ANM8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANM8_HUMAN
• UniProt AC: Q9NR22
• Protein Name: Protein arginine N-methyltransferase 8 {ECO:0000305}
• Gene Name: PRMT8 {ECO:0000244|HGNC:HGNC:5188}
• Organism: Homo sapiens (Human).
• Sequence Length: 394
• Subcellular Localization: Cell membrane ; Lipid-anchor ; Cytoplasmic side .
• Protein Description: S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer. [PubMed: 16051612]
• Protein Sequence: MGMKHSSRCLLLRRKMAENAAESTEVNSPPSQPPQPVVPAKPVQCVHHVSTQPSCPGRGKMSKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECSSISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWWENVYGFDMTCIRDVAMKEPLVDIVDPKQVVTNACLIKEVDIYTVKTEELSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRRGEEIYGTISMKPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR

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
2	N-myristoyl glycine	------MGMKHSSRC ------CCCCHHHHH	33.57	-
2	Myristoylation	------MGMKHSSRC ------CCCCHHHHH	33.57	16051612
15	Ubiquitination	RCLLLRRKMAENAAE HHHHHHHHHHHHHHH	35.71	-
58	Methylation	TQPSCPGRGKMSKLL CCCCCCCCCCHHHCC	27.05	17925405
71	Phosphorylation	LLNPEEMTSRDYYFD CCCHHHHCCCCHHHH	24.72	28152594
72	Phosphorylation	LNPEEMTSRDYYFDS CCHHHHCCCCHHHHH	23.11	28152594
73	Asymmetric dimethylarginine	NPEEMTSRDYYFDSY CHHHHCCCCHHHHHH	27.12	-
73	Methylation	NPEEMTSRDYYFDSY CHHHHCCCCHHHHHH	27.12	17925405
120	Phosphorylation	KVVLDVGSGTGILSM EEEEEECCCCCHHHH	32.79	20068231
122	Phosphorylation	VLDVGSGTGILSMFA EEEECCCCCHHHHHH	23.81	20068231
126	Phosphorylation	GSGTGILSMFAAKAG CCCCCHHHHHHHHHC	15.21	20068231
159 (in isoform 2)	Ubiquitination	-	36.41	21906983
168	Ubiquitination	IITIFKGKVEEVELP EEEEEECCCEEEECC	47.25	-
168 (in isoform 1)	Ubiquitination	-	47.25	21906983
168	Acetylation	IITIFKGKVEEVELP EEEEEECCCEEEECC	47.25	66725521
189	Phosphorylation	IISEWMGYCLFYESM EHHHHHHHHHHHHHH	3.07	-
193	Phosphorylation	WMGYCLFYESMLNTV HHHHHHHHHHHHHHH	8.31	-
222	Phosphorylation	FPDRAALYVVAIEDR CCCCEEEEEEEECCC	6.53	-
281	Phosphorylation	LIKEVDIYTVKTEEL EEEEEEEEEEECCEE	10.87	29978859
282	Phosphorylation	IKEVDIYTVKTEELS EEEEEEEEEECCEEE	18.83	29978859
338	Phosphorylation	PYTHWKQTVFYLEDY CCCCHHCEEEEEEEE	14.62	26074081
341	Phosphorylation	HWKQTVFYLEDYLTV CHHCEEEEEEEEEEE	12.58	26074081

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

Oops, there are no upstream regulatory protein records of ANM8_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ANM8_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ANM8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANM8_HUMAN	PRMT8	physical	16189514
ORF73_HHV8P	HHV8GK18_gp81	physical	22179613
ANM8_HUMAN	PRMT8	physical	19060904
RBP56_HUMAN	TAF15	physical	16051612
ANM1_HUMAN	PRMT1	physical	16051612
ANM8_HUMAN	PRMT8	physical	16051612
ANM1_HUMAN	PRMT1	physical	23455924
ANM8_HUMAN	PRMT8	physical	23455924
ANM8_HUMAN	PRMT8	physical	25416956
EWS_HUMAN	EWSR1	physical	26186194
NFM_HUMAN	NEFM	physical	26186194
VIME_HUMAN	VIM	physical	26186194
AINX_HUMAN	INA	physical	26186194
HNRPU_HUMAN	HNRNPU	physical	26186194
F120A_HUMAN	FAM120A	physical	26186194
DHX9_HUMAN	DHX9	physical	26186194
HNRPR_HUMAN	HNRNPR	physical	26186194
HNRPQ_HUMAN	SYNCRIP	physical	26186194
ANM1_HUMAN	PRMT1	physical	26186194
BCLF1_HUMAN	BCLAF1	physical	26186194
TR150_HUMAN	THRAP3	physical	26186194
LS14A_HUMAN	LSM14A	physical	26186194
PRC2C_HUMAN	PRRC2C	physical	26186194
HNRL2_HUMAN	HNRNPUL2	physical	26186194
ROA1_HUMAN	HNRNPA1	physical	26186194
CHTOP_HUMAN	CHTOP	physical	26186194
FBW1B_HUMAN	FBXW11	physical	26186194
SCAFB_HUMAN	SCAF11	physical	26186194
THOC4_HUMAN	ALYREF	physical	26186194
ANGE2_HUMAN	ANGEL2	physical	26186194
HNRPU_HUMAN	HNRNPU	physical	28514442
ANM1_HUMAN	PRMT1	physical	28514442
HNRPR_HUMAN	HNRNPR	physical	28514442
ANGE2_HUMAN	ANGEL2	physical	28514442
LS14A_HUMAN	LSM14A	physical	28514442
DHX9_HUMAN	DHX9	physical	28514442
CHTOP_HUMAN	CHTOP	physical	28514442
F120A_HUMAN	FAM120A	physical	28514442
HNRPQ_HUMAN	SYNCRIP	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
SCAFB_HUMAN	SCAF11	physical	28514442
HNRL2_HUMAN	HNRNPUL2	physical	28514442
HNRPK_HUMAN	HNRNPK	physical	28514442
THOC4_HUMAN	ALYREF	physical	28514442
VIME_HUMAN	VIM	physical	28514442
EWS_HUMAN	EWSR1	physical	28514442
BCLF1_HUMAN	BCLAF1	physical	28514442
ROA1_HUMAN	HNRNPA1	physical	28514442
AINX_HUMAN	INA	physical	28514442
FBW1B_HUMAN	FBXW11	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.

Related Literatures of Post-Translational Modification

Methylation

"Regulation of protein arginine methyltransferase 8 (PRMT8) activityby its N-terminal domain.";
Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.;
J. Biol. Chem. 282:36444-36453(2007).
Cited for: FUNCTION, N-TERMINAL REGION DOMAIN, SH3-BINDING MOTIF DOMAIN,AUTOMETHYLATION AT ARG-58 AND ARG-73, AND INTERACTION WITH PRMT2 ANDFYN.
PubMed: 17925405

Myristoylation

"PRMT8, a new membrane-bound tissue-specific member of the proteinarginine methyltransferase family.";
Lee J., Sayegh J., Daniel J., Clarke S., Bedford M.T.;
J. Biol. Chem. 280:32890-32896(2005).
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MYRISTOYLATION ATGLY-2, AND MUTAGENESIS OF GLY-2.
PubMed: 16051612