Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tubulin alpha chain-like 3

Gene

Tubal3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi149 – 155GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-437239 Recycling pathway of L1
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6807878 COPI-mediated anterograde transport
R-MMU-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-MMU-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8955332 Carboxyterminal post-translational modifications of tubulin
R-MMU-983189 Kinesins

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha chain-like 3
Gene namesi
Name:Tubal3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:3588215 Tubal3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003137101 – 446Tubulin alpha chain-like 3Add BLAST446

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.By similarity
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).By similarity

Proteomic databases

EPDiQ3UX10
MaxQBiQ3UX10
PaxDbiQ3UX10
PeptideAtlasiQ3UX10
PRIDEiQ3UX10

PTM databases

iPTMnetiQ3UX10
PhosphoSitePlusiQ3UX10

Expressioni

Gene expression databases

BgeeiENSMUSG00000021216
CleanExiMM_TUBAL3

Interactioni

Subunit structurei

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Protein-protein interaction databases

BioGridi231990, 1 interactor
IntActiQ3UX10, 1 interactor
STRINGi10090.ENSMUSP00000021639

Structurei

3D structure databases

ProteinModelPortaliQ3UX10
SMRiQ3UX10
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119060
HOGENOMiHOG000165711
HOVERGENiHBG000089
InParanoidiQ3UX10
KOiK07374
OMAiTFFCETR
OrthoDBiEOG091G093N
TreeFamiTF300314

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR002452 Alpha_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01162 ALPHATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit

Sequencei

Sequence statusi: Complete.

Q3UX10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRECLSIHIG QAGVQIGDAC WELYCLEHGI QPDGFILDHQ HDNLENPKVE
60 70 80 90 100
HMNASLDTFF HETRAGKHVP RTLFMDLEPT VIDGIRVGRY HSLFHPEQLV
110 120 130 140 150
NGKEDAANTY ARGRYSVGSE VIELVLERIR KLAEQCSGLQ GFLIYRSFGG
160 170 180 190 200
GTGSGFTSLL MERLSVEYCK KIKLEFSVYP SPRISTAVVE PYNAILTTHS
210 220 230 240 250
TIEYSDCAFM VDNEALYDIC QHKLGIERPS YASINRLIAQ VSSSITASLR
260 270 280 290 300
FEGPLNVDLI EFQTNLVPYP RIHFPITALA PIISAEKAYQ EQLSVSDVTA
310 320 330 340 350
SCFEVSNQLV KCDPRLGKYM ACCLLYRGDV VPKDVNEAIA AMKSRTSVQF
360 370 380 390 400
VDWCPTGFKV GINYQPPAVV PGGDLARVQR AVCMLSNTTA IVEAWARLDH
410 420 430 440
KFDLMYAKKA FLHWYITEGM ELGEFVEARE DLAALEKDYE EVGLSF
Length:446
Mass (Da):49,988
Last modified:July 27, 2011 - v2
Checksum:i8A8835DF891E8E80
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti227E → G in BAE22753 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK135971 mRNA Translation: BAE22753.1
BC147507 mRNA Translation: AAI47508.1
CCDSiCCDS49202.1
RefSeqiNP_001029051.2, NM_001033879.3
UniGeneiMm.313659

Genome annotation databases

EnsembliENSMUST00000021639; ENSMUSP00000021639; ENSMUSG00000021216
GeneIDi238463
KEGGimmu:238463
UCSCiuc007pjg.2 mouse

Similar proteinsi

Entry informationi

Entry nameiTBAL3_MOUSE
AccessioniPrimary (citable) accession number: Q3UX10
Secondary accession number(s): B9EJS3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 104 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health