CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024487
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin alpha chain-like 3 
Protein Synonyms/Alias
  
Gene Name
 TUBAL3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
318KCDPRLGKYMACCLLubiquitination[1]
401AWARLDHKFDLMYAKacetylation[2, 3, 4]
401AWARLDHKFDLMYAKubiquitination[1, 4, 5, 6, 7, 8]
408KFDLMYAKRAFLHWYacetylation[2, 3]
408KFDLMYAKRAFLHWYubiquitination[4, 5, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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]
 [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
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
 NP_BIND 149 155 GTP (Potential).  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Microtubule; Nucleotide-binding; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 446 AA 
Protein Sequence
MRECLSIHIG QAGIQIGDAC WELYCLEHGI QPNGVVLDTQ QDQLENAKME HTNASFDTFF 60
CETRAGKHVP RALFVDLEPT VIDGIRTGQH RSLFHPEQLL SGKEDAANNY ARGRYSVGSE 120
VIDLVLERTR KLAEQCGGLQ GFLIFRSFGG GTGSGFTSLL MERLTGEYSR KTKLEFSVYP 180
APRISTAVVE PYNSVLTTHS TTEHTDCTFM VDNEAVYDIC HRKLGVECPS HASINRLVVQ 240
VVSSITASLR FEGPLNVDLI EFQTNLVPYP RIHFPMTAFA PIVSADKAYH EQFSVSDITT 300
ACFESSNQLV KCDPRLGKYM ACCLLYRGDV VPKEVNAAIA ATKSRHSVQF VDWCPTGFKV 360
GINNRPPTVM PGGDLAKVHR SICMLSNTTA IVEAWARLDH KFDLMYAKRA FLHWYLREGM 420
EEAEFLEARE DLAALERDYE EVAQSF 446 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 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.