dbPTM

RL12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL12_HUMAN
UniProt AC	P30050
Protein Name	60S ribosomal protein L12
Gene Name	RPL12
Organism	Homo sapiens (Human).
Sequence Length	165
Subcellular Localization
Protein Description	Binds directly to 26S ribosomal RNA..
Protein Sequence	MPPKFDPNEIKVVYLRCTGGEVGATSALAPKIGPLGLSPKKVGDDIAKATGDWKGLRITVKLTIQNRQAQIEVVPSASALIIKALKEPPRDRKKQKNIKHSGNITFDEIVNIARQMRHRSLARELSGTIKEILGTAQSVGCNVDGRHPHDIIDDINSGAVECPAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Ubiquitination	KFDPNEIKVVYLRCT CCCHHCCEEEEEEEC	21.33	33845483
14	Phosphorylation	PNEIKVVYLRCTGGE HHCCEEEEEEECCCC	7.45	19658100
17	S-nitrosocysteine	IKVVYLRCTGGEVGA CEEEEEEECCCCCCC	3.70	-
17	S-nitrosylation	IKVVYLRCTGGEVGA CEEEEEEECCCCCCC	3.70	19483679
17	Glutathionylation	IKVVYLRCTGGEVGA CEEEEEEECCCCCCC	3.70	22555962
18	Phosphorylation	KVVYLRCTGGEVGAT EEEEEEECCCCCCCC	41.61	20068231
25	Phosphorylation	TGGEVGATSALAPKI CCCCCCCCCCCCCCC	14.49	21712546
26	Phosphorylation	GGEVGATSALAPKIG CCCCCCCCCCCCCCC	22.28	21712546
31	Ubiquitination	ATSALAPKIGPLGLS CCCCCCCCCCCCCCC	55.47	23000965
31	Acetylation	ATSALAPKIGPLGLS CCCCCCCCCCCCCCC	55.47	26051181
38	Phosphorylation	KIGPLGLSPKKVGDD CCCCCCCCHHHHCHH	32.64	19664994
40	Acetylation	GPLGLSPKKVGDDIA CCCCCCHHHHCHHHH	57.63	25953088
40	Ubiquitination	GPLGLSPKKVGDDIA CCCCCCHHHHCHHHH	57.63	33845483
40	2-Hydroxyisobutyrylation	GPLGLSPKKVGDDIA CCCCCCHHHHCHHHH	57.63	-
40	Malonylation	GPLGLSPKKVGDDIA CCCCCCHHHHCHHHH	57.63	26320211
40	Succinylation	GPLGLSPKKVGDDIA CCCCCCHHHHCHHHH	57.63	23954790
40	Sumoylation	GPLGLSPKKVGDDIA CCCCCCHHHHCHHHH	57.63	28112733
41	Ubiquitination	PLGLSPKKVGDDIAK CCCCCHHHHCHHHHH	55.63	29967540
48	Acetylation	KVGDDIAKATGDWKG HHCHHHHHHHCCCCC	46.98	25953088
48 (in isoform 1)	Ubiquitination	-	46.98	21890473
48	Ubiquitination	KVGDDIAKATGDWKG HHCHHHHHHHCCCCC	46.98	23000965
54	Succinylation	AKATGDWKGLRITVK HHHHCCCCCEEEEEE	53.45	23954790
54	Malonylation	AKATGDWKGLRITVK HHHHCCCCCEEEEEE	53.45	26320211
54	2-Hydroxyisobutyrylation	AKATGDWKGLRITVK HHHHCCCCCEEEEEE	53.45	-
54	Ubiquitination	AKATGDWKGLRITVK HHHHCCCCCEEEEEE	53.45	23000965
54	Acetylation	AKATGDWKGLRITVK HHHHCCCCCEEEEEE	53.45	19608861
61	Acetylation	KGLRITVKLTIQNRQ CCEEEEEEEEEECCC	31.12	26051181
61	Ubiquitination	KGLRITVKLTIQNRQ CCEEEEEEEEEECCC	31.12	33845483
66 (in isoform 2)	Ubiquitination	-	33.89	21890473
67	Methylation	VKLTIQNRQAQIEVV EEEEEECCCHHEEEE	19.48	115491655
76	Phosphorylation	AQIEVVPSASALIIK HHEEEECCHHHHHHH	24.20	28348404
78	Phosphorylation	IEVVPSASALIIKAL EEEECCHHHHHHHHH	28.13	24719451
83 (in isoform 1)	Ubiquitination	-	40.44	21890473
83	Acetylation	SASALIIKALKEPPR CHHHHHHHHHCCCCC	40.44	23954790
83	Ubiquitination	SASALIIKALKEPPR CHHHHHHHHHCCCCC	40.44	23000965
83	2-Hydroxyisobutyrylation	SASALIIKALKEPPR CHHHHHHHHHCCCCC	40.44	-
86	Ubiquitination	ALIIKALKEPPRDRK HHHHHHHCCCCCCHH	73.38	23000965
86	2-Hydroxyisobutyrylation	ALIIKALKEPPRDRK HHHHHHHCCCCCCHH	73.38	-
94	Ubiquitination	EPPRDRKKQKNIKHS CCCCCHHHHHCCCCC	68.36	22817900
96	Ubiquitination	PRDRKKQKNIKHSGN CCCHHHHHCCCCCCC	70.31	22817900
99	2-Hydroxyisobutyrylation	RKKQKNIKHSGNITF HHHHHCCCCCCCCCH	40.90	-
99 (in isoform 1)	Ubiquitination	-	40.90	21890473
99	Acetylation	RKKQKNIKHSGNITF HHHHHCCCCCCCCCH	40.90	25953088
99	Ubiquitination	RKKQKNIKHSGNITF HHHHHCCCCCCCCCH	40.90	22817900
101	Phosphorylation	KQKNIKHSGNITFDE HHHCCCCCCCCCHHH	28.65	21712546
105	Phosphorylation	IKHSGNITFDEIVNI CCCCCCCCHHHHHHH	29.09	21712546
114	Methylation	DEIVNIARQMRHRSL HHHHHHHHHHHHHHH	27.34	115491647
120	Phosphorylation	ARQMRHRSLARELSG HHHHHHHHHHHHHHH	21.91	29514088
126	Phosphorylation	RSLARELSGTIKEIL HHHHHHHHHHHHHHH	29.18	28355574
128	Phosphorylation	LARELSGTIKEILGT HHHHHHHHHHHHHCH	26.04	21712546
130	Ubiquitination	RELSGTIKEILGTAQ HHHHHHHHHHHCHHH	38.24	21963094
130	Acetylation	RELSGTIKEILGTAQ HHHHHHHHHHHCHHH	38.24	26051181
135	Phosphorylation	TIKEILGTAQSVGCN HHHHHHCHHHHCCCC	20.34	28464451
138	Phosphorylation	EILGTAQSVGCNVDG HHHCHHHHCCCCCCC	20.29	24732914
141	Glutathionylation	GTAQSVGCNVDGRHP CHHHHCCCCCCCCCH	4.15	22555962
141	S-nitrosylation	GTAQSVGCNVDGRHP CHHHHCCCCCCCCCH	4.15	22178444
141	S-nitrosocysteine	GTAQSVGCNVDGRHP CHHHHCCCCCCCCCH	4.15	-
157	Phosphorylation	DIIDDINSGAVECPA HCCCCCCCCCCCCCC	28.59	28985074
162	Glutathionylation	INSGAVECPAS---- CCCCCCCCCCC----	2.47	22555962
162	S-nitrosylation	INSGAVECPAS---- CCCCCCCCCCC----	2.47	19483679
162	S-nitrosocysteine	INSGAVECPAS---- CCCCCCCCCCC----	2.47	-
165	Phosphorylation	GAVECPAS------- CCCCCCCC-------	26.37	25159151

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
38	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL12_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 RL12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBA1A_MOUSE	Tuba1a	physical	16169070
A4_HUMAN	APP	physical	21832049
RL13_HUMAN	RPL13	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RL14_HUMAN	RPL14	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RL24_HUMAN	RPL24	physical	22939629
RL27_HUMAN	RPL27	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL7A_HUMAN	RPL7A	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
RS19_HUMAN	RPS19	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS24_HUMAN	RPS24	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
RS9_HUMAN	RPS9	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RL27A_HUMAN	RPL27A	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RS17_HUMAN	RPS17	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RLA1_HUMAN	RPLP1	physical	22939629
RL22_HUMAN	RPL22	physical	22939629
RL17_HUMAN	RPL17	physical	22939629
RL29_HUMAN	RPL29	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
RM12_HUMAN	MRPL12	physical	22939629
S10AA_HUMAN	S100A10	physical	22939629
STK24_HUMAN	STK24	physical	22939629
RACK1_HUMAN	GNB2L1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
STK25_HUMAN	STK25	physical	26344197
STK26_HUMAN	STK26	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 RL12_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-54, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-38, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-38, AND MASSSPECTROMETRY.	19369195 [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-38, AND MASSSPECTROMETRY.	19413330 [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-38, 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-38, AND MASSSPECTROMETRY.	18691976 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.	16964243 [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-38 AND SER-165, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-14, AND MASSSPECTROMETRY.	15592455 [Abstract]