TTLL4_HUMAN - dbPTM
TTLL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTLL4_HUMAN
UniProt AC Q14679
Protein Name Tubulin polyglutamylase TTLL4
Gene Name TTLL4
Organism Homo sapiens (Human).
Sequence Length 1199
Subcellular Localization Cell projection, cilium . Cytoplasm, cytoskeleton, cilium basal body . Located in cilia. In some cells, also found in basal bodies.
Protein Description Glutamylase which preferentially modifies beta-tubulin and non-tubulin proteins, such as NAP1L1, NAP1L4 and CGAS. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Involved in formation of short side-chains. Mediates initiation of polyglutamylation of nucleosome assembly proteins NAP1L1 and NAP1L4. Also acts as a monoglutamylase: generates monoglutamylation of CGAS, leading to impair the nucleotidyltransferase activity of CGAS..
Protein Sequence MASAGTQHYSIGLRQKNSFKQSGPSGTVPATPPEKPSEGRVWPQAHQQVKPIWKLEKKQVETLSAGLGPGLLGVPPQPAYFFCPSTLCSSGTTAVIAGHSSSCYLHSLPDLFNSTLLYRRSSYRQKPYQQLESFCLRSSPSEKSPFSLPQKSLPVSLTANKATSSMVFSMAQPMASSSTEPYLCLAAAGENPSGKSLASAISGKIPSPLSSSYKPMLNNNSFMWPNSTPVPLLQTTQGLKPVSPPKIQPVSWHHSGGTGDCAPQPVDHKVPKSIGTVPADASAHIALSTASSHDTSTTSVASSWYNRNNLAMRAEPLSCALDDSSDSQDPTKEIRFTEAVRKLTARGFEKMPRQGCQLEQSSFLNPSFQWNVLNRSRRWKPPAVNQQFPQEDAGSVRRVLPGASDTLGLDNTVFCTKRISIHLLASHASGLNHNPACESVIDSSAFGEGKAPGPPFPQTLGIANVATRLSSIQLGQSEKERPEEARELDSSDRDISSATDLQPDQAETEDTEEELVDGLEDCCSRDENEEEEGDSECSSLSAVSPSESVAMISRSCMEILTKPLSNHEKVVRPALIYSLFPNVPPTIYFGTRDERVEKLPWEQRKLLRWKMSTVTPNIVKQTIGRSHFKISKRNDDWLGCWGHHMKSPSFRSIREHQKLNHFPGSFQIGRKDRLWRNLSRMQSRFGKKEFSFFPQSFILPQDAKLLRKAWESSSRQKWIVKPPASARGIGIQVIHKWSQLPKRRPLLVQRYLHKPYLISGSKFDLRIYVYVTSYDPLRIYLFSDGLVRFASCKYSPSMKSLGNKFMHLTNYSVNKKNAEYQANADEMACQGHKWALKALWNYLSQKGVNSDAIWEKIKDVVVKTIISSEPYVTSLLKMYVRRPYSCHELFGFDIMLDENLKPWVLEVNISPSLHSSSPLDISIKGQMIRDLLNLAGFVLPNAEDIISSPSSCSSSTTSLPTSPGDKCRMAPEHVTAQKMKKAYYLTQKIPDQDFYASVLDVLTPDDVRILVEMEDEFSRRGQFERIFPSHISSRYLRFFEQPRYFNILTTQWEQKYHGNKLKGVDLLRSWCYKGFHMGVVSDSAPVWSLPTSLLTISKDDVILNAFSKSETSKLGKQSSCEVSLLLSEDGTTPKSKKTQAGLSPYPQKPSSSKDSEDTSKEPSLSTQTLPVIKCSGQTSRLSASSTFQSISDSLLAVSP
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
9PhosphorylationASAGTQHYSIGLRQK
CCCCCCCEECCCCCC		7.6817053785
58AcetylationPIWKLEKKQVETLSA
CCHHCCHHHHHHHHC		50.647395845
139PhosphorylationESFCLRSSPSEKSPF
HHHHCCCCCCCCCCC		26.4722617229
141PhosphorylationFCLRSSPSEKSPFSL
HHCCCCCCCCCCCCC		60.6522617229
144PhosphorylationRSSPSEKSPFSLPQK
CCCCCCCCCCCCCCC		27.4222617229
156PhosphorylationPQKSLPVSLTANKAT
CCCCCCEEEECCCCC		20.33-
158PhosphorylationKSLPVSLTANKATSS
CCCCEEEECCCCCHH		22.22-
207PhosphorylationAISGKIPSPLSSSYK
HHCCCCCCCCCCCCC		41.7825159151
221PhosphorylationKPMLNNNSFMWPNST
CCCCCCCCCCCCCCC		20.7129978859
227PhosphorylationNSFMWPNSTPVPLLQ
CCCCCCCCCCCCCEE		29.9729978859
228PhosphorylationSFMWPNSTPVPLLQT
CCCCCCCCCCCCEEE		34.6429978859
235PhosphorylationTPVPLLQTTQGLKPV
CCCCCEEECCCCCCC		22.5129978859
236PhosphorylationPVPLLQTTQGLKPVS
CCCCEEECCCCCCCC		14.0029978859
332UbiquitinationSDSQDPTKEIRFTEA
CCCCCCCHHHHHHHH		57.44-
350UbiquitinationLTARGFEKMPRQGCQ
HHHHCHHHCCCCCCC		52.52-
406PhosphorylationVLPGASDTLGLDNTV
CCCCCCCCCCCCCCE		21.89-
412PhosphorylationDTLGLDNTVFCTKRI
CCCCCCCCEEECHHH		18.02-
416PhosphorylationLDNTVFCTKRISIHL
CCCCEEECHHHHHHH		16.34-
420PhosphorylationVFCTKRISIHLLASH
EEECHHHHHHHHHHH		14.1622210691
443PhosphorylationACESVIDSSAFGEGK
HHHHHHCHHHCCCCC		16.6722210691
444PhosphorylationCESVIDSSAFGEGKA
HHHHHCHHHCCCCCC		24.7022210691
471PhosphorylationNVATRLSSIQLGQSE
HHHHHHHHHHCCCCH		20.95-
548PhosphorylationSAVSPSESVAMISRS
CCCCHHHHHHHHCHH		21.3622468782
620UbiquitinationTVTPNIVKQTIGRSH
CCCHHHHHHHHCCCC		37.62-
646AcetylationGCWGHHMKSPSFRSI
CCCCCCCCCCCHHHH		55.667675309
647PhosphorylationCWGHHMKSPSFRSIR
CCCCCCCCCCHHHHH		20.4324719451
665PhosphorylationKLNHFPGSFQIGRKD
HHCCCCCCCCCCCHH		17.76-
688UbiquitinationMQSRFGKKEFSFFPQ
HHHHHCCCCCCCCCH		65.4521890473
691PhosphorylationRFGKKEFSFFPQSFI
HHCCCCCCCCCHHHC		27.378724849
696PhosphorylationEFSFFPQSFILPQDA
CCCCCCHHHCCHHHH		17.9422817900
768PhosphorylationSKFDLRIYVYVTSYD
CEEEEEEEEEEEECC		4.55-
770PhosphorylationFDLRIYVYVTSYDPL
EEEEEEEEEEECCCC		4.88-
774PhosphorylationIYVYVTSYDPLRIYL
EEEEEEECCCCEEEE		16.53-
811PhosphorylationKFMHLTNYSVNKKNA
HHHHHHHCCCCCCCH		14.5724275569
812PhosphorylationFMHLTNYSVNKKNAE
HHHHHHCCCCCCCHH		22.6824275569
820PhosphorylationVNKKNAEYQANADEM
CCCCCHHHHCCHHHH		15.5424275569
833UbiquitinationEMACQGHKWALKALW
HHHHHHHHHHHHHHH		40.77-
844PhosphorylationKALWNYLSQKGVNSD
HHHHHHHHHCCCCCH		21.3424114839
856UbiquitinationNSDAIWEKIKDVVVK
CCHHHHHHHHHHHHH		39.81-
864PhosphorylationIKDVVVKTIISSEPY
HHHHHHHHHHCCCHH		16.3719835603
867PhosphorylationVVVKTIISSEPYVTS
HHHHHHHCCCHHHHH		25.4619835603
871PhosphorylationTIISSEPYVTSLLKM
HHHCCCHHHHHHHHH		16.5919835603
873PhosphorylationISSEPYVTSLLKMYV
HCCCHHHHHHHHHHH		14.0729759185
874PhosphorylationSSEPYVTSLLKMYVR
CCCHHHHHHHHHHHC		22.9724719451
879PhosphorylationVTSLLKMYVRRPYSC
HHHHHHHHHCCCCCH		6.8229759185
981UbiquitinationVTAQKMKKAYYLTQK
CCHHHHHHHHHHHCC		37.82-
1062UbiquitinationKYHGNKLKGVDLLRS
HHCCCCCCHHHHHHH		59.50-
1072PhosphorylationDLLRSWCYKGFHMGV
HHHHHHHHCCCCCCC		14.1120049867
1108UbiquitinationVILNAFSKSETSKLG
HHHHCCCHHHHCCCC		45.95-
1118PhosphorylationTSKLGKQSSCEVSLL
HCCCCCCCCCEEEEE		40.2028348404
1119PhosphorylationSKLGKQSSCEVSLLL
CCCCCCCCCEEEEEE		16.2928348404
1135PhosphorylationEDGTTPKSKKTQAGL
CCCCCCCCCCCCCCC		40.3629759185
1136UbiquitinationDGTTPKSKKTQAGLS
CCCCCCCCCCCCCCC		67.00-
1137UbiquitinationGTTPKSKKTQAGLSP
CCCCCCCCCCCCCCC		53.62-
1143PhosphorylationKKTQAGLSPYPQKPS
CCCCCCCCCCCCCCC		22.8225159151
1160UbiquitinationKDSEDTSKEPSLSTQ
CCCCCCCCCCCCCCC		75.61-
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 TTLL4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTLL4_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 TTLL4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TTLL4_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 TTLL4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-9, AND MASSSPECTROMETRY.

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