RTPT_YEAST - dbPTM
RTPT_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTPT_YEAST
UniProt AC P17558
Protein Name 37S ribosomal protein PET123, mitochondrial
Gene Name PET123
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 318
Subcellular Localization Mitochondrion . Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner memb
Protein Description Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane..
Protein Sequence MGKGAAKYGFKSGVFPTTRSILKSPTTKQTDIINKVKSPKPKGVLGIGYAKGVKHPKGSHRLSPKVNFIDVDNLIAKTVAEPQSIKSSNGSAQKVRLQKAELRRKFLIEAFRKEEARLLHKHEYLQKRTKELEKAKELELEKLNKEKSSDLTIMTLDKMMSQPLLRNRSPEESELLKLKRNYNRSLLNFQAHKKKLNELLNLYHVANEFIVTESQLLKKIDKVFNDETEEFTDAYDVTSNFTQFGNRKLLLSGNTTLQTQINNAIMGSLSNEKFFDISLVDSYLNKDLKNISNKIDSKLNPTSNGAGNNGNNNNTTNL
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
24PhosphorylationTTRSILKSPTTKQTD
CCHHHHHCCCCCCCC
24.8423749301
121AcetylationEEARLLHKHEYLQKR
HHHHHHHHHHHHHHH
37.7922865919
142AcetylationAKELELEKLNKEKSS
HHHHHHHHHHHHHCC
70.7324489116
155PhosphorylationSSDLTIMTLDKMMSQ
CCCCEEEEHHHHHCC
28.1427017623
169PhosphorylationQPLLRNRSPEESELL
CHHHHCCCHHHHHHH
39.9725704821
182PhosphorylationLLKLKRNYNRSLLNF
HHHHHHHCCHHHHHH
18.9119823750
185PhosphorylationLKRNYNRSLLNFQAH
HHHHCCHHHHHHHHH
33.3019823750
214PhosphorylationNEFIVTESQLLKKID
HHHHCCHHHHHHHHH
19.4327214570
302PhosphorylationIDSKLNPTSNGAGNN
HHHCCCCCCCCCCCC
33.4827017623

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 RTPT_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTPT_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 RTPT_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT05_YEASTMRPS5physical
16554755
RT24_YEASTRSM24physical
16554755
RT01_YEASTMRP1physical
16554755
RT13_YEASTMRP13physical
16554755
RT27_YEASTRSM27physical
16554755
RT04_YEASTMRP4physical
16554755
RT25_YEASTRSM25physical
16554755
RT26_YEASTRSM26physical
16554755
RT07_YEASTRSM7physical
16554755
RT18_YEASTMRPS18physical
16554755
RT19_YEASTRSM19physical
16554755
ATG17_YEASTATG17physical
11283351
SP382_YEASTSPP382physical
11283351
ATG17_YEASTATG17physical
18719252
COG2_YEASTCOG2physical
18719252
RT01_YEASTMRP1genetic
1848523
RL36A_YEASTRPL36Agenetic
29158977
DOM34_YEASTDOM34genetic
29158977

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTPT_YEAST

loading...

Related Literatures of Post-Translational Modification

TOP