RL26B_YEAST - dbPTM
RL26B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL26B_YEAST
UniProt AC P53221
Protein Name 60S ribosomal protein L26-B {ECO:0000303|PubMed:9559554}
Gene Name RPL26B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 127
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 MAKQSLDVSSDRRKARKAYFTAPSSERRVLLSAPLSKELRAQYGIKALPIRRDDEVLVVRGSKKGQEGKISSVYRLKFAVQVDKVTKEKVNGASVPINLHPSKLVITKLHLDKDRKALIQRKGGKLE
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
5Phosphorylation---MAKQSLDVSSDR
---CCCCCCCCCCHH		26.3225704821
9PhosphorylationAKQSLDVSSDRRKAR
CCCCCCCCCHHHHHH		26.6230377154
10PhosphorylationKQSLDVSSDRRKARK
CCCCCCCCHHHHHHH		34.6827214570
14UbiquitinationDVSSDRRKARKAYFT
CCCCHHHHHHHHHEE		54.1322817900
17AcetylationSDRRKARKAYFTAPS
CHHHHHHHHHEECCC		52.91-
17UbiquitinationSDRRKARKAYFTAPS
CHHHHHHHHHEECCC		52.9122817900
21PhosphorylationKARKAYFTAPSSERR
HHHHHHEECCCHHCE		25.6122369663
24PhosphorylationKAYFTAPSSERRVLL
HHHEECCCHHCEEEE		42.2220377248
25PhosphorylationAYFTAPSSERRVLLS
HHEECCCHHCEEEEE		33.7820377248
32PhosphorylationSERRVLLSAPLSKEL
HHCEEEEECCCCHHH		24.5522369663
36PhosphorylationVLLSAPLSKELRAQY
EEEECCCCHHHHHHH		24.0322369663
37UbiquitinationLLSAPLSKELRAQYG
EEECCCCHHHHHHHC		69.3323749301
46UbiquitinationLRAQYGIKALPIRRD
HHHHHCCCEEECCCC		39.2424961812
62PhosphorylationEVLVVRGSKKGQEGK
EEEEEECCCCCCCCC		22.1922369663
63UbiquitinationVLVVRGSKKGQEGKI
EEEEECCCCCCCCCC		64.8422817900
64UbiquitinationLVVRGSKKGQEGKIS
EEEECCCCCCCCCCC		68.4722817900
69UbiquitinationSKKGQEGKISSVYRL
CCCCCCCCCCEEEEE		38.3723749301
71PhosphorylationKGQEGKISSVYRLKF
CCCCCCCCEEEEEEE		19.7621440633
72PhosphorylationGQEGKISSVYRLKFA
CCCCCCCEEEEEEEE		27.0020377248
84UbiquitinationKFAVQVDKVTKEKVN
EEEEEEEECCHHHCC		53.6123749301
86PhosphorylationAVQVDKVTKEKVNGA
EEEEEECCHHHCCCE		38.9521440633
87UbiquitinationVQVDKVTKEKVNGAS
EEEEECCHHHCCCEE		59.5322817900
89UbiquitinationVDKVTKEKVNGASVP
EEECCHHHCCCEECC		42.4223749301
94PhosphorylationKEKVNGASVPINLHP
HHHCCCEECCCEECH		29.8022369663
102PhosphorylationVPINLHPSKLVITKL
CCCEECHHHEEEEEE		28.0721440633
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 RL26B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL26B_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 RL26B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERV46_YEASTERV46genetic
20093466
BMT2_YEASTBMT2genetic
20093466
HSP30_YEASTHSP30genetic
20093466
RIM1_YEASTRIM1genetic
20093466
IES1_YEASTIES1genetic
20093466
RTF1_YEASTRTF1genetic
20093466
VAM7_YEASTVAM7genetic
20093466
YG51_YEASTYGR237Cgenetic
20093466
PACC_YEASTRIM101genetic
20093466
SSF1_YEASTSSF1genetic
20093466
COPE_YEASTSEC28genetic
20093466
FIS1_YEASTFIS1genetic
20093466
SNX4_YEASTSNX4genetic
20093466
ELM1_YEASTELM1genetic
20093466
COX12_YEASTCOX12genetic
20093466
SIC1_YEASTSIC1genetic
20093466
RL26A_YEASTRPL26Agenetic
20093466
ATP10_YEASTATP10genetic
20093466
RIM13_YEASTRIM13genetic
20093466
COX7_YEASTCOX7genetic
20093466
SWS2_YEASTSWS2genetic
20093466
NOP12_YEASTNOP12genetic
20093466
SIN3_YEASTSIN3genetic
20093466
CY1_YEASTCYT1genetic
20093466
MCP1_YEASTMCP1genetic
20093466
NEW1_YEASTNEW1genetic
20093466
SYH1_YEASTSYH1genetic
20093466
QCR2_YEASTQCR2genetic
20093466
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL26B_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND MASSSPECTROMETRY.

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