDDTATS
CCCCCCCCCCCCCCC		32.9225266776
430PhosphorylationRRISDDDTATSDFCL
CCCCCCCCCCCCEEE		38.5425266776
432PhosphorylationISDDDTATSDFCLWP
CCCCCCCCCCEEECC		30.8141609085
433PhosphorylationSDDDTATSDFCLWPS
CCCCCCCCCEEECCH		26.6525168779
438 (in isoform 8)Phosphorylation-7.6025168779
441 (in isoform 8)Phosphorylation-32.3625168779
441PhosphorylationDFCLWPSSLSKKSQA
CEEECCHHHCHHHCC		32.3625168779
443 (in isoform 8)Phosphorylation-39.7325168779
444 (in isoform 8)Phosphorylation-62.8325168779
477MethylationESRFSNPRMHYPATF
CCCCCCCCCCCCEEE		28.85-
537PhosphorylationYLYYGTSSASYQFPM
EEEECCCCCEEECCC		22.52-
551PhosphorylationMVPGGDRSPSRMVPP
CCCCCCCCCCCCCCC		31.7812231506
585PhosphorylationDGVDADGSHSSSPTV
CCCCCCCCCCCCCEE		22.2712231506
587PhosphorylationVDADGSHSSSPTVLN
CCCCCCCCCCCEEEC		33.9225338131
589PhosphorylationADGSHSSSPTVLNSS
CCCCCCCCCEEECCC		27.8312231506
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
326SPhosphorylationKinasePRKCDQ05655
GPS
380SPhosphorylationKinaseMAPK3P27361
GPS
537SPhosphorylationKinaseCDK1P11440
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSmurf1Q9CUN6
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseSmurf2A2A5Z6
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseStub1Q9WUD1
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseWwp1Q8BZZ3
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseWwp2Q9DBH0
PMID:31160553
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
537SPhosphorylation

-
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PEBB_MOUSECbfbphysical
20211142
RB_MOUSERb1physical
20211142
RBL2_MOUSERbl2physical
20211142
MSX2_MOUSEMsx2physical
15060165
TLE1_MOUSETle1physical
15060165
VDR_RATVdrphysical
20236534
VDRA_DANREvdraphysical
20236534
ZN521_MOUSEZfp521physical
21173110
SMUF1_MOUSESmurf1physical
16299379
SMAD6_MOUSESmad6physical
16299379
MEN1_MOUSEMen1physical
15150273
WWOX_MOUSEWwoxphysical
18487609
HDAC4_MOUSEHdac4physical
15537544
SKP2_MOUSESkp2physical
26778333
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RUNX2_MOUSE

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Related Literatures of Post-Translational Modification

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