RL37_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL37_HUMAN
• UniProt AC: P61927
• Protein Name: 60S ribosomal protein L37
• Gene Name: RPL37
• Organism: Homo sapiens (Human).
• Sequence Length: 97
• Protein Description: Binds to the 23S rRNA..
• Protein Sequence: MTKGTSSFGKRRNKTHTLCRRCGSKAYHLQKSTCGKCGYPAKRKRKYNWSAKAKRRNTTGTGRMRHLKIVYRRFRHGFREGTTPKPKRAAVAASSSS

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
3	Ubiquitination	-----MTKGTSSFGK -----CCCCCCCCCC	59.91	24816145
6	Phosphorylation	--MTKGTSSFGKRRN --CCCCCCCCCCCCC	32.13	29396449
7	Phosphorylation	-MTKGTSSFGKRRNK -CCCCCCCCCCCCCC	37.54	29396449
10	Acetylation	KGTSSFGKRRNKTHT CCCCCCCCCCCCHHH	46.29	19608861
10	Ubiquitination	KGTSSFGKRRNKTHT CCCCCCCCCCCCHHH	46.29	19608861
14	Ubiquitination	SFGKRRNKTHTLCRR CCCCCCCCHHHHHHH	39.61	24816145
14	2-Hydroxyisobutyrylation	SFGKRRNKTHTLCRR CCCCCCCCHHHHHHH	39.61	-
25	Ubiquitination	LCRRCGSKAYHLQKS HHHHHCCCHHHCCCC	37.94	23000965
25	Acetylation	LCRRCGSKAYHLQKS HHHHHCCCHHHCCCC	37.94	26051181
27	Nitration	RRCGSKAYHLQKSTC HHHCCCHHHCCCCCC	13.55	-
31	Ubiquitination	SKAYHLQKSTCGKCG CCHHHCCCCCCCCCC	54.84	23000965
31	2-Hydroxyisobutyrylation	SKAYHLQKSTCGKCG CCHHHCCCCCCCCCC	54.84	-
31	Acetylation	SKAYHLQKSTCGKCG CCHHHCCCCCCCCCC	54.84	25825284
36	2-Hydroxyisobutyrylation	LQKSTCGKCGYPAKR CCCCCCCCCCCCCHH	27.00	-
36	Ubiquitination	LQKSTCGKCGYPAKR CCCCCCCCCCCCCHH	27.00	23000965
42	Ubiquitination	GKCGYPAKRKRKYNW CCCCCCCHHCCCCCC	54.68	23000965
42	Acetylation	GKCGYPAKRKRKYNW CCCCCCCHHCCCCCC	54.68	25953088
46	Acetylation	YPAKRKRKYNWSAKA CCCHHCCCCCCCHHC	46.07	27452117
46	Ubiquitination	YPAKRKRKYNWSAKA CCCHHCCCCCCCHHC	46.07	21963094
47	Phosphorylation	PAKRKRKYNWSAKAK CCHHCCCCCCCHHCC	26.37	23882029
50	Phosphorylation	RKRKYNWSAKAKRRN HCCCCCCCHHCCCCC	19.09	21712546
52	Acetylation	RKYNWSAKAKRRNTT CCCCCCHHCCCCCCC	49.26	25953088
52	Ubiquitination	RKYNWSAKAKRRNTT CCCCCCHHCCCCCCC	49.26	21963094
52	Methylation	RKYNWSAKAKRRNTT CCCCCCHHCCCCCCC	49.26	54413867
54	Ubiquitination	YNWSAKAKRRNTTGT CCCCHHCCCCCCCCC	51.70	-
59	Phosphorylation	KAKRRNTTGTGRMRH HCCCCCCCCCCHHHH	35.97	20363803
68	Ubiquitination	TGRMRHLKIVYRRFR CCHHHHHHHHHHHHH	24.81	23000965
68	2-Hydroxyisobutyrylation	TGRMRHLKIVYRRFR CCHHHHHHHHHHHHH	24.81	-
68	Acetylation	TGRMRHLKIVYRRFR CCHHHHHHHHHHHHH	24.81	26051181
82	Phosphorylation	RHGFREGTTPKPKRA HHCCCCCCCCCCCHH	34.86	20068231
83	Phosphorylation	HGFREGTTPKPKRAA HCCCCCCCCCCCHHH	39.92	30576142
85	Ubiquitination	FREGTTPKPKRAAVA CCCCCCCCCCHHHHH	62.16	24816145
94	Phosphorylation	KRAAVAASSSS---- CHHHHHHCCCC----	22.48	20363803
95	O-linked_Glycosylation	RAAVAASSSS----- HHHHHHCCCC-----	29.85	30059200
95	Phosphorylation	RAAVAASSSS----- HHHHHHCCCC-----	29.85	30266825
96	O-linked_Glycosylation	AAVAASSSS------ HHHHHCCCC------	37.26	30059200
96	Phosphorylation	AAVAASSSS------ HHHHHCCCC------	37.26	30266825
97	Phosphorylation	AVAASSSS------- HHHHCCCC-------	46.30	30266825

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

Oops, there are no upstream regulatory protein records of RL37_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL37_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 RL37_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RS9_HUMAN	RPS9	physical	22939629
MDM2_HUMAN	MDM2	physical	23874713
MDM4_HUMAN	MDM4	physical	23874713
WIF1_HUMAN	WIF1	physical	21988832
TFE2_HUMAN	TCF3	physical	21988832
SQSTM_HUMAN	SQSTM1	physical	21988832
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL40_HUMAN	UBA52	physical	26344197

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-10, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-97, AND MASSSPECTROMETRY.
PubMed: 18691976