dbPTM

RL23A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL23A_HUMAN
UniProt AC	P62750
Protein Name	60S ribosomal protein L23a
Gene Name	RPL23A
Organism	Homo sapiens (Human).
Sequence Length	156
Subcellular Localization
Protein Description	Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds a specific region on the 26S rRNA. May promote p53/TP53 degradation possibly through the stimulation of MDM2-mediated TP53 polyubiquitination. [PubMed: 26203195]
Protein Sequence	MAPKAKKEAPAPPKAEAKAKALKAKKAVLKGVHSHKKKKIRTSPTFRRPKTLRLRRQPKYPRKSAPRRNKLDHYAIIKFPLTTESAMKKIEDNNTLVFIVDVKANKHQIKQAVKKLYDIDVAKVNTLIRPDGEKKAYVRLAPDYDALDVANKIGII

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MAPKAKKEA ------CCCHHCCCC	17.82	-
7	Ubiquitination	-MAPKAKKEAPAPPK -CCCHHCCCCCCCCH	65.06	33845483
7	Acetylation	-MAPKAKKEAPAPPK -CCCHHCCCCCCCCH	65.06	26051181
14	Ubiquitination	KEAPAPPKAEAKAKA CCCCCCCHHHHHHHH	58.77	33845483
14	Acetylation	KEAPAPPKAEAKAKA CCCCCCCHHHHHHHH	58.77	26051181
14	Sumoylation	KEAPAPPKAEAKAKA CCCCCCCHHHHHHHH	58.77	28112733
18	Acetylation	APPKAEAKAKALKAK CCCHHHHHHHHHHHH	41.76	25953088
18	Ubiquitination	APPKAEAKAKALKAK CCCHHHHHHHHHHHH	41.76	33845483
20	Ubiquitination	PKAEAKAKALKAKKA CHHHHHHHHHHHHHH	54.25	33845483
23	Acetylation	EAKAKALKAKKAVLK HHHHHHHHHHHHHHH	64.12	19817317
30	2-Hydroxyisobutyrylation	KAKKAVLKGVHSHKK HHHHHHHHHHHHCCC	52.90	-
30	Ubiquitination	KAKKAVLKGVHSHKK HHHHHHHHHHHHCCC	52.90	32015554
36	2-Hydroxyisobutyrylation	LKGVHSHKKKKIRTS HHHHHHCCCCCCCCC	70.11	-
41	Citrullination	SHKKKKIRTSPTFRR HCCCCCCCCCCCCCC	37.72	-
41	Citrullination	SHKKKKIRTSPTFRR HCCCCCCCCCCCCCC	37.72	-
42	Phosphorylation	HKKKKIRTSPTFRRP CCCCCCCCCCCCCCC	42.40	25463755
43	Phosphorylation	KKKKIRTSPTFRRPK CCCCCCCCCCCCCCC	16.46	22167270
45	Phosphorylation	KKIRTSPTFRRPKTL CCCCCCCCCCCCCHH	29.55	22167270
59	Ubiquitination	LRLRRQPKYPRKSAP HHCCCCCCCCCCCCC	60.59	27667366
64	Phosphorylation	QPKYPRKSAPRRNKL CCCCCCCCCCCCCCC	44.80	24719451
70	Acetylation	KSAPRRNKLDHYAII CCCCCCCCCCEEEEE	54.18	23954790
70	2-Hydroxyisobutyrylation	KSAPRRNKLDHYAII CCCCCCCCCCEEEEE	54.18	-
70	Ubiquitination	KSAPRRNKLDHYAII CCCCCCCCCCEEEEE	54.18	23000965
74	Phosphorylation	RRNKLDHYAIIKFPL CCCCCCEEEEEECEE	10.12	25884760
78	Acetylation	LDHYAIIKFPLTTES CCEEEEEECEECCHH	34.51	26051181
78	2-Hydroxyisobutyrylation	LDHYAIIKFPLTTES CCEEEEEECEECCHH	34.51	-
78	Ubiquitination	LDHYAIIKFPLTTES CCEEEEEECEECCHH	34.51	23000965
82	Phosphorylation	AIIKFPLTTESAMKK EEEECEECCHHHHHH	28.84	30266825
83	Phosphorylation	IIKFPLTTESAMKKI EEECEECCHHHHHHH	35.31	30266825
85	Phosphorylation	KFPLTTESAMKKIED ECEECCHHHHHHHCC	31.41	30266825
87	Sulfoxidation	PLTTESAMKKIEDNN EECCHHHHHHHCCCC	6.73	21406390
88	Acetylation	LTTESAMKKIEDNNT ECCHHHHHHHCCCCE	50.76	25953088
88	Ubiquitination	LTTESAMKKIEDNNT ECCHHHHHHHCCCCE	50.76	32015554
95	Phosphorylation	KKIEDNNTLVFIVDV HHHCCCCEEEEEEEE	30.47	20068231
103	Ubiquitination	LVFIVDVKANKHQIK EEEEEEECCCHHHHH	41.60	33845483
106	Acetylation	IVDVKANKHQIKQAV EEEECCCHHHHHHHH	41.57	25825284
106	2-Hydroxyisobutyrylation	IVDVKANKHQIKQAV EEEECCCHHHHHHHH	41.57	-
106	Ubiquitination	IVDVKANKHQIKQAV EEEECCCHHHHHHHH	41.57	29967540
110	Succinylation	KANKHQIKQAVKKLY CCCHHHHHHHHHHHH	26.15	23954790
110	Ubiquitination	KANKHQIKQAVKKLY CCCHHHHHHHHHHHH	26.15	23000965
110	Acetylation	KANKHQIKQAVKKLY CCCHHHHHHHHHHHH	26.15	26210075
114	Ubiquitination	HQIKQAVKKLYDIDV HHHHHHHHHHHCCCH	39.82	23000965
115	2-Hydroxyisobutyrylation	QIKQAVKKLYDIDVA HHHHHHHHHHCCCHH	45.76	-
115	Acetylation	QIKQAVKKLYDIDVA HHHHHHHHHHCCCHH	45.76	26051181
115	Ubiquitination	QIKQAVKKLYDIDVA HHHHHHHHHHCCCHH	45.76	23000965
117	Nitration	KQAVKKLYDIDVAKV HHHHHHHHCCCHHHC	21.52	-
117	Phosphorylation	KQAVKKLYDIDVAKV HHHHHHHHCCCHHHC	21.52	28152594
123	2-Hydroxyisobutyrylation	LYDIDVAKVNTLIRP HHCCCHHHCCEEECC	35.55	-
123	Acetylation	LYDIDVAKVNTLIRP HHCCCHHHCCEEECC	35.55	26051181
123	Ubiquitination	LYDIDVAKVNTLIRP HHCCCHHHCCEEECC	35.55	23000965
126	Phosphorylation	IDVAKVNTLIRPDGE CCHHHCCEEECCCCC	26.92	23186163
134	2-Hydroxyisobutyrylation	LIRPDGEKKAYVRLA EECCCCCCEEEEEEC	48.51	-
134	Acetylation	LIRPDGEKKAYVRLA EECCCCCCEEEEEEC	48.51	26051181
134	Ubiquitination	LIRPDGEKKAYVRLA EECCCCCCEEEEEEC	48.51	16196087
135	Ubiquitination	IRPDGEKKAYVRLAP ECCCCCCEEEEEECC	40.42	29967540
137	Phosphorylation	PDGEKKAYVRLAPDY CCCCCEEEEEECCCC	8.59	26074081
144	Phosphorylation	YVRLAPDYDALDVAN EEEECCCCCHHHHHH	11.32	20068231
144	Nitration	YVRLAPDYDALDVAN EEEECCCCCHHHHHH	11.32	-
152	Ubiquitination	DALDVANKIGII--- CHHHHHHHHCCC---	32.35	21906983
152	2-Hydroxyisobutyrylation	DALDVANKIGII--- CHHHHHHHHCCC---	32.35	-

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 RL23A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL23A_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 RL23A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IPO5_HUMAN	IPO5	physical	11682607
IPO7_HUMAN	IPO7	physical	11682607
IPO8_HUMAN	IPO8	physical	11682607
TNPO1_HUMAN	TNPO1	physical	11682607
RL23_HUMAN	RPL23	physical	22939629
RL24_HUMAN	RPL24	physical	22939629
RL27A_HUMAN	RPL27A	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RL35_HUMAN	RPL35	physical	22939629
RL36_HUMAN	RPL36	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RL38_HUMAN	RPL38	physical	22939629
RL29_HUMAN	RPL29	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
UBIM_HUMAN	FAU	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
VASN_HUMAN	VASN	physical	22939629
AIMP1_HUMAN	AIMP1	physical	22863883
EIFCL_HUMAN	EIF3CL	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RL19_HUMAN	RPL19	physical	22863883
RL24_HUMAN	RPL24	physical	22863883
RL35_HUMAN	RPL35	physical	22863883
RLA0_HUMAN	RPLP0	physical	22863883
RS11_HUMAN	RPS11	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
SND1_HUMAN	SND1	physical	22863883
HNRPQ_HUMAN	SYNCRIP	physical	22863883
RM15_HUMAN	MRPL15	physical	26344197
RM16_HUMAN	MRPL16	physical	26344197
RT10_HUMAN	MRPS10	physical	26344197
RT07_HUMAN	MRPS7	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS12_HUMAN	RPS12	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
NOG2_HUMAN	GNL2	physical	26203195
MDM2_HUMAN	MDM2	physical	26203195

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 RL23A_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-70, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.	19007248 [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-43, AND MASSSPECTROMETRY.	17081983 [Abstract]