RL27B_YEAST - dbPTM
RL27B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL27B_YEAST
UniProt AC P0C2H7
Protein Name 60S ribosomal protein L27-B {ECO:0000303|PubMed:9559554}
Gene Name RPL27B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 136
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 MAKFLKAGKVAVVVRGRYAGKKVVIVKPHDEGSKSHPFGHALVAGIERYPSKVTKKHGAKKVAKRTKIKPFIKVVNYNHLLPTRYTLDVEAFKSVVSTETFEQPSQREEAKKVVKKAFEERHQAGKNQWFFSKLRF
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
6Ubiquitination--MAKFLKAGKVAVV
--CCHHHHCCCEEEE		59.2222817900
9UbiquitinationAKFLKAGKVAVVVRG
CHHHHCCCEEEEEEC		31.7023749301
21UbiquitinationVRGRYAGKKVVIVKP
EECEECCCEEEEEEC		33.9322817900
22UbiquitinationRGRYAGKKVVIVKPH
ECEECCCEEEEEECC		40.5923749301
27UbiquitinationGKKVVIVKPHDEGSK
CCEEEEEECCCCCCC		26.0523749301
33PhosphorylationVKPHDEGSKSHPFGH
EECCCCCCCCCCCCH		29.0121440633
34UbiquitinationKPHDEGSKSHPFGHA
ECCCCCCCCCCCCHH		64.7423749301
35PhosphorylationPHDEGSKSHPFGHAL
CCCCCCCCCCCCHHH		37.7822369663
64UbiquitinationHGAKKVAKRTKIKPF
HCCHHHHHHHCCCCE		64.6822817900
67UbiquitinationKKVAKRTKIKPFIKV
HHHHHHHCCCCEEEE		53.4123749301
69UbiquitinationVAKRTKIKPFIKVVN
HHHHHCCCCEEEEEE		35.1222817900
73UbiquitinationTKIKPFIKVVNYNHL
HCCCCEEEEEECCCC		40.2722817900
77PhosphorylationPFIKVVNYNHLLPTR
CEEEEEECCCCCCCE		7.7321082442
83PhosphorylationNYNHLLPTRYTLDVE
ECCCCCCCEEEEEHH		35.9621440633
85PhosphorylationNHLLPTRYTLDVEAF
CCCCCCEEEEEHHHH		17.7128889911
93UbiquitinationTLDVEAFKSVVSTET
EEEHHHHHHHHCCCC		49.7623749301
94PhosphorylationLDVEAFKSVVSTETF
EEHHHHHHHHCCCCC		22.6922369663
97PhosphorylationEAFKSVVSTETFEQP
HHHHHHHCCCCCCCH		20.5422369663
98PhosphorylationAFKSVVSTETFEQPS
HHHHHHCCCCCCCHH		27.6922369663
100PhosphorylationKSVVSTETFEQPSQR
HHHHCCCCCCCHHHH		32.3422369663
105PhosphorylationTETFEQPSQREEAKK
CCCCCCHHHHHHHHH		41.3822369663
111UbiquitinationPSQREEAKKVVKKAF
HHHHHHHHHHHHHHH		49.7522817900
112UbiquitinationSQREEAKKVVKKAFE
HHHHHHHHHHHHHHH		60.3522817900
115UbiquitinationEEAKKVVKKAFEERH
HHHHHHHHHHHHHHH		41.1822817900
116UbiquitinationEAKKVVKKAFEERHQ
HHHHHHHHHHHHHHH		46.8522817900
126UbiquitinationEERHQAGKNQWFFSK
HHHHHCCCCCCHHHC		49.3223749301
132PhosphorylationGKNQWFFSKLRF---
CCCCCHHHCCCC---		22.7021440633
133UbiquitinationKNQWFFSKLRF----
CCCCHHHCCCC----		38.2323749301
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 RL27B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL27B_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 RL27B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL27A_YEASTRPL27Agenetic
22377630
CDC24_YEASTCDC24genetic
27708008
CND2_YEASTBRN1genetic
27708008
RPAB1_YEASTRPB5genetic
27708008
UAP1_YEASTQRI1genetic
27708008
NHP2_YEASTNHP2genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
RSP5_YEASTRSP5genetic
27708008
NU145_YEASTNUP145genetic
27708008
SWC4_YEASTSWC4genetic
27708008
TEL2_YEASTTEL2genetic
27708008
DAM1_YEASTDAM1genetic
27708008
MED6_YEASTMED6genetic
27708008
MOB1_YEASTMOB1genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
CWC16_YEASTYJU2genetic
27708008
NTR2_YEASTNTR2genetic
27708008
BOS1_YEASTBOS1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
GPI12_YEASTGPI12genetic
27708008
CAP_YEASTSRV2genetic
27708008
DED1_YEASTDED1genetic
27708008
ULP1_YEASTULP1genetic
27708008
TF2B_YEASTSUA7genetic
27708008
GPR1_YEASTGPR1genetic
27708008
CDS1_YEASTCDS1genetic
27708008
ORC2_YEASTORC2genetic
27708008
TRS20_YEASTTRS20genetic
27708008
FBRL_YEASTNOP1genetic
27708008
CDC7_YEASTCDC7genetic
27708008
SUB2_YEASTSUB2genetic
27708008
DPOD_YEASTPOL3genetic
27708008
NSE4_YEASTNSE4genetic
27708008
CDC53_YEASTCDC53genetic
27708008
UPPS_YEASTNUS1genetic
27708008
PDC2_YEASTPDC2genetic
27708008
PP12_YEASTGLC7genetic
27708008
CDC4_YEASTCDC4genetic
27708008
PMM_YEASTSEC53genetic
27708008
PSB7_YEASTPRE4genetic
27708008
PRS8_YEASTRPT6genetic
27708008
DUO1_YEASTDUO1genetic
27708008
TAF1_YEASTTAF1genetic
27708008
BIG1_YEASTBIG1genetic
27708008
TIM16_YEASTPAM16genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
CDC16_YEASTCDC16genetic
27708008
ABF1_YEASTABF1genetic
27708008
SEC10_YEASTSEC10genetic
27708008
SC61A_YEASTSEC61genetic
27708008
SPC24_YEASTSPC24genetic
27708008
DCP2_YEASTDCP2genetic
27708008
XRN2_YEASTRAT1genetic
27708008
MED4_YEASTMED4genetic
27708008
DYR_YEASTDFR1genetic
27708008
PRS10_YEASTRPT4genetic
27708008
ATC3_YEASTDRS2genetic
27708008
UBC4_YEASTUBC4genetic
27708008
YPQ3_YEASTRTC2genetic
27708008
MCFS2_YEASTEHT1genetic
27708008
BUD31_YEASTBUD31genetic
27708008
KIN82_YEASTKIN82genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
SAP1_YEASTSAP1genetic
27708008
IES5_YEASTIES5genetic
27708008
ASK10_YEASTASK10genetic
27708008
KEL2_YEASTKEL2genetic
27708008
SHU1_YEASTSHU1genetic
27708008
CWP2_YEASTCWP2genetic
27708008
YL225_YEASTYLR225Cgenetic
27708008
GTR1_YEASTGTR1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
CTU2_YEASTNCS2genetic
27708008
VPS27_YEASTVPS27genetic
27708008
DNLI4_YEASTDNL4genetic
27708008
ROD1_YEASTROD1genetic
27708008
ELP3_YEASTELP3genetic
27708008
VPS4_YEASTVPS4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL27B_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-97 AND SER-105,AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY.

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