dbPTM

ANM5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANM5_HUMAN
UniProt AC	O14744
Protein Name	Protein arginine N-methyltransferase 5
Gene Name	PRMT5
Organism	Homo sapiens (Human).
Sequence Length	637
Subcellular Localization	Cytoplasm . Nucleus . Golgi apparatus .
Protein Description	Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. [PubMed: 10531356]
Protein Sequence	MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAMAVGGA ------CCCCCCCCC	13.12	22223895
4	Sulfoxidation	----MAAMAVGGAGG ----CCCCCCCCCCC	1.94	28465586
12	Phosphorylation	AVGGAGGSRVSSGRD CCCCCCCCCCCCCCC	28.70	29759185
15	Phosphorylation	GAGGSRVSSGRDLNC CCCCCCCCCCCCCCC	26.43	29759185
16	Phosphorylation	AGGSRVSSGRDLNCV CCCCCCCCCCCCCCC	34.68	29759185
22	S-palmitoylation	SSGRDLNCVPEIADT CCCCCCCCCHHHHHH	7.60	26865113
22	S-nitrosylation	SSGRDLNCVPEIADT CCCCCCCCCHHHHHH	7.60	19483679
22	Glutathionylation	SSGRDLNCVPEIADT CCCCCCCCCHHHHHH	7.60	22555962
22	S-nitrosocysteine	SSGRDLNCVPEIADT CCCCCCCCCHHHHHH	7.60	-
43	Ubiquitination	QGFDFLCMPVFHPRF CCCCEEEEECCCHHH	3.27	21890473
60	Ubiquitination	EFIQEPAKNRPGPQT HHCCCCCCCCCCCCC	65.29	21906983
68	Ubiquitination	NRPGPQTRSDLLLSG CCCCCCCHHHHHHCC	23.95	21890473
74	Phosphorylation	TRSDLLLSGRDWNTL CHHHHHHCCCCCCCE	31.58	-
78	Ubiquitination	LLLSGRDWNTLIVGK HHHCCCCCCCEEEEE	9.80	21890473
78	Ubiquitination	LLLSGRDWNTLIVGK HHHCCCCCCCEEEEE	9.80	21890473
80	Phosphorylation	LSGRDWNTLIVGKLS HCCCCCCCEEEEECC	17.38	-
81	Ubiquitination	SGRDWNTLIVGKLSP CCCCCCCEEEEECCC	2.42	-
85	Ubiquitination	WNTLIVGKLSPWIRP CCCEEEEECCCCCCC	34.59	21906983
95	Ubiquitination	PWIRPDSKVEKIRRN CCCCCCHHHHHHHHC	62.89	21890473
95	Ubiquitination	PWIRPDSKVEKIRRN CCCCCCHHHHHHHHC	62.89	21890473
132	Phosphorylation	PLNQEDNTNLARVLT ECCCCCCCCHHHHHH	43.88	-
139	Acetylation	TNLARVLTNHIHTGH CCHHHHHHHCCCCCC	23.15	19608861
139	Phosphorylation	TNLARVLTNHIHTGH CCHHHHHHHCCCCCC	23.15	-
144	Phosphorylation	VLTNHIHTGHHSSMF HHHHCCCCCCCCCCE	37.29	-
156	Acetylation	SMFWMRVPLVAPEDL CCEEEECCEECCHHH	15.68	19608861
162	Ubiquitination	VPLVAPEDLRDDIIE CCEECCHHHCCHHHH	46.04	21890473
173	Phosphorylation	DIIENAPTTHTEEYS HHHHCCCCCCCCCCC	28.88	28796482
174	Phosphorylation	IIENAPTTHTEEYSG HHHCCCCCCCCCCCC	26.24	28796482
176	Phosphorylation	ENAPTTHTEEYSGEE HCCCCCCCCCCCCCC	28.55	28796482
179	Nitration	PTTHTEEYSGEEKTW CCCCCCCCCCCCEEE	18.75	-
179	Phosphorylation	PTTHTEEYSGEEKTW CCCCCCCCCCCCEEE	18.75	28796482
180	Phosphorylation	TTHTEEYSGEEKTWM CCCCCCCCCCCEEEH	42.90	28796482
183	Ubiquitination	TEEYSGEEKTWMWWH CCCCCCCCEEEHHHH	60.35	21890473
183	Acetylation	TEEYSGEEKTWMWWH CCCCCCCCEEEHHHH	60.35	19608861
185	Phosphorylation	EYSGEEKTWMWWHNF CCCCCCEEEHHHHCH	24.67	29759185
187	Sulfoxidation	SGEEKTWMWWHNFRT CCCCEEEHHHHCHHH	3.17	28183972
194	Phosphorylation	MWWHNFRTLCDYSKR HHHHCHHHHHHHHHH	27.83	29759185
196	Ubiquitination	WHNFRTLCDYSKRIA HHCHHHHHHHHHHHH	4.57	21890473
198	Phosphorylation	NFRTLCDYSKRIAVA CHHHHHHHHHHHHHH	18.33	29759185
199	Phosphorylation	FRTLCDYSKRIAVAL HHHHHHHHHHHHHHH	11.38	28152594
200	Ubiquitination	RTLCDYSKRIAVALE HHHHHHHHHHHHHHH	41.41	19608861
200	Acetylation	RTLCDYSKRIAVALE HHHHHHHHHHHHHHH	41.41	19608861
200	2-Hydroxyisobutyrylation	RTLCDYSKRIAVALE HHHHHHHHHHHHHHH	41.41	-
210	Ubiquitination	AVALEIGADLPSNHV HHHHHCCCCCCCCCH	22.34	21890473
216	Ubiquitination	GADLPSNHVIDRWLG CCCCCCCCHHHHHCC	23.42	21890473
223	Ubiquitination	HVIDRWLGEPIKAAI CHHHHHCCCCCEEEE	31.51	21890473
227	Ubiquitination	RWLGEPIKAAILPTS HHCCCCCEEEEECCC	42.34	21890473
227	Ubiquitination	RWLGEPIKAAILPTS HHCCCCCEEEEECCC	42.34	21890473
240	Ubiquitination	TSIFLTNKKGFPVLS CCHHHCCCCCCHHHH	49.38	21890473
240	Ubiquitination	TSIFLTNKKGFPVLS CCHHHCCCCCCHHHH	49.38	21890473
240	Acetylation	TSIFLTNKKGFPVLS CCHHHCCCCCCHHHH	49.38	25953088
241	Ubiquitination	SIFLTNKKGFPVLSK CHHHCCCCCCHHHHH	68.78	-
280	Phosphorylation	SEKEFCSYLQYLEYL CHHHHHHHHHHHHHH	10.06	22817900
283	Phosphorylation	EFCSYLQYLEYLSQN HHHHHHHHHHHHHHC	10.02	22817900
286	Phosphorylation	SYLQYLEYLSQNRPP HHHHHHHHHHHCCCC	14.73	22817900
288	Phosphorylation	LQYLEYLSQNRPPPN HHHHHHHHHCCCCCC	25.22	22210691
297	Phosphorylation	NRPPPNAYELFAKGY CCCCCCHHHHHHCCH	21.58	21316606
304	Phosphorylation	YELFAKGYEDYLQSP HHHHHCCHHHHHCCC	12.62	21316606
307	Phosphorylation	FAKGYEDYLQSPLQP HHCCHHHHHCCCCHH	8.49	21316606
308	Ubiquitination	AKGYEDYLQSPLQPL HCCHHHHHCCCCHHH	6.68	21890473
310	Phosphorylation	GYEDYLQSPLQPLMD CHHHHHCCCCHHHHH	25.61	29496963
319	Ubiquitination	LQPLMDNLESQTYEV CHHHHHCHHHCCEEH	6.12	21890473
329	Ubiquitination	QTYEVFEKDPIKYSQ CCEEHHHCCCCCHHH	58.29	-
333	Ubiquitination	VFEKDPIKYSQYQQA HHHCCCCCHHHHHHH	44.21	21890473
334	Phosphorylation	FEKDPIKYSQYQQAI HHCCCCCHHHHHHHH	11.17	26074081
335	Phosphorylation	EKDPIKYSQYQQAIY HCCCCCHHHHHHHHH	19.87	26074081
337	Phosphorylation	DPIKYSQYQQAIYKC CCCCHHHHHHHHHHH	9.17	26074081
342	Phosphorylation	SQYQQAIYKCLLDRV HHHHHHHHHHHHHCC	9.92	26074081
343	Ubiquitination	QYQQAIYKCLLDRVP HHHHHHHHHHHHCCC	16.58	-
348	Methylation	IYKCLLDRVPEEEKD HHHHHHHCCCHHHCC	45.95	115488847
387	Ubiquitination	KQADRRIKLYAVEKN HHCCCCEEEEEEECC	33.36	21906983
418	Ubiquitination	SQVTVVSSDMREWVA CEEEEEECCHHCCCC	24.66	21890473
429	Ubiquitination	EWVAPEKADIIVSEL CCCCHHHHHHHHHHH	16.15	21890473
479	Ubiquitination	LAPISSSKLYNEVRA EEECCHHHHHHHHHH	57.87	21890473
490	Ubiquitination	EVRACREKDRDPEAQ HHHHHHHHCCCHHHH	38.42	2190698
490	Acetylation	EVRACREKDRDPEAQ HHHHHHHHCCCHHHH	38.42	25953088
529	Sulfoxidation	SHPNRDPMIDNNRYC CCCCCCCCCCCCCEE	7.62	30846556
566	Phosphorylation	LYQDITLSIRPETHS EEEEEEEEECCCCCC	14.11	24719451

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
80	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
132	T	Phosphorylation	Kinase	LKB1	Q15831	PSP
139	T	Phosphorylation	Kinase	LKB1	Q15831	PSP
144	T	Phosphorylation	Kinase	LKB1	Q15831	PSP
297	Y	Phosphorylation	Kinase	JAK2	O60674	PSP
304	Y	Phosphorylation	Kinase	JAK2	O60674	PSP
307	Y	Phosphorylation	Kinase	JAK2	O60674	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANM5_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 ANM5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ICLN_HUMAN	CLNS1A	physical	9556550
SPT5H_HUMAN	SUPT5H	physical	12718890
ANM5_HUMAN	PRMT5	physical	11152681
MBP_HUMAN	MBP	physical	11152681
JAK1_HUMAN	JAK1	physical	10531356
JAK2_HUMAN	JAK2	physical	10531356
JAK3_HUMAN	JAK3	physical	10531356
TYK2_HUMAN	TYK2	physical	10531356
ANM5_HUMAN	PRMT5	physical	10531356
ICLN_HUMAN	CLNS1A	physical	11756452
MEP50_HUMAN	WDR77	physical	11756452
PRDM1_HUMAN	PRDM1	physical	18992153
DNM3A_HUMAN	DNMT3A	physical	19234465
MEF2D_HUMAN	MEF2D	physical	19188441
MYOD1_HUMAN	MYOD1	physical	19188441
MYOG_HUMAN	MYOG	physical	19188441
ZN224_HUMAN	ZNF224	physical	19741270
ICLN_HUMAN	CLNS1A	physical	19520849
MBD2_HUMAN	MBD2	physical	16428440
SMCA4_HUMAN	SMARCA4	physical	14559996
SMCA2_HUMAN	SMARCA2	physical	14559996
SIN3A_HUMAN	SIN3A	physical	14559996
SMCE1_HUMAN	SMARCE1	physical	14559996
SNF5_HUMAN	SMARCB1	physical	14559996
H31_HUMAN	HIST1H3A	physical	14559996
CTDP1_HUMAN	CTDP1	physical	15670829
H2A2C_HUMAN	HIST2H2AC	physical	15670829
H31_HUMAN	HIST1H3A	physical	15670829
AJUBA_HUMAN	AJUBA	physical	18347060
H31_HUMAN	HIST1H3A	physical	15485929
JAK2_HUMAN	JAK2	physical	21316606
CCND1_HUMAN	CCND1	physical	20951943
CDK4_HUMAN	CDK4	physical	20951943
SMCA4_HUMAN	SMARCA4	physical	20951943
MEP50_HUMAN	WDR77	physical	20951943
RSMB_HUMAN	SNRPB	physical	17709427
H31_HUMAN	HIST1H3A	physical	22231400
MEP50_HUMAN	WDR77	physical	22169276
HXA9_HUMAN	HOXA9	physical	22269951
ORF73_HHV8P	HHV8GK18_gp81	physical	22179613
DYST_HUMAN	DST	physical	22939629
RU17_HUMAN	SNRNP70	physical	22365833
SF3A3_HUMAN	SF3A3	physical	22365833
RBM23_HUMAN	RBM23	physical	22365833
CCAR2_HUMAN	CCAR2	physical	22365833
ARGL1_HUMAN	ARGLU1	physical	22365833
ANM5_HUMAN	PRMT5	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
ICLN_HUMAN	CLNS1A	physical	22365833
MEP50_HUMAN	WDR77	physical	23071334
ANM5_HUMAN	PRMT5	physical	23071334
TF65_HUMAN	RELA	physical	23904475
CSN4_HUMAN	COPS4	physical	22863883
VASP_HUMAN	VASP	physical	22863883
PRDM1_MOUSE	Prdm1	physical	16699504
WDR5_HUMAN	WDR5	physical	22689669
ING2_HUMAN	ING2	physical	22689669
PYRG1_HUMAN	CTPS1	physical	26344197
DYHC1_HUMAN	DYNC1H1	physical	26344197
IF2A_HUMAN	EIF2S1	physical	26344197
NCBP1_HUMAN	NCBP1	physical	26344197
NSF1C_HUMAN	NSFL1C	physical	26344197
PDCD4_HUMAN	PDCD4	physical	26344197
PDIA6_HUMAN	PDIA6	physical	26344197
RRP12_HUMAN	RRP12	physical	26344197
SBNO1_HUMAN	SBNO1	physical	26344197
MEP50_HUMAN	WDR77	physical	26344197
MEP50_HUMAN	WDR77	physical	18404153
COPRS_HUMAN	COPRS	physical	18404153
MEP50_XENLA	wdr77	physical	25713080
CDK8_HUMAN	CDK8	physical	23749998
CDK19_HUMAN	CDK19	physical	23749998
TRAF4_HUMAN	TRAF4	physical	25704480
TF65_HUMAN	RELA	physical	25704480
SRBP1_HUMAN	SREBF1	physical	26759235
CHIP_HUMAN	STUB1	physical	26658161
RO52_HUMAN	TRIM21	physical	26658161
RBP2_HUMAN	RANBP2	physical	26658161
RPB1_HUMAN	POLR2A	physical	26700805
UHRF1_HUMAN	UHRF1	physical	26597461

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 ANM5_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND MASS SPECTROMETRY.	19608861 [Abstract]