RS18B_YEAST - dbPTM
RS18B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS18B_YEAST
UniProt AC P0CX56
Protein Name 40S ribosomal protein S18-B {ECO:0000303|PubMed:9559554}
Gene Name RPS18B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 146
Subcellular Localization Cytoplasm .
Protein Description Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel..
Protein Sequence MSLVVQEQGSFQHILRLLNTNVDGNIKIVYALTTIKGVGRRYSNLVCKKADVDLHKRAGELTQEELERIVQIMQNPTHYKIPAWFLNRQNDITDGKDYHTLANNVESKLRDDLERLKKIRAHRGIRHFWGLRVRGQHTKTTGRRRA
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
2Acetylation------MSLVVQEQG
------CCCEEECCC		29.8510601260
10PhosphorylationLVVQEQGSFQHILRL
CEEECCCCHHHHHHH		22.7930377154
20PhosphorylationHILRLLNTNVDGNIK
HHHHHHCCCCCCCEE		36.2728889911
27UbiquitinationTNVDGNIKIVYALTT
CCCCCCEEEEEEEEE		30.0717644757
30PhosphorylationDGNIKIVYALTTIKG
CCCEEEEEEEEECCC		10.2022369663
33PhosphorylationIKIVYALTTIKGVGR
EEEEEEEEECCCCCH		20.5023749301
34PhosphorylationKIVYALTTIKGVGRR
EEEEEEEECCCCCHH		22.8821440633
36UbiquitinationVYALTTIKGVGRRYS
EEEEEECCCCCHHHC		45.5123749301
42PhosphorylationIKGVGRRYSNLVCKK
CCCCCHHHCCCEEHH		10.6829136822
43PhosphorylationKGVGRRYSNLVCKKA
CCCCHHHCCCEEHHC		23.1329136822
48MethylationRYSNLVCKKADVDLH
HHCCCEEHHCCCCHH		43.4422522802
48UbiquitinationRYSNLVCKKADVDLH
HHCCCEEHHCCCCHH		43.4423749301
49UbiquitinationYSNLVCKKADVDLHK
HCCCEEHHCCCCHHH		44.7023749301
56UbiquitinationKADVDLHKRAGELTQ
HCCCCHHHHCCCCCH		51.7622817900
77PhosphorylationVQIMQNPTHYKIPAW
HHHHHCCCCCCCCHH		45.4428889911
80UbiquitinationMQNPTHYKIPAWFLN
HHCCCCCCCCHHHHC		34.3123749301
93PhosphorylationLNRQNDITDGKDYHT
HCCCCCCCCCCCHHH		41.3821440633
96UbiquitinationQNDITDGKDYHTLAN
CCCCCCCCCHHHHHH		58.9023749301
100PhosphorylationTDGKDYHTLANNVES
CCCCCHHHHHHHHHH		22.7221440633
107PhosphorylationTLANNVESKLRDDLE
HHHHHHHHHHHHHHH		32.4821440633
108UbiquitinationLANNVESKLRDDLER
HHHHHHHHHHHHHHH		33.7524961812
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 RS18B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS18B_YEAST !!
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 RS18B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP71_YEASTSSA1physical
19536198
ACT_YEASTACT1genetic
27708008
ARP4_YEASTARP4genetic
27708008
TIM14_YEASTPAM18genetic
27708008
SMC4_YEASTSMC4genetic
27708008
ARP7_YEASTARP7genetic
27708008
IWS1_YEASTSPN1genetic
27708008
SWC5_YEASTSWC5genetic
27708008
YCQ6_YEASTYCR016Wgenetic
27708008
GET3_YEASTGET3genetic
27708008
SSBP1_YEASTSBP1genetic
27708008
BFA1_YEASTBFA1genetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
PUR91_YEASTADE16genetic
27708008
CSI1_YEASTCSI1genetic
27708008
MKT1_YEASTMKT1genetic
27708008
VHS3_YEASTVHS3genetic
27708008
IES4_YEASTIES4genetic
27708008
DGK1_YEASTDGK1genetic
27708008
SRO7_YEASTSRO7genetic
27708008
CDC24_YEASTCDC24genetic
27708008
PSB6_YEASTPRE7genetic
27708008
CDC27_YEASTCDC27genetic
27708008
APC11_YEASTAPC11genetic
27708008
TECR_YEASTTSC13genetic
27708008
PRP11_YEASTPRP11genetic
27708008
LUC7_YEASTLUC7genetic
27708008
RPN6_YEASTRPN6genetic
27708008
CDC53_YEASTCDC53genetic
27708008
PDC2_YEASTPDC2genetic
27708008
ERF3_YEASTSUP35genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SNU56_YEASTSNU56genetic
27708008
RRP45_YEASTRRP45genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RSP5_YEASTRSP5genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PSA1_YEASTSCL1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
SP105_YEASTSPC105genetic
27708008
PRP38_YEASTPRP38genetic
27708008
YIP1_YEASTYIP1genetic
27708008
RPN1_YEASTRPN1genetic
27708008
CDC23_YEASTCDC23genetic
27708008
PRI1_YEASTPRI1genetic
27708008
MTR4_YEASTMTR4genetic
27708008
ESS1_YEASTESS1genetic
27708008
MIF2_YEASTMIF2genetic
27708008
RRN3_YEASTRRN3genetic
27708008
PRS7_YEASTRPT1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
CDC91_YEASTGAB1genetic
27708008
MCM1_YEASTMCM1genetic
27708008
UTP15_YEASTUTP15genetic
27708008
SPC24_YEASTSPC24genetic
27708008
SGT1_YEASTSGT1genetic
27708008
SMP3_YEASTSMP3genetic
27708008
PRS10_YEASTRPT4genetic
27708008
THIL_YEASTERG10genetic
27708008
SYLC_YEASTCDC60genetic
27708008
NSL1_YEASTNSL1genetic
27708008
SEC23_YEASTSEC23genetic
27708008
ECM15_YEASTECM15genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
SNF5_YEASTSNF5genetic
27708008
ELO2_YEASTELO2genetic
27708008
BLM10_YEASTBLM10genetic
27708008
GCN20_YEASTGCN20genetic
27708008
UBP6_YEASTUBP6genetic
27708008
PALF_YEASTRIM8genetic
27708008
GUP1_YEASTGUP1genetic
27708008
AAKG_YEASTSNF4genetic
27708008
SMI1_YEASTSMI1genetic
27708008
YIQ5_YEASTYIL165Cgenetic
27708008
3HAO_YEASTBNA1genetic
27708008
CTK1_YEASTCTK1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
MSH2_YEASTMSH2genetic
27708008
YO131_YEASTYOL131Wgenetic
27708008
WHI2_YEASTWHI2genetic
27708008
MNE1_YEASTMNE1genetic
27708008
YP272_YEASTPBI1genetic
27708008
SUE1_YEASTSUE1genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS18B_YEAST

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The action of N-terminal acetyltransferases on yeast ribosomalproteins.";
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
J. Biol. Chem. 274:37035-37040(1999).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory