RT18B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RT18B_HUMAN
• UniProt AC: Q9Y676
• Protein Name: 28S ribosomal protein S18b, mitochondrial
• Gene Name: MRPS18B
• Organism: Homo sapiens (Human).
• Sequence Length: 258
• Subcellular Localization: Mitochondrion .
• Protein Sequence: MAASVLNTVLRRLPMLSLFRGSHRVQVPLQTLCTKAPSEEDSLSSVPISPYKDEPWKYLESEEYQERYGSRPVWADYRRNHKGGVPPQRTRKTCIRRNKVVGNPCPICRDHKLHVDFRNVKLLEQFVCAHTGIIFYAPYTGVCVKQHKRLTQAIQKARDHGLLIYHIPQVEPRDLDFSTSHGAVSATPPAPTLVSGDPWYPWYNWKQPPERELSRLRRLYQGHLQEESGPPPESMPKMPPRTPAEASSTGQTGPQSAL

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
4	Phosphorylation	----MAASVLNTVLR ----CHHHHHHHHHH	20.00	29255136
8	Phosphorylation	MAASVLNTVLRRLPM CHHHHHHHHHHHCHH	19.43	29255136
17	Phosphorylation	LRRLPMLSLFRGSHR HHHCHHHHHHCCCCE	21.14	29978859
22	Phosphorylation	MLSLFRGSHRVQVPL HHHHHCCCCEECCCH	12.12	-
38	Phosphorylation	TLCTKAPSEEDSLSS HHCCCCCCCCCCCCC	59.48	30266825
42	Phosphorylation	KAPSEEDSLSSVPIS CCCCCCCCCCCCCCC	33.17	30266825
44	Phosphorylation	PSEEDSLSSVPISPY CCCCCCCCCCCCCCC	32.99	30266825
45	Phosphorylation	SEEDSLSSVPISPYK CCCCCCCCCCCCCCC	36.89	30266825
49	Phosphorylation	SLSSVPISPYKDEPW CCCCCCCCCCCCCCC	18.99	30266825
51	Phosphorylation	SSVPISPYKDEPWKY CCCCCCCCCCCCCCC	25.04	30266825
52	Ubiquitination	SVPISPYKDEPWKYL CCCCCCCCCCCCCCC	60.03	-
58	Phosphorylation	YKDEPWKYLESEEYQ CCCCCCCCCCCHHHH	16.31	27174698
61	Phosphorylation	EPWKYLESEEYQERY CCCCCCCCHHHHHHH	32.88	27174698
64	Phosphorylation	KYLESEEYQERYGSR CCCCCHHHHHHHCCC	16.18	27174698
68	Phosphorylation	SEEYQERYGSRPVWA CHHHHHHHCCCCCHH	20.78	27174698
70	Phosphorylation	EYQERYGSRPVWADY HHHHHHCCCCCHHHH	25.20	27174698
99	Ubiquitination	KTCIRRNKVVGNPCP HHHHHHCCCCCCCCC	36.16	-
112	Ubiquitination	CPICRDHKLHVDFRN CCCCCCCCCCEECCC	44.57	-
112	Acetylation	CPICRDHKLHVDFRN CCCCCCCCCCEECCC	44.57	25953088
156	2-Hydroxyisobutyrylation	RLTQAIQKARDHGLL HHHHHHHHHHHCCCE	39.00	-
156	Acetylation	RLTQAIQKARDHGLL HHHHHHHHHHHCCCE	39.00	25953088
156	Succinylation	RLTQAIQKARDHGLL HHHHHHHHHHHCCCE	39.00	27452117
165	Phosphorylation	RDHGLLIYHIPQVEP HHCCCEEEECCCCCC	8.15	27642862
200	Phosphorylation	LVSGDPWYPWYNWKQ CCCCCCCCCCCCCCC	6.84	27642862
203	Phosphorylation	GDPWYPWYNWKQPPE CCCCCCCCCCCCCCH	13.47	27642862
220	Phosphorylation	LSRLRRLYQGHLQEE HHHHHHHHHHHCCCC	15.61	27642862
228	Phosphorylation	QGHLQEESGPPPESM HHHCCCCCCCCCCCC	56.71	28348404
234	Phosphorylation	ESGPPPESMPKMPPR CCCCCCCCCCCCCCC	46.27	28348404
242	Phosphorylation	MPKMPPRTPAEASST CCCCCCCCCCCCCCC	32.40	30624053
247	Phosphorylation	PRTPAEASSTGQTGP CCCCCCCCCCCCCCC	21.67	26471730
248	Phosphorylation	RTPAEASSTGQTGPQ CCCCCCCCCCCCCCC	43.54	28857561
249	Phosphorylation	TPAEASSTGQTGPQS CCCCCCCCCCCCCCC	30.71	28857561
252	Phosphorylation	EASSTGQTGPQSAL- CCCCCCCCCCCCCC-	52.77	26471730
256	Phosphorylation	TGQTGPQSAL----- CCCCCCCCCC-----	34.37	-

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
49	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RT18B_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 RT18B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RT22_HUMAN	MRPS22	physical	22939629
RT25_HUMAN	MRPS25	physical	22939629
RT26_HUMAN	MRPS26	physical	22939629
RT35_HUMAN	MRPS35	physical	22939629
RT28_HUMAN	MRPS28	physical	22939629
SYK_HUMAN	KARS	physical	22939629
SYQ_HUMAN	QARS	physical	22939629
UBR5_HUMAN	UBR5	physical	22939629
EBNA4_EBVB9	EBNA3B	physical	18391203
RB_HUMAN	RB1	physical	18391203
RT06_HUMAN	MRPS6	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-49, AND MASSSPECTROMETRY.
PubMed: 18691976