RL35A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL35A_HUMAN
• UniProt AC: P18077
• Protein Name: 60S ribosomal protein L35a
• Gene Name: RPL35A
• Organism: Homo sapiens (Human).
• Sequence Length: 110
• Protein Description: Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site..
• Protein Sequence: MSGRLWSKAIFAGYKRGLRNQREHTALLKIEGVYARDETEFYLGKRCAYVYKAKNNTVTPGGKPNKTRVIWGKVTRAHGNSGMVRAKFRSNLPAKAIGHRIRVMLYPSRI

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
2	Phosphorylation	------MSGRLWSKA ------CCCCHHHHH	32.40	29514088
4	Methylation	----MSGRLWSKAIF ----CCCCHHHHHHH	26.19	115492145
8	Acetylation	MSGRLWSKAIFAGYK CCCCHHHHHHHHHHH	33.64	19608861
8	2-Hydroxyisobutyrylation	MSGRLWSKAIFAGYK CCCCHHHHHHHHHHH	33.64	-
8	Ubiquitination	MSGRLWSKAIFAGYK CCCCHHHHHHHHHHH	33.64	23000965
14	Phosphorylation	SKAIFAGYKRGLRNQ HHHHHHHHHHHHCCC	8.29	24719451
15	2-Hydroxyisobutyrylation	KAIFAGYKRGLRNQR HHHHHHHHHHHCCCC	38.79	-
15	Acetylation	KAIFAGYKRGLRNQR HHHHHHHHHHHCCCC	38.79	25953088
15	Ubiquitination	KAIFAGYKRGLRNQR HHHHHHHHHHHCCCC	38.79	27667366
25	Phosphorylation	LRNQREHTALLKIEG HCCCCCCEEEEEEEE	17.78	28152594
29	Ubiquitination	REHTALLKIEGVYAR CCCEEEEEEEEEECC	39.29	21963094
29	Acetylation	REHTALLKIEGVYAR CCCEEEEEEEEEECC	39.29	25825284
34	Phosphorylation	LLKIEGVYARDETEF EEEEEEEECCCCCEE	13.53	28102081
39	Phosphorylation	GVYARDETEFYLGKR EEECCCCCEEEECCE	35.37	28152594
42	Phosphorylation	ARDETEFYLGKRCAY CCCCCEEEECCEEEE	14.33	28152594
45	Ubiquitination	ETEFYLGKRCAYVYK CCEEEECCEEEEEEE	41.53	23000965
45	Succinylation	ETEFYLGKRCAYVYK CCEEEECCEEEEEEE	41.53	23954790
45	Acetylation	ETEFYLGKRCAYVYK CCEEEECCEEEEEEE	41.53	25953088
45	2-Hydroxyisobutyrylation	ETEFYLGKRCAYVYK CCEEEECCEEEEEEE	41.53	-
52	Methylation	KRCAYVYKAKNNTVT CEEEEEEECCCCEEC	42.72	115977043
52	Acetylation	KRCAYVYKAKNNTVT CEEEEEEECCCCEEC	42.72	25953088
52	Ubiquitination	KRCAYVYKAKNNTVT CEEEEEEECCCCEEC	42.72	-
54	Ubiquitination	CAYVYKAKNNTVTPG EEEEEECCCCEECCC	46.72	24816145
57	Phosphorylation	VYKAKNNTVTPGGKP EEECCCCEECCCCCC	34.84	25262027
59	Phosphorylation	KAKNNTVTPGGKPNK ECCCCEECCCCCCCC	17.74	25262027
63	Succinylation	NTVTPGGKPNKTRVI CEECCCCCCCCEEEE	51.86	-
63	Succinylation	NTVTPGGKPNKTRVI CEECCCCCCCCEEEE	51.86	27452117
63	Acetylation	NTVTPGGKPNKTRVI CEECCCCCCCCEEEE	51.86	-
63	Ubiquitination	NTVTPGGKPNKTRVI CEECCCCCCCCEEEE	51.86	27667366
66	2-Hydroxyisobutyrylation	TPGGKPNKTRVIWGK CCCCCCCCEEEEEEE	46.35	-
66	Ubiquitination	TPGGKPNKTRVIWGK CCCCCCCCEEEEEEE	46.35	22817900
73	Acetylation	KTRVIWGKVTRAHGN CEEEEEEEEEECCCC	25.99	25953088
73	Ubiquitination	KTRVIWGKVTRAHGN CEEEEEEEEEECCCC	25.99	73
83	Sulfoxidation	RAHGNSGMVRAKFRS ECCCCCCCCCHHHHC	1.53	30846556
90	Phosphorylation	MVRAKFRSNLPAKAI CCCHHHHCCCCHHHH	45.94	29514088
95	2-Hydroxyisobutyrylation	FRSNLPAKAIGHRIR HHCCCCHHHHCCEEE	38.30	-
95	Ubiquitination	FRSNLPAKAIGHRIR HHCCCCHHHHCCEEE	38.30	23000965
95	Acetylation	FRSNLPAKAIGHRIR HHCCCCHHHHCCEEE	38.30	25953088
106	Phosphorylation	HRIRVMLYPSRI--- CEEEEEEEECCC---	4.89	25884760
108	Phosphorylation	IRVMLYPSRI----- EEEEEEECCC-----	29.11	21406692
109	Methylation	RVMLYPSRI------ EEEEEECCC------	33.85	115492153

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

Oops, there are no upstream regulatory protein records of RL35A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL35A_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 RL35A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH3G3_HUMAN	SH3GL3	physical	16169070
SH3G3_HUMAN	SH3GL3	physical	21900206
HNRL2_HUMAN	HNRNPUL2	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL39_HUMAN	RPL39	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS27L_HUMAN	RPS27L	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RTF1_HUMAN	RTF1	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612528: Diamond-Blackfan anemia 5 (DBA5)
• 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-8, AND MASS SPECTROMETRY.
PubMed: 19608861