TBCE_HUMAN - dbPTM
TBCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBCE_HUMAN
UniProt AC Q15813
Protein Name Tubulin-specific chaperone E
Gene Name TBCE
Organism Homo sapiens (Human).
Sequence Length 527
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton.
Protein Description Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation. Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network..
Protein Sequence MSDTLTADVIGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFKCRHPTGGSFIRPNKVNFGTDFLTAIKNRYVLEDGPEEDRKEQIVTIGNKPVETIGFDSIMKQQSQLSKLQEVSLRNCAVSCAGEKGGVAEACPNIRKVDLSKNLLSSWDEVIHIADQLRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITWAEVLRCVAGCPGLEELYLESNNIFISERPTDVLQTVKLLDLSSNQLIDENQLYLIAHLPRLEQLILSDTGISSLHFPDAGIGCKTSMFPSLKYLVVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEDKEAETARLLIIASIGQLKTLNKCEILPEERRRAELDYRKAFGNEWKQAGGHKDPEKNRLSEEFLTAHPRYQFLCLKYGAPEDWELKTQQPLMLKNQLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCLLVRW
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------MSDTLTADV
------CCCCEEHHH		39.0222199227
2Acetylation------MSDTLTADV
------CCCCEEHHH		39.0219413330
4Phosphorylation----MSDTLTADVIG
----CCCCEEHHHCC		20.7822199227
6Phosphorylation--MSDTLTADVIGRR
--CCCCEEHHHCCCE		23.9320873877
48UbiquitinationWDNPERGKHDGSHEG
ECCCCCCCCCCCCCE		44.75-
60UbiquitinationHEGTVYFKCRHPTGG
CCEEEEEEEECCCCC		16.81-
60UbiquitinationHEGTVYFKCRHPTGG
CCEEEEEEEECCCCC		16.81-
65PhosphorylationYFKCRHPTGGSFIRP
EEEEECCCCCCCCCC		48.3128857561
68PhosphorylationCRHPTGGSFIRPNKV
EECCCCCCCCCCCCE		20.8828857561
86UbiquitinationTDFLTAIKNRYVLED
HHHHHHHHCCEECCC		32.67-
86UbiquitinationTDFLTAIKNRYVLED
HHHHHHHHCCEECCC		32.67-
109UbiquitinationQIVTIGNKPVETIGF
HEEEECCEECCCCCH		45.27-
121UbiquitinationIGFDSIMKQQSQLSK
CCHHHHHHHHHHHHH		43.44-
124PhosphorylationDSIMKQQSQLSKLQE
HHHHHHHHHHHHHHH		30.51-
127PhosphorylationMKQQSQLSKLQEVSL
HHHHHHHHHHHHHHH		24.55-
128UbiquitinationKQQSQLSKLQEVSLR
HHHHHHHHHHHHHHC		63.88-
128UbiquitinationKQQSQLSKLQEVSLR
HHHHHHHHHHHHHHC		63.88-
133PhosphorylationLSKLQEVSLRNCAVS
HHHHHHHHHCCCCHH		22.36-
145UbiquitinationAVSCAGEKGGVAEAC
CHHCCCCCCCHHHHC		61.11-
145AcetylationAVSCAGEKGGVAEAC
CHHCCCCCCCHHHHC		61.1125953088
152GlutathionylationKGGVAEACPNIRKVD
CCCHHHHCCCCCCCC		1.6722555962
192UbiquitinationNVSENKLKFPSGSVL
ECCCCCCCCCCCCCH		57.7621890473
192UbiquitinationNVSENKLKFPSGSVL
ECCCCCCCCCCCCCH		57.7621890473
195PhosphorylationENKLKFPSGSVLTGT
CCCCCCCCCCCHHCH		47.00-
200PhosphorylationFPSGSVLTGTLSVLK
CCCCCCHHCHHHHHH		26.43-
204PhosphorylationSVLTGTLSVLKVLVL
CCHHCHHHHHHHHHH		25.82-
301GlutathionylationFPDAGIGCKTSMFPS
CCCCCCCCCCCCCCC		4.0322555962
305SulfoxidationGIGCKTSMFPSLKYL
CCCCCCCCCCCCEEE		7.4821406390
333PhosphorylationNELEKLPSLRALSCL
HHHHCCCHHHHHHHH		40.7124719451
338AcetylationLPSLRALSCLRNPLT
CCHHHHHHHHCCCCC		15.3219608861
338PhosphorylationLPSLRALSCLRNPLT
CCHHHHHHHHCCCCC		15.3224719451
346UbiquitinationCLRNPLTKEDKEAET
HHCCCCCHHHHHHHH		72.15-
350AcetylationPLTKEDKEAETARLL
CCCHHHHHHHHHHHH		65.1519608861
350UbiquitinationPLTKEDKEAETARLL
CCCHHHHHHHHHHHH		65.1519608861
370UbiquitinationGQLKTLNKCEILPEE
HHHCCCCCCCCCHHH		36.04-
371GlutathionylationQLKTLNKCEILPEER
HHCCCCCCCCCHHHH		3.7022555962
387UbiquitinationRAELDYRKAFGNEWK
HHHHHHHHHHCHHHH		41.67-
394UbiquitinationKAFGNEWKQAGGHKD
HHHCHHHHHCCCCCC		24.88-
397UbiquitinationGNEWKQAGGHKDPEK
CHHHHHCCCCCCHHH		35.92-
408PhosphorylationDPEKNRLSEEFLTAH
CHHHCCCCHHHHHHC		31.6626055452
413PhosphorylationRLSEEFLTAHPRYQF
CCCHHHHHHCHHHHE		28.3920068231
417UbiquitinationEFLTAHPRYQFLCLK
HHHHHCHHHHEEHHH		28.19-
421UbiquitinationAHPRYQFLCLKYGAP
HCHHHHEEHHHCCCC		1.65-
424AcetylationRYQFLCLKYGAPEDW
HHHEEHHHCCCCCCC		40.4126051181
434UbiquitinationAPEDWELKTQQPLML
CCCCCCCCCCCCEEE		32.54-
438UbiquitinationWELKTQQPLMLKNQL
CCCCCCCCEEECCCE		15.21-
442UbiquitinationTQQPLMLKNQLLTLK
CCCCEEECCCEEEEE		28.78-
451AcetylationQLLTLKIKYPHQLDQ
CEEEEEECCCHHCCH		51.6623749302
451UbiquitinationQLLTLKIKYPHQLDQ
CEEEEEECCCHHCCH		51.6619608861
459UbiquitinationYPHQLDQKVLEKQLP
CCHHCCHHHHHHHCC		48.75-
463UbiquitinationLDQKVLEKQLPGSMT
CCHHHHHHHCCCCCH		53.632189047
463AcetylationLDQKVLEKQLPGSMT
CCHHHHHHHCCCCCH		53.6319608861
463UbiquitinationLDQKVLEKQLPGSMT
CCHHHHHHHCCCCCH		53.6321890473
479PhosphorylationQKVKGLLSRLLKVPV
HHHHHHHHHHHCCCH		26.4022617229
487PhosphorylationRLLKVPVSDLLLSYE
HHHCCCHHHHHHCCC		19.23-
492PhosphorylationPVSDLLLSYESPKKP
CHHHHHHCCCCCCCC		27.1627732954
493PhosphorylationVSDLLLSYESPKKPG
HHHHHHCCCCCCCCC		22.0129214152
493UbiquitinationVSDLLLSYESPKKPG
HHHHHHCCCCCCCCC		22.01-
495PhosphorylationDLLLSYESPKKPGRE
HHHHCCCCCCCCCCE		33.5125159151
502AcetylationSPKKPGREIELENDL
CCCCCCCEEEECCCH		46.89-
502AcetylationSPKKPGREIELENDL
CCCCCCCEEEECCCH		46.8919608861
514AcetylationNDLKSLQFYSVENGD
CCHHHCEEEEEECCC		6.27-
514AcetylationNDLKSLQFYSVENGD
CCHHHCEEEEEECCC		6.2719608861
514UbiquitinationNDLKSLQFYSVENGD
CCHHHCEEEEEECCC		6.2719608861
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
495SPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBCE_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 TBCE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OGFD1_HUMANOGFOD1physical
22863883
PYGL_HUMANPYGLphysical
22863883
RD23A_HUMANRAD23Aphysical
22863883
TBA1_YEASTTUB1physical
20204449
RPN10_YEASTRPN10physical
20204449
DJC13_HUMANDNAJC13physical
27173435
EDRF1_HUMANEDRF1physical
27173435
NMT1_HUMANNMT1physical
27173435
FYB2_HUMANC1orf168physical
27173435
I2BP1_HUMANIRF2BP1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
241410Hypoparathyroidism-retardation-dysmorphism syndrome (HRD)
244460Kenny-Caffey syndrome 1 (KCS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBCE_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-451 AND LYS-463, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASSSPECTROMETRY.

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