CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009918
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin beta-5 chain 
Protein Synonyms/Alias
  
Gene Name
 Tubb5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
58YNEATGGKYVPRAILacetylation[1]
58YNEATGGKYVPRAILubiquitination[2]
252QLNADLRKLAVNMVPubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
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 (By
 MOD_RES 172 172 Phosphoserine; by CDK1 (By similarity).
 MOD_RES 318 318 Omega-N-methylarginine (By similarity).
 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
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation; Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome; S-nitrosylation; 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; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005641; C:nuclear envelope lumen; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0032403; F:protein complex binding; IDA:RGD.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:Compara.
 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.