CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-044654
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Uncharacterized protein 
Protein Synonyms/Alias
  
Gene Name
 Tubb4b-ps1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
58YNEATGGKYVPRAVLacetylation[1, 2, 3]
58YNEATGGKYVPRAVLsuccinylation[3]
58YNEATGGKYVPRAVLubiquitination[4]
215DICFRTLKLTTPTYGubiquitination[4]
296TQQMFDAKNMMAACDubiquitination[4]
323FRGRMSMKEVDEQMLacetylation[1, 2, 3]
323FRGRMSMKEVDEQMLsuccinylation[3]
323FRGRMSMKEVDEQMLubiquitination[4]
335QMLNVQNKNSSYFVEubiquitination[4]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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
 444 AA 
Protein Sequence
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DTTGTYHGDS DLQLERINVY YNEATGGKYV 60
PRAVLVDLEP CTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 120
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL ISKIREEYPD RIMNTFSVVP SPKVSDTVVE 180
PYNATLSVHQ LVENTDETYC IDDEALYDIC FRTLKLTTPT YGDLNHLVSA TMSGVTTCLR 240
FPGQLNADLR KLAVNMVPFP RLHFFMPGFA PLTSRGSQQY RALTVPELTQ QMFDAKNMMA 300
ACDPRHGRYL TVAAVFRGRM SMKEVDEQML NVQNKNSSYF VEWIPNNVKT AVCDIPPRGL 360
KMSTTFIGNS TAIQELFKRI SEQFTAMFPR KTFLHWYTGE GMDEMEFTEA ESNMNDLVSE 420
YQQYQDATAE EEGEYEEEAE EEVA 444 
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
 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.