TYW1_YEAST - dbPTM
TYW1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TYW1_YEAST
UniProt AC Q08960
Protein Name S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
Gene Name TYW1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 810
Subcellular Localization Endoplasmic reticulum .
Protein Description Component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity)..
Protein Sequence MDGFRVAGALVVGALTAAYLYFGGRFSIALVIIVGYGIYCNEASGGSQDSQEKLDLNKQQKKPCCSDKKIADGGKKTGGCCSDKKNGGGKGGGCCSSKGGKKGGCCSSKGGKKGGCCSSKKNIGDNENTATEVEKAVNYPVTVDFTEVFRKPTKKRSSTPKVFSKNSSSNSRVGKKLSVSKKIGPDGLIKSALTISNETLLSSQIYVLYSSLQGAASKAAKSVYDKLKELDELTNEPKLLNLDDLSDFDDYFINVPVENALYVLVLPSYDIDCPLDYFLQTLEENANDFRVDSFPLRKLVGYTVLGLGDSESWPEKFCYQAKRADHWISRLGGRRIFPLGKVCMKTGGSAKIDEWTSLLAETLKDDEPIIYEYDENADSEEDEEEGNGSDELGDVEDIGGKGSNGKFSGADEIKQMVAKDSPTYKNLTKQGYKVIGSHSGVKICRWTKNELRGKGSCYKKSLFNIASSRCMELTPSLACSSKCVFCWRHGTNPVSKNWRWEVDEPEYILENALKGHYSMIKQMRGVPGVIAERFAKAFEVRHCALSLVGEPILYPHINKFIQLLHQKGITSFLVCNAQHPEALRNIVKVTQLYVSIDAPTKTELKKVDRPLYKDFWERMVECLEILKTVQNHQRTVFRLTLVKGFNMGDVSAYADLVQRGLPGFIEVKGATFSGSSDGNGNPLTMQNIPFYEECVKFVKAFTTELQRRGLHYDLAAEHAHSNCLLIADTKFKINGEWHTHIDFDKFFVLLNSGKDFTYMDYLEKTPEWALFGNGGFAPGNTRVYRKDKKKQNKENQETTTRETPLPPIPA
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
58UbiquitinationQEKLDLNKQQKKPCC
HHHHCCCHHCCCCCC		62.4923749301
82PhosphorylationKKTGGCCSDKKNGGG
CCCCCCCCCCCCCCC		57.4528889911
121UbiquitinationGGCCSSKKNIGDNEN
CCCCCCCCCCCCCCC		56.6023749301
135UbiquitinationNTATEVEKAVNYPVT
CHHHHHHHHHCCCEE		63.9117644757
151UbiquitinationDFTEVFRKPTKKRSS
CHHHHHCCCCCCCCC		45.6417644757
165UbiquitinationSTPKVFSKNSSSNSR
CCCCEECCCCCCCCC		49.7623749301
171PhosphorylationSKNSSSNSRVGKKLS
CCCCCCCCCCCCCCE		30.2327017623
322UbiquitinationEKFCYQAKRADHWIS
HHHHHHHHHHHHHHH		32.3717644757
373PhosphorylationDEPIIYEYDENADSE
CCCCEEEECCCCCCH		16.1619795423
379PhosphorylationEYDENADSEEDEEEG
EECCCCCCHHHHCCC		40.2419795423
389PhosphorylationDEEEGNGSDELGDVE
HHCCCCCCCCCCCCC		31.7319795423
406UbiquitinationGGKGSNGKFSGADEI
CCCCCCCCCCCHHHH		40.3823749301
414UbiquitinationFSGADEIKQMVAKDS
CCCHHHHHHHHHCCC		30.2323749301
421PhosphorylationKQMVAKDSPTYKNLT
HHHHHCCCCCHHHHH		20.5923749301
429UbiquitinationPTYKNLTKQGYKVIG
CCHHHHHHHCCEEEE		44.9123749301
437PhosphorylationQGYKVIGSHSGVKIC
HCCEEEECCCCCEEE		11.8927017623
439PhosphorylationYKVIGSHSGVKICRW
CEEEECCCCCEEEEE		47.1521440633
460UbiquitinationGKGSCYKKSLFNIAS
CCCCCCHHHHHHHHH		26.3917644757
496UbiquitinationHGTNPVSKNWRWEVD
CCCCCCCCCCEEEEC		61.8423749301
514UbiquitinationYILENALKGHYSMIK
HHHHHHHHHHHHHHH		41.0317644757
536UbiquitinationVIAERFAKAFEVRHC
HHHHHHHHHHHHHHH		51.3923749301
559UbiquitinationILYPHINKFIQLLHQ
CHHHHHHHHHHHHHH		43.1517644757
567UbiquitinationFIQLLHQKGITSFLV
HHHHHHHCCCCEEEE		41.3417644757
730UbiquitinationCLLIADTKFKINGEW
EEEEECEEEEECCEE		45.2517644757
758PhosphorylationNSGKDFTYMDYLEKT
CCCCCCCCHHHHHCC		6.4919779198
764UbiquitinationTYMDYLEKTPEWALF
CCHHHHHCCCCEEEC		67.7817644757
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 TYW1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TYW1_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 TYW1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSR1_YEASTCSR1physical
16554755
SSB2_YEASTSSB2physical
16429126
BFR1_YEASTBFR1genetic
16269340
DAP1_YEASTDAP1genetic
16269340
SSB1_YEASTSSB1physical
19536198
MTU1_YEASTSLM3genetic
20093466
PCP1_YEASTPCP1genetic
20093466
ECM34_YEASTECM34genetic
20093466
FYV4_YEASTFYV4genetic
20093466
PIR5_YEASTYJL160Cgenetic
20093466
YJ24_YEASTKCH1genetic
20093466
IME1_YEASTIME1genetic
20093466
YKZ5_YEASTYKR015Cgenetic
20093466
EOS1_YEASTEOS1genetic
20093466
PET8_YEASTPET8genetic
20093466
COQ2_YEASTCOQ2genetic
20093466
UGO1_YEASTUGO1genetic
21987634
RPOM_YEASTRPO41genetic
21987634
PT130_YEASTPET130genetic
21987634
ACON_YEASTACO1genetic
21987634
IPYR2_YEASTPPA2genetic
21987634
GATA_YEASTHER2genetic
21987634
GEP3_YEASTGEP3genetic
21987634
DPOG_YEASTMIP1genetic
21987634
DAP1_YEASTDAP1genetic
21987634
RBD2_YEASTRBD2genetic
21987634
PIR5_YEASTYJL160Cgenetic
27708008
NPL4_YEASTNPL4genetic
27708008
MTU1_YEASTSLM3genetic
27708008
RS29B_YEASTRPS29Bgenetic
27708008
INO2_YEASTINO2genetic
27708008
VPS72_YEASTVPS72genetic
27708008
RT31_YEASTYMR31genetic
27708008
RT102_YEASTRTT102genetic
27708008
DOG2_YEASTDOG2genetic
27708008
CYPB_YEASTCPR2genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
FLX1_YEASTFLX1genetic
27708008
ATG32_YEASTATG32genetic
27708008
YJ24_YEASTKCH1genetic
27708008
IME1_YEASTIME1genetic
27708008
DHOM_YEASTHOM6genetic
27708008
MDM35_YEASTMDM35genetic
27708008
CCC1_YEASTCCC1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TYW1_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 SER-439, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-496, AND MASSSPECTROMETRY.

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