RLI1_YEAST - dbPTM
RLI1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLI1_YEAST
UniProt AC Q03195
Protein Name Translation initiation factor RLI1
Gene Name RLI1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 608
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the nucleus and the cytoplasm.
Protein Description Component of the multifactor complex (MFC) involved in translation initiation. Required for the binding of MFC to the 40S ribosome. Required for the processing and nuclear export of the 60S and 40S ribosomal subunits..
Protein Sequence MSDKNSRIAIVSADKCKPKKCRQECKRSCPVVKTGKLCIEVTPTSKIAFISEILCIGCGICVKKCPFDAIQIINLPTNLEAHVTHRYSANSFKLHRLPTPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQEIIKYFRGSELQNYFTKMLEDDIKAIIKPQYVDNIPRAIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYGVPSVYGVVTLPASVREGINIFLDGHIPAENLRFRTEALQFRIADATEDLQNDSASRAFSYPSLKKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNVSMKPQKIAPKFPGTVRQLFFKKIRGQFLNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEGIPSKNAHARAPESLLTGCNRFLKNLNVTFRRDPNSFRPRINKLDSQMDKEQKSSGNYFFLDNTGI
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
6Phosphorylation--MSDKNSRIAIVSA
--CCCCCCCEEEEEC
30.7027717283
12PhosphorylationNSRIAIVSADKCKPK
CCCEEEEECCCCCCH
25.3327717283
36AcetylationCPVVKTGKLCIEVTP
CCEEECCCEEEEECC
45.4724489116
121AcetylationIGKSTALKILAGKQK
CCHHHHHHHHCCCCC
32.9622865919
165AcetylationKMLEDDIKAIIKPQY
HHHHHHHHHHHCHHH
40.2924489116
186AcetylationAIKGPVQKVGELLKL
HHCCHHHHHHHHHHH
53.0624489116
192AcetylationQKVGELLKLRMEKSP
HHHHHHHHHHCCCCH
46.8224489116
207AcetylationEDVKRYIKILQLENV
HHHHHHHHHHHHHHH
28.5624489116
216AcetylationLQLENVLKRDIEKLS
HHHHHHHHHHHHHHC
43.6824489116
221AcetylationVLKRDIEKLSGGELQ
HHHHHHHHHCCCCCC
48.5724489116
221UbiquitinationVLKRDIEKLSGGELQ
HHHHHHHHHCCCCCC
48.5723749301
342PhosphorylationQFRIADATEDLQNDS
EEECCCCCHHHCCCC
30.4928889911
349PhosphorylationTEDLQNDSASRAFSY
CHHHCCCCCCHHCCC
35.3822369663
351PhosphorylationDLQNDSASRAFSYPS
HHCCCCCCHHCCCHH
28.2622369663
355PhosphorylationDSASRAFSYPSLKKT
CCCCHHCCCHHHCCC
34.8427214570
396AcetylationTGKTTLIKLLAGALK
CCHHHHHHHHHCCCC
40.3324489116
403AcetylationKLLAGALKPDEGQDI
HHHHCCCCCCCCCCC
50.3024489116
425AcetylationKPQKIAPKFPGTVRQ
CHHHCCCCCCHHHHH
55.9924489116
508UbiquitinationEQRIICSKVIRRFIL
HHHHHHHHHHHHHHH
36.9523749301
566AcetylationTGCNRFLKNLNVTFR
HHHHHHHHHCCCEEC
57.5922865919

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 RLI1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLI1_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 RLI1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3J_YEASTHCR1physical
14759368
EIF3C_YEASTNIP1physical
14759368
RLI1_YEASTRLI1physical
14759368
RLA0_YEASTRPP0physical
14759368
YN00_YEASTLTO1physical
14759368
EIF3J_YEASTHCR1physical
15660134
RL3_YEASTRPL3physical
15660134
RL4A_YEASTRPL4Aphysical
15660134
RL4B_YEASTRPL4Bphysical
15660134
RL10_YEASTRPL10physical
15660134
RS3A1_YEASTRPS1Aphysical
15660134
RS3A2_YEASTRPS1Bphysical
15660134
RS4A_YEASTRPS4Aphysical
15660134
RS4B_YEASTRPS4Aphysical
15660134
RL8B_YEASTRPL8Bphysical
15660134
RL7A_YEASTRPL7Aphysical
15660134
RL7B_YEASTRPL7Bphysical
15660134
RL16A_YEASTRPL16Aphysical
15660134
RS8A_YEASTRPS8Aphysical
15660134
RS8B_YEASTRPS8Aphysical
15660134
RL13B_YEASTRPL13Bphysical
15660134
RL13A_YEASTRPL13Aphysical
15660134
RS17A_YEASTRPS17Aphysical
15660134
RS16A_YEASTRPS16Bphysical
15660134
RS16B_YEASTRPS16Bphysical
15660134
RLA3_YEASTRPP1Bphysical
16554755
CYAA_YEASTCYR1physical
16554755
YAE1_YEASTYAE1physical
16554755
STM1_YEASTSTM1physical
16554755
EIF3J_YEASTHCR1physical
16554755
YN00_YEASTLTO1physical
16554755
DBP2_YEASTDBP2physical
16429126
IMDH3_YEASTIMD3physical
16429126
RS17A_YEASTRPS17Aphysical
16429126
RS7A_YEASTRPS7Aphysical
16429126
RS22B_YEASTRPS22Bphysical
16429126
RS3A2_YEASTRPS1Bphysical
16429126
RL7A_YEASTRPL7Aphysical
16429126
RL8B_YEASTRPL8Bphysical
16429126
EIF3J_YEASTHCR1physical
11283351
NOP12_YEASTNOP12genetic
19061648
AIR1_YEASTAIR1genetic
19061648
LRP1_YEASTLRP1genetic
19061648
NOP16_YEASTNOP16genetic
19061648
SLS1_YEASTSLS1genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
NOP6_YEASTNOP6genetic
19061648
UPF3_YEASTUPF3genetic
19061648
IF2M_YEASTIFM1genetic
19061648
BUD21_YEASTBUD21genetic
19061648
NAM7_YEASTNAM7genetic
19061648
TMA23_YEASTTMA23genetic
19061648
SYKM_YEASTMSK1genetic
19061648
SYDM_YEASTMSD1genetic
19061648
NMD2_YEASTNMD2genetic
19061648
ERF3_YEASTSUP35physical
20062004
ERF1_YEASTSUP45physical
20062004
HEMH_YEASTHEM15physical
20062004
EIF3J_YEASTHCR1physical
20062004
ERF1_YEASTSUP45genetic
20062004
ERF3_YEASTSUP35genetic
20062004
SLA1_YEASTSLA1genetic
20093466
RT103_YEASTRTT103genetic
20093466
RV167_YEASTRVS167genetic
20093466
DCV1_YEASTDCV1genetic
20093466
UPF3_YEASTUPF3genetic
20093466
NMD2_YEASTNMD2genetic
20093466
URM1_YEASTURM1genetic
20093466
IST3_YEASTIST3genetic
20093466
DENR_YEASTTMA22genetic
20093466
PGM1_YEASTPGM1genetic
20093466
EF1G2_YEASTTEF4genetic
20093466
SWI6_YEASTSWI6genetic
20093466
CDC73_YEASTCDC73genetic
20093466
NAM7_YEASTNAM7genetic
20093466
COX7_YEASTCOX7genetic
20093466
DCAM_YEASTSPE2genetic
20093466
WHI5_YEASTWHI5genetic
20093466
NEW1_YEASTNEW1genetic
20093466
SPEE_YEASTSPE3genetic
20093466
ERF1_YEASTSUP45physical
22143755
DOM34_YEASTDOM34physical
22143755
YAE1_YEASTYAE1physical
23318452
YN00_YEASTLTO1physical
23318452
MET18_YEASTMET18physical
22678362
EIF3J_YEASTHCR1physical
24278036
EIF3A_YEASTRPG1physical
24278036
EIF3G_YEASTTIF35physical
24278036
ERF1_YEASTSUP45physical
24278036
ERF3_YEASTSUP35physical
24278036
SUI1_YEASTSUI1physical
24278036
ACT_YEASTACT1genetic
27708008
HSF_YEASTHSF1genetic
27708008
EXO70_YEASTEXO70genetic
27708008
SEC12_YEASTSEC12genetic
27708008
PROF_YEASTPFY1genetic
27708008
BUR1_YEASTSGV1genetic
27708008
SNF5_YEASTSNF5genetic
27708008
DFM1_YEASTDFM1genetic
27708008
YG2W_YEASTYGR111Wgenetic
27708008
GPP1_YEASTGPP1genetic
27708008
MMM1_YEASTMMM1genetic
27708008
PEX13_YEASTPEX13genetic
27708008
CDA2_YEASTCDA2genetic
27708008
MGR3_YEASTMGR3genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
CTU2_YEASTNCS2genetic
27708008
DCAM_YEASTSPE2genetic
27708008
GAS4_YEASTGAS4genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
PMP1_YEASTPMP1physical
26404137
RPB3_YEASTRPB3physical
25182531

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RLI1_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 THR-342; SER-349 ANDSER-351, AND MASS SPECTROMETRY.

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