ANM1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANM1_RAT
• UniProt AC: Q63009
• Protein Name: Protein arginine N-methyltransferase 1
• Gene Name: Prmt1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 353
• Subcellular Localization: Nucleus. Nucleus, nucleoplasm. Cytoplasm, cytosol . Cytoplasm . Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity)..
• Protein Description: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4 and SERBP1. [PubMed: 12737817]
• Protein Sequence: MAAAEAANCIMEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR

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
70	Acetylation	FHNRHLFKDKVVLDV CCCCCCCCCEEEEEE	64.10	22902405
102	Phosphorylation	KVIGIECSSISDYAV EEEEEECCCCCHHHH	20.23	28432305
103	Phosphorylation	VIGIECSSISDYAVK EEEEECCCCCHHHHH	37.46	23984901
105	Phosphorylation	GIECSSISDYAVKIV EEECCCCCHHHHHHH	26.90	28432305
116	Acetylation	VKIVKANKLDHVVTI HHHHHHCCCCEEEEE	61.22	22902405
116	Succinylation	VKIVKANKLDHVVTI HHHHHHCCCCEEEEE	61.22	-
116	Succinylation	VKIVKANKLDHVVTI HHHHHHCCCCEEEEE	61.22	-
127	Acetylation	VVTIIKGKVEEVELP EEEEEECCCEEEECC	41.28	-
210	Acetylation	GFDMSCIKDVAIKEP CCCHHHHCCCEECCC	50.94	-
215	Acetylation	CIKDVAIKEPLVDVV HHCCCEECCCCCCCC	43.47	-
286	Phosphorylation	KRTGFSTSPESPYTH CCCCCCCCCCCCCCC	26.02	-
289	Phosphorylation	GFSTSPESPYTHWKQ CCCCCCCCCCCCCCC	26.96	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ANM1_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
127	K	ubiquitylation	Polyubiquitinated at Lys-127 by the SCF(FBXL17) complex, leading to its subsequent degradation.	-
210	K	Acetylation	Acetylation at Lys-210 and Lys-215 regulates ubiquitination by the SCF(FBXL17) complex.	-
210	K	Acetylation	Deacetylated at Lys-210 and Lys-215 by SIRT1.	-
210	K	Acetylation	Ubiquitination is regulated by acetylation at Lys-210 and Lys-215.	-
210	K	ubiquitylation	Acetylation at Lys-210 and Lys-215 regulates ubiquitination by the SCF(FBXL17) complex.	-
210	K	ubiquitylation	Ubiquitination is regulated by acetylation at Lys-210 and Lys-215.	-
215	K	Acetylation	Acetylated at Lys-215 by p300/EP300.	-
215	K	Acetylation	Acetylation at Lys-210 and Lys-215 regulates ubiquitination by the SCF(FBXL17) complex.	-
215	K	Acetylation	Deacetylated at Lys-210 and Lys-215 by SIRT1.	-
215	K	Acetylation	Ubiquitination is regulated by acetylation at Lys-210 and Lys-215.	-
215	K	ubiquitylation	Acetylation at Lys-210 and Lys-215 regulates ubiquitination by the SCF(FBXL17) complex.	-
215	K	ubiquitylation	Ubiquitination is regulated by acetylation at Lys-210 and Lys-215.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ANM1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of ANM1_RAT !!

Drug and Disease Associations

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