RL37A_YEAST - dbPTM
RL37A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL37A_YEAST
UniProt AC P49166
Protein Name 60S ribosomal protein L37-A {ECO:0000303|PubMed:9559554}
Gene Name RPL37A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 88
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 MGKGTPSFGKRHNKSHTLCNRCGRRSFHVQKKTCSSCGYPAAKTRSYNWGAKAKRRHTTGTGRMRYLKHVSRRFKNGFQTGSASKASA
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
7Phosphorylation-MGKGTPSFGKRHNK
-CCCCCCCCCCCCCC		46.6029734811
102-HydroxyisobutyrylationKGTPSFGKRHNKSHT
CCCCCCCCCCCCCCC		48.77-
15PhosphorylationFGKRHNKSHTLCNRC
CCCCCCCCCCCHHHC		27.3323749301
17PhosphorylationKRHNKSHTLCNRCGR
CCCCCCCCCHHHCCC		39.8523749301
31UbiquitinationRRSFHVQKKTCSSCG
CCEEEECCCCCCCCC		49.3022817900
32UbiquitinationRSFHVQKKTCSSCGY
CEEEECCCCCCCCCC		37.3623749301
35PhosphorylationHVQKKTCSSCGYPAA
EECCCCCCCCCCCCH		33.6223749301
43UbiquitinationSCGYPAAKTRSYNWG
CCCCCCHHCCCCCCC		46.7223749301
44PhosphorylationCGYPAAKTRSYNWGA
CCCCCHHCCCCCCCC		21.8123749301
46PhosphorylationYPAAKTRSYNWGAKA
CCCHHCCCCCCCCCC		28.2223749301
47PhosphorylationPAAKTRSYNWGAKAK
CCHHCCCCCCCCCCC		16.1928889911
52AcetylationRSYNWGAKAKRRHTT
CCCCCCCCCCCCCCC		50.9724489116
52UbiquitinationRSYNWGAKAKRRHTT
CCCCCCCCCCCCCCC		50.9723749301
54UbiquitinationYNWGAKAKRRHTTGT
CCCCCCCCCCCCCCC		49.6222817900
682-HydroxyisobutyrylationTGRMRYLKHVSRRFK
CCHHHHHHHHHHHHH		32.78-
68AcetylationTGRMRYLKHVSRRFK
CCHHHHHHHHHHHHH		32.7825381059
75AcetylationKHVSRRFKNGFQTGS
HHHHHHHHCCCCCCC		55.1122865919
75UbiquitinationKHVSRRFKNGFQTGS
HHHHHHHHCCCCCCC		55.1122817900
80PhosphorylationRFKNGFQTGSASKAS
HHHCCCCCCCCCCCC		30.7323749301
82PhosphorylationKNGFQTGSASKASA-
HCCCCCCCCCCCCC-		32.5322369663
84PhosphorylationGFQTGSASKASA---
CCCCCCCCCCCC---		30.3722369663
85UbiquitinationFQTGSASKASA----
CCCCCCCCCCC----		46.1823749301
87PhosphorylationTGSASKASA------
CCCCCCCCC------		37.9422369663
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 RL37A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL37A_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 RL37A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHK1_YEASTCHK1genetic
20093466
THRC_YEASTTHR4genetic
20093466
ARF1_YEASTARF1genetic
20093466
RMD1_YEASTRMD1genetic
20093466
CRF1_YEASTCRF1genetic
20093466
UBP6_YEASTUBP6genetic
20093466
KIP3_YEASTKIP3genetic
20093466
XRN1_YEASTXRN1genetic
20093466
PUR4_YEASTADE6genetic
20093466
UPF3_YEASTUPF3genetic
20093466
G3P3_YEASTTDH3genetic
20093466
ERP5_YEASTERP5genetic
20093466
THP2_YEASTTHP2genetic
20093466
FMO1_YEASTFMO1genetic
20093466
DENR_YEASTTMA22genetic
20093466
DHOM_YEASTHOM6genetic
20093466
NAP1_YEASTNAP1genetic
20093466
GBLP_YEASTASC1genetic
20093466
PYRX_YEASTURA10genetic
20093466
EOS1_YEASTEOS1genetic
20093466
VPS27_YEASTVPS27genetic
20093466
RM50_YEASTMRPL50genetic
20093466
WHI5_YEASTWHI5genetic
20093466
SUR1_YEASTSUR1genetic
20093466
CISY3_YEASTCIT3genetic
20093466
RL37B_YEASTRPL37Bgenetic
22377630
CHK1_YEASTCHK1genetic
22282571
RS25A_YEASTRPS25Agenetic
24217298
RPN4_YEASTRPN4genetic
27708008
UBP6_YEASTUBP6genetic
27708008
XRN1_YEASTXRN1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
GBLP_YEASTASC1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL37A_YEAST

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Related Literatures of Post-Translational Modification

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