CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009853
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin alpha-1B chain 
Protein Synonyms/Alias
 Alpha-tubulin ubiquitous; Tubulin K-alpha-1; Tubulin alpha-ubiquitous chain 
Gene Name
 TUBA1B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
60FSETGAGKHVPRAVFacetylation[1]
60FSETGAGKHVPRAVFubiquitination[2, 3, 4]
96PEQLITGKEDAANNYubiquitination[2, 3, 4]
112RGHYTIGKEIIDLVLacetylation[1]
112RGHYTIGKEIIDLVLubiquitination[2, 3, 4]
163RLSVDYGKKSKLEFSacetylation[1]
163RLSVDYGKKSKLEFSubiquitination[2, 3, 4]
164LSVDYGKKSKLEFSIubiquitination[2, 4]
280APVISAEKAYHEQLSubiquitination[3, 4]
304EPANQMVKCDPRHGKubiquitination[2, 3, 4]
311KCDPRHGKYMACCLLacetylation[1]
311KCDPRHGKYMACCLLubiquitination[2, 3, 4]
326YRGDVVPKDVNAAIAacetylation[1]
326YRGDVVPKDVNAAIAubiquitination[2, 3, 4, 5]
336NAAIATIKTKRSIQFubiquitination[2, 3, 4]
338AIATIKTKRSIQFVDubiquitination[2, 3, 4]
352DWCPTGFKVGINYQPubiquitination[3, 4]
370VPGGDLAKVQRAVCMacetylation[1]
370VPGGDLAKVQRAVCMubiquitination[2, 3, 4, 5]
394AWARLDHKFDLMYAKubiquitination[2, 3, 4]
401KFDLMYAKRAFVHWYubiquitination[2, 3, 4]
430EDMAALEKDYEEVGVubiquitination[4, 6, 7]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
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.
 MOD_RES 282 282 Nitrated tyrosine (By similarity).
 MOD_RES 319 319 Phosphotyrosine (By similarity).
 MOD_RES 339 339 Omega-N-methylarginine.
 MOD_RES 432 432 Phosphotyrosine (By similarity).
 MOD_RES 439 439 Phosphoserine (By similarity).
 CROSSLNK 326 326 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 370 370 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation; Microtubule; Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 451 AA 
Protein Sequence
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 60
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD 120
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA 180
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA 240
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP 360
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 420
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y 451 
Gene Ontology
 GO:0005881; C:cytoplasmic microtubule; IEA:Compara.
 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:Compara.
 GO:0005198; F:structural molecule activity; TAS:BHF-UCL.
 GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
 GO:0051301; P:cell division; TAS:BHF-UCL.
 GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
 GO:0000226; P:microtubule cytoskeleton organization; IEA:Compara.
 GO:0007017; P:microtubule-based process; TAS:BHF-UCL.
 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.