ANM1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANM1_MOUSE
• UniProt AC: Q9JIF0
• Protein Name: Protein arginine N-methyltransferase 1
• Gene Name: Prmt1
• Organism: Mus musculus (Mouse).
• Sequence Length: 371
• 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.
• 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: 15327772]
• Protein Sequence: MAAAEAANCIMENFVATLANGMSLQPPLEEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR

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
14 (in isoform 2)	Phosphorylation	-	2.23	29514104
49	Phosphorylation	PNAEDMTSKDYYFDS CCHHHCCCCCHHHHH	19.52	27841257
113	Acetylation	AAKAGARKVIGIECS HHHCCCCEEEEEECC	37.36	22826441
119	Glutathionylation	RKVIGIECSSISDYA CEEEEEECCCCCHHH	3.50	24333276
120	Phosphorylation	KVIGIECSSISDYAV EEEEEECCCCCHHHH	20.23	26824392
121	Phosphorylation	VIGIECSSISDYAVK EEEEECCCCCHHHHH	37.46	26824392
123	Phosphorylation	GIECSSISDYAVKIV EEECCCCCHHHHHHH	26.90	26643407
131	Ubiquitination	DYAVKIVKANKLDHV HHHHHHHHHCCCCEE	50.11	22790023
134	Ubiquitination	VKIVKANKLDHVVTI HHHHHHCCCCEEEEE	61.22	-
134	Acetylation	VKIVKANKLDHVVTI HHHHHHCCCCEEEEE	61.22	23806337
134	Succinylation	VKIVKANKLDHVVTI HHHHHHCCCCEEEEE	61.22	23806337
134	Succinylation	VKIVKANKLDHVVTI HHHHHHCCCCEEEEE	61.22	-
145	Acetylation	VVTIIKGKVEEVELP EEEEEECCCEEEECC	41.28	23236377
183	Acetylation	TVLHARDKWLAPDGL HHHHHHCCCCCCCCC	38.26	22826441
228	Acetylation	GFDMSCIKDVAIKEP CCCHHHHCCCEECCC	50.94	28883095
233	Acetylation	CIKDVAIKEPLVDVV HHCCCEECCCCCCCC	43.47	28883095
233	Ubiquitination	CIKDVAIKEPLVDVV HHCCCEECCCCCCCC	43.47	22790023
272	Glutathionylation	LTFTSPFCLQVKRND CEECCCEEEEEECCC	2.70	24333276
272	S-nitrosylation	LTFTSPFCLQVKRND CEECCCEEEEEECCC	2.70	22178444
272	S-nitrosocysteine	LTFTSPFCLQVKRND CEECCCEEEEEECCC	2.70	-
303	Phosphorylation	HKRTGFSTSPESPYT CCCCCCCCCCCCCCC	46.14	25338131
304	Phosphorylation	KRTGFSTSPESPYTH CCCCCCCCCCCCCCC	26.02	-
307	Phosphorylation	GFSTSPESPYTHWKQ CCCCCCCCCCCCCCC	26.96	23608596
309	Phosphorylation	STSPESPYTHWKQTV CCCCCCCCCCCCCEE	22.10	22817900
310	Phosphorylation	TSPESPYTHWKQTVF CCCCCCCCCCCCEEE	25.33	23984901
324	Phosphorylation	FYMEDYLTVKTGEEI EEEECEEEEECCCCE	17.46	-
342	Ubiquitination	IGMRPNAKNNRDLDF CCCCCCCCCCCCCEE	62.49	22790023
364	S-nitrosocysteine	GQLCELSCSTDYRMR CCEEEEECCCCCCCC	8.74	-
364	S-nitrosylation	GQLCELSCSTDYRMR CCEEEEECCCCCCCC	8.74	20925432

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
-	K	Ubiquitination	E3 ubiquitin ligase	Fbxl17	Q9QZN1	PMID:28883095

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
145	K	ubiquitylation	Polyubiquitinated at Lys-145 by the SCF(FBXL17) complex, leading to its subsequent degradation.	28883095
228	K	Acetylation	Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the SCF(FBXL17) complex.	28883095
228	K	Acetylation	Deacetylated at Lys-228 and Lys-233 by SIRT1.	28883095
228	K	Acetylation	Ubiquitination is regulated by acetylation at Lys-228 and Lys-233.	28883095
228	K	ubiquitylation	Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the SCF(FBXL17) complex.	28883095
228	K	ubiquitylation	Ubiquitination is regulated by acetylation at Lys-228 and Lys-233.	28883095
233	K	Acetylation	Acetylated at Lys-233 by p300/EP300.	28883095
233	K	Acetylation	Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the SCF(FBXL17) complex.	28883095
233	K	Acetylation	Deacetylated at Lys-228 and Lys-233 by SIRT1.	28883095
233	K	Acetylation	Ubiquitination is regulated by acetylation at Lys-228 and Lys-233.	28883095
233	K	ubiquitylation	Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the SCF(FBXL17) complex.	28883095
233	K	ubiquitylation	Ubiquitination is regulated by acetylation at Lys-228 and Lys-233.	28883095

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RMXL1_MOUSE	Rbmxl1	physical	19858291
YBOX3_MOUSE	Ybx3	physical	19858291
CHTOP_MOUSE	Chtop	physical	19858291
HNRPU_MOUSE	Hnrnpu	physical	19858291
PAIRB_MOUSE	Serbp1	physical	19858291
NOP56_MOUSE	Nop56	physical	19858291
LS14A_MOUSE	Lsm14a	physical	19858291
AXIN1_MOUSE	Axin1	physical	21242974

Drug and Disease Associations

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