RS27_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS27_HUMAN
• UniProt AC: P42677
• Protein Name: 40S ribosomal protein S27
• Gene Name: RPS27
• Organism: Homo sapiens (Human).
• Sequence Length: 84
• Protein Description: Component of the small ribosomal subunit. [PubMed: 8706699 Required for proper rRNA processing and maturation of 18S rRNAs]
• Protein Sequence: MPLAKDLLHPSPEEEKRKHKKKRLVQSPNSYFMDVKCPGCYKITTVFSHAQTVVLCVGCSTVLCQPTGGKARLTEGCSFRRKQH

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
5	Acetylation	---MPLAKDLLHPSP ---CCCHHHHCCCCH	57.50	19608861
5	2-Hydroxyisobutyrylation	---MPLAKDLLHPSP ---CCCHHHHCCCCH	57.50	-
5	Sumoylation	---MPLAKDLLHPSP ---CCCHHHHCCCCH	57.50	19608861
5	Methylation	---MPLAKDLLHPSP ---CCCHHHHCCCCH	57.50	22635421
5	Sumoylation	---MPLAKDLLHPSP ---CCCHHHHCCCCH	57.50	-
5	Ubiquitination	---MPLAKDLLHPSP ---CCCHHHHCCCCH	57.50	23000965
11	Phosphorylation	AKDLLHPSPEEEKRK HHHHCCCCHHHHHHH	33.91	29255136
16	Acetylation	HPSPEEEKRKHKKKR CCCHHHHHHHHHHHH	70.76	23749302
16	2-Hydroxyisobutyrylation	HPSPEEEKRKHKKKR CCCHHHHHHHHHHHH	70.76	-
16	Ubiquitination	HPSPEEEKRKHKKKR CCCHHHHHHHHHHHH	70.76	21906983
18	Ubiquitination	SPEEEKRKHKKKRLV CHHHHHHHHHHHHHH	71.49	22817900
20	Ubiquitination	EEEKRKHKKKRLVQS HHHHHHHHHHHHHCC	64.13	22817900
21	Ubiquitination	EEKRKHKKKRLVQSP HHHHHHHHHHHHCCC	42.73	22817900
22	Sumoylation	EKRKHKKKRLVQSPN HHHHHHHHHHHCCCC	56.63	-
22	Sumoylation	EKRKHKKKRLVQSPN HHHHHHHHHHHCCCC	56.63	-
22	Ubiquitination	EKRKHKKKRLVQSPN HHHHHHHHHHHCCCC	56.63	23503661
27	Phosphorylation	KKKRLVQSPNSYFMD HHHHHHCCCCCCCCC	20.69	29255136
30	Phosphorylation	RLVQSPNSYFMDVKC HHHCCCCCCCCCCCC	24.11	21945579
31	Phosphorylation	LVQSPNSYFMDVKCP HHCCCCCCCCCCCCC	15.01	29255136
33	Sulfoxidation	QSPNSYFMDVKCPGC CCCCCCCCCCCCCCE	4.38	21406390
36	Ubiquitination	NSYFMDVKCPGCYKI CCCCCCCCCCCEEEE	30.37	16196087
70	Ubiquitination	LCQPTGGKARLTEGC EECCCCCCEECCCCC	31.51	-
72	Methylation	QPTGGKARLTEGCSF CCCCCCEECCCCCCC	45.70	-
74	Phosphorylation	TGGKARLTEGCSFRR CCCCEECCCCCCCCC	25.44	24702127
77	S-palmitoylation	KARLTEGCSFRRKQH CEECCCCCCCCCCCC	2.57	29575903
77	Glutathionylation	KARLTEGCSFRRKQH CEECCCCCCCCCCCC	2.57	22555962
78	Phosphorylation	ARLTEGCSFRRKQH- EECCCCCCCCCCCC-	32.42	29255136

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
27	S	Phosphorylation	Kinase	CDK2	P24941	PSP
27	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS27_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 RS27_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_HUMAN	MDM2	physical	21170087
ENOPH_HUMAN	ENOPH1	physical	21900206
SYMC_HUMAN	MARS	physical	21900206
RTN4_HUMAN	RTN4	physical	21900206
WDCP_HUMAN	C2orf44	physical	21900206
NSG2_HUMAN	HMP19	physical	21900206
NACAD_HUMAN	NACAD	physical	21900206
CXCL7_HUMAN	PPBP	physical	21900206
TOM1_HUMAN	TOM1	physical	21988832
SKIL_HUMAN	SKIL	physical	21988832
EIFCL_HUMAN	EIF3CL	physical	22863883
ROA0_HUMAN	HNRNPA0	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
PNO1_HUMAN	PNO1	physical	22863883
PTBP1_HUMAN	PTBP1	physical	22863883
RANB9_HUMAN	RANBP9	physical	22863883
RL35_HUMAN	RPL35	physical	22863883
RS13_HUMAN	RPS13	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS26_HUMAN	RPS26	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
SND1_HUMAN	SND1	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
POTEF_HUMAN	POTEF	physical	28514442
ATP7A_HUMAN	ATP7A	physical	28514442
SRC_HUMAN	SRC	physical	28514442
ERIC5_HUMAN	ERICH5	physical	28514442
TBA4A_HUMAN	TUBA4A	physical	28514442
PHAG1_HUMAN	PAG1	physical	28514442
FUS_HUMAN	FUS	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
2A5E_HUMAN	PPP2R5E	physical	28514442
2A5D_HUMAN	PPP2R5D	physical	28514442
TBA1A_HUMAN	TUBA1A	physical	28514442
DPOE4_HUMAN	POLE4	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
EF1A1_HUMAN	EEF1A1	physical	28514442
TBB3_HUMAN	TUBB3	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.

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-5, AND MASS 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-27; SER-30 AND SER-78,AND MASS SPECTROMETRY.
PubMed: 19369195

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-11; SER-27 AND SER-78,AND MASS SPECTROMETRY.
PubMed: 18691976

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-78, AND MASSSPECTROMETRY.
PubMed: 17081983

"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, AND MASSSPECTROMETRY.
PubMed: 19534553

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, AND MASSSPECTROMETRY.
PubMed: 18083107