dbPTM

RL24_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL24_HUMAN
UniProt AC	P83731
Protein Name	60S ribosomal protein L24
Gene Name	RPL24
Organism	Homo sapiens (Human).
Sequence Length	157
Subcellular Localization
Protein Description
Protein Sequence	MKVELCSFSGYKIYPGHGRRYARTDGKVFQFLNAKCESAFLSKRNPRQINWTVLYRRKHKKGQSEEIQKKRTRRAVKFQRAITGASLADIMAKRNQKPEVRKAQREQAIRAAKEAKKAKQASKKTAMAAAKAPTKAAPKQKIVKPVKVSAPRVGGKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Ubiquitination	------MKVELCSFS ------CCEEECCCC	44.40	21890473
2	Sumoylation	------MKVELCSFS ------CCEEECCCC	44.40	28112733
2	2-Hydroxyisobutyrylation	------MKVELCSFS ------CCEEECCCC	44.40	-
2	Sumoylation	------MKVELCSFS ------CCEEECCCC	44.40	-
6	S-nitrosocysteine	--MKVELCSFSGYKI --CCEEECCCCCCEE	2.15	-
6	Glutathionylation	--MKVELCSFSGYKI --CCEEECCCCCCEE	2.15	22555962
6	S-nitrosylation	--MKVELCSFSGYKI --CCEEECCCCCCEE	2.15	19483679
7	Phosphorylation	-MKVELCSFSGYKIY -CCEEECCCCCCEEC	34.76	28450419
9	Phosphorylation	KVELCSFSGYKIYPG CEEECCCCCCEECCC	25.56	28450419
11	Phosphorylation	ELCSFSGYKIYPGHG EECCCCCCEECCCCC	7.94	28450419
11	Nitration	ELCSFSGYKIYPGHG EECCCCCCEECCCCC	7.94	-
12	Acetylation	LCSFSGYKIYPGHGR ECCCCCCEECCCCCC	39.01	23236377
12	Ubiquitination	LCSFSGYKIYPGHGR ECCCCCCEECCCCCC	39.01	21890473
14	Phosphorylation	SFSGYKIYPGHGRRY CCCCCEECCCCCCCE	10.06	28152594
19	Methylation	KIYPGHGRRYARTDG EECCCCCCCEEECCC	23.82	115491893
24	Phosphorylation	HGRRYARTDGKVFQF CCCCEEECCCCHHHH	40.72	19194518
27	Ubiquitination	RYARTDGKVFQFLNA CEEECCCCHHHHHHH	42.56	20639865
27	Sumoylation	RYARTDGKVFQFLNA CEEECCCCHHHHHHH	42.56	-
27	Malonylation	RYARTDGKVFQFLNA CEEECCCCHHHHHHH	42.56	26320211
27	Acetylation	RYARTDGKVFQFLNA CEEECCCCHHHHHHH	42.56	19608861
27	2-Hydroxyisobutyrylation	RYARTDGKVFQFLNA CEEECCCCHHHHHHH	42.56	-
27	Sumoylation	RYARTDGKVFQFLNA CEEECCCCHHHHHHH	42.56	28112733
35	Ubiquitination	VFQFLNAKCESAFLS HHHHHHHHHHHHHHH	37.14	21890473
35	Sumoylation	VFQFLNAKCESAFLS HHHHHHHHHHHHHHH	37.14	28112733
35	Acetylation	VFQFLNAKCESAFLS HHHHHHHHHHHHHHH	37.14	25953088
35	2-Hydroxyisobutyrylation	VFQFLNAKCESAFLS HHHHHHHHHHHHHHH	37.14	-
36	Glutathionylation	FQFLNAKCESAFLSK HHHHHHHHHHHHHHC	4.67	22555962
36	S-palmitoylation	FQFLNAKCESAFLSK HHHHHHHHHHHHHHC	4.67	29575903
38	Phosphorylation	FLNAKCESAFLSKRN HHHHHHHHHHHHCCC	33.52	29396449
42	Phosphorylation	KCESAFLSKRNPRQI HHHHHHHHCCCHHHC	24.10	29396449
43	Acetylation	CESAFLSKRNPRQIN HHHHHHHCCCHHHCC	59.34	23749302
43	Ubiquitination	CESAFLSKRNPRQIN HHHHHHHCCCHHHCC	59.34	21890473
43	2-Hydroxyisobutyrylation	CESAFLSKRNPRQIN HHHHHHHCCCHHHCC	59.34	-
61	Ubiquitination	LYRRKHKKGQSEEIQ EEECCCCCCCCHHHH	63.00	21906983
64	Phosphorylation	RKHKKGQSEEIQKKR CCCCCCCCHHHHHHH	45.96	21815630
69	Succinylation	GQSEEIQKKRTRRAV CCCHHHHHHHHHHHH	50.30	23954790
69	Acetylation	GQSEEIQKKRTRRAV CCCHHHHHHHHHHHH	50.30	26051181
69	Ubiquitination	GQSEEIQKKRTRRAV CCCHHHHHHHHHHHH	50.30	-
70	Ubiquitination	QSEEIQKKRTRRAVK CCHHHHHHHHHHHHH	42.50	-
77	Ubiquitination	KRTRRAVKFQRAITG HHHHHHHHHHHHHHH	34.49	19608861
77	Acetylation	KRTRRAVKFQRAITG HHHHHHHHHHHHHHH	34.49	19608861
83	Phosphorylation	VKFQRAITGASLADI HHHHHHHHHHHHHHH	26.22	29255136
86	Phosphorylation	QRAITGASLADIMAK HHHHHHHHHHHHHHH	25.99	29255136
91	Sulfoxidation	GASLADIMAKRNQKP HHHHHHHHHHCCCCH	3.56	21406390
93	Sumoylation	SLADIMAKRNQKPEV HHHHHHHHCCCCHHH	34.21	-
93	2-Hydroxyisobutyrylation	SLADIMAKRNQKPEV HHHHHHHHCCCCHHH	34.21	-
93	Ubiquitination	SLADIMAKRNQKPEV HHHHHHHHCCCCHHH	34.21	21890473
93	Succinylation	SLADIMAKRNQKPEV HHHHHHHHCCCCHHH	34.21	23954790
93	Acetylation	SLADIMAKRNQKPEV HHHHHHHHCCCCHHH	34.21	19608861
93	Sumoylation	SLADIMAKRNQKPEV HHHHHHHHCCCCHHH	34.21	19608861
97	Ubiquitination	IMAKRNQKPEVRKAQ HHHHCCCCHHHHHHH	46.85	21906983
97	2-Hydroxyisobutyrylation	IMAKRNQKPEVRKAQ HHHHCCCCHHHHHHH	46.85	-
97	Acetylation	IMAKRNQKPEVRKAQ HHHHCCCCHHHHHHH	46.85	26051181
113	Acetylation	EQAIRAAKEAKKAKQ HHHHHHHHHHHHHHH	58.16	21339330
113	Ubiquitination	EQAIRAAKEAKKAKQ HHHHHHHHHHHHHHH	58.16	-
116	Acetylation	IRAAKEAKKAKQASK HHHHHHHHHHHHHHH	55.12	21339330
117	Acetylation	RAAKEAKKAKQASKK HHHHHHHHHHHHHHH	68.79	21339330
119	Acetylation	AKEAKKAKQASKKTA HHHHHHHHHHHHHHH	56.10	21339330
124	Ubiquitination	KAKQASKKTAMAAAK HHHHHHHHHHHHHHH	38.73	-
124	Acetylation	KAKQASKKTAMAAAK HHHHHHHHHHHHHHH	38.73	26051181
125	Phosphorylation	AKQASKKTAMAAAKA HHHHHHHHHHHHHHC	25.96	29457462
127	Sulfoxidation	QASKKTAMAAAKAPT HHHHHHHHHHHHCCC	2.93	30846556
131	Succinylation	KTAMAAAKAPTKAAP HHHHHHHHCCCCCCC	50.61	21906983
131	Succinylation	KTAMAAAKAPTKAAP HHHHHHHHCCCCCCC	50.61	-
131	Acetylation	KTAMAAAKAPTKAAP HHHHHHHHCCCCCCC	50.61	25953088
131	Ubiquitination	KTAMAAAKAPTKAAP HHHHHHHHCCCCCCC	50.61	-
134	Phosphorylation	MAAAKAPTKAAPKQK HHHHHCCCCCCCCCC	37.87	29457462
135	2-Hydroxyisobutyrylation	AAAKAPTKAAPKQKI HHHHCCCCCCCCCCC	41.30	-
135	Acetylation	AAAKAPTKAAPKQKI HHHHCCCCCCCCCCC	41.30	25953088
135	Ubiquitination	AAAKAPTKAAPKQKI HHHHCCCCCCCCCCC	41.30	-
139	Acetylation	APTKAAPKQKIVKPV CCCCCCCCCCCCCCE	60.54	26051181
141	Acetylation	TKAAPKQKIVKPVKV CCCCCCCCCCCCEEE	56.44	12431411
144	Ubiquitination	APKQKIVKPVKVSAP CCCCCCCCCEEECCC	47.79	-
147	Sumoylation	QKIVKPVKVSAPRVG CCCCCCEEECCCCCC	38.71	28112733
147	Ubiquitination	QKIVKPVKVSAPRVG CCCCCCEEECCCCCC	38.71	2097226
147	Sumoylation	QKIVKPVKVSAPRVG CCCCCCEEECCCCCC	38.71	-
147	Acetylation	QKIVKPVKVSAPRVG CCCCCCEEECCCCCC	38.71	25953088
147	Methylation	QKIVKPVKVSAPRVG CCCCCCEEECCCCCC	38.71	8275829
149	Phosphorylation	IVKPVKVSAPRVGGK CCCCEEECCCCCCCC	27.17	29255136
156	Acetylation	SAPRVGGKR------ CCCCCCCCC------	49.35	8275841

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 RL24_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL24_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 RL24_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL31_HUMAN	RPL31	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS17_HUMAN	RPS17	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL27A_HUMAN	RPL27A	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
TIM13_HUMAN	TIMM13	physical	22939629
STRAP_HUMAN	STRAP	physical	22939629
HIRP3_HUMAN	HIRIP3	physical	22863883
OXR1_HUMAN	OXR1	physical	22863883
PURB_HUMAN	PURB	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
SF01_HUMAN	SF1	physical	22863883
HNRPQ_HUMAN	SYNCRIP	physical	22863883
VPS35_HUMAN	VPS35	physical	22863883
EF1A1_HUMAN	EEF1A1	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL10L_HUMAN	RPL10L	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RL22_HUMAN	RPL22	physical	26344197
RL23_HUMAN	RPL23	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL26_HUMAN	RPL26	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	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.

Regulatory Network of RL24_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-27; LYS-77 AND LYS-93, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.	19369195 [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 THR-83 AND SER-86, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, AND MASSSPECTROMETRY.	17287340 [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 THR-83, AND MASSSPECTROMETRY.	17081983 [Abstract]