dbPTM

RL34_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL34_HUMAN
UniProt AC	P49207
Protein Name	60S ribosomal protein L34
Gene Name	RPL34
Organism	Homo sapiens (Human).
Sequence Length	117
Subcellular Localization	Cytoplasm, cytosol . Cytoplasm . Endoplasmic reticulum . Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).
Protein Description	Component of the large ribosomal subunit..
Protein Sequence	MVQRLTYRRRLSYNTASNKTRLSRTPGNRIVYLYTKKVGKAPKSACGVCPGRLRGVRAVRPKVLMRLSKTKKHVSRAYGGSMCAKCVRDRIKRAFLIEEQKIVVKVLKAQAQSQKAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MVQRLTYRRRLSY --CCCHHHHHHHHCC	19.71	23882029
10	Methylation	QRLTYRRRLSYNTAS CHHHHHHHHCCCCCC	20.98	115492105
12	Phosphorylation	LTYRRRLSYNTASNK HHHHHHHCCCCCCCC	17.96	22617229
13	Phosphorylation	TYRRRLSYNTASNKT HHHHHHCCCCCCCCE	22.56	23927012
13	Nitration	TYRRRLSYNTASNKT HHHHHHCCCCCCCCE	22.56	-
15	Phosphorylation	RRRLSYNTASNKTRL HHHHCCCCCCCCEEE	24.19	23927012
17	Phosphorylation	RLSYNTASNKTRLSR HHCCCCCCCCEEECC	36.50	23927012
19	Ubiquitination	SYNTASNKTRLSRTP CCCCCCCCEEECCCC	32.31	21890473
19	Acetylation	SYNTASNKTRLSRTP CCCCCCCCEEECCCC	32.31	25953088
20	Phosphorylation	YNTASNKTRLSRTPG CCCCCCCEEECCCCC	40.88	27080861
29	Methylation	LSRTPGNRIVYLYTK ECCCCCCEEEEEEEC	26.18	115492113
32	Phosphorylation	TPGNRIVYLYTKKVG CCCCEEEEEEECCCC	7.51	28152594
34	Phosphorylation	GNRIVYLYTKKVGKA CCEEEEEEECCCCCC	9.99	28152594
35	Phosphorylation	NRIVYLYTKKVGKAP CEEEEEEECCCCCCC	23.07	28152594
36	Acetylation	RIVYLYTKKVGKAPK EEEEEEECCCCCCCH	31.72	19608861
36	Ubiquitination	RIVYLYTKKVGKAPK EEEEEEECCCCCCCH	31.72	21906983
37	Ubiquitination	IVYLYTKKVGKAPKS EEEEEECCCCCCCHH	48.71	-
37	Acetylation	IVYLYTKKVGKAPKS EEEEEECCCCCCCHH	48.71	12429849
43	2-Hydroxyisobutyrylation	KKVGKAPKSACGVCP CCCCCCCHHHCCCCC	56.39	-
43	Ubiquitination	KKVGKAPKSACGVCP CCCCCCCHHHCCCCC	56.39	-
43	Acetylation	KKVGKAPKSACGVCP CCCCCCCHHHCCCCC	56.39	26210075
44	Phosphorylation	KVGKAPKSACGVCPG CCCCCCHHHCCCCCC	27.94	28102081
62	Acetylation	GVRAVRPKVLMRLSK CCCHHCHHHHHHHHH	37.12	26051181
62	Ubiquitination	GVRAVRPKVLMRLSK CCCHHCHHHHHHHHH	37.12	21890473
68	Phosphorylation	PKVLMRLSKTKKHVS HHHHHHHHHCCHHHH	28.10	29514088
70	Phosphorylation	VLMRLSKTKKHVSRA HHHHHHHCCHHHHHH	41.78	-
76	Methylation	KTKKHVSRAYGGSMC HCCHHHHHHHCCCHH	30.64	18583643
78	Phosphorylation	KKHVSRAYGGSMCAK CHHHHHHHCCCHHHH	22.40	28102081
81	Phosphorylation	VSRAYGGSMCAKCVR HHHHHCCCHHHHHHH	13.31	28102081
82	Sulfoxidation	SRAYGGSMCAKCVRD HHHHCCCHHHHHHHH	2.66	30846556
85	2-Hydroxyisobutyrylation	YGGSMCAKCVRDRIK HCCCHHHHHHHHHHH	28.47	-
85	Ubiquitination	YGGSMCAKCVRDRIK HCCCHHHHHHHHHHH	28.47	21890473
85	Acetylation	YGGSMCAKCVRDRIK HCCCHHHHHHHHHHH	28.47	25953088
88	Methylation	SMCAKCVRDRIKRAF CHHHHHHHHHHHHHH	36.64	18583651
101	Acetylation	AFLIEEQKIVVKVLK HHCCCHHHHHHHHHH	40.52	26051181
101	Ubiquitination	AFLIEEQKIVVKVLK HHCCCHHHHHHHHHH	40.52	21890473
105	Acetylation	EEQKIVVKVLKAQAQ CHHHHHHHHHHHHHH	30.84	25953088
105	Ubiquitination	EEQKIVVKVLKAQAQ CHHHHHHHHHHHHHH	30.84	21890473
105	2-Hydroxyisobutyrylation	EEQKIVVKVLKAQAQ CHHHHHHHHHHHHHH	30.84	-
105	Malonylation	EEQKIVVKVLKAQAQ CHHHHHHHHHHHHHH	30.84	32601280
108	Sumoylation	KIVVKVLKAQAQSQK HHHHHHHHHHHHHHH	41.25	28112733
108	Acetylation	KIVVKVLKAQAQSQK HHHHHHHHHHHHHHH	41.25	25953088
108	2-Hydroxyisobutyrylation	KIVVKVLKAQAQSQK HHHHHHHHHHHHHHH	41.25	-
108	Ubiquitination	KIVVKVLKAQAQSQK HHHHHHHHHHHHHHH	41.25	-
115	Acetylation	KAQAQSQKAK----- HHHHHHHHCC-----	64.49	19826731
115	Ubiquitination	KAQAQSQKAK----- HHHHHHHHCC-----	64.49	-

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 RL34_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL34_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 RL34_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK5_HUMAN	CDK5	physical	10049762
CDK4_HUMAN	CDK4	physical	10049762
A4_HUMAN	APP	physical	21832049
IF6_HUMAN	EIF6	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL21_HUMAN	RPL21	physical	26344197
RL23_HUMAN	RPL23	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL24_HUMAN	RPL24	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS21_HUMAN	RPS21	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
RL40_HUMAN	UBA52	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 RL34_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-36, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-12, AND MASSSPECTROMETRY.	19369195 [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-12, AND MASSSPECTROMETRY.	18691976 [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-12, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.	17924679 [Abstract]