dbPTM

RL13A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL13A_HUMAN
UniProt AC	P40429
Protein Name	60S ribosomal protein L13a
Gene Name	RPL13A
Organism	Homo sapiens (Human).
Sequence Length	203
Subcellular Localization	Cytoplasm .
Protein Description	Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. Involved in methylation of rRNA..
Protein Sequence	MAEVQVLVLDGRGHLLGRLAAIVAKQVLLGRKVVVVRCEGINISGNFYRNKLKYLAFLRKRMNTNPSRGPYHFRAPSRIFWRTVRGMLPHKTKRGQAALDRLKVFDGIPPPYDKKKRMVVPAALKVVRLKPTRKFAYLGRLAHEVGWKYQAVTATLEEKRKEKAKIHYRKKKQLMRLRKQAEKNVEKKIDKYTEVLKTHGLLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEVQVLVL ------CCEEEEEEE	26.18	12962325
12	Methylation	QVLVLDGRGHLLGRL EEEEECCCCHHHHHH	29.08	115491679
25	Acetylation	RLAAIVAKQVLLGRK HHHHHHHHHHHCCCC	30.00	26051181
25	Ubiquitination	RLAAIVAKQVLLGRK HHHHHHHHHHHCCCC	30.00	21890473
25	2-Hydroxyisobutyrylation	RLAAIVAKQVLLGRK HHHHHHHHHHHCCCC	30.00	-
51	Ubiquitination	SGNFYRNKLKYLAFL CCCCHHHHHHHHHHH	37.04	21890473
53	Ubiquitination	NFYRNKLKYLAFLRK CCHHHHHHHHHHHHH	39.57	21890473
53	Acetylation	NFYRNKLKYLAFLRK CCHHHHHHHHHHHHH	39.57	25953088
54	Phosphorylation	FYRNKLKYLAFLRKR CHHHHHHHHHHHHHH	17.44	20068231
59	Citrullination	LKYLAFLRKRMNTNP HHHHHHHHHHCCCCC	20.34	-
59	Citrullination	LKYLAFLRKRMNTNP HHHHHHHHHHCCCCC	20.34	-
64	Phosphorylation	FLRKRMNTNPSRGPY HHHHHCCCCCCCCCC	38.88	28152594
67	Phosphorylation	KRMNTNPSRGPYHFR HHCCCCCCCCCCCCC	52.52	28152594
68	Methylation	RMNTNPSRGPYHFRA HCCCCCCCCCCCCCC	51.90	115491699
71	Phosphorylation	TNPSRGPYHFRAPSR CCCCCCCCCCCCCCH	19.20	28152594
74	Methylation	SRGPYHFRAPSRIFW CCCCCCCCCCCHHHH	32.07	115491689
77	Phosphorylation	PYHFRAPSRIFWRTV CCCCCCCCHHHHHHH	36.70	18995835
91	Ubiquitination	VRGMLPHKTKRGQAA HHHCCCCCCHHHHHH	54.52	-
93	Ubiquitination	GMLPHKTKRGQAALD HCCCCCCHHHHHHHH	60.37	-
101	Methylation	RGQAALDRLKVFDGI HHHHHHHHHCCCCCC	36.94	115491709
103	Ubiquitination	QAALDRLKVFDGIPP HHHHHHHCCCCCCCC	41.57	21906983
114	Ubiquitination	GIPPPYDKKKRMVVP CCCCCCCHHHCCHHH	55.11	21906983
114	Acetylation	GIPPPYDKKKRMVVP CCCCCCCHHHCCHHH	55.11	26051181
114	2-Hydroxyisobutyrylation	GIPPPYDKKKRMVVP CCCCCCCHHHCCHHH	55.11	-
115	Ubiquitination	IPPPYDKKKRMVVPA CCCCCCHHHCCHHHH	42.59	-
118	Sulfoxidation	PYDKKKRMVVPAALK CCCHHHCCHHHHEEE	4.97	30846556
125	Ubiquitination	MVVPAALKVVRLKPT CHHHHEEEEEECCCC	33.68	21890473
125	2-Hydroxyisobutyrylation	MVVPAALKVVRLKPT CHHHHEEEEEECCCC	33.68	-
125	Acetylation	MVVPAALKVVRLKPT CHHHHEEEEEECCCC	33.68	25953088
134	2-Hydroxyisobutyrylation	VRLKPTRKFAYLGRL EECCCCCCHHHHHHH	36.50	-
134	Acetylation	VRLKPTRKFAYLGRL EECCCCCCHHHHHHH	36.50	26051181
134	Ubiquitination	VRLKPTRKFAYLGRL EECCCCCCHHHHHHH	36.50	21906983
137	Phosphorylation	KPTRKFAYLGRLAHE CCCCCHHHHHHHHHH	16.90	25884760
140	Citrullination	RKFAYLGRLAHEVGW CCHHHHHHHHHHHHH	26.55	-
140	Citrullination	RKFAYLGRLAHEVGW CCHHHHHHHHHHHHH	26.55	-
148	2-Hydroxyisobutyrylation	LAHEVGWKYQAVTAT HHHHHHHHHHHHCCC	22.89	-
148	Ubiquitination	LAHEVGWKYQAVTAT HHHHHHHHHHHHCCC	22.89	21890473
148	Acetylation	LAHEVGWKYQAVTAT HHHHHHHHHHHHCCC	22.89	23954790
148	Methylation	LAHEVGWKYQAVTAT HHHHHHHHHHHHCCC	22.89	66725961
149	Phosphorylation	AHEVGWKYQAVTATL HHHHHHHHHHHCCCH	8.66	28152594
153	Phosphorylation	GWKYQAVTATLEEKR HHHHHHHCCCHHHHH	19.55	26434776
155	Phosphorylation	KYQAVTATLEEKRKE HHHHHCCCHHHHHHH	25.90	26434776
159	Ubiquitination	VTATLEEKRKEKAKI HCCCHHHHHHHHHHH	60.44	20972266
159	2-Hydroxyisobutyrylation	VTATLEEKRKEKAKI HCCCHHHHHHHHHHH	60.44	-
161	Ubiquitination	ATLEEKRKEKAKIHY CCHHHHHHHHHHHHH	74.71	-
163	Acetylation	LEEKRKEKAKIHYRK HHHHHHHHHHHHHHH	59.00	19809457
165	Ubiquitination	EKRKEKAKIHYRKKK HHHHHHHHHHHHHHH	40.87	-
188	Ubiquitination	AEKNVEKKIDKYTEV HHHHHHHHHHHHHHH	42.50	21906983
188	Acetylation	AEKNVEKKIDKYTEV HHHHHHHHHHHHHHH	42.50	21339330
191	Malonylation	NVEKKIDKYTEVLKT HHHHHHHHHHHHHHH	58.51	26320211
191	2-Hydroxyisobutyrylation	NVEKKIDKYTEVLKT HHHHHHHHHHHHHHH	58.51	-
191	Ubiquitination	NVEKKIDKYTEVLKT HHHHHHHHHHHHHHH	58.51	21890473
191	Acetylation	NVEKKIDKYTEVLKT HHHHHHHHHHHHHHH	58.51	19608861
192	Phosphorylation	VEKKIDKYTEVLKTH HHHHHHHHHHHHHHC	12.37	28152594
193	Phosphorylation	EKKIDKYTEVLKTHG HHHHHHHHHHHHHCC	25.92	28152594
197	2-Hydroxyisobutyrylation	DKYTEVLKTHGLLV- HHHHHHHHHCCCCC-	43.59	-
197	Acetylation	DKYTEVLKTHGLLV- HHHHHHHHHCCCCC-	43.59	26051181
197	Ubiquitination	DKYTEVLKTHGLLV- HHHHHHHHHCCCCC-	43.59	-

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
77	S	Phosphorylation	Kinase	DAPK1	P53355	PSP
77	S	Phosphorylation	Kinase	DAPK3	O43293	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
77	S	Phosphorylation		18995835
Phosphorylation at Ser-77 upon interferon-gamma treatment in monocytes involves a DAPK1-DAPK3 kinase cascade and is causing release from the ribosome, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition.

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 RL13A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STOM_HUMAN	STOM	physical	21988832
RL30_HUMAN	RPL30	physical	21988832
VTNC_HUMAN	VTN	physical	21988832
IF6_HUMAN	EIF6	physical	26344197
FBRL_HUMAN	FBL	physical	26344197
PABP1_HUMAN	PABPC1	physical	26344197
PABP4_HUMAN	PABPC4	physical	26344197
RPAC1_HUMAN	POLR1C	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL5_HUMAN	RPL5	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
RS14_HUMAN	RPS14	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	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 RL13A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Characterization and analysis of posttranslational modifications ofthe human large cytoplasmic ribosomal subunit proteins by massspectrometry and Edman sequencing."; Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,Karpova G.G.; J. Protein Chem. 22:249-258(2003). Cited for: MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT ALA-2.	12962325 [Abstract]
"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-191, AND MASS SPECTROMETRY.	19608861 [Abstract]

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