CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009854
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin alpha-4A chain 
Protein Synonyms/Alias
 Alpha-tubulin 1; Testis-specific alpha-tubulin; Tubulin H2-alpha; Tubulin alpha-1 chain 
Gene Name
 TUBA4A 
Gene Synonyms/Alias
 TUBA1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
96PEQLITGKEDAANNYubiquitination[1, 2]
112RGHYTIGKEIIDPVLubiquitination[2, 3, 4, 5]
163RLSVDYGKKSKLEFSubiquitination[2]
164LSVDYGKKSKLEFSIubiquitination[2]
280APVISAEKAYHEQLSubiquitination[2]
304EPANQMVKCDPRHGKubiquitination[2]
311KCDPRHGKYMACCLLubiquitination[2]
326YRGDVVPKDVNAAIAubiquitination[6, 7]
336NAAIAAIKTKRSIQFubiquitination[2, 4, 5]
338AIAAIKTKRSIQFVDubiquitination[4]
352DWCPTGFKVGINYQPubiquitination[2, 3]
370VPGGDLAKVQRAVCMubiquitination[1, 2]
394AWARLDHKFDLMYAKubiquitination[2]
401KFDLMYAKRAFVHWYubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 
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 142 148 GTP (Potential).
 MOD_RES 6 6 Phosphoserine (By similarity).
 MOD_RES 48 48 Phosphoserine.
 MOD_RES 83 83 Nitrated tyrosine (By similarity).
 MOD_RES 232 232 Phosphoserine (By similarity).
 MOD_RES 282 282 Nitrated tyrosine (By similarity).
 MOD_RES 319 319 Phosphotyrosine (By similarity).
 MOD_RES 432 432 Phosphotyrosine (By similarity).
 MOD_RES 439 439 Phosphoserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Microtubule; Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 448 AA 
Protein Sequence
MRECISVHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT TFFCETGAGK 60
HVPRAVFVDL EPTVIDEIRN GPYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDPVLD 120
RIRKLSDQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA 180
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA 240
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG FKVGINYQPP 360
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 420
AREDMAALEK DYEEVGIDSY EDEDEGEE 448 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005576; C:extracellular region; TAS:Reactome.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 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:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007017; P:microtubule-based process; IEA:InterPro.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 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.