RL24B_YEAST - dbPTM
RL24B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL24B_YEAST
UniProt AC P24000
Protein Name 60S ribosomal protein L24-B {ECO:0000303|PubMed:9559554}
Gene Name RPL24B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 155
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 MKVEVDSFSGAKIYPGRGTLFVRGDSKIFRFQNSKSASLFKQRKNPRRIAWTVLFRKHHKKGITEEVAKKRSRKTVKAQRPITGASLDLIKERRSLKPEVRKANREEKLKANKEKKRAEKAARKAEKAKSAGVQGSKVSKQQAKGAFQKVAATSR
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
2Ubiquitination------MKVEVDSFS
------CCEEEECCC		47.2917644757
7Phosphorylation-MKVEVDSFSGAKIY
-CCEEEECCCCCEEE		26.8722369663
9PhosphorylationKVEVDSFSGAKIYPG
CEEEECCCCCEEECC		41.6222369663
12SuccinylationVDSFSGAKIYPGRGT
EECCCCCEEECCCCE		46.4223954790
12AcetylationVDSFSGAKIYPGRGT
EECCCCCEEECCCCE		46.4224489116
12UbiquitinationVDSFSGAKIYPGRGT
EECCCCCEEECCCCE		46.4223749301
19PhosphorylationKIYPGRGTLFVRGDS
EEECCCCEEEEECCC		18.7021440633
26PhosphorylationTLFVRGDSKIFRFQN
EEEEECCCEEEEEEC		30.4022369663
27UbiquitinationLFVRGDSKIFRFQNS
EEEECCCEEEEEECC		51.0823749301
34PhosphorylationKIFRFQNSKSASLFK
EEEEEECCCCHHHHH		19.7321551504
35UbiquitinationIFRFQNSKSASLFKQ
EEEEECCCCHHHHHH		58.5523749301
38PhosphorylationFQNSKSASLFKQRKN
EECCCCHHHHHHCCC		41.2421440633
41UbiquitinationSKSASLFKQRKNPRR
CCCHHHHHHCCCHHH		55.2623749301
44UbiquitinationASLFKQRKNPRRIAW
HHHHHHCCCHHHHHH		69.6622817900
52PhosphorylationNPRRIAWTVLFRKHH
CHHHHHHHHHHHHHH		9.7922369663
57UbiquitinationAWTVLFRKHHKKGIT
HHHHHHHHHHHCCCC		42.6022817900
60UbiquitinationVLFRKHHKKGITEEV
HHHHHHHHCCCCHHH		53.0322817900
61UbiquitinationLFRKHHKKGITEEVA
HHHHHHHCCCCHHHH		51.7123749301
64PhosphorylationKHHKKGITEEVAKKR
HHHHCCCCHHHHHHH		34.4623749301
69UbiquitinationGITEEVAKKRSRKTV
CCCHHHHHHHCCCCC		54.6217644757
70UbiquitinationITEEVAKKRSRKTVK
CCHHHHHHHCCCCCH		45.9617644757
74UbiquitinationVAKKRSRKTVKAQRP
HHHHHCCCCCHHCCC		59.9422817900
77UbiquitinationKRSRKTVKAQRPITG
HHCCCCCHHCCCCCC		43.9923749301
83PhosphorylationVKAQRPITGASLDLI
CHHCCCCCCHHHHHH		29.4022369663
86PhosphorylationQRPITGASLDLIKER
CCCCCCHHHHHHHHH		24.6222369663
91UbiquitinationGASLDLIKERRSLKP
CHHHHHHHHHHCCCH		53.0923749301
95PhosphorylationDLIKERRSLKPEVRK
HHHHHHHCCCHHHHH		47.1419823750
97UbiquitinationIKERRSLKPEVRKAN
HHHHHCCCHHHHHHH		40.1423749301
102UbiquitinationSLKPEVRKANREEKL
CCCHHHHHHHHHHHH		56.0117644757
120UbiquitinationKEKKRAEKAARKAEK
HHHHHHHHHHHHHHH		46.4922817900
124UbiquitinationRAEKAARKAEKAKSA
HHHHHHHHHHHHHHC		57.0522817900
127UbiquitinationKAARKAEKAKSAGVQ
HHHHHHHHHHHCCCC		67.0122817900
129UbiquitinationARKAEKAKSAGVQGS
HHHHHHHHHCCCCCC		52.4822817900
130PhosphorylationRKAEKAKSAGVQGSK
HHHHHHHHCCCCCCC		34.8128889911
136PhosphorylationKSAGVQGSKVSKQQA
HHCCCCCCCCCHHHH		16.8823749301
137UbiquitinationSAGVQGSKVSKQQAK
HCCCCCCCCCHHHHH		58.3023749301
139PhosphorylationGVQGSKVSKQQAKGA
CCCCCCCCHHHHHHH		28.6020377248
140UbiquitinationVQGSKVSKQQAKGAF
CCCCCCCHHHHHHHH		49.7922817900
140AcetylationVQGSKVSKQQAKGAF
CCCCCCCHHHHHHHH		49.7925381059
144UbiquitinationKVSKQQAKGAFQKVA
CCCHHHHHHHHHHHH		46.5723749301
149UbiquitinationQAKGAFQKVAATSR-
HHHHHHHHHHHCCC-		27.6423749301
153PhosphorylationAFQKVAATSR-----
HHHHHHHCCC-----		18.4624909858
154PhosphorylationFQKVAATSR------
HHHHHHCCC------		31.1324909858
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 RL24B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL24B_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 RL24B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
REI1_YEASTREI1physical
16651379
RL5_YEASTRPL5physical
19797079
YAJ9_YEASTYAR029Wgenetic
27708008
CSG2_YEASTCSG2genetic
27708008
BMT2_YEASTBMT2genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
SGF29_YEASTSGF29genetic
27708008
RPN4_YEASTRPN4genetic
27708008
RL24A_YEASTRPL24Agenetic
27708008
AAKG_YEASTSNF4genetic
27708008
DAL81_YEASTDAL81genetic
27708008
BNA3_YEASTBNA3genetic
27708008
YKE44_YEASTYKL044Wgenetic
27708008
TSR2_YEASTTSR2genetic
27708008
AP1_YEASTYAP1genetic
27708008
COG8_YEASTCOG8genetic
27708008
BUB2_YEASTBUB2genetic
27708008
INP2_YEASTINP2genetic
27708008
GYL1_YEASTGYL1genetic
27708008
YO014_YEASTYOL014Wgenetic
27708008
VPS5_YEASTVPS5genetic
27708008
TBP6_YEASTYTA6genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL24B_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-7 AND SER-9, AND MASSSPECTROMETRY.
"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-7, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.

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