TYW1_HUMAN - dbPTM
TYW1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TYW1_HUMAN
UniProt AC Q9NV66
Protein Name S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
Gene Name TYW1
Organism Homo sapiens (Human).
Sequence Length 732
Subcellular Localization
Protein Description Probable 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 MDPSADTWDLFSPLISLWINRFYIYLGFAVSISLWICVQIVIKTQGKNLQEKSVPKAAQDLMTNGYVSLQEKDIFVSGVKIFYGSQTGTAKGFATVLAEAVTSLDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRYAVFGLGNSAYASHFNKVGKNVDKWLWMLGAHRVMSRGEGDCDVVKSKHGSIEADFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSHEQDELHHRDTEEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPALREALTKQGYQLIGSHSGVKLCRWTKSMLRGRGGCYKHTFYGIESHRCMETTPSLACANKCVFCWRHHTNPVGTEWRWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPLFKDFWQRFLDSLKALAVKQQRTVYRLTLVKAWNVDELQAYAQLVSLGNPDFIEVKGVTYCGESSASSLTMAHVPWHEEVVQFVHELVDLIPEYEIACEHEHSNCLLIAHRKFKIGGEWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGASERGFDPKDTRHQRKNKSKAISGC
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
52UbiquitinationQGKNLQEKSVPKAAQ
CCCCCHHCCCCHHHH		43.7427667366
166UbiquitinationSIDFRFGKTYLKGMR
CCCEECCCHHHCCCE		31.14-
167O-linked_GlycosylationIDFRFGKTYLKGMRY
CCEECCCHHHCCCEE		34.1730379171
170MethylationRFGKTYLKGMRYAVF
ECCCHHHCCCEEEEE		40.00-
182PhosphorylationAVFGLGNSAYASHFN
EEECCCHHHHHHHHH		22.36-
184PhosphorylationFGLGNSAYASHFNKV
ECCCHHHHHHHHHHH		14.4122210691
186PhosphorylationLGNSAYASHFNKVGK
CCHHHHHHHHHHHCC		18.8822210691
219UbiquitinationEGDCDVVKSKHGSIE
CCCCCEECCCCCCHH		54.3527667366
221UbiquitinationDCDVVKSKHGSIEAD
CCCEECCCCCCHHHH		46.39-
235UbiquitinationDFRAWKTKFISQLQA
HHHHHHHHHHHHHHH		36.6527667366
245UbiquitinationSQLQALQKGERKKSC
HHHHHHHHCCCCCCC		64.6929967540
268PhosphorylationCESHQHGSEEREEGS
CCCCCCCCHHCCCCC		33.8729449344
275PhosphorylationSEEREEGSHEQDELH
CHHCCCCCCCCCHHC		27.4229449344
294PhosphorylationEEEEPFESSSEEEFG
CCCCCCCCCCCCHHC		39.2726471730
295PhosphorylationEEEPFESSSEEEFGG
CCCCCCCCCCCHHCC		34.2726471730
296PhosphorylationEEPFESSSEEEFGGE
CCCCCCCCCCHHCCC		59.3026471730
307PhosphorylationFGGEDHQSLNSIVDV
HCCCCCCCHHCCCCH		26.5426471730
310PhosphorylationEDHQSLNSIVDVEDL
CCCCCHHCCCCHHHH		29.3126471730
337UbiquitinationEKEQQEEKSGLFRNM
HHHHHHHHCCCCCCC		49.4229967540
338PhosphorylationKEQQEEKSGLFRNMG
HHHHHHHCCCCCCCC		43.9726074081
366UbiquitinationALREALTKQGYQLIG
HHHHHHHHHCCHHHH		42.4429967540
374PhosphorylationQGYQLIGSHSGVKLC
HCCHHHHCCCCHHHH		13.9023312004
376PhosphorylationYQLIGSHSGVKLCRW
CHHHHCCCCHHHHHH		47.1525159151
385UbiquitinationVKLCRWTKSMLRGRG
HHHHHHHHHHHCCCC		27.23-
396UbiquitinationRGRGGCYKHTFYGIE
CCCCCCHHHCCCEEC		40.0019608861
396AcetylationRGRGGCYKHTFYGIE
CCCCCCHHHCCCEEC		40.0023954790
438UbiquitinationVGTEWRWKMDQPEMI
CCCCCEECCCCHHHH		24.83-
447UbiquitinationDQPEMILKEAIENHQ
CCHHHHHHHHHHHHH		33.8929967540
456UbiquitinationAIENHQNMIKQFKGV
HHHHHHHHHHHHCCC		3.0521890473
458 (in isoform 1)Ubiquitination-38.6221890473
458UbiquitinationENHQNMIKQFKGVPG
HHHHHHHHHHCCCCC		38.6221890473
461UbiquitinationQNMIKQFKGVPGVKA
HHHHHHHCCCCCCCC		57.41-
467UbiquitinationFKGVPGVKAERFEEG
HCCCCCCCCHHHCCC		50.9029967540
472UbiquitinationGVKAERFEEGMTVKH
CCCCHHHCCCCCHHH		60.9227667366
483PhosphorylationTVKHCALSLVGEPIM
CHHHHHHHHHCCCCH		11.5025850435
499UbiquitinationPEINRFLKLLHQCKI
HHHHHHHHHHHHCCC		46.41-
505UbiquitinationLKLLHQCKISSFLVT
HHHHHHCCCCEEEEC		38.77-
543UbiquitinationSTKDSLKKIDRPLFK
CCHHHHHHCCCHHHH		55.95-
550 (in isoform 1)Ubiquitination-60.7521890473
550UbiquitinationKIDRPLFKDFWQRFL
HCCCHHHHHHHHHHH		60.7521890473
561UbiquitinationQRFLDSLKALAVKQQ
HHHHHHHHHHHHHHC		45.3529967540
566UbiquitinationSLKALAVKQQRTVYR
HHHHHHHHHCCCEEE		34.8027667366
600UbiquitinationSLGNPDFIEVKGVTY
HCCCCCEEEEECEEE		8.5122505724
606PhosphorylationFIEVKGVTYCGESSA
EEEEECEEEECCCCC		23.05-
622UbiquitinationSLTMAHVPWHEEVVQ
CCEECCCCCHHHHHH		19.4824816145
682PhosphorylationFQELIQEYEDSGGSK
HHHHHHHHHHCCCCE		14.5228796482
685PhosphorylationLIQEYEDSGGSKTFS
HHHHHHHCCCCEEEC		32.8728796482
688PhosphorylationEYEDSGGSKTFSAKD
HHHHCCCCEEECHHH		31.8628796482
689 (in isoform 1)Ubiquitination-57.7921890473
689UbiquitinationYEDSGGSKTFSAKDY
HHHCCCCEEECHHHH		57.7921906983
692PhosphorylationSGGSKTFSAKDYMAR
CCCCEEECHHHHHHC		39.3721712546
694UbiquitinationGSKTFSAKDYMARTP
CCEEECHHHHHHCCC		48.4722505724
700PhosphorylationAKDYMARTPHWALFG
HHHHHHCCCCHHHHC		15.23-
709PhosphorylationHWALFGASERGFDPK
CHHHHCCHHHCCCCC		28.3628857561
716UbiquitinationSERGFDPKDTRHQRK
HHHCCCCCCCHHHHH		73.8424816145
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TYW1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TYW1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TYW1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND MASS SPECTROMETRY.

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