Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00049
Entry Name
UniProt Accession
Theoretical PI
4.78
Molecular Weight
49906.97
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Tubulin beta-2A chain
Protein Synonyms/Alias
Gene Name
Tubb2a
Gene Synonyms/Alias
Created Date
03-APR-2007
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
12
Canonical
VHIQAGQCGNQIGAK
[1]
S-Palmitoylation
129
Canonical
KESESCDCLQGFQLT
[1]
S-Palmitoylation
239
Canonical
TMSGVTTCLRFPGQL
[1]
S-Palmitoylation
303
Canonical
SKNMMAACDPRHGRY
[1]
S-Palmitoylation
354
Canonical
NNVKTAVCDIPPRGL
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Zhao Z, Hou J, Xie Z, Deng J, Wang X, Chen D, Yang F, Gong W. Acyl-biotinylexchange chemistry and mass spectrometry-based analysis of palmitoylation sitesof in vitro palmitoylated rat brain tubulin. Protein J. 2010 Nov;29(8):531-7.doi: 10.1007/s10930-010-9285-x.[PMID:20976533]
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
Nucleotide-binding: 140 146 GTP.
Modified residue: 172 172 Phosphoserine; by CDK1.
Protein Length
445 AA.
Protein Sequence
(Canonical)
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV  60
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV  120
RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV  180
EPYNATLSVH QLVENTDETY SIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL  240
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM  300
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG  360
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS  420
EYQQYQDATA DEQGEFEEEE GEDEA                                        445
FASTA
(Canonical)
>LipidDB-10116-00049|P85108
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVV
EPYNATLSVHQLVENTDETYSIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMM
AACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEEGEDEA
Gene Ontology
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005874; C:microtubule; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IEA:Ensembl
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
InterPro; IPR013838; Beta-tubulin_BS
InterPro; IPR002453; Beta_tubulin
InterPro; IPR008280; Tub_FtsZ_C
InterPro; IPR000217; Tubulin
InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom
InterPro; IPR023123; Tubulin_C
InterPro; IPR017975; Tubulin_CS
InterPro; IPR003008; Tubulin_FtsZ_GTPase
Pfam
Pfam; PF00091; Tubulin;
Pfam; PF03953; Tubulin_C;
SMART
SMART; SM00864; Tubulin;
SMART; SM00865; Tubulin_C;
PROSITE
PROSITE; PS00227; TUBULIN;
PROSITE; PS00228; TUBULIN_B_AUTOREG;
PRINTS
PRINTS; PR01163; BETATUBULIN;
PRINTS; PR01161; TUBULIN;