dbPTM

RL28_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL28_HUMAN
UniProt AC	P46779
Protein Name	60S ribosomal protein L28
Gene Name	RPL28
Organism	Homo sapiens (Human).
Sequence Length	137
Subcellular Localization
Protein Description	Component of the large ribosomal subunit..
Protein Sequence	MSAHLQWMVVRNCSSFLIKRNKQTYSTEPNNLKARNSFRYNGLIHRKTVGVEPAADGKGVVVVIKRRSGQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQKPVMVKRKRTRPTKSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSAHLQWMV ------CCHHHHHHH	25.13	12962325
2	Acetylation	------MSAHLQWMV ------CCHHHHHHH	25.13	12962325
8	Sulfoxidation	MSAHLQWMVVRNCSS CCHHHHHHHHCCCHH	0.97	28183972
11	Methylation	HLQWMVVRNCSSFLI HHHHHHHCCCHHHHE	27.33	115491993
13	S-palmitoylation	QWMVVRNCSSFLIKR HHHHHCCCHHHHECC	2.24	29575903
13	S-nitrosylation	QWMVVRNCSSFLIKR HHHHHCCCHHHHECC	2.24	2212679
13	Glutathionylation	QWMVVRNCSSFLIKR HHHHHCCCHHHHECC	2.24	22555962
14	Phosphorylation	WMVVRNCSSFLIKRN HHHHCCCHHHHECCC	27.89	28450419
15	Phosphorylation	MVVRNCSSFLIKRNK HHHCCCHHHHECCCC	26.69	28450419
19	Acetylation	NCSSFLIKRNKQTYS CCHHHHECCCCCCCC	52.65	25953088
19	Ubiquitination	NCSSFLIKRNKQTYS CCHHHHECCCCCCCC	52.65	27667366
19	Ubiquitination	NCSSFLIKRNKQTYS CCHHHHECCCCCCCC	52.65	21890473
19	Ubiquitination	NCSSFLIKRNKQTYS CCHHHHECCCCCCCC	52.65	21890473
22	Ubiquitination	SFLIKRNKQTYSTEP HHHECCCCCCCCCCC	48.31	21906983
22	Acetylation	SFLIKRNKQTYSTEP HHHECCCCCCCCCCC	48.31	26051181
22	Ubiquitination	SFLIKRNKQTYSTEP HHHECCCCCCCCCCC	48.31	21890473
22	2-Hydroxyisobutyrylation	SFLIKRNKQTYSTEP HHHECCCCCCCCCCC	48.31	-
22	Ubiquitination	SFLIKRNKQTYSTEP HHHECCCCCCCCCCC	48.31	21890473
24	Phosphorylation	LIKRNKQTYSTEPNN HECCCCCCCCCCCCC	22.50	28152594
25	Phosphorylation	IKRNKQTYSTEPNNL ECCCCCCCCCCCCCC	15.88	28152594
26	Phosphorylation	KRNKQTYSTEPNNLK CCCCCCCCCCCCCCC	29.67	28152594
27	Phosphorylation	RNKQTYSTEPNNLKA CCCCCCCCCCCCCCC	45.08	28152594
33	2-Hydroxyisobutyrylation	STEPNNLKARNSFRY CCCCCCCCCCCCEEE	47.63	-
33	Ubiquitination	STEPNNLKARNSFRY CCCCCCCCCCCCEEE	47.63	21890473
33	Ubiquitination	STEPNNLKARNSFRY CCCCCCCCCCCCEEE	47.63	21890473
33	Acetylation	STEPNNLKARNSFRY CCCCCCCCCCCCEEE	47.63	25953088
33	Methylation	STEPNNLKARNSFRY CCCCCCCCCCCCEEE	47.63	21671109
33	Sumoylation	STEPNNLKARNSFRY CCCCCCCCCCCCEEE	47.63	-
33	Sumoylation	STEPNNLKARNSFRY CCCCCCCCCCCCEEE	47.63	-
33	Ubiquitination	STEPNNLKARNSFRY CCCCCCCCCCCCEEE	47.63	23000965
37	Phosphorylation	NNLKARNSFRYNGLI CCCCCCCCEEECCEE	12.92	28450419
40	Phosphorylation	KARNSFRYNGLIHRK CCCCCEEECCEEEEE	16.15	30624053
47	Ubiquitination	YNGLIHRKTVGVEPA ECCEEEEEEEECEEC	33.14	21890473
47	2-Hydroxyisobutyrylation	YNGLIHRKTVGVEPA ECCEEEEEEEECEEC	33.14	-
47	Ubiquitination	YNGLIHRKTVGVEPA ECCEEEEEEEECEEC	33.14	21890473
47	Ubiquitination	YNGLIHRKTVGVEPA ECCEEEEEEEECEEC	33.14	27667366
47	Acetylation	YNGLIHRKTVGVEPA ECCEEEEEEEECEEC	33.14	26051181
48	Phosphorylation	NGLIHRKTVGVEPAA CCEEEEEEEECEECC	23.58	29514088
58	2-Hydroxyisobutyrylation	VEPAADGKGVVVVIK CEECCCCCEEEEEEE	49.43	-
58	Ubiquitination	VEPAADGKGVVVVIK CEECCCCCEEEEEEE	49.43	21890473
58	Sumoylation	VEPAADGKGVVVVIK CEECCCCCEEEEEEE	49.43	28112733
58	Ubiquitination	VEPAADGKGVVVVIK CEECCCCCEEEEEEE	49.43	21890473
58	Ubiquitination	VEPAADGKGVVVVIK CEECCCCCEEEEEEE	49.43	21906983
58	Acetylation	VEPAADGKGVVVVIK CEECCCCCEEEEEEE	49.43	26051181
65	Ubiquitination	KGVVVVIKRRSGQRK CEEEEEEECCCCCCC	30.10	33845483
65	Sumoylation	KGVVVVIKRRSGQRK CEEEEEEECCCCCCC	30.10	28112733
65	Ubiquitination	KGVVVVIKRRSGQRK CEEEEEEECCCCCCC	30.10	21890473
65	2-Hydroxyisobutyrylation	KGVVVVIKRRSGQRK CEEEEEEECCCCCCC	30.10	-
68	Phosphorylation	VVVIKRRSGQRKPAT EEEEECCCCCCCCCE	43.22	26278961
72	Ubiquitination	KRRSGQRKPATSYVR ECCCCCCCCCEEEEE	30.99	27667366
75	Phosphorylation	SGQRKPATSYVRTTI CCCCCCCEEEEEHHC	29.17	28152594
76	Phosphorylation	GQRKPATSYVRTTIN CCCCCCEEEEEHHCC	24.60	28152594
77	Nitration	QRKPATSYVRTTINK CCCCCEEEEEHHCCC	6.92	-
77	Phosphorylation	QRKPATSYVRTTINK CCCCCEEEEEHHCCC	6.92	28152594
80	Phosphorylation	PATSYVRTTINKNAR CCEEEEEHHCCCCHH	23.22	-
84	2-Hydroxyisobutyrylation	YVRTTINKNARATLS EEEHHCCCCHHHHHH	48.40	-
84	Acetylation	YVRTTINKNARATLS EEEHHCCCCHHHHHH	48.40	26051181
84	Ubiquitination	YVRTTINKNARATLS EEEHHCCCCHHHHHH	48.40	21906983
89	Phosphorylation	INKNARATLSSIRHM CCCCHHHHHHHHHHH	22.94	30266825
91	Phosphorylation	KNARATLSSIRHMIR CCHHHHHHHHHHHHH	21.26	30266825
92	Phosphorylation	NARATLSSIRHMIRK CHHHHHHHHHHHHHH	27.10	30266825
99	Ubiquitination	SIRHMIRKNKYRPDL HHHHHHHHCCCCCHH	47.03	23503661
101	Ubiquitination	RHMIRKNKYRPDLRM HHHHHHCCCCCHHHH	45.75	21890473
101	Acetylation	RHMIRKNKYRPDLRM HHHHHHCCCCCHHHH	45.75	19608861
101	Sumoylation	RHMIRKNKYRPDLRM HHHHHHCCCCCHHHH	45.75	-
101	Sumoylation	RHMIRKNKYRPDLRM HHHHHHCCCCCHHHH	45.75	-
101	Ubiquitination	RHMIRKNKYRPDLRM HHHHHHCCCCCHHHH	45.75	19608861
102	Phosphorylation	HMIRKNKYRPDLRMA HHHHHCCCCCHHHHH	36.45	-
107	Methylation	NKYRPDLRMAAIRRA CCCCCHHHHHHHHHH	21.77	115492001
115	Phosphorylation	MAAIRRASAILRSQK HHHHHHHHHHHHCCC	17.65	30266825
120	Phosphorylation	RASAILRSQKPVMVK HHHHHHHCCCCEEEE	38.83	29083192
122	Ubiquitination	SAILRSQKPVMVKRK HHHHHCCCCEEEEEC	40.60	27667366
122	Sumoylation	SAILRSQKPVMVKRK HHHHHCCCCEEEEEC	40.60	-
122	Sumoylation	SAILRSQKPVMVKRK HHHHHCCCCEEEEEC	40.60	-
122	Acetylation	SAILRSQKPVMVKRK HHHHHCCCCEEEEEC	40.60	26051181
122	2-Hydroxyisobutyrylation	SAILRSQKPVMVKRK HHHHHCCCCEEEEEC	40.60	-
125	Sulfoxidation	LRSQKPVMVKRKRTR HHCCCCEEEEECCCC	3.89	30846556
127	Ubiquitination	SQKPVMVKRKRTRPT CCCCEEEEECCCCCC	33.82	22817900
127	2-Hydroxyisobutyrylation	SQKPVMVKRKRTRPT CCCCEEEEECCCCCC	33.82	-
127	Acetylation	SQKPVMVKRKRTRPT CCCCEEEEECCCCCC	33.82	25953088
129	Ubiquitination	KPVMVKRKRTRPTKS CCEEEEECCCCCCCC	53.02	23503661
149 (in isoform 3)	Phosphorylation	-		25599653
150 (in isoform 3)	Phosphorylation	-		25599653
151 (in isoform 3)	Phosphorylation	-		25599653

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 RL28_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL28_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 RL28_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS10_HUMAN	RPS10	physical	22863883
RS18_HUMAN	RPS18	physical	22863883
RS19_HUMAN	RPS19	physical	22863883
RS23_HUMAN	RPS23	physical	22863883
RS29_HUMAN	RPS29	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS3A_HUMAN	RPS3A	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
CCDB1_HUMAN	CCNDBP1	physical	25416956
RL23A_HUMAN	RPL23A	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
H13_HUMAN	HIST1H1D	physical	28514442
H11_HUMAN	HIST1H1A	physical	28514442
H12_HUMAN	HIST1H1C	physical	28514442
PTPRK_HUMAN	PTPRK	physical	28514442
KLH21_HUMAN	KLHL21	physical	28514442
FAT4_HUMAN	FAT4	physical	28514442
ZDBF2_HUMAN	ZDBF2	physical	28514442
HASP_HUMAN	GSG2	physical	28514442
FAT3_HUMAN	FAT3	physical	28514442
SI1L2_HUMAN	SIPA1L2	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
TROP_HUMAN	TRO	physical	28514442
K0232_HUMAN	KIAA0232	physical	28514442
MRCKA_HUMAN	CDC42BPA	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
RL18A_HUMAN	RPL18A	physical	28514442
IFFO1_HUMAN	IFFO1	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
CELR2_HUMAN	CELSR2	physical	28514442
FREM2_HUMAN	FREM2	physical	28514442
RBM34_HUMAN	RBM34	physical	28514442
RLA2_HUMAN	RPLP2	physical	28514442
AKA11_HUMAN	AKAP11	physical	28514442
PLCH1_HUMAN	PLCH1	physical	28514442
RL4_HUMAN	RPL4	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
DPOE2_HUMAN	POLE2	physical	28514442
GLYR1_HUMAN	GLYR1	physical	28514442
Z354A_HUMAN	ZNF354A	physical	28514442
NSD2_HUMAN	WHSC1	physical	28514442
RLA0_HUMAN	RPLP0	physical	28514442
RL36_HUMAN	RPL36	physical	28514442
ZCHC7_HUMAN	ZCCHC7	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28514442
SPB1_HUMAN	FTSJ3	physical	28514442
DPOE1_HUMAN	POLE	physical	28514442
RL3_HUMAN	RPL3	physical	28514442
ZN644_HUMAN	ZNF644	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
RL32_HUMAN	RPL32	physical	28514442
PTPRD_HUMAN	PTPRD	physical	28514442
RL30_HUMAN	RPL30	physical	28514442
RL27_HUMAN	RPL27	physical	28514442
RL5_HUMAN	RPL5	physical	28514442
TBA4A_HUMAN	TUBA4A	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
RL18_HUMAN	RPL18	physical	28514442
GPR98_HUMAN	GPR98	physical	28514442
RL6_HUMAN	RPL6	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
ZN184_HUMAN	ZNF184	physical	28514442
CENPU_HUMAN	CENPU	physical	28514442
RL19_HUMAN	RPL19	physical	28514442
GASP2_HUMAN	GPRASP2	physical	28514442
RL8_HUMAN	RPL8	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
SDCB1_HUMAN	SDCBP	physical	28514442
RL7A_HUMAN	RPL7A	physical	28514442
PEX14_HUMAN	PEX14	physical	28514442
ZN865_HUMAN	ZNF865	physical	28514442
KLH15_HUMAN	KLHL15	physical	28514442
RS8_HUMAN	RPS8	physical	28514442
RL14_HUMAN	RPL14	physical	28514442
NUCL_HUMAN	NCL	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 RL28_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Characterization and analysis of posttranslational modifications ofthe human large cytoplasmic ribosomal subunit proteins by massspectrometry and Edman sequencing."; Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,Karpova G.G.; J. Protein Chem. 22:249-258(2003). Cited for: MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT SER-2.	12962325 [Abstract]
"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-101, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-115, AND MASSSPECTROMETRY.	19007248 [Abstract]