dbPTM

RS10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS10_HUMAN
UniProt AC	P46783
Protein Name	40S ribosomal protein S10
Gene Name	RPS10
Organism	Homo sapiens (Human).
Sequence Length	165
Subcellular Localization	Cytoplasm . Nucleus, nucleolus . Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus.
Protein Description	Component of the 40S ribosomal subunit..
Protein Sequence	MLMPKKNRIAIYELLFKEGVMVAKKDVHMPKHPELADKNVPNLHVMKAMQSLKSRGYVKEQFAWRHFYWYLTNEGIQYLRDYLHLPPEIVPATLRRSRPETGRPRPKGLEGERPARLTRGEADRDTYRRSAVPPGADKKAEAGAGSATEFQFRGGFGRGRGQPPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MLMPKKNRIAIYE --CCCCCCCCCHHHH	45.66	24816145
12	Phosphorylation	KKNRIAIYELLFKEG CCCCCHHHHHHHHCC	7.48	27273156
17	Acetylation	AIYELLFKEGVMVAK HHHHHHHHCCCEEEE	54.23	133657
17	Ubiquitination	AIYELLFKEGVMVAK HHHHHHHHCCCEEEE	54.23	16196087
24	Acetylation	KEGVMVAKKDVHMPK HCCCEEEECCCCCCC	37.79	25953088
24	Ubiquitination	KEGVMVAKKDVHMPK HCCCEEEECCCCCCC	37.79	-
25	Ubiquitination	EGVMVAKKDVHMPKH CCCEEEECCCCCCCC	56.07	-
31	Acetylation	KKDVHMPKHPELADK ECCCCCCCCHHHHCC	65.30	26822725
31	Ubiquitination	KKDVHMPKHPELADK ECCCCCCCCHHHHCC	65.30	33845483
38	Acetylation	KHPELADKNVPNLHV CCHHHHCCCCCCHHH	54.99	23954790
38	Ubiquitination	KHPELADKNVPNLHV CCHHHHCCCCCCHHH	54.99	21963094
47	Acetylation	VPNLHVMKAMQSLKS CCCHHHHHHHHHHHH	39.35	25953088
47	Ubiquitination	VPNLHVMKAMQSLKS CCCHHHHHHHHHHHH	39.35	23000965
53	Acetylation	MKAMQSLKSRGYVKE HHHHHHHHHCCCEEH	43.27	26051181
53	Succinylation	MKAMQSLKSRGYVKE HHHHHHHHHCCCEEH	43.27	23954790
53	Ubiquitination	MKAMQSLKSRGYVKE HHHHHHHHHCCCEEH	43.27	23000965
59	Ubiquitination	LKSRGYVKEQFAWRH HHHCCCEEHHHHHHH	37.00	23000965
59	Acetylation	LKSRGYVKEQFAWRH HHHCCCEEHHHHHHH	37.00	25825284
68	Phosphorylation	QFAWRHFYWYLTNEG HHHHHHHHHHHHHHH	6.24	29496907
70	Phosphorylation	AWRHFYWYLTNEGIQ HHHHHHHHHHHHHHH	7.71	29496907
78	Phosphorylation	LTNEGIQYLRDYLHL HHHHHHHHHHHHHCC	11.20	-
82	Phosphorylation	GIQYLRDYLHLPPEI HHHHHHHHHCCCHHH	6.92	28152594
93	Phosphorylation	PPEIVPATLRRSRPE CHHHHCHHHHCCCCC	18.09	30576142
97	Phosphorylation	VPATLRRSRPETGRP HCHHHHCCCCCCCCC	45.83	23312004
101	Phosphorylation	LRRSRPETGRPRPKG HHCCCCCCCCCCCCC	40.97	29978859
107	Ubiquitination	ETGRPRPKGLEGERP CCCCCCCCCCCCCCC	76.91	23000965
107	Sumoylation	ETGRPRPKGLEGERP CCCCCCCCCCCCCCC	76.91	-
107	Acetylation	ETGRPRPKGLEGERP CCCCCCCCCCCCCCC	76.91	27452117
118	Phosphorylation	GERPARLTRGEADRD CCCCCCCCCCCCCHH	30.95	23917254
119	Methylation	ERPARLTRGEADRDT CCCCCCCCCCCCHHH	45.61	12018791
126	Phosphorylation	RGEADRDTYRRSAVP CCCCCHHHHHHHCCC	21.59	28152594
127	Phosphorylation	GEADRDTYRRSAVPP CCCCHHHHHHHCCCC	14.33	28152594
130	Phosphorylation	DRDTYRRSAVPPGAD CHHHHHHHCCCCCCC	25.31	25159151
138	Sumoylation	AVPPGADKKAEAGAG CCCCCCCCCCCCCCC	54.04	-
138	Neddylation	AVPPGADKKAEAGAG CCCCCCCCCCCCCCC	54.04	32015554
138	Ubiquitination	AVPPGADKKAEAGAG CCCCCCCCCCCCCCC	54.04	27667366
139	Sumoylation	VPPGADKKAEAGAGS CCCCCCCCCCCCCCC	52.59	-
139	Sumoylation	VPPGADKKAEAGAGS CCCCCCCCCCCCCCC	52.59	-
139	Ubiquitination	VPPGADKKAEAGAGS CCCCCCCCCCCCCCC	52.59	23000965
139	Methylation	VPPGADKKAEAGAGS CCCCCCCCCCCCCCC	52.59	23644510
146	Phosphorylation	KAEAGAGSATEFQFR CCCCCCCCCCEEEEC	31.33	19664994
148	Phosphorylation	EAGAGSATEFQFRGG CCCCCCCCEEEECCC	38.74	30266825
153	Methylation	SATEFQFRGGFGRGR CCCEEEECCCCCCCC	33.28	30989255
158	Methylation	QFRGGFGRGRGQPPQ EECCCCCCCCCCCCC	29.40	20159986
158	Dimethylation	QFRGGFGRGRGQPPQ EECCCCCCCCCCCCC	29.40	-
160	Methylation	RGGFGRGRGQPPQ-- CCCCCCCCCCCCC--	38.93	20159986
160	Dimethylation	RGGFGRGRGQPPQ-- CCCCCCCCCCCCC--	38.93	-

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
118	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	MKRN1	Q9UHC7	PMID:31640799

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS10_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 RS10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HAP1_HUMAN	HAP1	physical	16169070
HIP1_HUMAN	HIP1	physical	16169070
KAT7_HUMAN	KAT7	physical	16169070
PROF2_HUMAN	PFN2	physical	16169070
PTTG1_HUMAN	PTTG1	physical	9915854
WIZ_HUMAN	WIZ	physical	21900206
DVL3_HUMAN	DVL3	physical	21900206
HAP1_HUMAN	HAP1	physical	21900206
TCF25_HUMAN	TCF25	physical	21900206
EED_HUMAN	EED	physical	21900206
XRCC6_HUMAN	XRCC6	physical	21900206
DNM3B_HUMAN	DNMT3B	physical	21900206
DMPK_HUMAN	DMPK	physical	21900206
A4_HUMAN	APP	physical	21832049
RS13_HUMAN	RPS13	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS29_HUMAN	RPS29	physical	22939629
TMCO1_HUMAN	TMCO1	physical	22939629
EIF3A_HUMAN	EIF3A	physical	22863883
EIF3E_HUMAN	EIF3E	physical	22863883
EIF3K_HUMAN	EIF3K	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
RS11_HUMAN	RPS11	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS17_HUMAN	RPS17	physical	22863883
RS19_HUMAN	RPS19	physical	22863883
RS23_HUMAN	RPS23	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS4X_HUMAN	RPS4X	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
PAIRB_HUMAN	SERBP1	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
NRDE2_HUMAN	NRDE2	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL23_HUMAN	RPL23	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RRP7A_HUMAN	RRP7A	physical	26344197
TOM22_HUMAN	TOMM22	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613308	Diamond-Blackfan anemia 9 (DBA9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RS10_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Methylation of ribosomal protein S10 by protein-argininemethyltransferase 5 regulates ribosome biogenesis."; Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.; J. Biol. Chem. 285:12695-12705(2010). Cited for: SUBCELLULAR LOCATION, METHYLATION AT ARG-158 AND ARG-160, INTERACTIONWITH PRMT5 AND NPM1, AND MUTAGENESIS OF ARG-158 AND ARG-160.	20159986 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12 AND SER-146, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 TYR-12 AND SER-146, AND MASSSPECTROMETRY.	18669648 [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-146, 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-130, AND MASSSPECTROMETRY.	19007248 [Abstract]
"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-12, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, AND MASSSPECTROMETRY.	17389395 [Abstract]
"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-12, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, AND MASSSPECTROMETRY.	15592455 [Abstract]