RS4Y2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS4Y2_HUMAN
• UniProt AC: Q8TD47
• Protein Name: 40S ribosomal protein S4, Y isoform 2
• Gene Name: RPS4Y2
• Organism: Homo sapiens (Human).
• Sequence Length: 263
• Protein Sequence: MARGPKKHLKRVAAPKHWMLDKLTGVFAPRPSTGPHKLRECLPLIVFLRNRLKYALTGDEVKKICMQHFLKIDGKVRVDITYPAGFIDVISIEKTGEHFRLVYNTKGCFAVHRITVEEAKYKLCKVRKITVGTKGIPHLVTHDARTIRYPDPLIKVNDTVQIDLGTGKITSFIKFDTGNVCMVIAGANLGRVGVITNRERHPGSCDVVHVKDANGNSFATRISNIFVIGNGNKPWISLPRGKGIRLTIAEERDKRLAAKQSSG

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
7	Ubiquitination	-MARGPKKHLKRVAA -CCCCCHHHHHHHHC	58.25	24816145
7	Methylation	-MARGPKKHLKRVAA -CCCCCHHHHHHHHC	58.25	72616607
10	Ubiquitination	RGPKKHLKRVAAPKH CCCHHHHHHHHCCCC	44.54	23000965
16	Acetylation	LKRVAAPKHWMLDKL HHHHHCCCCHHHHHC	45.21	-
16	Ubiquitination	LKRVAAPKHWMLDKL HHHHHCCCCHHHHHC	45.21	23000965
22	Acetylation	PKHWMLDKLTGVFAP CCCHHHHHCCCCCCC	43.94	22635387
22	Ubiquitination	PKHWMLDKLTGVFAP CCCHHHHHCCCCCCC	43.94	23000965
24	Phosphorylation	HWMLDKLTGVFAPRP CHHHHHCCCCCCCCC	36.72	20363803
32	Phosphorylation	GVFAPRPSTGPHKLR CCCCCCCCCCCCHHH	47.47	28450419
33	Phosphorylation	VFAPRPSTGPHKLRE CCCCCCCCCCCHHHH	58.37	28450419
37	Ubiquitination	RPSTGPHKLRECLPL CCCCCCCHHHHHHHH	52.99	21890473
53	Methylation	VFLRNRLKYALTGDE HHHHHCHHHHHHHHH	25.82	164157
53	Acetylation	VFLRNRLKYALTGDE HHHHHCHHHHHHHHH	25.82	164157
53	Ubiquitination	VFLRNRLKYALTGDE HHHHHCHHHHHHHHH	25.82	23000965
54	Phosphorylation	FLRNRLKYALTGDEV HHHHCHHHHHHHHHH	16.07	28152594
57	Phosphorylation	NRLKYALTGDEVKKI HCHHHHHHHHHHHHH	34.12	28152594
62	Ubiquitination	ALTGDEVKKICMQHF HHHHHHHHHHHHHHH	34.08	21906983
62	Acetylation	ALTGDEVKKICMQHF HHHHHHHHHHHHHHH	34.08	24470773
62	Neddylation	ALTGDEVKKICMQHF HHHHHHHHHHHHHHH	34.08	32015554
63	Ubiquitination	LTGDEVKKICMQHFL HHHHHHHHHHHHHHC	46.44	22817900
75	Ubiquitination	HFLKIDGKVRVDITY HHCEECCEEEEEEEE	24.10	-
91	Phosphorylation	AGFIDVISIEKTGEH CCEEEEEEEEECCCE	25.25	-
125	Ubiquitination	EAKYKLCKVRKITVG HHHHEEECEEEEEEC	56.35	-
130	Phosphorylation	LCKVRKITVGTKGIP EECEEEEEECCCCCC	18.87	20860994
133	Phosphorylation	VRKITVGTKGIPHLV EEEEEECCCCCCCEE	23.04	20860994
145	Methylation	HLVTHDARTIRYPDP CEEECCCCCCCCCCC	36.42	-
146	Phosphorylation	LVTHDARTIRYPDPL EEECCCCCCCCCCCE	16.13	28152594
148	Methylation	THDARTIRYPDPLIK ECCCCCCCCCCCEEE	36.00	-
149	Phosphorylation	HDARTIRYPDPLIKV CCCCCCCCCCCEEEC	14.24	28152594
171	Phosphorylation	LGTGKITSFIKFDTG CCCCCEEEEEEECCC	28.57	24719451
211	Ubiquitination	SCDVVHVKDANGNSF CCEEEEEECCCCCCE	35.92	22817900
217	Phosphorylation	VKDANGNSFATRISN EECCCCCCEEEEEEE	20.04	20068231
220	Phosphorylation	ANGNSFATRISNIFV CCCCCEEEEEEEEEE	26.90	20068231
233	Acetylation	FVIGNGNKPWISLPR EEECCCCCCEEECCC	43.03	66724929
233	Ubiquitination	FVIGNGNKPWISLPR EEECCCCCCEEECCC	43.03	22817900
233	Neddylation	FVIGNGNKPWISLPR EEECCCCCCEEECCC	43.03	32015554
237	Phosphorylation	NGNKPWISLPRGKGI CCCCCEEECCCCCCE	28.58	28450419
247	Phosphorylation	RGKGIRLTIAEERDK CCCCEEEEEEHHHHH	14.32	19007248
259	Ubiquitination	RDKRLAAKQSSG--- HHHHHHHHHCCC---	45.14	33845483
261	Phosphorylation	KRLAAKQSSG----- HHHHHHHCCC-----	36.00	29514088
262	Phosphorylation	RLAAKQSSG------ HHHHHHCCC------	46.13	29514088

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

Oops, there are no upstream regulatory protein records of RS4Y2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS4Y2_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 RS4Y2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of RS4Y2_HUMAN !!

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

Acetylation

"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-22, AND MASS SPECTROMETRY.
PubMed: 19608861