dbPTM

ANM6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANM6_HUMAN
UniProt AC	Q96LA8
Protein Name	Protein arginine N-methyltransferase 6
Gene Name	PRMT6
Organism	Homo sapiens (Human).
Sequence Length	375
Subcellular Localization	Nucleus .
Protein Description	Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. [PubMed: 17898714]
Protein Sequence	MSQPKKRKLESGGGGEGGEGTEEEDGAEREAALERPRRTKRERDQLYYECYSDVSVHEEMIADRVRTDAYRLGILRNWAALRGKTVLDVGAGTGILSIFCAQAGARRVYAVEASAIWQQAREVVRFNGLEDRVHVLPGPVETVELPEQVDAIVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFIAPISDQMLEWRLGFWSQVKQHYGVDMSCLEGFATRCLMGHSEIVVQGLSGEDVLARPQRFAQLELSRAGLEQELEAGVGGRFRCSCYGSAPMHGFAIWFQVTFPGGESEKPLVLSTSPFHPATHWKQALLYLNEPVQVEQDTDVSGEITLLPSRDNPRRLRVLLRYKVGDQEEKTKDFAMED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	PKKRKLESGGGGEGG CCCCCCCCCCCCCCC	53.85	20873877
21	Phosphorylation	GGEGGEGTEEEDGAE CCCCCCCCCCCCHHH	35.60	23401153
29	Methylation	EEEDGAEREAALERP CCCCHHHHHHHHHCC	38.02	23866860
31 (in isoform 2)	Phosphorylation	-	24.46	23879269
35	Methylation	EREAALERPRRTKRE HHHHHHHCCCCCHHH	30.76	23866860
37	Methylation	EAALERPRRTKRERD HHHHHCCCCCHHHHH	66.19	23866860
38	Methylation	AALERPRRTKRERDQ HHHHCCCCCHHHHHH	47.48	115488871
40	Methylation	LERPRRTKRERDQLY HHCCCCCHHHHHHHH	50.91	115488879
43	Methylation	PRRTKRERDQLYYEC CCCCHHHHHHHHHHH	40.80	82797475
47	Phosphorylation	KRERDQLYYECYSDV HHHHHHHHHHHHCCC	7.50	26657352
48	Phosphorylation	RERDQLYYECYSDVS HHHHHHHHHHHCCCC	14.23	26657352
215	Phosphorylation	WSQVKQHYGVDMSCL HHHHHHHHCCCHHHH	19.15	21214269
221	S-nitrosylation	HYGVDMSCLEGFATR HHCCCHHHHHHHHHH	3.00	24105792
227	Phosphorylation	SCLEGFATRCLMGHS HHHHHHHHHHHHCCC	21.47	21214269
229	S-nitrosylation	LEGFATRCLMGHSEI HHHHHHHHHHCCCEE	2.39	24105792
308	Phosphorylation	SEKPLVLSTSPFHPA CCCCEEEECCCCCCC	21.25	28634298
309	Phosphorylation	EKPLVLSTSPFHPAT CCCEEEECCCCCCCC	35.94	28634298
310	Phosphorylation	KPLVLSTSPFHPATH CCEEEECCCCCCCCC	23.38	28634298
324	Phosphorylation	HWKQALLYLNEPVQV CHHHHHHHHCCCEEE	14.34	-
346	Phosphorylation	GEITLLPSRDNPRRL CEEEEEECCCCHHHE	52.84	25278378
359	Phosphorylation	RLRVLLRYKVGDQEE HEEEEEEEECCCHHH	15.25	27794612

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
Oops, there are no upstream regulatory protein records of ANM6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANM6_HUMAN !!

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 ANM6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HMGA1_HUMAN	HMGA1	physical	16293633
HMGA2_HUMAN	HMGA2	physical	16293633
PABP1_HUMAN	PABPC1	physical	16293633
HMGA1_MOUSE	Hmga1	physical	16293633
HMGA2_MOUSE	Hmga2	physical	16293633
FBRL_HUMAN	FBL	physical	16157300
HMGA1_HUMAN	HMGA1	physical	16157300
H32_HUMAN	HIST2H3C	physical	18079182
ORF73_HHV8P	HHV8GK18_gp81	physical	22179613
H32_HUMAN	HIST2H3C	physical	23349634
H2B2E_HUMAN	HIST2H2BE	physical	23349634
H2A2A_HUMAN	HIST2H2AA3	physical	23349634
KIF9_HUMAN	KIF9	physical	25416956
UBR4_HUMAN	UBR4	physical	26186194
AT1A3_HUMAN	ATP1A3	physical	26186194
TFCP2_HUMAN	TFCP2	physical	26186194
UBIP1_HUMAN	UBP1	physical	26186194
DJC12_HUMAN	DNAJC12	physical	26186194
KIRR1_HUMAN	KIRREL	physical	26186194
PPR1A_HUMAN	PPP1R1A	physical	26186194
DC2L1_HUMAN	DYNC2LI1	physical	26186194
ENAH_HUMAN	ENAH	physical	26186194
S23IP_HUMAN	SEC23IP	physical	26186194
MADD_HUMAN	MADD	physical	26186194
FOXC1_HUMAN	FOXC1	physical	26186194
P73_HUMAN	TP73	physical	26186194
N42L2_HUMAN	N4BP2L2	physical	26186194
SMG7_HUMAN	SMG7	physical	26186194
GPS2_HUMAN	GPS2	physical	26070566
UBIP1_HUMAN	UBP1	physical	28514442
TFCP2_HUMAN	TFCP2	physical	28514442
PPR1A_HUMAN	PPP1R1A	physical	28514442
S23IP_HUMAN	SEC23IP	physical	28514442
DJC12_HUMAN	DNAJC12	physical	28514442
ENAH_HUMAN	ENAH	physical	28514442
KIRR1_HUMAN	KIRREL	physical	28514442
N42L2_HUMAN	N4BP2L2	physical	28514442
MADD_HUMAN	MADD	physical	28514442

Drug and Disease Associations

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

Regulatory Network of ANM6_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND MASSSPECTROMETRY.	18691976 [Abstract]