CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029461
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin alpha-4A chain 
Protein Synonyms/Alias
 Tubulin, alpha 1 (Testis specific), isoform CRA_a; cDNA FLJ58687, highly similar to Tubulin alpha-4 chain 
Gene Name
 TUBA4A 
Gene Synonyms/Alias
 TUBA1; hCG_2013418 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
81PEQLITGKEDAANNYacetylation[1]
81PEQLITGKEDAANNYubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
97RGHYTIGKEIIDPVLubiquitination[5, 6, 9, 10]
148RLSVDYGKKSKLEFSacetylation[1, 11]
148RLSVDYGKKSKLEFSubiquitination[1, 4, 5, 6, 8, 9]
149LSVDYGKKSKLEFSIubiquitination[1, 4, 5, 6, 9]
265APVISAEKAYHEQLSubiquitination[1, 5, 6, 8, 9]
289EPANQMVKCDPRHGKubiquitination[1, 4, 5, 6, 8, 9]
296KCDPRHGKYMACCLLacetylation[1]
296KCDPRHGKYMACCLLubiquitination[1, 4, 5, 6, 8, 9]
311YRGDVVPKDVNAAIAubiquitination[4, 9]
321NAAIAAIKTKRSIQFubiquitination[5, 6, 9, 10]
337DWCPTGFKVGINYQPubiquitination[1, 5, 6, 8, 9]
355VPGGDLAKVQRAVCMacetylation[1]
355VPGGDLAKVQRAVCMubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
386KFDLMYAKRAFVHWYubiquitination[9]
415EDMAALEKDYEEVGIubiquitination[9]
Reference
 [1] 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]
 [2] 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]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [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] 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]
 [11] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 
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 (By similarity). 
Sequence Annotation
  
Keyword
 Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 433 AA 
Protein Sequence
MGNACWELYC LEHGIQPDGQ MPSDKTIGGG DDSFTTFFCE TGAGKHVPRA VFVDLEPTVI 60
DEIRNGPYRQ LFHPEQLITG KEDAANNYAR GHYTIGKEII DPVLDRIRKL SDQCTGLQGF 120
LVFHSFGGGT GSGFTSLLME RLSVDYGKKS KLEFSIYPAP QVSTAVVEPY NSILTTHTTL 180
EHSDCAFMVD NEAIYDICRR NLDIERPTYT NLNRLISQIV SSITASLRFD GALNVDLTEF 240
QTNLVPYPRI HFPLATYAPV ISAEKAYHEQ LSVAEITNAC FEPANQMVKC DPRHGKYMAC 300
CLLYRGDVVP KDVNAAIAAI KTKRSIQFVD WCPTGFKVGI NYQPPTVVPG GDLAKVQRAV 360
CMLSNTTAIA EAWARLDHKF DLMYAKRAFV HWYVGEGMEE GEFSEAREDM AALEKDYEEV 420
GIDSYEDEDE GEE 433 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
 GO:0007017; P:microtubule-based process; IEA:InterPro.
 GO:0051258; P:protein polymerization; IEA:InterPro. 
Interpro
 IPR002452; Alpha_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
 PR01162; ALPHATUBULIN.
 PR01161; TUBULIN.