RT18B_HUMAN - dbPTM
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 Description
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 Orthologous
Protein Cluster
4Phosphorylation----MAASVLNTVLR
----CHHHHHHHHHH
20.0029255136
8PhosphorylationMAASVLNTVLRRLPM
CHHHHHHHHHHHCHH
19.4329255136
17PhosphorylationLRRLPMLSLFRGSHR
HHHCHHHHHHCCCCE
21.1429978859
22PhosphorylationMLSLFRGSHRVQVPL
HHHHHCCCCEECCCH
12.12-
38PhosphorylationTLCTKAPSEEDSLSS
HHCCCCCCCCCCCCC
59.4830266825
42PhosphorylationKAPSEEDSLSSVPIS
CCCCCCCCCCCCCCC
33.1730266825
44PhosphorylationPSEEDSLSSVPISPY
CCCCCCCCCCCCCCC
32.9930266825
45PhosphorylationSEEDSLSSVPISPYK
CCCCCCCCCCCCCCC
36.8930266825
49PhosphorylationSLSSVPISPYKDEPW
CCCCCCCCCCCCCCC
18.9930266825
51PhosphorylationSSVPISPYKDEPWKY
CCCCCCCCCCCCCCC
25.0430266825
52UbiquitinationSVPISPYKDEPWKYL
CCCCCCCCCCCCCCC
60.03-
58PhosphorylationYKDEPWKYLESEEYQ
CCCCCCCCCCCHHHH
16.3127174698
61PhosphorylationEPWKYLESEEYQERY
CCCCCCCCHHHHHHH
32.8827174698
64PhosphorylationKYLESEEYQERYGSR
CCCCCHHHHHHHCCC
16.1827174698
68PhosphorylationSEEYQERYGSRPVWA
CHHHHHHHCCCCCHH
20.7827174698
70PhosphorylationEYQERYGSRPVWADY
HHHHHHCCCCCHHHH
25.2027174698
99UbiquitinationKTCIRRNKVVGNPCP
HHHHHHCCCCCCCCC
36.16-
112UbiquitinationCPICRDHKLHVDFRN
CCCCCCCCCCEECCC
44.57-
112AcetylationCPICRDHKLHVDFRN
CCCCCCCCCCEECCC
44.5725953088
1562-HydroxyisobutyrylationRLTQAIQKARDHGLL
HHHHHHHHHHHCCCE
39.00-
156AcetylationRLTQAIQKARDHGLL
HHHHHHHHHHHCCCE
39.0025953088
156SuccinylationRLTQAIQKARDHGLL
HHHHHHHHHHHCCCE
39.0027452117
165PhosphorylationRDHGLLIYHIPQVEP
HHCCCEEEECCCCCC
8.1527642862
200PhosphorylationLVSGDPWYPWYNWKQ
CCCCCCCCCCCCCCC
6.8427642862
203PhosphorylationGDPWYPWYNWKQPPE
CCCCCCCCCCCCCCH
13.4727642862
220PhosphorylationLSRLRRLYQGHLQEE
HHHHHHHHHHHCCCC
15.6127642862
228PhosphorylationQGHLQEESGPPPESM
HHHCCCCCCCCCCCC
56.7128348404
234PhosphorylationESGPPPESMPKMPPR
CCCCCCCCCCCCCCC
46.2728348404
242PhosphorylationMPKMPPRTPAEASST
CCCCCCCCCCCCCCC
32.4030624053
247PhosphorylationPRTPAEASSTGQTGP
CCCCCCCCCCCCCCC
21.6726471730
248PhosphorylationRTPAEASSTGQTGPQ
CCCCCCCCCCCCCCC
43.5428857561
249PhosphorylationTPAEASSTGQTGPQS
CCCCCCCCCCCCCCC
30.7128857561
252PhosphorylationEASSTGQTGPQSAL-
CCCCCCCCCCCCCC-
52.7726471730
256PhosphorylationTGQTGPQSAL-----
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
49SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RT18B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT22_HUMANMRPS22physical
22939629
RT25_HUMANMRPS25physical
22939629
RT26_HUMANMRPS26physical
22939629
RT35_HUMANMRPS35physical
22939629
RT28_HUMANMRPS28physical
22939629
SYK_HUMANKARSphysical
22939629
SYQ_HUMANQARSphysical
22939629
UBR5_HUMANUBR5physical
22939629
EBNA4_EBVB9EBNA3Bphysical
18391203
RB_HUMANRB1physical
18391203
RT06_HUMANMRPS6physical
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 RT18B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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