CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012638
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin-specific chaperone E 
Protein Synonyms/Alias
 Tubulin-folding cofactor E 
Gene Name
 TBCE 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
192NVSENKLKFPSGSVLubiquitination[1]
451QLLTLKIKYPHQLDQacetylation[2]
463LDQKVLEKQLPGSMTacetylation[2]
463LDQKVLEKQLPGSMTubiquitination[1]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation. 
Sequence Annotation
 DOMAIN 27 71 CAP-Gly.
 REPEAT 154 175 LRR 1.
 REPEAT 180 200 LRR 2.
 REPEAT 205 226 LRR 3.
 REPEAT 230 252 LRR 4.
 REPEAT 253 274 LRR 5.
 REPEAT 278 299 LRR 6.
 REPEAT 308 329 LRR 7.
 DOMAIN 342 384 LRRCT.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 463 463 N6-acetyllysine.
 MOD_RES 495 495 Phosphoserine.  
Keyword
 Acetylation; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Dwarfism; Leucine-rich repeat; Mental retardation; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 527 AA 
Protein Sequence
MSDTLTADVI GRRVEVNGEH ATVRFAGVVP PVAGPWLGVE WDNPERGKHD GSHEGTVYFK 60
CRHPTGGSFI RPNKVNFGTD FLTAIKNRYV LEDGPEEDRK EQIVTIGNKP VETIGFDSIM 120
KQQSQLSKLQ EVSLRNCAVS CAGEKGGVAE ACPNIRKVDL SKNLLSSWDE VIHIADQLRH 180
LEVLNVSENK LKFPSGSVLT GTLSVLKVLV LNQTGITWAE VLRCVAGCPG LEELYLESNN 240
IFISERPTDV LQTVKLLDLS SNQLIDENQL YLIAHLPRLE QLILSDTGIS SLHFPDAGIG 300
CKTSMFPSLK YLVVNDNQIS QWSFFNELEK LPSLRALSCL RNPLTKEDKE AETARLLIIA 360
SIGQLKTLNK CEILPEERRR AELDYRKAFG NEWKQAGGHK DPEKNRLSEE FLTAHPRYQF 420
LCLKYGAPED WELKTQQPLM LKNQLLTLKI KYPHQLDQKV LEKQLPGSMT IQKVKGLLSR 480
LLKVPVSDLL LSYESPKKPG REIELENDLK SLQFYSVENG DCLLVRW 527 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005874; C:microtubule; TAS:ProtInc.
 GO:0051087; F:chaperone binding; TAS:ProtInc.
 GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
 GO:0008344; P:adult locomotory behavior; IEA:Compara.
 GO:0048589; P:developmental growth; IEA:Compara.
 GO:0000226; P:microtubule cytoskeleton organization; IEA:Compara.
 GO:0014889; P:muscle atrophy; IEA:Compara.
 GO:0048936; P:peripheral nervous system neuron axonogenesis; IEA:Compara.
 GO:0007023; P:post-chaperonin tubulin folding pathway; IDA:UniProtKB.
 GO:0009791; P:post-embryonic development; IEA:Compara. 
Interpro
 IPR000938; CAP-Gly_domain. 
Pfam
 PF01302; CAP_GLY 
SMART
 SM01052; CAP_GLY 
PROSITE
 PS00845; CAP_GLY_1
 PS50245; CAP_GLY_2 
PRINTS