Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01140
Entry Name
UniProt Accession
Theoretical PI
4.93
Molecular Weight
49924.4
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Tubulin alpha-4A chain
Protein Synonyms/Alias
Alpha-tubulin 4; Tubulin alpha-4 chain;
Gene Name
Tuba4a
Gene Synonyms/Alias
Tuba4;
Created Date
29-MAY-2007
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
20
Canonical
GVQMGNACWELYCLE
[1]
S-Palmitoylation
54
Canonical
DSFTTFFCETGAGKH
[1]
S-Palmitoylation
129
Canonical
IRKLSDQCTGLQGFL
[1]
S-Palmitoylation
213
Canonical
NEAIYDICRRNLDIE
[1]
S-Palmitoylation
295
Canonical
VAEITNACFEPANQM
[1]
S-Palmitoylation
305
Canonical
PANQMVKCDPRHGKY
[1]
S-Palmitoylation
316
Canonical
HGKYMACCLLYRGDV
[1]
S-Palmitoylation
347
Canonical
SIQFVDWCPTGFKVG
[1]
S-Palmitoylation
376
Canonical
AKVQRAVCMLSNTTA
[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: 142 148 GTP.
Modified residue: 48 48 Phosphoserine.
Modified residue: 83 83 Nitrated tyrosine.
Modified residue: 282 282 Nitrated tyrosine.
Modified residue: 432 432 Phosphotyrosine.
Modified residue: 439 439 Phosphoserine.
Protein Length
448 AA.
Protein Sequence
(Canonical)
MRECISVHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT TFFCETGAGK  60
HVPRAVFVDL EPTVIDEIRN GPYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDPVLD  120
RIRKLSDQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA  180
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA  240
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN  300
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG FKVGINYQPP  360
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE  420
AREDMAALEK DYEEVGIDSY EDEDEGEE                                     448
FASTA
(Canonical)
>LipidDB-10116-01140|Q5XIF6
MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGK
HVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLD
RIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGIDSYEDEDEGEE
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: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; IPR002452; Alpha_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;
PRINTS
PRINTS; PR01162; ALPHATUBULIN;
PRINTS; PR01161; TUBULIN;