RL27A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL27A_HUMAN
• UniProt AC: P46776
• Protein Name: 60S ribosomal protein L27a
• Gene Name: RPL27A
• Organism: Homo sapiens (Human).
• Sequence Length: 148
• Protein Sequence: MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGLHHHRINFDKYHPGYFGKVGMKHYHLKRNQSFCPTVNLDKLWTLVSEQTRVNAAKNKTGAAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKSVGGACVLVA

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	Phosphorylation	-----MPSRLRKTRK -----CCCHHHHHHH	42.52	24425749
12	Methylation	LRKTRKLRGHVSHGH HHHHHHHCCCCCCCC	35.89	115491977
16	Phosphorylation	RKLRGHVSHGHGRIG HHHCCCCCCCCCCCC	20.34	-
39	Hydroxylation	RGNAGGLHHHRINFD CCCCCCCCCCCCCCC	20.27	23103944
47	Acetylation	HHRINFDKYHPGYFG CCCCCCCCCCCCCCC	41.12	19608861
47	Ubiquitination	HHRINFDKYHPGYFG CCCCCCCCCCCCCCC	41.12	23000965
48	Phosphorylation	HRINFDKYHPGYFGK CCCCCCCCCCCCCCC	18.32	20090780
52	Phosphorylation	FDKYHPGYFGKVGMK CCCCCCCCCCCCCCC	17.38	28152594
55	Methylation	YHPGYFGKVGMKHYH CCCCCCCCCCCCEEE	26.22	22635765
55	Acetylation	YHPGYFGKVGMKHYH CCCCCCCCCCCCEEE	26.22	19608861
55	Ubiquitination	YHPGYFGKVGMKHYH CCCCCCCCCCCCEEE	26.22	23000965
59	Ubiquitination	YFGKVGMKHYHLKRN CCCCCCCCEEECCCC	34.77	23000965
59	Acetylation	YFGKVGMKHYHLKRN CCCCCCCCEEECCCC	34.77	26051181
59	Sumoylation	YFGKVGMKHYHLKRN CCCCCCCCEEECCCC	34.77	-
59	Sumoylation	YFGKVGMKHYHLKRN CCCCCCCCEEECCCC	34.77	-
65	Methylation	MKHYHLKRNQSFCPT CCEEECCCCCCCCCC	53.43	115491985
68	Phosphorylation	YHLKRNQSFCPTVNL EECCCCCCCCCCCCH	32.15	29255136
70	Glutathionylation	LKRNQSFCPTVNLDK CCCCCCCCCCCCHHH	3.15	22555962
72	Phosphorylation	RNQSFCPTVNLDKLW CCCCCCCCCCHHHHH	24.17	28450419
77	Ubiquitination	CPTVNLDKLWTLVSE CCCCCHHHHHHHHCH	49.44	22817900
86	Phosphorylation	WTLVSEQTRVNAAKN HHHHCHHHHHHHHHC	32.31	29514088
92	Ubiquitination	QTRVNAAKNKTGAAP HHHHHHHHCCCCCCC	57.47	23000965
94	Ubiquitination	RVNAAKNKTGAAPII HHHHHHCCCCCCCHH	47.86	23000965
94	Acetylation	RVNAAKNKTGAAPII HHHHHHCCCCCCCHH	47.86	27452117
94	Malonylation	RVNAAKNKTGAAPII HHHHHHCCCCCCCHH	47.86	26320211
95	Phosphorylation	VNAAKNKTGAAPIID HHHHHCCCCCCCHHH	41.25	23911959
110	2-Hydroxyisobutyrylation	VVRSGYYKVLGKGKL HHHHCCEEECCCCCC	23.62	-
110	Ubiquitination	VVRSGYYKVLGKGKL HHHHCCEEECCCCCC	23.62	21963094
110	Acetylation	VVRSGYYKVLGKGKL HHHHCCEEECCCCCC	23.62	19608861
110	Succinylation	VVRSGYYKVLGKGKL HHHHCCEEECCCCCC	23.62	23954790
114	Ubiquitination	GYYKVLGKGKLPKQP CCEEECCCCCCCCCC	49.03	22817900
116	Ubiquitination	YKVLGKGKLPKQPVI EEECCCCCCCCCCEE	66.17	-
119	Ubiquitination	LGKGKLPKQPVIVKA CCCCCCCCCCEEEEE	77.12	33845483
125	2-Hydroxyisobutyrylation	PKQPVIVKAKFFSRR CCCCEEEEEEECCHH	34.43	-
125	Ubiquitination	PKQPVIVKAKFFSRR CCCCEEEEEEECCHH	34.43	27667366
125	Acetylation	PKQPVIVKAKFFSRR CCCCEEEEEEECCHH	34.43	25953088
127	Ubiquitination	QPVIVKAKFFSRRAE CCEEEEEEECCHHHH	41.02	22817900
127	Acetylation	QPVIVKAKFFSRRAE CCEEEEEEECCHHHH	41.02	26051181
130	Phosphorylation	IVKAKFFSRRAEEKI EEEEEECCHHHHHHH	24.80	25394399
136	Acetylation	FSRRAEEKIKSVGGA CCHHHHHHHHHHCCE	47.11	26051181
138	Ubiquitination	RRAEEKIKSVGGACV HHHHHHHHHHCCEEE	50.59	-
144	S-palmitoylation	IKSVGGACVLVA--- HHHHCCEEEEEC---	2.48	29575903

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

Oops, there are no upstream regulatory protein records of RL27A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
39	H	Hydroxylation	Hydroxylated on His-39 by MINA.	23103944

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RL27A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL37A_HUMAN	RPL37A	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RL35_HUMAN	RPL35	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL36_HUMAN	RPL36	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
UBIM_HUMAN	FAU	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
AIMP1_HUMAN	AIMP1	physical	22863883
AIMP2_HUMAN	AIMP2	physical	22863883
SYDC_HUMAN	DARS	physical	22863883
ROA1_HUMAN	HNRNPA1	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
CCAR2_HUMAN	CCAR2	physical	22863883
SYMC_HUMAN	MARS	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
SIAH1_HUMAN	SIAH1	physical	25416956
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36L_HUMAN	RPL36AL	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS7_HUMAN	RPS7	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.

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-47; LYS-55 AND LYS-110, ANDMASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-68, AND MASSSPECTROMETRY.
PubMed: 19369195

"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-68, AND MASSSPECTROMETRY.
PubMed: 18691976