TYW4_HUMAN - dbPTM
TYW4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TYW4_HUMAN
UniProt AC O60294
Protein Name tRNA wybutosine-synthesizing protein 4
Gene Name LCMT2
Organism Homo sapiens (Human).
Sequence Length 686
Subcellular Localization
Protein Description Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a 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 (By similarity). May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues..
Protein Sequence MGPRSRERRAGAVQNTNDSSALSKRSLAARGYVQDPFAALLVPGAARRAPLIHRGYYVRARAVRHCVRAFLEQIGAPQAALRAQILSLGAGFDSLYFRLKTAGRLARAAVWEVDFPDVARRKAERIGETPELCALTGPFERGEPASALCFESADYCILGLDLRQLQRVEEALGAAGLDAASPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRPQDAFGQFMLQHFRQLNSPLHGLERFPDVEAQRRRFLQAGWTACGAVDMNEFYHCFLPAEERRRVENIEPFDEFEEWHLKCAHYFILAASRGDTLSHTLVFPSSEAFPRVNPASPSGVFPASVVSSEGQVPNLKRYGHASVFLSPDVILSAGGFGEQEGRHCRVSQFHLLSRDCDSEWKGSQIGSCGTGVQWDGRLYHTMTRLSESRVLVLGGRLSPVSPALGVLQLHFFKSEDNNTEDLKVTITKAGRKDDSTLCCWRHSTTEVSCQNQEYLFVYGGRSVVEPVLSDWHFLHVGTMAWVRIPVEGEVPEARHSHSACTWQGGALIAGGLGASEEPLNSVLFLRPISCGFLWESVDIQPPITPRYSHTAHVLNGKLLLVGGIWIHSSSFPGVTVINLTTGLSSEYQIDTTYVPWPLMLHNHTSILLPEEQQLLLLGGGGNCFSFGTYFNPHTVTLDLSSLSAGQ
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
9MethylationGPRSRERRAGAVQNT
CCCCHHHHHCCCCCC
115481911
16PhosphorylationRAGAVQNTNDSSALS
HHCCCCCCCCHHHHH
23312004
19PhosphorylationAVQNTNDSSALSKRS
CCCCCCCHHHHHHHH
29255136
20PhosphorylationVQNTNDSSALSKRSL
CCCCCCHHHHHHHHH
29255136
23PhosphorylationTNDSSALSKRSLAAR
CCCHHHHHHHHHHHC
29255136
24UbiquitinationNDSSALSKRSLAARG
CCHHHHHHHHHHHCC
21906983
218PhosphorylationPNALFVVYEQMRPQD
CCEEEEEEEECCCCC
25404012
316PhosphorylationLAASRGDTLSHTLVF
EEECCCCCCEEEEEE
-
318PhosphorylationASRGDTLSHTLVFPS
ECCCCCCEEEEEECC
-
338PhosphorylationRVNPASPSGVFPASV
CCCCCCCCCCCCHHH
25332170
356UbiquitinationEGQVPNLKRYGHASV
CCCCCCCCCCCCEEE
21906983
358PhosphorylationQVPNLKRYGHASVFL
CCCCCCCCCCEEEEE
22468782
362PhosphorylationLKRYGHASVFLSPDV
CCCCCCEEEEECCCE
22468782
372PhosphorylationLSPDVILSAGGFGEQ
ECCCEEEECCCCCCC
22468782
401UbiquitinationRDCDSEWKGSQIGSC
CCCCCCCCCCCCCCC
21963094
410PhosphorylationSQIGSCGTGVQWDGR
CCCCCCCCCCEECCH
28555341
426PhosphorylationYHTMTRLSESRVLVL
EEEEECCCCCEEEEE
-
428PhosphorylationTMTRLSESRVLVLGG
EEECCCCCEEEEECC
-
438PhosphorylationLVLGGRLSPVSPALG
EEECCCCCCCCHHHH
-
441PhosphorylationGGRLSPVSPALGVLQ
CCCCCCCCHHHHHHE
-
453SumoylationVLQLHFFKSEDNNTE
HHEEEEEECCCCCCC
-
454PhosphorylationLQLHFFKSEDNNTED
HEEEEEECCCCCCCE
-
459PhosphorylationFKSEDNNTEDLKVTI
EECCCCCCCEEEEEE
-
463UbiquitinationDNNTEDLKVTITKAG
CCCCCEEEEEEEECC
21906983
463AcetylationDNNTEDLKVTITKAG
CCCCCEEEEEEEECC
23954790
465O-linked_GlycosylationNTEDLKVTITKAGRK
CCCEEEEEEEECCCC
30379171
467PhosphorylationEDLKVTITKAGRKDD
CEEEEEEEECCCCCC
-
468UbiquitinationDLKVTITKAGRKDDS
EEEEEEEECCCCCCC
22817900
472UbiquitinationTITKAGRKDDSTLCC
EEEECCCCCCCCEEE
-

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
-KUbiquitinationE3 ubiquitin ligaseRNF144BQ7Z419
PMID:12853982

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TYW4_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 TYW4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBAC1_HUMANUBAC1physical
28514442
RN123_HUMANRNF123physical
28514442
DNJC7_HUMANDNAJC7physical
28514442
TCPB_HUMANCCT2physical
28514442

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
DB00149L-Leucine
Regulatory Network of TYW4_HUMAN

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Related Literatures of Post-Translational Modification

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