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Tubulin alpha-1B chain (Alpha-tubulin 2) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain]

 TBA1B_RAT               Reviewed;         451 AA.
Q6P9V9;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 123.
RecName: Full=Tubulin alpha-1B chain;
AltName: Full=Alpha-tubulin 2;
AltName: Full=Tubulin alpha-2 chain;
Contains:
RecName: Full=Detyrosinated tubulin alpha-1B chain;
Name=Tuba1b; Synonyms=Tuba2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, and Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
PROTEIN SEQUENCE OF 41-60; 230-243 AND 265-280, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[3]
TYROSINATION.
PubMed=9108330; DOI=10.1046/j.1440-169X.1997.t01-1-00005.x;
Arregui C.O., Mas C.R., Argarana C.E., Barra H.S.;
"Tubulin tyrosine ligase: protein and mRNA expression in developing
rat skeletal muscle.";
Dev. Growth Differ. 39:167-178(1997).
-!- FUNCTION: 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.
-!- SUBUNIT: 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.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- PTM: 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. {ECO:0000250|UniProtKB:P68369}.
-!- PTM: 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).
{ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
-!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
microtubule lumen. This modification has been correlated with
increased microtubule stability, intracellular transport and
ciliary assembly. {ECO:0000250|UniProtKB:Q71U36}.
-!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic
microtubules and is required for normal mitosis and cytokinesis
contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.
-!- PTM: Nitration of Tyr-451 is irreversible and interferes with
normal dynein intracellular distribution.
{ECO:0000250|UniProtKB:Q71U36}.
-!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic
removal and re-addition of a C-terminal tyrosine residue by the
enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin
tyrosine ligase (TTL), respectively. {ECO:0000269|PubMed:9108330}.
-!- PTM: Tubulin alpha-1B chain: Tyrosination promotes microtubule
interaction with CAP-Gly domain-containing proteins such as CLIP1,
CLIP2 and DCTN1 (By similarity). Tyrosination regulates the
initiation of dynein-dynactin motility via interaction with DCTN1,
which brings the dynein-dynactin complex into contact with
microtubules. In neurons, tyrosinated tubulins mediate the
initiation of retrograde vesicle transport (By similarity).
{ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
-!- PTM: Detyrosinated tubulin alpha-1B chain: Detyrosination is
involved in metaphase plate congression by guiding chromosomes
during mitosis: detyrosination promotes interaction with CENPE,
promoting pole-proximal transport of chromosomes toward the
equator (By similarity). Detyrosination increases microtubules-
dependent mechanotransduction in dystrophic cardiac and skeletal
muscle. In cardiomyocytes, detyrosinated microtubules are required
to resist to contractile compression during contraction:
detyrosination promotes association with desmin (DES) at force-
generating sarcomeres, leading to buckled microtubules and
mechanical resistance to contraction (By similarity).
{ECO:0000250|UniProtKB:P05213, ECO:0000250|UniProtKB:P68363}.
-!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC060572; AAH60572.1; -; mRNA.
EMBL; BC076379; AAH76379.1; -; mRNA.
RefSeq; NP_001037735.1; NM_001044270.2.
UniGene; Rn.234326; -.
UniGene; Rn.99661; -.
ProteinModelPortal; Q6P9V9; -.
SMR; Q6P9V9; -.
BioGrid; 272236; 1.
CORUM; Q6P9V9; -.
IntAct; Q6P9V9; 5.
MINT; Q6P9V9; -.
iPTMnet; Q6P9V9; -.
PhosphoSitePlus; Q6P9V9; -.
PRIDE; Q6P9V9; -.
Ensembl; ENSRNOT00000081355; ENSRNOP00000070868; ENSRNOG00000053468.
GeneID; 500929; -.
KEGG; rno:500929; -.
UCSC; RGD:1565476; rat.
CTD; 10376; -.
RGD; 1565476; Tuba1b.
eggNOG; KOG1376; Eukaryota.
eggNOG; COG5023; LUCA.
GeneTree; ENSGT00760000119060; -.
HOVERGEN; HBG000089; -.
InParanoid; Q6P9V9; -.
KO; K07374; -.
OMA; IKMRECI; -.
OrthoDB; EOG091G0736; -.
Reactome; R-RNO-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
Reactome; R-RNO-2132295; MHC class II antigen presentation.
Reactome; R-RNO-2467813; Separation of Sister Chromatids.
Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-RNO-437239; Recycling pathway of L1.
Reactome; R-RNO-5620924; Intraflagellar transport.
Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-RNO-68877; Mitotic Prometaphase.
Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-RNO-8955332; Carboxyterminal post-translational modifications of tubulin.
Reactome; R-RNO-983189; Kinesins.
PRO; PR:Q6P9V9; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000053468; -.
Genevisible; Q6P9V9; RN.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IDA:CAFA.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
Gene3D; 1.10.287.600; -; 1.
Gene3D; 3.30.1330.20; -; 1.
Gene3D; 3.40.50.1440; -; 1.
InterPro; IPR002452; Alpha_tubulin.
InterPro; IPR008280; Tub_FtsZ_C.
InterPro; IPR000217; Tubulin.
InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
InterPro; IPR037103; Tubulin/FtsZ_C_sf.
InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
InterPro; IPR023123; Tubulin_C.
InterPro; IPR017975; Tubulin_CS.
InterPro; IPR003008; Tubulin_FtsZ_GTPase.
PANTHER; PTHR11588; PTHR11588; 1.
Pfam; PF00091; Tubulin; 1.
Pfam; PF03953; Tubulin_C; 1.
PRINTS; PR01162; ALPHATUBULIN.
PRINTS; PR01161; TUBULIN.
SMART; SM00864; Tubulin; 1.
SMART; SM00865; Tubulin_C; 1.
SUPFAM; SSF52490; SSF52490; 1.
SUPFAM; SSF55307; SSF55307; 1.
PROSITE; PS00227; TUBULIN; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation;
Microtubule; Nitration; Nucleotide-binding; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 451 Tubulin alpha-1B chain.
/FTId=PRO_0000048127.
CHAIN 1 450 Detyrosinated tubulin alpha-1B chain.
{ECO:0000250|UniProtKB:P68363}.
/FTId=PRO_0000437390.
NP_BIND 142 148 GTP. {ECO:0000255}.
SITE 451 451 Involved in polymerization.
{ECO:0000250}.
MOD_RES 40 40 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P68363}.
MOD_RES 40 40 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P68363}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:P68363}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000250|UniProtKB:P68363}.
MOD_RES 282 282 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P68373}.
MOD_RES 339 339 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P68363}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000250|UniProtKB:P68373}.
MOD_RES 445 445 5-glutamyl polyglutamate.
{ECO:0000250|UniProtKB:P68369}.
MOD_RES 451 451 3'-nitrotyrosine.
{ECO:0000250|UniProtKB:Q71U36}.
CROSSLNK 326 326 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P68363}.
CROSSLNK 370 370 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P68363}.
SEQUENCE 451 AA; 50152 MW; 94355B4EC2086429 CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y


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