TBCK_HUMAN - dbPTM
TBCK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBCK_HUMAN
UniProt AC Q8TEA7
Protein Name TBC domain-containing protein kinase-like protein
Gene Name TBCK {ECO:0000303|PubMed:12471243}
Organism Homo sapiens (Human).
Sequence Length 893
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, spindle . Midbody . Mainly localized in the cytoplasm during interphase. During metaphase, TBCK accumulates at the mitotic spindle. At the end of mitosis, it is detected at the midbody.
Protein Description Involved in the modulation of mTOR signaling and expression of mTOR complex components. [PubMed: 27040691]
Protein Sequence MFPLKDAEMGAFTFFASALPHDVCGSNGLPLTPNSIKILGRFQILKTITHPRLCQYVDISRGKHERLVVVAEHCERSLEDLLRERKPVSCSTVLCIAFEVLQGLQYMNKHGIVHRALSPHNILLDRKGHIKLAKFGLYHMTAHGDDVDFPIGYPSYLAPEVIAQGIFKTTDHMPSKKPLPSGPKSDVWSLGIILFELCVGRKLFQSLDISERLKFLLTLDCVDDTLIVLAEEHGCLDIIKELPETVIDLLNKCLTFHPSKRPTPDQLMKDKVFSEVSPLYTPFTKPASLFSSSLRCADLTLPEDISQLCKDINNDYLAERSIEEVYYLWCLAGGDLEKELVNKEIIRSKPPICTLPNFLFEDGESFGQGRDRSSLLDDTTVTLSLCQLRNRLKDVGGEAFYPLLEDDQSNLPHSNSNNELSAAATLPLIIREKDTEYQLNRIILFDRLLKAYPYKKNQIWKEARVDIPPLMRGLTWAALLGVEGAIHAKYDAIDKDTPIPTDRQIEVDIPRCHQYDELLSSPEGHAKFRRVLKAWVVSHPDLVYWQGLDSLCAPFLYLNFNNEALAYACMSAFIPKYLYNFFLKDNSHVIQEYLTVFSQMIAFHDPELSNHLNEIGFIPDLYAIPWFLTMFTHVFPLHKIFHLWDTLLLGNSSFPFCIGVAILQQLRDRLLANGFNECILLFSDLPEIDIERCVRESINLFCWTPKSATYRQHAQPPKPSSDSSGGRSSAPYFSAECPDPPKTDLSRESIPLNDLKSEVSPRISAEDLIDLCELTVTGHFKTPSKKTKSSKPKLLVVDIRNSEDFIRGHISGSINIPFSAAFTAEGELTQGPYTAMLQNFKGKVIVIVGHVAKHTAEFAAHLVKMKYPRICILDGGINKIKPTGLLTIPSPQI
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
77PhosphorylationVAEHCERSLEDLLRE
EHHHHHHHHHHHHHH		17.5127794612
118PhosphorylationGIVHRALSPHNILLD
CCCCCCCCHHHEEEC		24.11-
138 (in isoform 2)Phosphorylation-7.0225332170
141 (in isoform 2)Phosphorylation-11.3725332170
153PhosphorylationDVDFPIGYPSYLAPE
CCCCCCCCHHHCCHH		6.96-
169PhosphorylationIAQGIFKTTDHMPSK
HHCCCCCCCCCCCCC		27.06-
271UbiquitinationPDQLMKDKVFSEVSP
HHHHHHCCCHHCCCC		39.39-
285UbiquitinationPLYTPFTKPASLFSS
CCCCCCCCCHHHHCC		38.68-
343UbiquitinationLEKELVNKEIIRSKP
HHHHHHCHHHHHCCC		42.69-
349UbiquitinationNKEIIRSKPPICTLP
CHHHHHCCCCCCCCC		44.99-
409PhosphorylationPLLEDDQSNLPHSNS
HHHCCCCCCCCCCCC		47.5326657352
414PhosphorylationDQSNLPHSNSNNELS
CCCCCCCCCCCCCCC		39.7627251275
416PhosphorylationSNLPHSNSNNELSAA
CCCCCCCCCCCCCHH		44.0124076635
433UbiquitinationLPLIIREKDTEYQLN
HCEEECCCCCHHHHH		61.16-
450UbiquitinationILFDRLLKAYPYKKN
HHHHHHHHHCCCCHH		50.93-
456UbiquitinationLKAYPYKKNQIWKEA
HHHCCCCHHHHHHHH		48.52-
461UbiquitinationYKKNQIWKEARVDIP
CCHHHHHHHHCCCCH		43.03-
495UbiquitinationAKYDAIDKDTPIPTD
HCCCCCCCCCCCCCC		58.34-
503MethylationDTPIPTDRQIEVDIP
CCCCCCCCEEEEECC		41.68115918281
704PhosphorylationSINLFCWTPKSATYR
HCEEEEECCCCCCHH		23.2429083192
706UbiquitinationNLFCWTPKSATYRQH
EEEEECCCCCCHHHC		45.40-
707PhosphorylationLFCWTPKSATYRQHA
EEEECCCCCCHHHCC		27.3529083192
709PhosphorylationCWTPKSATYRQHAQP
EECCCCCCHHHCCCC		26.7429083192
710PhosphorylationWTPKSATYRQHAQPP
ECCCCCCHHHCCCCC		14.1629083192
718UbiquitinationRQHAQPPKPSSDSSG
HHCCCCCCCCCCCCC		65.30-
728PhosphorylationSDSSGGRSSAPYFSA
CCCCCCCCCCCCEEC		33.8421945579
729PhosphorylationDSSGGRSSAPYFSAE
CCCCCCCCCCCEECC		31.7221945579
732PhosphorylationGGRSSAPYFSAECPD
CCCCCCCCEECCCCC		15.1921945579
734PhosphorylationRSSAPYFSAECPDPP
CCCCCCEECCCCCCC		19.8121945579
743PhosphorylationECPDPPKTDLSRESI
CCCCCCCCCCCCCCC		48.2026552605
746PhosphorylationDPPKTDLSRESIPLN
CCCCCCCCCCCCCHH		36.4926552605
756UbiquitinationSIPLNDLKSEVSPRI
CCCHHHHCCCCCCCC		47.65-
757PhosphorylationIPLNDLKSEVSPRIS
CCHHHHCCCCCCCCC		50.9920860994
760PhosphorylationNDLKSEVSPRISAED
HHHCCCCCCCCCHHH		12.3820860994
787PhosphorylationFKTPSKKTKSSKPKL
CCCCCCCCCCCCCEE		39.6429083192
789PhosphorylationTPSKKTKSSKPKLLV
CCCCCCCCCCCEEEE		49.1529083192
790PhosphorylationPSKKTKSSKPKLLVV
CCCCCCCCCCEEEEE		55.3129083192
879UbiquitinationILDGGINKIKPTGLL
EEECCCCCCCCCCCE		50.62-
881UbiquitinationDGGINKIKPTGLLTI
ECCCCCCCCCCCEEE		37.83-
883PhosphorylationGINKIKPTGLLTIPS
CCCCCCCCCCEEECC		35.1423403867
887PhosphorylationIKPTGLLTIPSPQI-
CCCCCCEEECCCCC-		35.5729255136
890PhosphorylationTGLLTIPSPQI----
CCCEEECCCCC----		26.1129255136
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 TBCK_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBCK_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 TBCK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 TBCK_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-890, AND MASSSPECTROMETRY.

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