CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002504
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin beta chain 
Protein Synonyms/Alias
 Tubulin beta-5 chain 
Gene Name
 TUBB 
Gene Synonyms/Alias
 TUBB5; OK/SW-cl.56 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
58YNEATGGKYVPRAILacetylation[1]
58YNEATGGKYVPRAILubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
103GAGNNWAKGHYTEGAubiquitination[9]
216DICFRTLKLTTPTYGubiquitination[5, 8]
252QLNADLRKLAVNMVPacetylation[10]
252QLNADLRKLAVNMVPubiquitination[5, 7, 9]
297TQQVFDAKNMMAACDubiquitination[3, 4, 5, 8, 9, 11, 12, 13, 14, 15]
324FRGRMSMKEVDEQMLacetylation[10, 15, 16]
324FRGRMSMKEVDEQMLubiquitination[2, 4, 5, 6, 7, 8, 9, 11, 12, 13, 14, 15]
336QMLNVQNKNSSYFVEubiquitination[5, 8, 9, 12, 13, 14]
350EWIPNNVKTAVCDIPubiquitination[5, 8, 9]
362DIPPRGLKMAVTFIGubiquitination[9]
379TAIQELFKRISEQFTubiquitination[4, 5, 6, 8, 9]
Reference
 [1] 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]
 [2] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [3] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [4] 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]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] 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]
 [9] 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]
 [10] A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation.
 Chu CW, Hou F, Zhang J, Phu L, Loktev AV, Kirkpatrick DS, Jackson PK, Zhao Y, Zou H.
 Mol Biol Cell. 2011 Feb 15;22(4):448-56. [PMID: 21177827]
 [11] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [12] 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]
 [13] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [14] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [15] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [16] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. 
Sequence Annotation
 NP_BIND 140 146 GTP (Potential).
 MOD_RES 36 36 Phosphotyrosine (By similarity).
 MOD_RES 58 58 N6-acetyllysine; alternate.
 MOD_RES 172 172 Phosphoserine; by CDK1 (By similarity).
 MOD_RES 318 318 Omega-N-methylarginine.
 MOD_RES 340 340 Phosphotyrosine (By similarity).
 MOD_RES 382 382 Phosphoserine (By similarity).
 CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 324 324 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation; Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 444 AA 
Protein Sequence
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV 60
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 120
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV 180
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 240
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 300
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 360
LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 420
EYQQYQDATA EEEEDFGEEA EEEA 444 
Gene Ontology
 GO:0044297; C:cell body; IDA:DFLAT.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0005641; C:nuclear envelope lumen; IDA:DFLAT.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:Compara.
 GO:0005198; F:structural molecule activity; TAS:BHF-UCL.
 GO:0051301; P:cell division; TAS:BHF-UCL.
 GO:0006928; P:cellular component movement; TAS:UniProtKB.
 GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007017; P:microtubule-based process; TAS:BHF-UCL.
 GO:0042267; P:natural killer cell mediated cytotoxicity; NAS:UniProtKB.
 GO:0051258; P:protein polymerization; IEA:InterPro.
 GO:0051225; P:spindle assembly; IEA:Compara. 
Interpro
 IPR013838; Beta-tubulin_BS.
 IPR002453; Beta_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
 PS00228; TUBULIN_B_AUTOREG 
PRINTS
 PR01163; BETATUBULIN.
 PR01161; TUBULIN.