RL12B_YEAST - dbPTM
RL12B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL12B_YEAST
UniProt AC P0CX54
Protein Name 60S ribosomal protein L12-B {ECO:0000303|PubMed:9559554}
Gene Name RPL12B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 165
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 MPPKFDPNEVKYLYLRAVGGEVGASAALAPKIGPLGLSPKKVGEDIAKATKEFKGIKVTVQLKIQNRQAAASVVPSASSLVITALKEPPRDRKKDKNVKHSGNIQLDEIIEIARQMRDKSFGRTLASVTKEILGTAQSVGCRVDFKNPHDIIEGINAGEIEIPEN
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
2Methylation------MPPKFDPNE
------CCCCCCHHH		40.5718957409
4Methylation----MPPKFDPNEVK
----CCCCCCHHHCE		57.4317005568
4"N6,N6,N6-trimethyllysine"----MPPKFDPNEVK
----CCCCCCHHHCE		57.43-
11MethylationKFDPNEVKYLYLRAV
CCCHHHCEEEEEEHH		24.2917005568
11"N6,N6,N6-trimethyllysine"KFDPNEVKYLYLRAV
CCCHHHCEEEEEEHH		24.29-
25PhosphorylationVGGEVGASAALAPKI
HCCCCCCCHHHCCCC		14.2422369663
31UbiquitinationASAALAPKIGPLGLS
CCHHHCCCCCCCCCC		55.4723749301
38PhosphorylationKIGPLGLSPKKVGED
CCCCCCCCHHHHCHH		32.6422369663
40UbiquitinationGPLGLSPKKVGEDIA
CCCCCCHHHHCHHHH		57.6323749301
41UbiquitinationPLGLSPKKVGEDIAK
CCCCCHHHHCHHHHH		59.8823749301
48UbiquitinationKVGEDIAKATKEFKG
HHCHHHHHHHHHCCC		57.8523749301
51UbiquitinationEDIAKATKEFKGIKV
HHHHHHHHHCCCCEE		67.0422817900
67MethylationVQLKIQNRQAAASVV
EEEEECCHHHHHHHC		15.9018957409
72PhosphorylationQNRQAAASVVPSASS
CCHHHHHHHCCCHHH		20.9422369663
76PhosphorylationAAASVVPSASSLVIT
HHHHHCCCHHHHHHH		29.2222369663
78PhosphorylationASVVPSASSLVITAL
HHHCCCHHHHHHHHH		28.6622369663
79PhosphorylationSVVPSASSLVITALK
HHCCCHHHHHHHHHC		26.7722369663
83PhosphorylationSASSLVITALKEPPR
CHHHHHHHHHCCCCC		20.6122369663
86UbiquitinationSLVITALKEPPRDRK
HHHHHHHCCCCCCCC		66.7524961812
94UbiquitinationEPPRDRKKDKNVKHS
CCCCCCCCCCCCCCC		74.8722817900
96UbiquitinationPRDRKKDKNVKHSGN
CCCCCCCCCCCCCCC		72.9522817900
99UbiquitinationRKKDKNVKHSGNIQL
CCCCCCCCCCCCCCH		41.2523749301
101PhosphorylationKDKNVKHSGNIQLDE
CCCCCCCCCCCCHHH		28.0225521595
119UbiquitinationIARQMRDKSFGRTLA
HHHHHCCCCHHHHHH		37.0022817900
120PhosphorylationARQMRDKSFGRTLAS
HHHHCCCCHHHHHHH		36.9021440633
124PhosphorylationRDKSFGRTLASVTKE
CCCCHHHHHHHHHHH		27.3621440633
127PhosphorylationSFGRTLASVTKEILG
CHHHHHHHHHHHHHC		33.1721440633
129PhosphorylationGRTLASVTKEILGTA
HHHHHHHHHHHHCCC		22.0621440633
130UbiquitinationRTLASVTKEILGTAQ
HHHHHHHHHHHCCCC		40.3723749301
138PhosphorylationEILGTAQSVGCRVDF
HHHCCCCCCCCCCCC		20.2921440633
146UbiquitinationVGCRVDFKNPHDIIE
CCCCCCCCCHHHHHC		66.1723749301
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 RL12B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
11KMethylation

17005568
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 RL12B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RMT2_YEASTRMT2physical
18719252
PSB3_YEASTPUP3genetic
27708008
PP12_YEASTGLC7genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
SWI6_YEASTSWI6genetic
27708008
IRA2_YEASTIRA2genetic
27708008
CDC24_YEASTCDC24genetic
27708008
CDC15_YEASTCDC15genetic
27708008
KPC1_YEASTPKC1genetic
27708008
CALM_YEASTCMD1genetic
27708008
SLI15_YEASTSLI15genetic
27708008
MPS1_YEASTMPS1genetic
27708008
COPA_YEASTCOP1genetic
27708008
DAD1_YEASTDAD1genetic
27708008
MSS4_YEASTMSS4genetic
27708008
CAK1_YEASTCAK1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
NU145_YEASTNUP145genetic
27708008
CDC20_YEASTCDC20genetic
27708008
SMD1_YEASTSMD1genetic
27708008
DAM1_YEASTDAM1genetic
27708008
CDC23_YEASTCDC23genetic
27708008
CTF8_YEASTCTF8genetic
27708008
MOB1_YEASTMOB1genetic
27708008
NU159_YEASTNUP159genetic
27708008
IMB1_YEASTKAP95genetic
27708008
SEC65_YEASTSEC65genetic
27708008
MCM1_YEASTMCM1genetic
27708008
PDS5_YEASTPDS5genetic
27708008
LST8_YEASTLST8genetic
27708008
CAP_YEASTSRV2genetic
27708008
SGT1_YEASTSGT1genetic
27708008
OST2_YEASTOST2genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
PSA7_YEASTPRE10genetic
27708008
MOT1_YEASTMOT1genetic
27708008
IPL1_YEASTIPL1genetic
27708008
ASA1_YEASTASA1genetic
27708008
SHE1_YEASTSHE1genetic
27708008
NPL4_YEASTNPL4genetic
27708008
DCC1_YEASTDCC1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
PAN2_YEASTPAN2genetic
27708008
MON1_YEASTMON1genetic
27708008
MDM34_YEASTMDM34genetic
27708008
VMA21_YEASTVMA21genetic
27708008
GIC1_YEASTGIC1genetic
27708008
LSM1_YEASTLSM1genetic
27708008
MPCP_YEASTMIR1genetic
27708008
FPS1_YEASTFPS1genetic
27708008
ERG3_YEASTERG3genetic
27708008
FKS1_YEASTFKS1genetic
27708008
PUB1_YEASTPUB1genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
SIA1_YEASTSIA1genetic
27708008
SERC_YEASTSER1genetic
27708008
CTF19_YEASTCTF19genetic
27708008
KAPB_YEASTTPK2genetic
27708008
DOM34_YEASTDOM34genetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL12B_YEAST

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Identification of protein N-terminal methyltransferases in yeast andhumans.";
Webb K.J., Lipson R.S., Al-Hadid Q., Whitelegge J.P., Clarke S.G.;
Biochemistry 49:5225-5235(2010).
Cited for: METHYLATION AT PRO-2 BY NTM1/TAE1.
"Identification of two SET domain proteins required for methylation oflysine residues in yeast ribosomal protein Rpl42ab.";
Webb K.J., Laganowsky A., Whitelegge J.P., Clarke S.G.;
J. Biol. Chem. 283:35561-35568(2008).
Cited for: METHYLATION AT PRO-2; LYS-4 AND ARG-67.
"Yeast ribosomal protein L12 is a substrate of protein-argininemethyltransferase 2.";
Chern M.-K., Chang K.-N., Liu L.-F., Tam T.-C.S., Liu Y.-C.,Liang Y.-L., Tam M.F.;
J. Biol. Chem. 277:15345-15353(2002).
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION AT ARG-67, ANDMUTAGENESIS OF ARG-67.
"A novel SET domain methyltransferase in yeast: Rkm2-dependenttrimethylation of ribosomal protein L12ab at lysine 10.";
Porras-Yakushi T.R., Whitelegge J.P., Clarke S.;
J. Biol. Chem. 281:35835-35845(2006).
Cited for: PROTEIN SEQUENCE OF 2-16, METHYLATION AT LYS-4 AND LYS-11, AND MASSSPECTROMETRY.
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-38 AND SER-78, 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-38, 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-38, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.

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