TTBK2_HUMAN - dbPTM
TTBK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTBK2_HUMAN
UniProt AC Q6IQ55
Protein Name Tau-tubulin kinase 2
Gene Name TTBK2
Organism Homo sapiens (Human).
Sequence Length 1244
Subcellular Localization Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytosol. Nucleus. Localizes to the transition zone in primary cilia in response to cell cyc
Protein Description Serine/threonine kinase that acts as a key regulator of ciliogenesis: controls the initiation of ciliogenesis by binding to the distal end of the basal body and promoting the removal of CCP110, which caps the mother centriole, leading to the recruitment of IFT proteins, which build the ciliary axoneme. Has some substrate preference for proteins that are already phosphorylated on a Tyr residue at the +2 position relative to the phosphorylation site. Able to phosphorylate tau on serines in vitro..
Protein Sequence MSGGGEQLDILSVGILVKERWKVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFDNSIKTFGVIESDPFDWEKTGNDGSLTTTTTSTTPQLHTRLTPAAIGIANATPIPGDLLRENTDEVFPDEQLSDGENGIPVGVSPDKLPGSLGHPRPQEKDVWEEMDANKNKIKLGICKAATEEENSHGQANGLLNAPSLGSPIRVRSEITQPDRDIPLVRKLRSIHSFELEKRLTLEPKPDTDKFLETCLEKMQKDTSAGKESILPALLHKPCVPAVSRTDHIWHYDEEYLPDASKPASANTPEQADGGGSNGFIAVNLSSCKQEIDSKEWVIVDKEQDLQDFRTNEAVGHKTTGSPSDEEPEVLQVLEASPQDEKLQLGPWAENDHLKKETSGVVLALSAEGPPTAASEQYTDRLELQPGAASQFIAATPTSLMEAQAEGPLTAITIPRPSVASTQSTSGSFHCGQQPEKKDLQPMEPTVELYSPRENFSGLVVTEGEPPSGGSRTDLGLQIDHIGHDMLPNIRESNKSQDLGPKELPDHNRLVVREFENLPGETEEKSILLESDNEDEKLSRGQHCIEISSLPGDLVIVEKDHSATTEPLDVTKTQTFSVVPNQDKNNEIMKLLTVGTSEISSRDIDPHVEGQIGQVAEMQKNKISKDDDIMSEDLPGHQGDLSTFLHQEGKREKITPRNGELFHCVSENEHGAPTRKDMVRSSFVTRHSRIPVLAQEIDSTLESSSPVSAKEKLLQKKAYQPDLVKLLVEKRQFKSFLGDLSSASDKLLEEKLATVPAPFCEEEVLTPFSRLTVDSHLSRSAEDSFLSPIISQSRKSKIPRPVSWVNTDQVNSSTSSQFFPRPPPGKPPTRPGVEARLRRYKVLGSSNSDSDLFSRLAQILQNGSQKPRSTTQCKSPGSPHNPKTPPKSPVVPRRSPSASPRSSSLPRTSSSSPSRAGRPHHDQRSSSPHLGRSKSPPSHSGSSSSRRSCQQEHCKPSKNGLKGSGSLHHHSASTKTPQGKSKPASKLSR
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
2Phosphorylation------MSGGGEQLD
------CCCCCCCCE
58.4024043423
12PhosphorylationGEQLDILSVGILVKE
CCCCEEEEEEHHHHH
20.7324043423
70SumoylationMEVAVLKKLQGKDHV
HHHHHHHHHCCCCCE
41.71-
70SumoylationMEVAVLKKLQGKDHV
HHHHHHHHHCCCCCE
41.71-
109PhosphorylationADLRRSQSRGTFTIS
HHHHHHHCCCCEEEH
33.6424043423
112PhosphorylationRRSQSRGTFTISTTL
HHHHCCCCEEEHHHH
19.2524043423
114PhosphorylationSQSRGTFTISTTLRL
HHCCCCEEEHHHHHH
17.5424043423
116PhosphorylationSRGTFTISTTLRLGR
CCCCEEEHHHHHHHH
16.5724043423
117PhosphorylationRGTFTISTTLRLGRQ
CCCEEEHHHHHHHHH
26.4624043423
118PhosphorylationGTFTISTTLRLGRQI
CCEEEHHHHHHHHHH
11.7724043423
211PhosphorylationGRHDDLWSLFYMLVE
CCCHHHHHHHHHHHH
18.85-
242PhosphorylationVGSIKERYDHRLMLK
HCCHHHHHCHHHHHH
19.72-
305PhosphorylationEKTGNDGSLTTTTTS
HHCCCCCCCEEEECC
25.9627732954
307PhosphorylationTGNDGSLTTTTTSTT
CCCCCCCEEEECCCC
24.6427732954
308PhosphorylationGNDGSLTTTTTSTTP
CCCCCCEEEECCCCC
27.6927732954
309PhosphorylationNDGSLTTTTTSTTPQ
CCCCCEEEECCCCCC
23.8827732954
310PhosphorylationDGSLTTTTTSTTPQL
CCCCEEEECCCCCCC
19.3627732954
311PhosphorylationGSLTTTTTSTTPQLH
CCCEEEECCCCCCCC
23.2227732954
312PhosphorylationSLTTTTTSTTPQLHT
CCEEEECCCCCCCCC
28.3527732954
313PhosphorylationLTTTTTSTTPQLHTR
CEEEECCCCCCCCCC
40.1627732954
314PhosphorylationTTTTTSTTPQLHTRL
EEEECCCCCCCCCCC
14.5928985074
319PhosphorylationSTTPQLHTRLTPAAI
CCCCCCCCCCCHHHH
35.6527732954
322PhosphorylationPQLHTRLTPAAIGIA
CCCCCCCCHHHHCCC
13.9527050516
332PhosphorylationAIGIANATPIPGDLL
HHCCCCCCCCCCCHH
22.8927080861
371PhosphorylationSPDKLPGSLGHPRPQ
CCCCCCCCCCCCCCC
29.2825159151
402PhosphorylationLGICKAATEEENSHG
EEEEHHHCCCCCCCC
49.1125850435
407PhosphorylationAATEEENSHGQANGL
HHCCCCCCCCCCCCC
32.0725850435
419PhosphorylationNGLLNAPSLGSPIRV
CCCCCCCCCCCCEEE
42.8425921289
422PhosphorylationLNAPSLGSPIRVRSE
CCCCCCCCCEEEECC
23.5825921289
428PhosphorylationGSPIRVRSEITQPDR
CCCEEEECCCCCCCC
30.4125850435
431PhosphorylationIRVRSEITQPDRDIP
EEEECCCCCCCCCCH
29.9625850435
445PhosphorylationPLVRKLRSIHSFELE
HHHHHHHCCCCEEEE
34.7823401153
448PhosphorylationRKLRSIHSFELEKRL
HHHHCCCCEEEECCE
20.8125159151
463PhosphorylationTLEPKPDTDKFLETC
ECCCCCCHHHHHHHH
50.01-
476UbiquitinationTCLEKMQKDTSAGKE
HHHHHHHHCCCCCHH
60.52-
478PhosphorylationLEKMQKDTSAGKESI
HHHHHHCCCCCHHCH
27.7528450419
479PhosphorylationEKMQKDTSAGKESIL
HHHHHCCCCCHHCHH
45.2028450419
484PhosphorylationDTSAGKESILPALLH
CCCCCHHCHHHHHHC
32.6728450419
499PhosphorylationKPCVPAVSRTDHIWH
CCCCCCCCCCCCEEE
31.4120068231
574PhosphorylationNEAVGHKTTGSPSDE
CCCCCCCCCCCCCCC
30.6227732954
575PhosphorylationEAVGHKTTGSPSDEE
CCCCCCCCCCCCCCC
40.2327732954
577PhosphorylationVGHKTTGSPSDEEPE
CCCCCCCCCCCCCCH
21.0927732954
579PhosphorylationHKTTGSPSDEEPEVL
CCCCCCCCCCCCHHH
60.3927732954
592PhosphorylationVLQVLEASPQDEKLQ
HHHHHHCCCCCCCCC
17.4527732954
613PhosphorylationNDHLKKETSGVVLAL
CHHCCCCCCCEEEEE
39.3922468782
614PhosphorylationDHLKKETSGVVLALS
HHCCCCCCCEEEEEE
30.59-
621PhosphorylationSGVVLALSAEGPPTA
CCEEEEEECCCCCCC
20.76-
633PhosphorylationPTAASEQYTDRLELQ
CCCCCHHHCCCEECC
13.4222468782
668PhosphorylationEGPLTAITIPRPSVA
CCCEEEEEECCCCCC
23.5924719451
701PhosphorylationDLQPMEPTVELYSPR
CCCCCCCEEEEECCC
17.2022468782
706PhosphorylationEPTVELYSPRENFSG
CCEEEEECCCCCCCC
30.0628122231
751PhosphorylationNIRESNKSQDLGPKE
CHHHCCCCCCCCCCC
32.93-
777PhosphorylationFENLPGETEEKSILL
ECCCCCCCCCEEEEE
56.1927732954
781PhosphorylationPGETEEKSILLESDN
CCCCCCEEEEEECCC
23.0330576142
786PhosphorylationEKSILLESDNEDEKL
CEEEEEECCCCCCCC
45.7830266825
794PhosphorylationDNEDEKLSRGQHCIE
CCCCCCCCCCCCEEE
45.4925159151
817PhosphorylationVIVEKDHSATTEPLD
EEEECCCCCCCCCCC
37.1329255136
819PhosphorylationVEKDHSATTEPLDVT
EECCCCCCCCCCCCC
34.4129255136
820O-linked_GlycosylationEKDHSATTEPLDVTK
ECCCCCCCCCCCCCC
35.01OGP
820PhosphorylationEKDHSATTEPLDVTK
ECCCCCCCCCCCCCC
35.0128450419
828PhosphorylationEPLDVTKTQTFSVVP
CCCCCCCCEEEEECC
24.39-
830PhosphorylationLDVTKTQTFSVVPNQ
CCCCCCEEEEECCCC
24.10-
845AcetylationDKNNEIMKLLTVGTS
CCCCCEEEHEEECCC
46.1119828417
851PhosphorylationMKLLTVGTSEISSRD
EEHEEECCCCCCCCC
20.8927732954
852PhosphorylationKLLTVGTSEISSRDI
EHEEECCCCCCCCCC
27.3127732954
855PhosphorylationTVGTSEISSRDIDPH
EECCCCCCCCCCCCC
18.4427732954
856PhosphorylationVGTSEISSRDIDPHV
ECCCCCCCCCCCCCC
39.3727732954
877AcetylationVAEMQKNKISKDDDI
HHHHHHCCCCCCCCH
56.2319828425
879PhosphorylationEMQKNKISKDDDIMS
HHHHCCCCCCCCHHC
31.48-
936PhosphorylationTRKDMVRSSFVTRHS
CHHHHHHHHHHCCCC
19.4023322592
937PhosphorylationRKDMVRSSFVTRHSR
HHHHHHHHHHCCCCC
17.1123322592
940PhosphorylationMVRSSFVTRHSRIPV
HHHHHHHCCCCCCCH
22.2124719451
943PhosphorylationSSFVTRHSRIPVLAQ
HHHHCCCCCCCHHHH
28.7223322592
958PhosphorylationEIDSTLESSSPVSAK
HHHHHCCCCCCCCHH
38.9527732954
959PhosphorylationIDSTLESSSPVSAKE
HHHHCCCCCCCCHHH
29.3227732954
960PhosphorylationDSTLESSSPVSAKEK
HHHCCCCCCCCHHHH
38.3027732954
963PhosphorylationLESSSPVSAKEKLLQ
CCCCCCCCHHHHHHH
36.6927732954
985UbiquitinationLVKLLVEKRQFKSFL
HHHHHHHHHHHHHHH
43.98-
1035PhosphorylationVDSHLSRSAEDSFLS
CCCHHHCCCCCCCHH
32.4129083192
1039PhosphorylationLSRSAEDSFLSPIIS
HHCCCCCCCHHHHHC
21.4221712546
1042PhosphorylationSAEDSFLSPIISQSR
CCCCCCHHHHHCCCC
16.4321712546
1046PhosphorylationSFLSPIISQSRKSKI
CCHHHHHCCCCCCCC
23.8723403867
1048PhosphorylationLSPIISQSRKSKIPR
HHHHHCCCCCCCCCC
34.5823403867
1101PhosphorylationRYKVLGSSNSDSDLF
HEEECCCCCCCHHHH
38.2628857561
1103PhosphorylationKVLGSSNSDSDLFSR
EECCCCCCCHHHHHH
40.2021548880
1105PhosphorylationLGSSNSDSDLFSRLA
CCCCCCCHHHHHHHH
35.7127732954
1130PhosphorylationRSTTQCKSPGSPHNP
CCCCCCCCCCCCCCC
41.9627732954
1133PhosphorylationTQCKSPGSPHNPKTP
CCCCCCCCCCCCCCC
26.7727732954
1139PhosphorylationGSPHNPKTPPKSPVV
CCCCCCCCCCCCCCC
46.1920363803
1143PhosphorylationNPKTPPKSPVVPRRS
CCCCCCCCCCCCCCC
28.8020363803
1150PhosphorylationSPVVPRRSPSASPRS
CCCCCCCCCCCCCCC
25.2030266825
1152PhosphorylationVVPRRSPSASPRSSS
CCCCCCCCCCCCCCC
42.5030266825
1154PhosphorylationPRRSPSASPRSSSLP
CCCCCCCCCCCCCCC
25.7830266825
1157PhosphorylationSPSASPRSSSLPRTS
CCCCCCCCCCCCCCC
27.8826699800
1158PhosphorylationPSASPRSSSLPRTSS
CCCCCCCCCCCCCCC
36.8526699800
1159PhosphorylationSASPRSSSLPRTSSS
CCCCCCCCCCCCCCC
43.5724719451
1180PhosphorylationRPHHDQRSSSPHLGR
CCCCCCCCCCCCCCC
29.5428348404
1181PhosphorylationPHHDQRSSSPHLGRS
CCCCCCCCCCCCCCC
50.5128348404
1182PhosphorylationHHDQRSSSPHLGRSK
CCCCCCCCCCCCCCC
20.0028348404
1240PhosphorylationQGKSKPASKLSR---
CCCCCCCHHHCC---
42.53-
1243PhosphorylationSKPASKLSR------
CCCCHHHCC------
39.4124719451

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 TTBK2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTBK2_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 TTBK2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CE164_HUMANCEP164physical
22863007

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604432Spinocerebellar ataxia 11 (SCA11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTBK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, AND MASSSPECTROMETRY.

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