RT07_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RT07_HUMAN
• UniProt AC: Q9Y2R9
• Protein Name: 28S ribosomal protein S7, mitochondrial
• Gene Name: MRPS7
• Organism: Homo sapiens (Human).
• Sequence Length: 242
• Subcellular Localization: Mitochondrion .
• Protein Sequence: MAAPAVKVARGWSGLALGVRRAVLQLPGLTQVRWSRYSPEFKDPLIDKEYYRKPVEELTEEEKYVRELKKTQLIKAAPAGKTSSVFEDPVISKFTNMMMIGGNKVLARSLMIQTLEAVKRKQFEKYHAASAEEQATIERNPYTIFHQALKNCEPMIGLVPILKGGRFYQVPVPLPDRRRRFLAMKWMITECRDKKHQRTLMPEKLSHKLLEAFHNQGPVIKRKHDLHKMAEANRALAHYRWW

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
7	Ubiquitination	-MAAPAVKVARGWSG -CCCCCHHHCCCCCH	32.08	-
38	Phosphorylation	QVRWSRYSPEFKDPL EEEECCCCCCCCCCC	19.49	28348404
42	Ubiquitination	SRYSPEFKDPLIDKE CCCCCCCCCCCCCHH	57.69	21890473
48	2-Hydroxyisobutyrylation	FKDPLIDKEYYRKPV CCCCCCCHHHHCCCH	40.39	-
48	Ubiquitination	FKDPLIDKEYYRKPV CCCCCCCHHHHCCCH	40.39	21890473
50	Phosphorylation	DPLIDKEYYRKPVEE CCCCCHHHHCCCHHH	17.82	28152594
51	Phosphorylation	PLIDKEYYRKPVEEL CCCCHHHHCCCHHHH	17.16	28152594
53	Ubiquitination	IDKEYYRKPVEELTE CCHHHHCCCHHHHCH	36.98	21890473
59	Phosphorylation	RKPVEELTEEEKYVR CCCHHHHCHHHHHHH	44.63	24719451
63	Ubiquitination	EELTEEEKYVRELKK HHHCHHHHHHHHHHH	52.94	-
75	Ubiquitination	LKKTQLIKAAPAGKT HHHHCEEECCCCCCC	47.27	-
81	Ubiquitination	IKAAPAGKTSSVFED EECCCCCCCCCHHCC	47.54	21890473
95	Phosphorylation	DPVISKFTNMMMIGG CHHHHHHCCEEEECC	26.41	-
109	Phosphorylation	GNKVLARSLMIQTLE CCHHHHHHHHHHHHH	19.38	24719451
111	Sulfoxidation	KVLARSLMIQTLEAV HHHHHHHHHHHHHHH	1.94	21406390
114	Phosphorylation	ARSLMIQTLEAVKRK HHHHHHHHHHHHHHH	18.68	30301811
119	2-Hydroxyisobutyrylation	IQTLEAVKRKQFEKY HHHHHHHHHHHHHHH	62.01	-
119	Ubiquitination	IQTLEAVKRKQFEKY HHHHHHHHHHHHHHH	62.01	-
125	Acetylation	VKRKQFEKYHAASAE HHHHHHHHHHCCCHH	43.56	23954790
125	Ubiquitination	VKRKQFEKYHAASAE HHHHHHHHHHCCCHH	43.56	21890473
130	Phosphorylation	FEKYHAASAEEQATI HHHHHCCCHHHHHHH	36.68	-
136	Phosphorylation	ASAEEQATIERNPYT CCHHHHHHHHCCHHH	24.06	-
152	Glutathionylation	FHQALKNCEPMIGLV HHHHHHCCCCCCCEE	6.25	22555962
155	Sulfoxidation	ALKNCEPMIGLVPIL HHHCCCCCCCEEEEE	1.45	21406390
163	Ubiquitination	IGLVPILKGGRFYQV CCEEEEECCCEEEEE	61.10	21890473
163	Acetylation	IGLVPILKGGRFYQV CCEEEEECCCEEEEE	61.10	25953088
168	Phosphorylation	ILKGGRFYQVPVPLP EECCCEEEEECCCCC	13.77	28152594
199	Phosphorylation	RDKKHQRTLMPEKLS CCHHHHHCCCHHHHH	22.34	20068231
204	Acetylation	QRTLMPEKLSHKLLE HHCCCHHHHHHHHHH	49.79	25953088
204	Ubiquitination	QRTLMPEKLSHKLLE HHCCCHHHHHHHHHH	49.79	-
204	Malonylation	QRTLMPEKLSHKLLE HHCCCHHHHHHHHHH	49.79	26320211
208	Ubiquitination	MPEKLSHKLLEAFHN CHHHHHHHHHHHHHH	51.93	19608861
208	Acetylation	MPEKLSHKLLEAFHN CHHHHHHHHHHHHHH	51.93	19608861
208	Malonylation	MPEKLSHKLLEAFHN CHHHHHHHHHHHHHH	51.93	26320211
221	Acetylation	HNQGPVIKRKHDLHK HHCCCCCCCHHHHHH	56.48	25953088
221	Ubiquitination	HNQGPVIKRKHDLHK HHCCCCCCCHHHHHH	56.48	21890473
221	2-Hydroxyisobutyrylation	HNQGPVIKRKHDLHK HHCCCCCCCHHHHHH	56.48	-
228	Acetylation	KRKHDLHKMAEANRA CCHHHHHHHHHHHHH	47.29	19608861
239	Phosphorylation	ANRALAHYRWW---- HHHHHHHHCCC----	11.43	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RT07_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 RT07_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RT25_HUMAN	MRPS25	physical	22939629
RT09_HUMAN	MRPS9	physical	22939629
EFGM_HUMAN	GFM1	physical	26344197
RT09_HUMAN	MRPS9	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
EFTU_HUMAN	TUFM	physical	26344197
UBP28_HUMAN	USP28	physical	28514442
FEZ2_HUMAN	FEZ2	physical	28514442
GUF1_HUMAN	GUF1	physical	28514442
RT27_HUMAN	MRPS27	physical	28514442
RT15_HUMAN	MRPS15	physical	28514442
RT31_HUMAN	MRPS31	physical	28514442
TM1L1_HUMAN	TOM1L1	physical	28514442
CALU_HUMAN	CALU	physical	28514442
TP53B_HUMAN	TP53BP1	physical	28514442
GPC6_HUMAN	GPC6	physical	28514442
ROA1_HUMAN	HNRNPA1	physical	28514442
RS8_HUMAN	RPS8	physical	28514442
RT02_HUMAN	MRPS2	physical	28514442
CK5P3_HUMAN	CDK5RAP3	physical	28514442
RL7_HUMAN	RPL7	physical	28514442
ANR28_HUMAN	ANKRD28	physical	28514442
CTBP2_HUMAN	CTBP2	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-208 AND LYS-228, AND MASSSPECTROMETRY.
PubMed: 19608861