RL38_YEAST - dbPTM
RL38_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL38_YEAST
UniProt AC P49167
Protein Name 60S ribosomal protein L38 {ECO:0000303|PubMed:9559554}
Gene Name RPL38 {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 78
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 MAREITDIKQFLELTRRADVKTATVKINKKLNKAGKPFRQTKFKVRGSSSLYTLVINDAGKAKKLIQSLPPTLKVNRL
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
9SuccinylationAREITDIKQFLELTR
CCCHHHHHHHHHHHH		37.4923954790
9AcetylationAREITDIKQFLELTR
CCCHHHHHHHHHHHH		37.4924489116
9UbiquitinationAREITDIKQFLELTR
CCCHHHHHHHHHHHH		37.4924961812
212-HydroxyisobutyrylationLTRRADVKTATVKIN
HHHCCCCCEEEHHHH		32.75-
21UbiquitinationLTRRADVKTATVKIN
HHHCCCCCEEEHHHH		32.7523749301
262-HydroxyisobutyrylationDVKTATVKINKKLNK
CCCEEEHHHHHHHHH		35.89-
26UbiquitinationDVKTATVKINKKLNK
CCCEEEHHHHHHHHH		35.8922817900
48PhosphorylationTKFKVRGSSSLYTLV
CEEEEECCCCEEEEE		13.2422369663
49PhosphorylationKFKVRGSSSLYTLVI
EEEEECCCCEEEEEE		27.4722369663
50PhosphorylationFKVRGSSSLYTLVIN
EEEECCCCEEEEEEC		27.3922369663
52PhosphorylationVRGSSSLYTLVINDA
EECCCCEEEEEECCC		10.4422890988
53PhosphorylationRGSSSLYTLVINDAG
ECCCCEEEEEECCCH		21.6022890988
61AcetylationLVINDAGKAKKLIQS
EEECCCHHHHHHHHH		59.7724489116
61UbiquitinationLVINDAGKAKKLIQS
EEECCCHHHHHHHHH		59.7723749301
612-HydroxyisobutyrylationLVINDAGKAKKLIQS
EEECCCHHHHHHHHH		59.77-
63UbiquitinationINDAGKAKKLIQSLP
ECCCHHHHHHHHHCC		52.1522817900
64UbiquitinationNDAGKAKKLIQSLPP
CCCHHHHHHHHHCCC		56.5323749301
68PhosphorylationKAKKLIQSLPPTLKV
HHHHHHHHCCCCCCC		35.5322369663
72PhosphorylationLIQSLPPTLKVNRL-
HHHHCCCCCCCCCC-		36.9522369663
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 RL38_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL38_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 RL38_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP73_YEASTSSA3physical
16554755
LSM12_YEASTLSM12physical
16554755
SMD3_YEASTSMD3physical
16554755
CND2_YEASTBRN1genetic
27708008
ESP1_YEASTESP1genetic
27708008
SED5_YEASTSED5genetic
27708008
CLP1_YEASTCLP1genetic
27708008
MED20_YEASTSRB2genetic
27708008
CALM_YEASTCMD1genetic
27708008
CDK1_YEASTCDC28genetic
27708008
CDC10_YEASTCDC10genetic
27708008
GLE1_YEASTGLE1genetic
27708008
LCB2_YEASTLCB2genetic
27708008
PDC2_YEASTPDC2genetic
27708008
RRP1_YEASTRRP1genetic
27708008
CDC37_YEASTCDC37genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
SPC19_YEASTSPC19genetic
27708008
CDC4_YEASTCDC4genetic
27708008
GNA1_YEASTGNA1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
ALG2_YEASTALG2genetic
27708008
PESC_YEASTNOP7genetic
27708008
DAM1_YEASTDAM1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
CDC12_YEASTCDC12genetic
27708008
ARP4_YEASTARP4genetic
27708008
CDC6_YEASTCDC6genetic
27708008
HSP77_YEASTSSC1genetic
27708008
CDC11_YEASTCDC11genetic
27708008
MED14_YEASTRGR1genetic
27708008
ERB1_YEASTERB1genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
NOP2_YEASTNOP2genetic
27708008
DPOA_YEASTPOL1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
RPC6_YEASTRPC34genetic
27708008
HRP1_YEASTHRP1genetic
27708008
SGT1_YEASTSGT1genetic
27708008
TYSY_YEASTCDC21genetic
27708008
GRPE_YEASTMGE1genetic
27708008
APC5_YEASTAPC5genetic
27708008
YTM1_YEASTYTM1genetic
27708008
IPL1_YEASTIPL1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
ATC3_YEASTDRS2genetic
27708008
UBC4_YEASTUBC4genetic
27708008
SGF29_YEASTSGF29genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
SIC1_YEASTSIC1genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
SUR1_YEASTSUR1genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
DCC1_YEASTDCC1genetic
29674565
BUD31_YEASTBUD31genetic
29674565
WDR59_YEASTMTC5genetic
29674565
SAC3_YEASTSAC3genetic
29674565
TCPZ_YEASTCCT6genetic
29674565
TCPA_YEASTTCP1genetic
29674565
TRS23_YEASTTRS23genetic
29674565
RPB7_YEASTRPB7genetic
29674565
PUF6_YEASTPUF6genetic
29674565
ATC1_YEASTPMR1genetic
29674565
HUR1_YEASTHUR1genetic
29674565
RL11B_YEASTRPL11Bgenetic
29674565
RSSA1_YEASTRPS0Agenetic
29674565
SDS3_YEASTSDS3genetic
29674565
VPS24_YEASTVPS24genetic
29674565
RS21A_YEASTRPS21Agenetic
29674565
BAS1_YEASTBAS1genetic
29674565
SSL1_YEASTSSL1genetic
29674565
RL6B_YEASTRPL6Bgenetic
29674565
MSC1_YEASTMSC1genetic
29674565
PFD4_YEASTGIM3genetic
29674565
SIN3_YEASTSIN3genetic
29674565
SFL1_YEASTSFL1genetic
29674565
BEM4_YEASTBEM4genetic
29674565
YAR1_YEASTYAR1genetic
29674565
ELM1_YEASTELM1genetic
29674565
DYN3_YEASTDYN3genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL38_YEAST

loading...

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-48 AND SER-49, 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-49, AND MASSSPECTROMETRY.

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