dbPTM

RL30_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL30_HUMAN
UniProt AC	P62888
Protein Name	60S ribosomal protein L30
Gene Name	RPL30
Organism	Homo sapiens (Human).
Sequence Length	115
Subcellular Localization
Protein Description
Protein Sequence	MVAAKKTKKSLESINSRLQLVMKSGKYVLGYKQTLKMIRQGKAKLVILANNCPALRKSEIEYYAMLAKTGVHHYSGNNIELGTACGKYYRVCTLAIIDPGDSDIIRSMPEQTGEK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Acetylation	--MVAAKKTKKSLES --CCCCHHHHHHHHH	61.93	18584459
7	Phosphorylation	-MVAAKKTKKSLESI -CCCCHHHHHHHHHH	42.89	24732914
8	Acetylation	MVAAKKTKKSLESIN CCCCHHHHHHHHHHH	49.60	18584467
8	Ubiquitination	MVAAKKTKKSLESIN CCCCHHHHHHHHHHH	49.60	-
9	Acetylation	VAAKKTKKSLESINS CCCHHHHHHHHHHHH	66.56	18584475
9	Ubiquitination	VAAKKTKKSLESINS CCCHHHHHHHHHHHH	66.56	21890473
9	Malonylation	VAAKKTKKSLESINS CCCHHHHHHHHHHHH	66.56	26320211
10	Phosphorylation	AAKKTKKSLESINSR CCHHHHHHHHHHHHH	38.64	29255136
13	Phosphorylation	KTKKSLESINSRLQL HHHHHHHHHHHHHHH	32.15	30266825
16	Phosphorylation	KSLESINSRLQLVMK HHHHHHHHHHHHHHH	32.47	25159151
23	Ubiquitination	SRLQLVMKSGKYVLG HHHHHHHHCCCEEEE	48.88	21890473
23	Acetylation	SRLQLVMKSGKYVLG HHHHHHHHCCCEEEE	48.88	25953088
24	Phosphorylation	RLQLVMKSGKYVLGY HHHHHHHCCCEEEEH	23.56	28152594
26	Malonylation	QLVMKSGKYVLGYKQ HHHHHCCCEEEEHHH	39.00	26320211
26	Sumoylation	QLVMKSGKYVLGYKQ HHHHHCCCEEEEHHH	39.00	28112733
26	2-Hydroxyisobutyrylation	QLVMKSGKYVLGYKQ HHHHHCCCEEEEHHH	39.00	-
26	Ubiquitination	QLVMKSGKYVLGYKQ HHHHHCCCEEEEHHH	39.00	21890473
26	Acetylation	QLVMKSGKYVLGYKQ HHHHHCCCEEEEHHH	39.00	19608861
27	Phosphorylation	LVMKSGKYVLGYKQT HHHHCCCEEEEHHHH	12.39	28152594
31	Phosphorylation	SGKYVLGYKQTLKMI CCCEEEEHHHHHHHH	8.86	28152594
32	Ubiquitination	GKYVLGYKQTLKMIR CCEEEEHHHHHHHHH	34.70	-
32	2-Hydroxyisobutyrylation	GKYVLGYKQTLKMIR CCEEEEHHHHHHHHH	34.70	-
32	Methylation	GKYVLGYKQTLKMIR CCEEEEHHHHHHHHH	34.70	72586243
32	Succinylation	GKYVLGYKQTLKMIR CCEEEEHHHHHHHHH	34.70	23954790
32	Acetylation	GKYVLGYKQTLKMIR CCEEEEHHHHHHHHH	34.70	27452117
34	Phosphorylation	YVLGYKQTLKMIRQG EEEEHHHHHHHHHCC	24.97	23186163
36	Acetylation	LGYKQTLKMIRQGKA EEHHHHHHHHHCCCC	35.35	25953088
36	Ubiquitination	LGYKQTLKMIRQGKA EEHHHHHHHHHCCCC	35.35	-
44	Malonylation	MIRQGKAKLVILANN HHHCCCCEEEEECCC	46.93	26320211
44	2-Hydroxyisobutyrylation	MIRQGKAKLVILANN HHHCCCCEEEEECCC	46.93	-
44	Acetylation	MIRQGKAKLVILANN HHHCCCCEEEEECCC	46.93	25953088
44	Ubiquitination	MIRQGKAKLVILANN HHHCCCCEEEEECCC	46.93	-
52	Glutathionylation	LVILANNCPALRKSE EEEECCCCHHHCHHH	1.77	22555962
52	S-nitrosylation	LVILANNCPALRKSE EEEECCCCHHHCHHH	1.77	22178444
52	S-nitrosocysteine	LVILANNCPALRKSE EEEECCCCHHHCHHH	1.77	-
52	S-palmitoylation	LVILANNCPALRKSE EEEECCCCHHHCHHH	1.77	29575903
57	2-Hydroxyisobutyrylation	NNCPALRKSEIEYYA CCCHHHCHHHHHHHH	53.98	-
57	Acetylation	NNCPALRKSEIEYYA CCCHHHCHHHHHHHH	53.98	26051181
57	Ubiquitination	NNCPALRKSEIEYYA CCCHHHCHHHHHHHH	53.98	21890473
58	Phosphorylation	NCPALRKSEIEYYAM CCHHHCHHHHHHHHH	37.05	28152594
62	Phosphorylation	LRKSEIEYYAMLAKT HCHHHHHHHHHHHHH	11.37	28152594
63	Phosphorylation	RKSEIEYYAMLAKTG CHHHHHHHHHHHHHC	3.46	28152594
65	Sulfoxidation	SEIEYYAMLAKTGVH HHHHHHHHHHHHCCC	1.85	30846556
68	Ubiquitination	EYYAMLAKTGVHHYS HHHHHHHHHCCCCCC	41.68	21890473
68	Acetylation	EYYAMLAKTGVHHYS HHHHHHHHHCCCCCC	41.68	25953088
69	Phosphorylation	YYAMLAKTGVHHYSG HHHHHHHHCCCCCCC	38.54	28152594
74	Phosphorylation	AKTGVHHYSGNNIEL HHHCCCCCCCCCEEC	11.91	28152594
75	Phosphorylation	KTGVHHYSGNNIELG HHCCCCCCCCCEECC	30.59	28152594
83	Phosphorylation	GNNIELGTACGKYYR CCCEECCCCCCCEEE	31.25	20068231
85	S-nitrosylation	NIELGTACGKYYRVC CEECCCCCCCEEEEE	4.92	2212679
85	Glutathionylation	NIELGTACGKYYRVC CEECCCCCCCEEEEE	4.92	22555962
87	Ubiquitination	ELGTACGKYYRVCTL ECCCCCCCEEEEEEE	38.71	-
87	Acetylation	ELGTACGKYYRVCTL ECCCCCCCEEEEEEE	38.71	25825284
87	2-Hydroxyisobutyrylation	ELGTACGKYYRVCTL ECCCCCCCEEEEEEE	38.71	-
92	S-nitrosylation	CGKYYRVCTLAIIDP CCCEEEEEEEEEECC	1.59	22178444
92	Glutathionylation	CGKYYRVCTLAIIDP CCCEEEEEEEEEECC	1.59	22555962
92	S-palmitoylation	CGKYYRVCTLAIIDP CCCEEEEEEEEEECC	1.59	29575903
92	S-nitrosocysteine	CGKYYRVCTLAIIDP CCCEEEEEEEEEECC	1.59	-
93	Phosphorylation	GKYYRVCTLAIIDPG CCEEEEEEEEEECCC	19.17	-
102	Phosphorylation	AIIDPGDSDIIRSMP EEECCCCCHHHHHCC	36.30	20068231
106	Methylation	PGDSDIIRSMPEQTG CCCCHHHHHCCCCCC	27.51	115492041
107	Phosphorylation	GDSDIIRSMPEQTGE CCCHHHHHCCCCCCC	28.42	29396449
108	Sulfoxidation	DSDIIRSMPEQTGEK CCHHHHHCCCCCCCC	2.80	30846556
112	Phosphorylation	IRSMPEQTGEK---- HHHCCCCCCCC----	45.72	27251275
115	Ubiquitination	MPEQTGEK------- CCCCCCCC-------	67.97	-
115	Acetylation	MPEQTGEK------- CCCCCCCC-------	67.97	7479759

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 RL30_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL30_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 RL30_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RS11_HUMAN	RPS11	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RL36_HUMAN	RPL36	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RL35_HUMAN	RPL35	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RL38_HUMAN	RPL38	physical	22939629
RS29_HUMAN	RPS29	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RL37_HUMAN	RPL37	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
RS11_HUMAN	RPS11	physical	21988832
ZFN2A_HUMAN	ZFAND2A	physical	21988832
UBP14_HUMAN	USP14	physical	22863883
EF1A1_HUMAN	EEF1A1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
H12_HUMAN	HIST1H1C	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
REXO4_HUMAN	REXO4	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
ZN184_HUMAN	ZNF184	physical	28514442
NSD2_HUMAN	WHSC1	physical	28514442
PK1IP_HUMAN	PAK1IP1	physical	28514442
NOP2_HUMAN	NOP2	physical	28514442
SPB1_HUMAN	FTSJ3	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
RL36_HUMAN	RPL36	physical	28514442
ZNF70_HUMAN	ZNF70	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
Z354A_HUMAN	ZNF354A	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
CC137_HUMAN	CCDC137	physical	28514442
RL27_HUMAN	RPL27	physical	28514442
DDX31_HUMAN	DDX31	physical	28514442
DDX27_HUMAN	DDX27	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
ZC3HA_HUMAN	ZC3H10	physical	28514442
RL7A_HUMAN	RPL7A	physical	28514442
ZFP62_HUMAN	ZFP62	physical	28514442
PRD15_HUMAN	PRDM15	physical	28514442
RL32_HUMAN	RPL32	physical	28514442
GLYR1_HUMAN	GLYR1	physical	28514442
RL12_HUMAN	RPL12	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
STAU1_HUMAN	STAU1	physical	28514442
NSUN4_HUMAN	NSUN4	physical	28514442
NIP7_HUMAN	NIP7	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
IMP4_HUMAN	IMP4	physical	28514442
ZN189_HUMAN	ZNF189	physical	28514442
NMNA1_HUMAN	NMNAT1	physical	28514442
RL4_HUMAN	RPL4	physical	28514442
CENPN_HUMAN	CENPN	physical	28514442
DHX30_HUMAN	DHX30	physical	28514442
RL26_HUMAN	RPL26	physical	28514442
RL3_HUMAN	RPL3	physical	28514442
TTF1_HUMAN	TTF1	physical	28514442
RS13_HUMAN	RPS13	physical	28514442
MBB1A_HUMAN	MYBBP1A	physical	28514442
FCF1_HUMAN	FCF1	physical	28514442
NLE1_HUMAN	NLE1	physical	28514442
ZN771_HUMAN	ZNF771	physical	28514442
ZN668_HUMAN	ZNF668	physical	28514442
RL5_HUMAN	RPL5	physical	28514442
ZSC25_HUMAN	ZSCAN25	physical	28514442
ZN574_HUMAN	ZNF574	physical	28514442
TAF1A_HUMAN	TAF1A	physical	28514442
LLPH_HUMAN	LLPH	physical	28514442
DDX10_HUMAN	DDX10	physical	28514442
PRKRA_HUMAN	PRKRA	physical	28514442
ZN142_HUMAN	ZNF142	physical	28514442
DDX21_HUMAN	DDX21	physical	28514442
GZF1_HUMAN	GZF1	physical	28514442
LYAR_HUMAN	LYAR	physical	28514442
RL7L_HUMAN	RPL7L1	physical	28514442
PAPD5_HUMAN	PAPD5	physical	28514442
SURF6_HUMAN	SURF6	physical	28514442
RS9_HUMAN	RPS9	physical	28514442
RLP24_HUMAN	RSL24D1	physical	28514442
RLA0_HUMAN	RPLP0	physical	28514442
SMCA5_HUMAN	SMARCA5	physical	28514442
DDX56_HUMAN	DDX56	physical	28514442

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 RL30_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-26, 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-10, AND MASSSPECTROMETRY.	19690332 [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-10, AND MASSSPECTROMETRY.	18669648 [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-10, AND MASSSPECTROMETRY.	19007248 [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-10, AND MASSSPECTROMETRY.	16964243 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, AND MASSSPECTROMETRY.	19534553 [Abstract]