dbPTM

ASML_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ASML_HUMAN
UniProt AC	O95671
Protein Name	N-acetylserotonin O-methyltransferase-like protein
Gene Name	ASMTL
Organism	Homo sapiens (Human).
Sequence Length	621
Subcellular Localization
Protein Description	Unknown. The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity..
Protein Sequence	MVLCPVIGKLLHKRVVLASASPRRQEILSNAGLRFEVVPSKFKEKLDKASFATPYGYAMETAKQKALEVANRLYQKDLRAPDVVIGADTIVTVGGLILEKPVDKQDAYRMLSRLSGREHSVFTGVAIVHCSSKDHQLDTRVSEFYEETKVKFSELSEELLWEYVHSGEPMDKAGGYGIQALGGMLVESVHGDFLNVVGFPLNHFCKQLVKLYYPPRPEDLRRSVKHDSIPAADTFEDLSDVEGGGSEPTQRDAGSRDEKAEAGEAGQATAEAECHRTRETLPPFPTRLLELIEGFMLSKGLLTACKLKVFDLLKDEAPQKAADIASKVDASACGMERLLDICAAMGLLEKTEQGYSNTETANVYLASDGEYSLHGFIMHNNDLTWNLFTYLEFAIREGTNQHHRALGKKAEDLFQDAYYQSPETRLRFMRAMHGMTKLTACQVATAFNLSRFSSACDVGGCTGALARELAREYPRMQVTVFDLPDIIELAAHFQPPGPQAVQIHFAAGDFFRDPLPSAELYVLCRILHDWPDDKVHKLLSRVAESCKPGAGLLLVETLLDEEKRVAQRALMQSLNMLVQTEGKERSLGEYQCLLELHGFHQVQVVHLGGVLDAILATKVAP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Phosphorylation	HKRVVLASASPRRQE HHHHHEECCCHHHHH	25.72	30266825
21	Phosphorylation	RVVLASASPRRQEIL HHHEECCCHHHHHHH	19.22	19664994
41	Ubiquitination	RFEVVPSKFKEKLDK CEEECCHHHHHHHHH	55.15	21890473
41	Ubiquitination	RFEVVPSKFKEKLDK CEEECCHHHHHHHHH	55.15	21890473
41	Acetylation	RFEVVPSKFKEKLDK CEEECCHHHHHHHHH	55.15	25953088
41 (in isoform 1)	Ubiquitination	-	55.15	21890473
41 (in isoform 2)	Ubiquitination	-	55.15	21890473
48	Ubiquitination	KFKEKLDKASFATPY HHHHHHHHCCCCCCC	57.26	-
53	Phosphorylation	LDKASFATPYGYAME HHHCCCCCCCHHHHH	18.29	-
55	Phosphorylation	KASFATPYGYAMETA HCCCCCCCHHHHHHH	20.58	22817900
57	Phosphorylation	SFATPYGYAMETAKQ CCCCCCHHHHHHHHH	9.27	22817900
61	Phosphorylation	PYGYAMETAKQKALE CCHHHHHHHHHHHHH	26.52	-
63	Ubiquitination	GYAMETAKQKALEVA HHHHHHHHHHHHHHH	60.80	-
63 (in isoform 2)	Ubiquitination	-	60.80	-
65	Malonylation	AMETAKQKALEVANR HHHHHHHHHHHHHHH	54.99	26320211
65	Ubiquitination	AMETAKQKALEVANR HHHHHHHHHHHHHHH	54.99	-
72	Methylation	KALEVANRLYQKDLR HHHHHHHHHHHHCCC	25.65	-
74	Phosphorylation	LEVANRLYQKDLRAP HHHHHHHHHHCCCCC	15.41	22817900
74 (in isoform 2)	Phosphorylation	-	15.41	20068231
76 (in isoform 2)	Phosphorylation	-	45.21	-
76	Malonylation	VANRLYQKDLRAPDV HHHHHHHHCCCCCCE	45.21	26320211
76	Ubiquitination	VANRLYQKDLRAPDV HHHHHHHHCCCCCCE	45.21	-
100	Ubiquitination	VGGLILEKPVDKQDA ECCEEEECCCCHHHH	47.07	-
104	Ubiquitination	ILEKPVDKQDAYRML EEECCCCHHHHHHHH	50.76	-
112	Phosphorylation	QDAYRMLSRLSGREH HHHHHHHHHHCCCCC	23.10	23403867
133 (in isoform 2)	Ubiquitination	-	42.83	21890473
133	Ubiquitination	AIVHCSSKDHQLDTR EEEEECCCCCCHHHH	42.83	-
149 (in isoform 1)	Ubiquitination	-	46.86	21890473
149	Ubiquitination	SEFYEETKVKFSELS HHHHHHHCCCHHHHH	46.86	21906983
153	Phosphorylation	EETKVKFSELSEELL HHHCCCHHHHHHHHH	31.73	21406692
156	Phosphorylation	KVKFSELSEELLWEY CCCHHHHHHHHHHHH	25.60	21406692
163	Phosphorylation	SEELLWEYVHSGEPM HHHHHHHHHHCCCCC	7.59	21406692
166	Phosphorylation	LLWEYVHSGEPMDKA HHHHHHHCCCCCCCC	34.50	21406692
210	Acetylation	HFCKQLVKLYYPPRP HHHHHHHHHHCCCCH	39.09	25953088
212	Phosphorylation	CKQLVKLYYPPRPED HHHHHHHHCCCCHHH	14.28	22461510
223	Phosphorylation	RPEDLRRSVKHDSIP CHHHHHHHCCCCCCC	29.14	23927012
225	Ubiquitination	EDLRRSVKHDSIPAA HHHHHHCCCCCCCCC	42.83	-
228	Phosphorylation	RRSVKHDSIPAADTF HHHCCCCCCCCCCCC	30.14	23927012
234	Phosphorylation	DSIPAADTFEDLSDV CCCCCCCCCCCHHCC	24.97	22167270
239	Phosphorylation	ADTFEDLSDVEGGGS CCCCCCHHCCCCCCC	52.51	22167270
246	Phosphorylation	SDVEGGGSEPTQRDA HCCCCCCCCCCCCCC	43.61	25159151
249	Phosphorylation	EGGGSEPTQRDAGSR CCCCCCCCCCCCCCH	31.98	23927012
255	Phosphorylation	PTQRDAGSRDEKAEA CCCCCCCCHHHHHHH	37.97	23401153
269	Phosphorylation	AGEAGQATAEAECHR HHHHHHHHHHHHHHC	19.69	23312004
274	S-nitrosylation	QATAEAECHRTRETL HHHHHHHHHCCCCCC	3.20	22178444
292 (in isoform 2)	Ubiquitination	-	3.39	21890473
299	Acetylation	IEGFMLSKGLLTACK HHHHHHCCHHHHHHH	50.01	26051181
299	Ubiquitination	IEGFMLSKGLLTACK HHHHHHCCHHHHHHH	50.01	-
304 (in isoform 2)	Ubiquitination	-	6.60	21890473
306	Ubiquitination	KGLLTACKLKVFDLL CHHHHHHHHHHHHHH	49.21	-
308	Ubiquitination	LLTACKLKVFDLLKD HHHHHHHHHHHHHCC	26.76	21890473
308 (in isoform 1)	Ubiquitination	-	26.76	21890473
308	Ubiquitination	LLTACKLKVFDLLKD HHHHHHHHHHHHHCC	26.76	21890473
308	Acetylation	LLTACKLKVFDLLKD HHHHHHHHHHHHHCC	26.76	26051181
314	Ubiquitination	LKVFDLLKDEAPQKA HHHHHHHCCCCCHHH	61.90	-
320	Ubiquitination	LKDEAPQKAADIASK HCCCCCHHHHHHHHH	44.47	21906983
320 (in isoform 1)	Ubiquitination	-	44.47	21890473
327	Ubiquitination	KAADIASKVDASACG HHHHHHHHCCHHHHC	34.80	-
335	Sulfoxidation	VDASACGMERLLDIC CCHHHHCHHHHHHHH	2.45	30846556
393 (in isoform 2)	Ubiquitination	-	6.72	21890473
409	Ubiquitination	HHRALGKKAEDLFQD HHHHHHHHHHHHHHH	56.03	2190698
409 (in isoform 1)	Ubiquitination	-	56.03	21890473
418	Phosphorylation	EDLFQDAYYQSPETR HHHHHHHHHCCHHHH	15.44	23403867
419	Phosphorylation	DLFQDAYYQSPETRL HHHHHHHHCCHHHHH	12.30	23403867
421	Phosphorylation	FQDAYYQSPETRLRF HHHHHHCCHHHHHHH	14.47	23401153
424	Phosphorylation	AYYQSPETRLRFMRA HHHCCHHHHHHHHHH	38.09	23403867
437	Ubiquitination	RAMHGMTKLTACQVA HHHCCCCHHHHHHHH	34.64	-
439	Phosphorylation	MHGMTKLTACQVATA HCCCCHHHHHHHHHH	27.26	29083192
445	Phosphorylation	LTACQVATAFNLSRF HHHHHHHHHHCHHHC	32.69	29083192
450	Phosphorylation	VATAFNLSRFSSACD HHHHHCHHHCCCCCC	32.17	29083192
473	Phosphorylation	ARELAREYPRMQVTV HHHHHHHCCCCEEEE	7.21	25278378
517	Phosphorylation	FFRDPLPSAELYVLC CCCCCCCHHHHHHHH	41.90	20068231
521	Phosphorylation	PLPSAELYVLCRILH CCCHHHHHHHHHHHC	5.27	20068231
537	Ubiquitination	WPDDKVHKLLSRVAE CCCHHHHHHHHHHHH	54.86	-
547	Ubiquitination	SRVAESCKPGAGLLL HHHHHHCCCCCEEEE	56.62	-
557	Phosphorylation	AGLLLVETLLDEEKR CEEEEEHHCCCHHHH	25.74	-
563	Ubiquitination	ETLLDEEKRVAQRAL HHCCCHHHHHHHHHH	50.56	-
563	2-Hydroxyisobutyrylation	ETLLDEEKRVAQRAL HHCCCHHHHHHHHHH	50.56	-
567 (in isoform 2)	Ubiquitination	-	28.46	-
573	Phosphorylation	AQRALMQSLNMLVQT HHHHHHHHHHHHHHC	14.03	29978859
580	Phosphorylation	SLNMLVQTEGKERSL HHHHHHHCCCHHCCH	38.95	29978859
583	Ubiquitination	MLVQTEGKERSLGEY HHHHCCCHHCCHHHH	43.66	-

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 ASML_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASML_HUMAN	ASMTL	physical	16189514
A4_HUMAN	APP	physical	21832049
DRB4_HUMAN	HLA-DRB4	physical	21988832
WDR4_HUMAN	WDR4	physical	22863883
ASML_HUMAN	ASMTL	physical	25416956
PNMA1_HUMAN	PNMA1	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956

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 ASML_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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 SER-21 AND SER-239, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY.	17081983 [Abstract]