RL14B_YEAST - dbPTM
RL14B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL14B_YEAST
UniProt AC P38754
Protein Name 60S ribosomal protein L14-B {ECO:0000303|PubMed:9559554}
Gene Name RPL14B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 138
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 MSTDSIVKASNWRLVEVGRVVLIKKGQSAGKLAAIVEIIDQKKVLIDGPKAGVPRQAINLGQVVLTPLTFALPRGARTATVSKKWAAAGVCEKWAASSWAKKIAQRERRAALTDFERFQVMVLRKQKRYTVKKALAKA
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------MSTDSIVKA
------CCHHHHHHH		40.70-
2Phosphorylation------MSTDSIVKA
------CCHHHHHHH		40.7019795423
3Phosphorylation-----MSTDSIVKAS
-----CCHHHHHHHC		32.2519795423
5Phosphorylation---MSTDSIVKASNW
---CCHHHHHHHCCE		29.3919795423
8UbiquitinationMSTDSIVKASNWRLV
CCHHHHHHHCCEEEE		44.4124961812
10PhosphorylationTDSIVKASNWRLVEV
HHHHHHHCCEEEEEE		31.0717287358
31UbiquitinationKKGQSAGKLAAIVEI
ECCCCCCHHHHHEEE		34.3723749301
42UbiquitinationIVEIIDQKKVLIDGP
HEEEECCCCEEECCC		40.8922817900
43UbiquitinationVEIIDQKKVLIDGPK
EEEECCCCEEECCCC		36.3223749301
50UbiquitinationKVLIDGPKAGVPRQA
CEEECCCCCCCCHHH		64.4023749301
78PhosphorylationALPRGARTATVSKKW
ECCCCCCEEEECHHH		26.5821440633
82PhosphorylationGARTATVSKKWAAAG
CCCEEEECHHHHHHC		24.9421440633
83UbiquitinationARTATVSKKWAAAGV
CCEEEECHHHHHHCH		48.2622817900
84UbiquitinationRTATVSKKWAAAGVC
CEEEECHHHHHHCHH		34.2622817900
93UbiquitinationAAAGVCEKWAASSWA
HHHCHHHHHHHHHHH		36.6923749301
93AcetylationAAAGVCEKWAASSWA
HHHCHHHHHHHHHHH		36.6924489116
97PhosphorylationVCEKWAASSWAKKIA
HHHHHHHHHHHHHHH		20.7522369663
98PhosphorylationCEKWAASSWAKKIAQ
HHHHHHHHHHHHHHH		26.7321440633
101UbiquitinationWAASSWAKKIAQRER
HHHHHHHHHHHHHHH		38.1523749301
102UbiquitinationAASSWAKKIAQRERR
HHHHHHHHHHHHHHH		35.2122817900
127UbiquitinationVMVLRKQKRYTVKKA
HHHHHHCCCHHHHHH		50.8622817900
132UbiquitinationKQKRYTVKKALAKA-
HCCCHHHHHHHHCC-		25.2422817900
133UbiquitinationQKRYTVKKALAKA--
CCCHHHHHHHHCC--		44.2722817900
137UbiquitinationTVKKALAKA------
HHHHHHHCC------		56.3222817900
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 RL14B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL14B_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 RL14B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAR3_YEASTFAR3physical
16429126
FAR8_YEASTFAR8physical
16429126
RAD4_YEASTRAD4genetic
20093466
CBT1_YEASTCBT1genetic
20093466
HAP4_YEASTHAP4genetic
20093466
MMM1_YEASTMMM1genetic
20093466
RL22A_YEASTRPL22Agenetic
20093466
COA4_YEASTCOA4genetic
20093466
SWS2_YEASTSWS2genetic
20093466
INO4_YEASTINO4genetic
20093466
WHI2_YEASTWHI2genetic
20093466
CY1_YEASTCYT1genetic
20093466
QCR2_YEASTQCR2genetic
20093466
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
RPN6_YEASTRPN6genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PSA7_YEASTPRE10genetic
27708008
PSB5_YEASTPRE2genetic
27708008
RIM1_YEASTRIM1genetic
27708008
ELO2_YEASTELO2genetic
27708008
THRC_YEASTTHR4genetic
27708008
PAT1_YEASTPAT1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
ODO2_YEASTKGD2genetic
27708008
NUM1_YEASTNUM1genetic
27708008
BEM2_YEASTBEM2genetic
27708008
RAD4_YEASTRAD4genetic
27708008
IES1_YEASTIES1genetic
27708008
QCR9_YEASTQCR9genetic
27708008
VPS53_YEASTVPS53genetic
27708008
LPLA_YEASTAIM22genetic
27708008
LSM1_YEASTLSM1genetic
27708008
MMM1_YEASTMMM1genetic
27708008
SDHB_YEASTSDH2genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
COA4_YEASTCOA4genetic
27708008
ATP10_YEASTATP10genetic
27708008
PHO80_YEASTPHO80genetic
27708008
ASE1_YEASTASE1genetic
27708008
CY1_YEASTCYT1genetic
27708008
MSS18_YEASTMSS18genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL14B_YEAST

loading...

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-10, AND MASSSPECTROMETRY.

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