RL29_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL29_HUMAN
• UniProt AC: P47914
• Protein Name: 60S ribosomal protein L29
• Gene Name: RPL29
• Organism: Homo sapiens (Human).
• Sequence Length: 159
• Protein Description: Component of the large ribosomal subunit..
• Protein Sequence: MAKSKNHTTHNQSRKWHRNGIKKPRSQRYESLKGVDPKFLRNMRFAKKHNKKGLKKMQANNAKAMSARAEAIKALVKPKEVKPKIPKGVSRKLDRLAYIAHPKLGKRARARIAKGLRLCRPKAKAKAKAKDQTKAQAAAPASVPAQAPKRTQAPTKASE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MAKSKNHTTH -----CCCCCCCCCC	61.74	24816145
4	O-linked_Glycosylation	----MAKSKNHTTHN ----CCCCCCCCCCH	29.20	28510447
5	Methylation	---MAKSKNHTTHNQ ---CCCCCCCCCCHH	52.63	12962325
8	Phosphorylation	MAKSKNHTTHNQSRK CCCCCCCCCCHHHHH	38.86	28152594
9	Phosphorylation	AKSKNHTTHNQSRKW CCCCCCCCCHHHHHH	15.98	28152594
13	O-linked_Glycosylation	NHTTHNQSRKWHRNG CCCCCHHHHHHHHCC	40.94	28510447
23	Ubiquitination	WHRNGIKKPRSQRYE HHHCCCCCCHHHHHH	43.68	24816145
26	Phosphorylation	NGIKKPRSQRYESLK CCCCCCHHHHHHHHC	27.77	28152594
29	Phosphorylation	KKPRSQRYESLKGVD CCCHHHHHHHHCCCC	11.39	28152594
31	Phosphorylation	PRSQRYESLKGVDPK CHHHHHHHHCCCCHH	26.84	23401153
33	Acetylation	SQRYESLKGVDPKFL HHHHHHHCCCCHHHH	67.19	19608861
33	Ubiquitination	SQRYESLKGVDPKFL HHHHHHHCCCCHHHH	67.19	23000965
33	Ubiquitination	SQRYESLKGVDPKFL HHHHHHHCCCCHHHH	67.19	21890473
38	Ubiquitination	SLKGVDPKFLRNMRF HHCCCCHHHHHHHHH	53.20	23000965
38	Ubiquitination	SLKGVDPKFLRNMRF HHCCCCHHHHHHHHH	53.20	21890473
38	Acetylation	SLKGVDPKFLRNMRF HHCCCCHHHHHHHHH	53.20	25953088
56	Ubiquitination	HNKKGLKKMQANNAK HCHHHHHHHHHHHHH	41.09	21906983
63	Ubiquitination	KMQANNAKAMSARAE HHHHHHHHHHHHHHH	46.90	23000965
63	Acetylation	KMQANNAKAMSARAE HHHHHHHHHHHHHHH	46.90	25953088
66	Phosphorylation	ANNAKAMSARAEAIK HHHHHHHHHHHHHHH	21.33	22199227
73	Ubiquitination	SARAEAIKALVKPKE HHHHHHHHHHHCCHH	42.59	21890473
73	Acetylation	SARAEAIKALVKPKE HHHHHHHHHHHCCHH	42.59	25953088
73	Ubiquitination	SARAEAIKALVKPKE HHHHHHHHHHHCCHH	42.59	23000965
77	Acetylation	EAIKALVKPKEVKPK HHHHHHHCCHHCCCC	51.74	26051181
77	Ubiquitination	EAIKALVKPKEVKPK HHHHHHHCCHHCCCC	51.74	23000965
79	Ubiquitination	IKALVKPKEVKPKIP HHHHHCCHHCCCCCC	70.22	23000965
82	Ubiquitination	LVKPKEVKPKIPKGV HHCCHHCCCCCCCCH	41.50	24816145
82	Acetylation	LVKPKEVKPKIPKGV HHCCHHCCCCCCCCH	41.50	19608861
84	Ubiquitination	KPKEVKPKIPKGVSR CCHHCCCCCCCCHHH	66.96	-
90	Phosphorylation	PKIPKGVSRKLDRLA CCCCCCHHHHHHHHH	32.16	27282143
95	Methylation	GVSRKLDRLAYIAHP CHHHHHHHHHHHHCH	31.49	115492009
98	Phosphorylation	RKLDRLAYIAHPKLG HHHHHHHHHHCHHCC	11.84	22461510
103	Ubiquitination	LAYIAHPKLGKRARA HHHHHCHHCCHHHHH	61.06	21890473
103	Acetylation	LAYIAHPKLGKRARA HHHHHCHHCCHHHHH	61.06	23236377
103	Ubiquitination	LAYIAHPKLGKRARA HHHHHCHHCCHHHHH	61.06	21906983
106	Ubiquitination	IAHPKLGKRARARIA HHCHHCCHHHHHHHH	54.01	-
114	Ubiquitination	RARARIAKGLRLCRP HHHHHHHHHHHHHCH	56.99	27667366
114	Methylation	RARARIAKGLRLCRP HHHHHHHHHHHHHCH	56.99	72620571
119	S-palmitoylation	IAKGLRLCRPKAKAK HHHHHHHHCHHHHHH	5.90	29575903
122	2-Hydroxyisobutyrylation	GLRLCRPKAKAKAKA HHHHHCHHHHHHHHH	43.07	-
128	Ubiquitination	PKAKAKAKAKDQTKA HHHHHHHHHHHHHHH	56.09	23503661
130	Acetylation	AKAKAKAKDQTKAQA HHHHHHHHHHHHHHH	50.06	26051181
130	Ubiquitination	AKAKAKAKDQTKAQA HHHHHHHHHHHHHHH	50.06	22817900
134	Acetylation	AKAKDQTKAQAAAPA HHHHHHHHHHHHCCC	32.63	23236377
134	Ubiquitination	AKAKDQTKAQAAAPA HHHHHHHHHHHHCCC	32.63	21906983
142	O-linked_Glycosylation	AQAAAPASVPAQAPK HHHHCCCCCCCCCCC	27.81	28510447
142	Phosphorylation	AQAAAPASVPAQAPK HHHHCCCCCCCCCCC	27.81	30266825
149	Acetylation	SVPAQAPKRTQAPTK CCCCCCCCCCCCCCC	71.71	26051181
149	2-Hydroxyisobutyrylation	SVPAQAPKRTQAPTK CCCCCCCCCCCCCCC	71.71	-
149	Ubiquitination	SVPAQAPKRTQAPTK CCCCCCCCCCCCCCC	71.71	23000965
149	Methylation	SVPAQAPKRTQAPTK CCCCCCCCCCCCCCC	71.71	24506953
151	O-linked_Glycosylation	PAQAPKRTQAPTKAS CCCCCCCCCCCCCCC	34.90	28510447
151	Phosphorylation	PAQAPKRTQAPTKAS CCCCCCCCCCCCCCC	34.90	24732914
155	Phosphorylation	PKRTQAPTKASE--- CCCCCCCCCCCC---	42.11	24732914
156	Ubiquitination	KRTQAPTKASE---- CCCCCCCCCCC----	49.18	33845483
158	Phosphorylation	TQAPTKASE------ CCCCCCCCC------	45.45	28355574

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RL29_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL29_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RL29_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYBU_HUMAN	SYBU	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
RL6_HUMAN	RPL6	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
RL38_HUMAN	RPL38	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
PRS8_HUMAN	PSMC5	physical	22863883
RL9_HUMAN	RPL9	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-33 AND LYS-82, AND MASSSPECTROMETRY.
PubMed: 19608861

Methylation

"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: PROTEIN SEQUENCE OF 2-15, MASS SPECTROMETRY, AND METHYLATION AT LYS-5.
PubMed: 12962325

Phosphorylation

"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-142, AND MASSSPECTROMETRY.
PubMed: 19007248

"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 SER-142, AND MASSSPECTROMETRY.
PubMed: 17287340

Ubiquitylation

"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-73, AND MASSSPECTROMETRY.
PubMed: 17370265