CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023037
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin epsilon chain 
Protein Synonyms/Alias
 Epsilon-tubulin 
Gene Name
 TUBE1 
Gene Synonyms/Alias
 TUBE 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
34EHAAVNQKGIYDEAIubiquitination[1, 2, 3]
61GDGGSISKGKICSLKubiquitination[1, 2]
63GGSISKGKICSLKARubiquitination[2]
68KGKICSLKARAVLIDubiquitination[2]
96LRDVFDTKQLITDISubiquitination[1, 2, 3]
114NNWAVGHKVFGSLYQubiquitination[1]
127YQDQILEKFRKSAEHubiquitination[1, 2]
229DLMVNSGKLGTTVKPubiquitination[2]
235GKLGTTVKPKSLVTSubiquitination[2]
249SSSGALKKQHKKPFDubiquitination[2]
329MFSDAFSKDHQLLRAubiquitination[2, 3]
339QLLRADPKHSLYLACubiquitination[3]
367RRNIERLKPSLQFVSubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
  
Sequence Annotation
 NP_BIND 148 154 GTP (Potential).  
Keyword
 Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 475 AA 
Protein Sequence
MTQSVVVQVG QCGNQIGCCF WDLALREHAA VNQKGIYDEA ISSFFRNVDT RVVGDGGSIS 60
KGKICSLKAR AVLIDMEEGV VNEILQGPLR DVFDTKQLIT DISGSGNNWA VGHKVFGSLY 120
QDQILEKFRK SAEHCDCLQC FFIIHSMGGG TGSGLGTFLL KVLEDEFPEV YRFVTSIYPS 180
GEDDVITSPY NSILAMKELN EHADCVLPID NQSLFDIISK IDLMVNSGKL GTTVKPKSLV 240
TSSSGALKKQ HKKPFDAMNN IVANLLLNLT SSARFEGSLN MDLNEISMNL VPFPQLHYLV 300
SSLTPLYTLT DVNIPPRRLD QMFSDAFSKD HQLLRADPKH SLYLACALMV RGNVQISDLR 360
RNIERLKPSL QFVSWNQEGW KTSLCSVPPV GHSHSLLALA NNTCVKPTFM ELKERFMRLY 420
KKKAHLHHYL QVEGMEESCF TEAVSSLSAL IQEYDQLDAT KNMPVQDLPR LSIAM 475 
Gene Ontology
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0000242; C:pericentriolar material; TAS:ProtInc.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0007098; P:centrosome cycle; TAS:ProtInc.
 GO:0051258; P:protein polymerization; IEA:InterPro. 
Interpro
 IPR004057; Epsilon_tubulin.
 IPR008280; Tub_FtsZ_C.
 IPR000217; Tubulin.
 IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
 IPR023123; Tubulin_C.
 IPR017975; Tubulin_CS.
 IPR003008; Tubulin_FtsZ_GTPase. 
Pfam
 PF00091; Tubulin
 PF03953; Tubulin_C 
SMART
 SM00864; Tubulin
 SM00865; Tubulin_C 
PROSITE
 PS00227; TUBULIN 
PRINTS
 PR01519; EPSLNTUBULIN.
 PR01161; TUBULIN.