TTLL5_HUMAN - dbPTM
TTLL5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTLL5_HUMAN
UniProt AC Q6EMB2
Protein Name Tubulin polyglutamylase TTLL5
Gene Name TTLL5
Organism Homo sapiens (Human).
Sequence Length 1281
Subcellular Localization Cell projection, cilium . Cytoplasm, cytoskeleton, cilium basal body . Nucleus . Cytoplasm . Localized to the base of the connecting cilium between the basal body and the adjacent daughter centriole of the cilium. In osteosarcoma cells, found in both
Protein Description Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Required for CCSAP localization to both spindle and cilia microtubules. Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction. [PubMed: 17116691]
Protein Sequence MPIVMARDLEETASSSEDEEVISQEDHPCIMWTGGCRRIPVLVFHADAILTKDNNIRVIGERYHLSYKIVRTDSRLVRSILTAHGFHEVHPSSTDYNLMWTGSHLKPFLLRTLSEAQKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKAFHILPQTFLLPAEYAEFCNSYSKDRGPWIVKPVASSRGRGVYLINNPNQISLEENILVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGAKNIRNQFMHLTNYSVNKKSGDYVSCDDPEVEDYGNKWSMSAMLRYLKQEGRDTTALMAHVEDLIIKTIISAELAIATACKTFVPHRSSCFELYGFDVLIDSTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVVGFVCQDPAQRASTRPIYPTFESSRRNPFQKPQRCRPLSASDAEMKNLVGSAREKGPGKLGGSVLGLSMEEIKVLRRVKEENDRRGGFIRIFPTSETWEIYGSYLEHKTSMNYMLATRLFQDRMTADGAPELKIESLNSKAKLHAALYERKLLSLEVRKRRRRSSRLRAMRPKYPVITQPAEMNVKTETESEEEEEVALDNEDEEQEASQEESAGFLRENQAKYTPSLTALVENTPKENSMKVREWNNKGGHCCKLETQELEPKFNLMQILQDNGNLSKMQARIAFSAYLQHVQIRLMKDSGGQTFSASWAAKEDEQMELVVRFLKRASNNLQHSLRMVLPSRRLALLERRRILAHQLGDFIIVYNKETEQMAEKKSKKKVEEEEEDGVNMENFQEFIRQASEAELEEVLTFYTQKNKSASVFLGTHSKISKNNNNYSDSGAKGDHPETIMEEVKIKPPKQQQTTEIHSDKLSRFTTSAEKEAKLVYSNSSSGPTATLQKIPNTHLSSVTTSDLSPGPCHHSSLSQIPSAIPSMPHQPTILLNTVSASASPCLHPGAQNIPSPTGLPRCRSGSHTIGPFSSFQSAAHIYSQKLSRPSSAKAGSCYLNKHHSGIAKTQKEGEDASLYSKRYNQSMVTAELQRLAEKQAARQYSPSSHINLLTQQVTNLNLATGIINRSSASAPPTLRPIISPSGPTWSTQSDPQAPENHSSSPGSRSLQTGGFAWEGEVENNVYSQATGVVPQHKYHPTAGSYQLQFALQQLEQQKLQSRQLLDQSRARHQAIFGSQTLPNSNLWTMNNGAGCRISSATASGQKPTTLPQKVVPPPSSCASLVPKPPPNHEQVLRRATSQKASKGSSAEGQLNGLQSSLNPAAFVPITSSTDPAHTKI
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
118UbiquitinationRTLSEAQKVNHFPRS
HHHCHHHHCCCCCCC		52.64-
125PhosphorylationKVNHFPRSYELTRKD
HCCCCCCCHHCCCHH		24.1727251275
129PhosphorylationFPRSYELTRKDRLYK
CCCCHHCCCHHHHHH		24.5927251275
180UbiquitinationDRGPWIVKPVASSRG
CCCCCEEECCCCCCC		25.33-
227PhosphorylationFKFDVRLYVLVTSYD
CCEEEEEEEEEECCC		4.91-
233PhosphorylationLYVLVTSYDPLVIYL
EEEEEECCCCEEEEE		16.53-
239PhosphorylationSYDPLVIYLYEEGLA
CCCCEEEEEECCCCH		8.85-
241PhosphorylationDPLVIYLYEEGLARF
CCEEEEEECCCCHHE		8.58-
256 (in isoform 3)Phosphorylation-35.3022210691
258UbiquitinationVRYDQGAKNIRNQFM
EECCCCCHHHHHHHH		60.78-
274UbiquitinationLTNYSVNKKSGDYVS
HHCCCCCCCCCCCEE		46.2729967540
275UbiquitinationTNYSVNKKSGDYVSC
HCCCCCCCCCCCEEC		55.2429967540
295PhosphorylationEDYGNKWSMSAMLRY
CCCCCCCCHHHHHHH		12.4122210691
297PhosphorylationYGNKWSMSAMLRYLK
CCCCCCHHHHHHHHH		12.6622210691
302PhosphorylationSMSAMLRYLKQEGRD
CHHHHHHHHHHCCCC		17.8122210691
414PhosphorylationSTRPIYPTFESSRRN
CCCCCCCCCHHHCCC		24.06-
433PhosphorylationPQRCRPLSASDAEMK
CCCCCCCCCCHHHHH		28.5425850435
435PhosphorylationRCRPLSASDAEMKNL
CCCCCCCCHHHHHHH		33.7025850435
440UbiquitinationSASDAEMKNLVGSAR
CCCHHHHHHHHHCHH		38.34-
449AcetylationLVGSAREKGPGKLGG
HHHCHHHHCCCCCCC		65.9219815563
453UbiquitinationAREKGPGKLGGSVLG
HHHHCCCCCCCHHCC		47.2829967540
457PhosphorylationGPGKLGGSVLGLSME
CCCCCCCHHCCCCHH		16.6330622161
462PhosphorylationGGSVLGLSMEEIKVL
CCHHCCCCHHHHHHH		23.5030622161
467AcetylationGLSMEEIKVLRRVKE
CCCHHHHHHHHHHHH		38.2019815571
515PhosphorylationMLATRLFQDRMTADG
HHHHHHHHHCCCCCC		41.8317081983
519PhosphorylationRLFQDRMTADGAPEL
HHHHHCCCCCCCCCC		23.6122817900
534UbiquitinationKIESLNSKAKLHAAL
EEECCCCHHHHHHHH		48.7629967540
542PhosphorylationAKLHAALYERKLLSL
HHHHHHHHHHHHHHH		14.68-
548PhosphorylationLYERKLLSLEVRKRR
HHHHHHHHHHHHHHH		32.6822210691
558PhosphorylationVRKRRRRSSRLRAMR
HHHHHHHHHHHHHHC		20.2823882029
559PhosphorylationRKRRRRSSRLRAMRP
HHHHHHHHHHHHHCC		33.2623882029
581PhosphorylationPAEMNVKTETESEEE
CCCCCCCCCCCCHHH		43.8026657352
583PhosphorylationEMNVKTETESEEEEE
CCCCCCCCCCHHHHH		50.4726657352
585PhosphorylationNVKTETESEEEEEVA
CCCCCCCCHHHHHHC		58.7026657352
617UbiquitinationFLRENQAKYTPSLTA
HHHHCHHHCCCCHHH		39.6329967540
619PhosphorylationRENQAKYTPSLTALV
HHCHHHCCCCHHHHH		12.9930622161
621PhosphorylationNQAKYTPSLTALVEN
CHHHCCCCHHHHHHC		30.4728348404
623PhosphorylationAKYTPSLTALVENTP
HHCCCCHHHHHHCCC		23.4530622161
629PhosphorylationLTALVENTPKENSMK
HHHHHHCCCCCCCCC		23.4128122231
643UbiquitinationKVREWNNKGGHCCKL
CCEECCCCCCCCCCC		64.1629967540
649UbiquitinationNKGGHCCKLETQELE
CCCCCCCCCCCCCCC		55.5429967540
652PhosphorylationGHCCKLETQELEPKF
CCCCCCCCCCCCCCC		37.4727050516
658UbiquitinationETQELEPKFNLMQIL
CCCCCCCCCCHHHHH		37.1929967540
723PhosphorylationVRFLKRASNNLQHSL
HHHHHHHHHHHHHHH		30.2224719451
736PhosphorylationSLRMVLPSRRLALLE
HHHHHCCHHHHHHHH		26.3524719451
759PhosphorylationLGDFIIVYNKETEQM
HCCEEEEEEHHHHHH		15.31-
796PhosphorylationQEFIRQASEAELEEV
HHHHHHHHHHHHHHH		29.06-
810UbiquitinationVLTFYTQKNKSASVF
HHHHHHCCCCCEEEE		59.5529967540
812UbiquitinationTFYTQKNKSASVFLG
HHHHCCCCCEEEEEE		55.2029967540
823UbiquitinationVFLGTHSKISKNNNN
EEEECCCCCCCCCCC		43.3129967540
826UbiquitinationGTHSKISKNNNNYSD
ECCCCCCCCCCCCCC		68.14-
837UbiquitinationNYSDSGAKGDHPETI
CCCCCCCCCCCHHHH		69.2829967540
865UbiquitinationTTEIHSDKLSRFTTS
CEEECHHHHHHCCCC		51.9129967540
875UbiquitinationRFTTSAEKEAKLVYS
HCCCCHHHHHEEEEC		63.79-
878UbiquitinationTSAEKEAKLVYSNSS
CCHHHHHEEEECCCC		39.31-
881PhosphorylationEKEAKLVYSNSSSGP
HHHHEEEECCCCCCC		16.7525159151
965PhosphorylationTGLPRCRSGSHTIGP
CCCCCCCCCCCCCCC		48.5524719451
994UbiquitinationLSRPSSAKAGSCYLN
CCCCCCCCCCCCCCC		56.0529967540
997PhosphorylationPSSAKAGSCYLNKHH
CCCCCCCCCCCCCCC		12.40-
1002UbiquitinationAGSCYLNKHHSGIAK
CCCCCCCCCCCCCCC		39.8529967540
1009UbiquitinationKHHSGIAKTQKEGED
CCCCCCCCCCCCCCC		49.9529967540
1012UbiquitinationSGIAKTQKEGEDASL
CCCCCCCCCCCCCHH		73.29-
1020PhosphorylationEGEDASLYSKRYNQS
CCCCCHHHHHHHCHH		15.0625839225
1022UbiquitinationEDASLYSKRYNQSMV
CCCHHHHHHHCHHHH		45.4029967540
1039UbiquitinationELQRLAEKQAARQYS
HHHHHHHHHHHHHCC		39.3629967540
1045PhosphorylationEKQAARQYSPSSHIN
HHHHHHHCCCCHHHH		19.5924043423
1046PhosphorylationKQAARQYSPSSHINL
HHHHHHCCCCHHHHH		15.2324043423
1048PhosphorylationAARQYSPSSHINLLT
HHHHCCCCHHHHHHH		28.7124043423
1049PhosphorylationARQYSPSSHINLLTQ
HHHCCCCHHHHHHHH		31.6024043423
1055PhosphorylationSSHINLLTQQVTNLN
CHHHHHHHHHHHHCH		21.8124043423
1059PhosphorylationNLLTQQVTNLNLATG
HHHHHHHHHCHHCCC		29.6524043423
1065PhosphorylationVTNLNLATGIINRSS
HHHCHHCCCCCCCCC		31.8924043423
1084PhosphorylationPTLRPIISPSGPTWS
CCCCCCCCCCCCCCC		17.4625332170
1091PhosphorylationSPSGPTWSTQSDPQA
CCCCCCCCCCCCCCC		21.0325332170
1092PhosphorylationPSGPTWSTQSDPQAP
CCCCCCCCCCCCCCC		24.5325332170
1139PhosphorylationGVVPQHKYHPTAGSY
CCCCCCCCCCCCCHH		15.7729496907
1142PhosphorylationPQHKYHPTAGSYQLQ
CCCCCCCCCCHHHHH		30.2729496907
1159UbiquitinationLQQLEQQKLQSRQLL
HHHHHHHHHHHHHHH		48.46-
1199PhosphorylationNGAGCRISSATASGQ
CCCCCEEEECCCCCC		8.45-
1200PhosphorylationGAGCRISSATASGQK
CCCCEEEECCCCCCC		27.54-
1207UbiquitinationSATASGQKPTTLPQK
ECCCCCCCCCCCCCC		48.10-
1221O-linked_GlycosylationKVVPPPSSCASLVPK
CCCCCCCHHCCCCCC		21.3430059200
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 TTLL5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTLL5_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 TTLL5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CREB3_HUMANCREB3physical
20546900
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615860Cone-rod dystrophy 19 (CORD19)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTLL5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519, AND MASSSPECTROMETRY.

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