RUNX1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RUNX1_RAT
• UniProt AC: Q63046
• Protein Name: Runt-related transcription factor 1
• Gene Name: Runx1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 450
• Subcellular Localization: Nucleus.
• Protein Description: 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, LCK, IL-3 and GM-CSF promoters. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. Isoform AML-1L interferes with the transactivation activity of RUNX1. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter. Inhibits KAT6B-dependent transcriptional activation. Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells (By similarity). Positively regulates the expression of RORC in T-helper 17 cells (By similarity)..
• Protein Sequence: MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDGGAALASKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDARQIQPSPPWSYDQSYQYLGSITSSVHPATPISPGRASGMTSLSAELSSRLSTAPDLTAFGDPRQFPTLPSISDPRMHYPGAFTYSPPVTSGIGIGMSAMSSTSRYHTYLPPPYPGSSQAQAGPFQTGSPSYHLYYGTSAGSYQFSMVGGERSPPRILPPCTNASTGAALLNPSLPSQSDVVETEGSHSNSPTNMPPARLEEAVWRPY

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
9	Phosphorylation	RIPVDASTSRRFTPP CCCCCCCCCCCCCCC	28.15	25575281
10	Phosphorylation	IPVDASTSRRFTPPS CCCCCCCCCCCCCCC	20.97	25575281
14	Phosphorylation	ASTSRRFTPPSTALS CCCCCCCCCCCCCCC	32.26	28432305
17	Phosphorylation	SRRFTPPSTALSPGK CCCCCCCCCCCCCCC	27.76	28432305
18	Phosphorylation	RRFTPPSTALSPGKM CCCCCCCCCCCCCCC	37.07	28432305
21	Phosphorylation	TPPSTALSPGKMSEA CCCCCCCCCCCCCCC	29.19	22817900
24	Acetylation	STALSPGKMSEALPL CCCCCCCCCCCCCCC	42.51	22902405
43	Acetylation	GGAALASKLRSGDRS CHHHHHHHHHCCCCC	42.17	22902405
193	Phosphorylation	QTKPGSLSFSERLSE CCCCCCCCHHHHHHH	28.55	-
199	Phosphorylation	LSFSERLSELEQLRR CCHHHHHHHHHHHHH	46.48	30181290
207	Phosphorylation	ELEQLRRTAMRVSPH HHHHHHHHHHHHCCC	20.55	25575281
212	Phosphorylation	RRTAMRVSPHHPAPT HHHHHHHCCCCCCCC	14.25	43304811
219	Phosphorylation	SPHHPAPTPNPRASL CCCCCCCCCCCCCCC	37.49	25575281
249	Phosphorylation	DARQIQPSPPWSYDQ CHHHHCCCCCCCCCC	27.50	22673903
253	Phosphorylation	IQPSPPWSYDQSYQY HCCCCCCCCCCCCCC	25.30	22673903
254	Phosphorylation	QPSPPWSYDQSYQYL CCCCCCCCCCCCCCH	17.71	22673903
265	Phosphorylation	YQYLGSITSSVHPAT CCCHHCCCCCCCCCC	19.35	22673903
266	Phosphorylation	QYLGSITSSVHPATP CCHHCCCCCCCCCCC	28.79	22673903
267	Phosphorylation	YLGSITSSVHPATPI CHHCCCCCCCCCCCC	18.78	22673903
272	Phosphorylation	TSSVHPATPISPGRA CCCCCCCCCCCCCCC	26.13	22673903
275	Phosphorylation	VHPATPISPGRASGM CCCCCCCCCCCCCCC	23.62	22673903
295	Phosphorylation	ELSSRLSTAPDLTAF HHHHHCCCCCCHHHC	46.96	-
343	Phosphorylation	GIGMSAMSSTSRYHT CCCCCCCCCCCCCCC	30.13	26022182
344	Phosphorylation	IGMSAMSSTSRYHTY CCCCCCCCCCCCCCC	19.81	26022182
345	Phosphorylation	GMSAMSSTSRYHTYL CCCCCCCCCCCCCCC	15.20	26022182
395	Phosphorylation	SMVGGERSPPRILPP EECCCCCCCCCCCCC	34.65	28551015
433	Phosphorylation	TEGSHSNSPTNMPPA CCCCCCCCCCCCCHH	35.80	-

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
249	S	Phosphorylation	Kinase	HIPK2	-	Uniprot
272	T	Phosphorylation	Kinase	HIPK2	-	Uniprot
275	S	Phosphorylation	Kinase	HIPK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
249	S	Phosphorylation	Phosphorylated in Ser-249 Thr-272 and Ser-275 by HIPK2 when associated with CBFB and DNA.	-
272	T	Phosphorylation	Phosphorylated in Ser-249 Thr-272 and Ser-275 by HIPK2 when associated with CBFB and DNA.	-
275	S	Phosphorylation	Phosphorylated in Ser-249 Thr-272 and Ser-275 by HIPK2 when associated with CBFB and DNA.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RUNX1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of RUNX1_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.