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Protein

Tubulin alpha-4A chain

Gene

Tuba4a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-5620924. Intraflagellar transport.
R-RNO-5632684. Hedgehog 'on' state.
R-RNO-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-4A chain
Alternative name(s):
Alpha-tubulin 4
Tubulin alpha-4 chain
Gene namesi
Name:Tuba4a
Synonyms:Tuba4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi1359623. Tuba4a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Tubulin alpha-4A chainPRO_0000288715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-acetyllysineBy similarity
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei83 – 831Nitrated tyrosineBy similarity
Modified residuei432 – 4321PhosphotyrosineBy similarity
Modified residuei439 – 4391PhosphoserineCombined sources

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
Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity).By similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

PaxDbiQ5XIF6.
PRIDEiQ5XIF6.

PTM databases

iPTMnetiQ5XIF6.
PhosphoSiteiQ5XIF6.

Expressioni

Gene expression databases

GenevisibleiQ5XIF6. RN.

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

BioGridi261372. 4 interactions.
IntActiQ5XIF6. 3 interactions.
STRINGi10116.ENSRNOP00000004797.

Structurei

3D structure databases

ProteinModelPortaliQ5XIF6.
SMRiQ5XIF6. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ5XIF6.
KOiK07374.
OMAiSEGREDM.
OrthoDBiEOG7TBC1W.
PhylomeDBiQ5XIF6.
TreeFamiTF300314.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5XIF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRECISVHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT
60 70 80 90 100
TFFCETGAGK HVPRAVFVDL EPTVIDEIRN GPYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDPVLD RIRKLSDQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGIDSY EDEDEGEE
Length:448
Mass (Da):49,924
Last modified:November 23, 2004 - v1
Checksum:iC00ED90A183FE8F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083726 mRNA. Translation: AAH83726.1.
RefSeqiNP_001007005.1. NM_001007004.1.
UniGeneiRn.92961.

Genome annotation databases

EnsembliENSRNOT00000004797; ENSRNOP00000004797; ENSRNOG00000003597.
GeneIDi316531.
KEGGirno:316531.
UCSCiRGD:1359623. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083726 mRNA. Translation: AAH83726.1.
RefSeqiNP_001007005.1. NM_001007004.1.
UniGeneiRn.92961.

3D structure databases

ProteinModelPortaliQ5XIF6.
SMRiQ5XIF6. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi261372. 4 interactions.
IntActiQ5XIF6. 3 interactions.
STRINGi10116.ENSRNOP00000004797.

PTM databases

iPTMnetiQ5XIF6.
PhosphoSiteiQ5XIF6.

Proteomic databases

PaxDbiQ5XIF6.
PRIDEiQ5XIF6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004797; ENSRNOP00000004797; ENSRNOG00000003597.
GeneIDi316531.
KEGGirno:316531.
UCSCiRGD:1359623. rat.

Organism-specific databases

CTDi7277.
RGDi1359623. Tuba4a.

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ5XIF6.
KOiK07374.
OMAiSEGREDM.
OrthoDBiEOG7TBC1W.
PhylomeDBiQ5XIF6.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-5620924. Intraflagellar transport.
R-RNO-5632684. Hedgehog 'on' state.
R-RNO-8854518. AURKA Activation by TPX2.

Miscellaneous databases

PROiQ5XIF6.

Gene expression databases

GenevisibleiQ5XIF6. RN.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTBA4A_RAT
AccessioniPrimary (citable) accession number: Q5XIF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 23, 2004
Last modified: June 8, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This tubulin does not have a C-terminal tyrosine.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.