dbPTM

RL31_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL31_HUMAN
UniProt AC	P62899
Protein Name	60S ribosomal protein L31
Gene Name	RPL31
Organism	Homo sapiens (Human).
Sequence Length	125
Subcellular Localization
Protein Description
Protein Sequence	MAPAKKGGEKKKGRSAINEVVTREYTINIHKRIHGVGFKKRAPRALKEIRKFAMKEMGTPDVRIDTRLNKAVWAKGIRNVPYRIRVRLSRKRNEDEDSPNKLYTLVTYVPVTTFKNLQTVNVDEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MAPAKKGG -------CCCCCCCC	10.20	22814378
6	Ubiquitination	--MAPAKKGGEKKKG --CCCCCCCCCCCCC	74.40	24816145
14	Methylation	GGEKKKGRSAINEVV CCCCCCCCHHHHHHH	31.62	115492057
15	Phosphorylation	GEKKKGRSAINEVVT CCCCCCCHHHHHHHC	42.01	25159151
22	Phosphorylation	SAINEVVTREYTINI HHHHHHHCEEEEEEE	23.98	29449344
25	Phosphorylation	NEVVTREYTINIHKR HHHHCEEEEEEEHHH	15.05	28152594
26	Phosphorylation	EVVTREYTINIHKRI HHHCEEEEEEEHHHH	11.64	28152594
31	2-Hydroxyisobutyrylation	EYTINIHKRIHGVGF EEEEEEHHHHCCCCC	49.61	-
31	Ubiquitination	EYTINIHKRIHGVGF EEEEEEHHHHCCCCC	49.61	33845483
31	Methylation	EYTINIHKRIHGVGF EEEEEEHHHHCCCCC	49.61	72614729
31	Acetylation	EYTINIHKRIHGVGF EEEEEEHHHHCCCCC	49.61	26051181
31	Succinylation	EYTINIHKRIHGVGF EEEEEEHHHHCCCCC	49.61	23954790
39	Methylation	RIHGVGFKKRAPRAL HHCCCCCCHHHHHHH	35.11	130849
39	Ubiquitination	RIHGVGFKKRAPRAL HHCCCCCCHHHHHHH	35.11	32015554
39	Acetylation	RIHGVGFKKRAPRAL HHCCCCCCHHHHHHH	35.11	23749302
40	Ubiquitination	IHGVGFKKRAPRALK HCCCCCCHHHHHHHH	52.08	-
51	Ubiquitination	RALKEIRKFAMKEMG HHHHHHHHHHHHHHC	43.04	23000965
55	Ubiquitination	EIRKFAMKEMGTPDV HHHHHHHHHHCCCCC	40.91	21890473
55	Ubiquitination	EIRKFAMKEMGTPDV HHHHHHHHHHCCCCC	40.91	23000965
55	Succinylation	EIRKFAMKEMGTPDV HHHHHHHHHHCCCCC	40.91	-
55	Ubiquitination	EIRKFAMKEMGTPDV HHHHHHHHHHCCCCC	40.91	21890473
55	Acetylation	EIRKFAMKEMGTPDV HHHHHHHHHHCCCCC	40.91	23236377
55	Succinylation	EIRKFAMKEMGTPDV HHHHHHHHHHCCCCC	40.91	23954790
57	Sulfoxidation	RKFAMKEMGTPDVRI HHHHHHHHCCCCCEE	6.38	28183972
59	Phosphorylation	FAMKEMGTPDVRIDT HHHHHHCCCCCEEHH	18.27	21815630
63	Methylation	EMGTPDVRIDTRLNK HHCCCCCEEHHHCCH	28.57	115492049
70	2-Hydroxyisobutyrylation	RIDTRLNKAVWAKGI EEHHHCCHHHHHCCC	49.24	-
70	Ubiquitination	RIDTRLNKAVWAKGI EEHHHCCHHHHHCCC	49.24	21890473
70	Malonylation	RIDTRLNKAVWAKGI EEHHHCCHHHHHCCC	49.24	26320211
70	Succinylation	RIDTRLNKAVWAKGI EEHHHCCHHHHHCCC	49.24	-
70	Acetylation	RIDTRLNKAVWAKGI EEHHHCCHHHHHCCC	49.24	27178108
70	Ubiquitination	RIDTRLNKAVWAKGI EEHHHCCHHHHHCCC	49.24	21890473
70	Ubiquitination	RIDTRLNKAVWAKGI EEHHHCCHHHHHCCC	49.24	23000965
70	Succinylation	RIDTRLNKAVWAKGI EEHHHCCHHHHHCCC	49.24	-
75	2-Hydroxyisobutyrylation	LNKAVWAKGIRNVPY CCHHHHHCCCCCCCE	38.88	-
75	Succinylation	LNKAVWAKGIRNVPY CCHHHHHCCCCCCCE	38.88	19608861
75	Ubiquitination	LNKAVWAKGIRNVPY CCHHHHHCCCCCCCE	38.88	21890473
75	Ubiquitination	LNKAVWAKGIRNVPY CCHHHHHCCCCCCCE	38.88	21890473
75	Acetylation	LNKAVWAKGIRNVPY CCHHHHHCCCCCCCE	38.88	19608861
75	Succinylation	LNKAVWAKGIRNVPY CCHHHHHCCCCCCCE	38.88	-
75	Ubiquitination	LNKAVWAKGIRNVPY CCHHHHHCCCCCCCE	38.88	23000965
89	Phosphorylation	YRIRVRLSRKRNEDE EEEEEEEECCCCCCC	25.78	-
98	Phosphorylation	KRNEDEDSPNKLYTL CCCCCCCCCCCEEEE	28.46	26055452
101	Ubiquitination	EDEDSPNKLYTLVTY CCCCCCCCEEEEEEE	46.37	29967540
101	Acetylation	EDEDSPNKLYTLVTY CCCCCCCCEEEEEEE	46.37	23236377
103 (in isoform 3)	Phosphorylation	-	10.31	29116813
103	Phosphorylation	EDSPNKLYTLVTYVP CCCCCCEEEEEEEEE	10.31	21945579
104	Phosphorylation	DSPNKLYTLVTYVPV CCCCCEEEEEEEEEE	25.78	21945579
107	Phosphorylation	NKLYTLVTYVPVTTF CCEEEEEEEEEEEEC	23.16	21945579
108	Phosphorylation	KLYTLVTYVPVTTFK CEEEEEEEEEEEECC	8.69	21945579
112	Phosphorylation	LVTYVPVTTFKNLQT EEEEEEEEECCCCEE	22.05	21945579
113	Phosphorylation	VTYVPVTTFKNLQTV EEEEEEEECCCCEEE	32.61	21945579
115	Methylation	YVPVTTFKNLQTVNV EEEEEECCCCEEEEC	55.44	115977011
115	Ubiquitination	YVPVTTFKNLQTVNV EEEEEECCCCEEEEC	55.44	23000965
116 (in isoform 3)	Phosphorylation	-	32.94	-
119	Phosphorylation	TTFKNLQTVNVDEN- EECCCCEEEECCCC-	19.74	25159151
119 (in isoform 3)	Phosphorylation	-	19.74	-
123	Phosphorylation	NLQTVNVDEN----- CCEEEECCCC-----	44.51	-
123 (in isoform 2)	Phosphorylation	-	44.51	-

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 RL31_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL31_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 RL31_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RL37A_HUMAN	RPL37A	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS10_HUMAN	RPS10	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS17_HUMAN	RPS17	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL35_HUMAN	RPL35	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
DDX27_HUMAN	DDX27	physical	26344197
IF6_HUMAN	EIF6	physical	26344197
LYAR_HUMAN	LYAR	physical	26344197
MK67I_HUMAN	NIFK	physical	26344197
PESC_HUMAN	PES1	physical	26344197
RL10A_HUMAN	RPL10A	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
RL21_HUMAN	RPL21	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL24_HUMAN	RPL24	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL34_HUMAN	RPL34	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	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
RLA1_HUMAN	RPLP1	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS12_HUMAN	RPS12	physical	26344197
RS13_HUMAN	RPS13	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
LA_HUMAN	SSB	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 RL31_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-75, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-98, AND MASSSPECTROMETRY.	18669648 [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-15, AND MASSSPECTROMETRY.	19007248 [Abstract]
"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-98, AND MASSSPECTROMETRY.	17081983 [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-103 AND TYR-108, ANDMASS SPECTROMETRY.	15592455 [Abstract]