ID TBA1B_MOUSE Reviewed; 451 AA. AC P05213; Q3TY23; Q3U8B1; Q3UAW8; Q4KMW2; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 10-MAY-2017, entry version 175. DE RecName: Full=Tubulin alpha-1B chain; DE AltName: Full=Alpha-tubulin 2; DE AltName: Full=Alpha-tubulin isotype M-alpha-2; DE AltName: Full=Tubulin alpha-2 chain; DE Contains: DE RecName: Full=Detyrosinated tubulin alpha-1B chain; GN Name=Tuba1b; Synonyms=Tuba2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3785200; DOI=10.1128/MCB.6.7.2409; RA Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.; RT "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis- RT specific expression of two sister genes."; RL Mol. Cell. Biol. 6:2409-2419(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Amnion, Bone marrow, Eye, Kidney, Liver, Thymus, and RC Visual cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, Czech II, and FVB/N; RC TISSUE=Limb, Mammary tumor, Olfactory epithelium, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-304; 312-320; RP 327-336; 340-370; 374-390; 395-401 AND 403-432, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-451. RX PubMed=3839797; DOI=10.1083/jcb.101.3.852; RA Lewis S.A., Lee M.G.-S., Cowan N.J.; RT "Five mouse tubulin isotypes and their regulated expression during RT development."; RL J. Cell Biol. 101:852-861(1985). RN [6] RP PROTEIN SEQUENCE OF 440-448, AND GLUTAMYLATION AT GLU-445. RX PubMed=1967194; DOI=10.1126/science.1967194; RA Edde B., Rossier J., Le Caer J.P., Desbruyeres E., Gros F., RA Denoulet P.; RT "Posttranslational glutamylation of alpha-tubulin."; RL Science 247:83-85(1990). RN [7] RP GLUTAMYLATION. RX PubMed=15890843; DOI=10.1126/science.1113010; RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., RA Suryavanshi S., Gaertig J., Edde B.; RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein RT family."; RL Science 308:1758-1762(2005). RN [8] RP TYROSINATION. RX PubMed=16954346; DOI=10.1083/jcb.200512058; RA Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K., RA Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J., RA Andrieux A., Job D.; RT "Tubulin tyrosination is a major factor affecting the recruitment of RT CAP-Gly proteins at microtubule plus ends."; RL J. Cell Biol. 174:839-849(2006). RN [9] RP GLYCYLATION. RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020; RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., RA Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., RA Janke C.; RT "Evolutionary divergence of enzymatic mechanisms for posttranslational RT polyglycylation."; RL Cell 137:1076-1087(2009). RN [10] RP TYROSINATION. RX PubMed=19564401; DOI=10.1083/jcb.200902142; RA Peris L., Wagenbach M., Lafanechere L., Brocard J., Moore A.T., RA Kozielski F., Job D., Wordeman L., Andrieux A.; RT "Motor-dependent microtubule disassembly driven by tubulin RT tyrosination."; RL J. Cell Biol. 185:1159-1166(2009). RN [11] RP DETYROSINATION. RX PubMed=26446751; DOI=10.1038/ncomms9526; RA Kerr J.P., Robison P., Shi G., Bogush A.I., Kempema A.M., Hexum J.K., RA Becerra N., Harki D.A., Martin S.S., Raiteri R., Prosser B.L., RA Ward C.W.; RT "Detyrosinated microtubules modulate mechanotransduction in heart and RT skeletal muscle."; RL Nat. Commun. 6:8526-8526(2015). RN [12] RP DETYROSINATION. RX PubMed=27102488; DOI=10.1126/science.aaf0659; RA Robison P., Caporizzo M.A., Ahmadzadeh H., Bogush A.I., Chen C.Y., RA Margulies K.B., Shenoy V.B., Prosser B.L.; RT "Detyrosinated microtubules buckle and bear load in contracting RT cardiomyocytes."; RL Science 352:417-428(2016). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a non-exchangeable site on the alpha chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is CC a hollow water-filled tube with an outer diameter of 25 nm and an CC inner diameter of 15 nM. Alpha-beta heterodimers associate head- CC to-tail to form protofilaments running lengthwise along the CC microtubule wall with the beta-tubulin subunit facing the CC microtubule plus end conferring a structural polarity. CC Microtubules usually have 13 protofilaments but different CC protofilament numbers can be found in some organisms and CC specialized cells. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in CC spleen, thymus and immature brain. CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated, CC resulting in polyglycine chains on the gamma-carboxyl group. CC Glycylation is mainly limited to tubulin incorporated into CC axonemes (cilia and flagella) whereas glutamylation is prevalent CC in neuronal cells, centrioles, axonemes, and the mitotic spindle. CC Both modifications can coexist on the same protein on adjacent CC residues, and lowering polyglycylation levels increases CC polyglutamylation, and reciprocally. The precise function of CC polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}. CC -!- PTM: Some glutamate residues at the C-terminus are CC polyglutamylated, resulting in polyglutamate chains on the gamma- CC carboxyl group (PubMed:1967194, PubMed:15890843). CC Polyglutamylation plays a key role in microtubule severing by CC spastin (SPAST). SPAST preferentially recognizes and acts on CC microtubules decorated with short polyglutamate tails: severing CC activity by SPAST increases as the number of glutamates per CC tubulin rises from one to eight, but decreases beyond this CC glutamylation threshold (By similarity). CC {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843, CC ECO:0000269|PubMed:1967194}. CC -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the CC microtubule lumen. This modification has been correlated with CC increased microtubule stability, intracellular transport and CC ciliary assembly. {ECO:0000269|PubMed:16954346, CC ECO:0000269|PubMed:19564401}. CC -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic CC microtubules and is required for normal mitosis and cytokinesis CC contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}. CC -!- PTM: Nitration of Tyr-451 is irreversible and interferes with CC normal dynein intracellular distribution. CC {ECO:0000250|UniProtKB:Q71U36}. CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic CC removal and re-addition of a C-terminal tyrosine residue by the CC enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin CC tyrosine ligase (TTL), respectively. {ECO:0000269|PubMed:16954346, CC ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751, CC ECO:0000269|PubMed:27102488}. CC -!- PTM: Tubulin alpha-1B chain: Tyrosination promotes microtubule CC interaction with CAP-Gly domain-containing proteins such as CLIP1, CC CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination CC regulates the initiation of dynein-dynactin motility via CC interaction with DCTN1, which brings the dynein-dynactin complex CC into contact with microtubules. In neurons, tyrosinated tubulins CC mediate the initiation of retrograde vesicle transport (By CC similarity). {ECO:0000250|UniProtKB:Q71U36, CC ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401}. CC -!- PTM: Detyrosinated tubulin alpha-1B chain: Detyrosination is CC involved in metaphase plate congression by guiding chromosomes CC during mitosis: detyrosination promotes interaction with CENPE, CC promoting pole-proximal transport of chromosomes toward the CC equator (By similarity). Detyrosination increases microtubules- CC dependent mechanotransduction in dystrophic cardiac and skeletal CC muscle (PubMed:26446751). In cardiomyocytes, detyrosinated CC microtubules are required to resist to contractile compression CC during contraction: detyrosination promotes association with CC desmin (DES) at force-generating sarcomeres, leading to buckled CC microtubules and mechanical resistance to contraction CC (PubMed:27102488). {ECO:0000250|UniProtKB:P68363, CC ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}. CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13446; AAA40500.1; -; mRNA. DR EMBL; AK075955; BAC36080.1; -; mRNA. DR EMBL; AK137885; BAE23512.1; -; mRNA. DR EMBL; AK150128; BAE29327.1; -; mRNA. DR EMBL; AK150179; BAE29362.1; -; mRNA. DR EMBL; AK150968; BAE29999.1; -; mRNA. DR EMBL; AK151199; BAE30196.1; -; mRNA. DR EMBL; AK151809; BAE30708.1; -; mRNA. DR EMBL; AK152298; BAE31107.1; -; mRNA. DR EMBL; AK153064; BAE31690.1; -; mRNA. DR EMBL; AK153254; BAE31845.1; -; mRNA. DR EMBL; AK158958; BAE34741.1; -; mRNA. DR EMBL; AK164428; BAE37783.1; -; mRNA. DR EMBL; AK168770; BAE40606.1; -; mRNA. DR EMBL; AK169075; BAE40860.1; -; mRNA. DR EMBL; AK169092; BAE40875.1; -; mRNA. DR EMBL; AK169130; BAE40909.1; -; mRNA. DR EMBL; AK169665; BAE41287.1; -; mRNA. DR EMBL; BC002219; AAH02219.1; -; mRNA. DR EMBL; BC008117; AAH08117.1; -; mRNA. DR EMBL; BC063777; AAH63777.1; -; mRNA. DR EMBL; BC083120; AAH83120.1; -; mRNA. DR EMBL; BC098321; AAH98321.1; -; mRNA. DR EMBL; BC108337; AAI08338.1; -; mRNA. DR EMBL; BC108394; AAI08395.1; -; mRNA. DR EMBL; M28727; AAA40507.1; -; mRNA. DR CCDS; CCDS37195.1; -. DR PIR; I77425; I77425. DR PIR; S29013; A61275. DR RefSeq; NP_035784.1; NM_011654.2. DR UniGene; Mm.392113; -. DR UniGene; Mm.491454; -. DR ProteinModelPortal; P05213; -. DR SMR; P05213; -. DR BioGrid; 204373; 12. DR IntAct; P05213; 18. DR MINT; MINT-1869669; -. DR STRING; 10090.ENSMUSP00000076777; -. DR iPTMnet; P05213; -. DR PhosphoSitePlus; P05213; -. DR SwissPalm; P05213; -. DR REPRODUCTION-2DPAGE; P05213; -. DR EPD; P05213; -. DR MaxQB; P05213; -. DR PaxDb; P05213; -. DR PeptideAtlas; P05213; -. DR PRIDE; P05213; -. DR TopDownProteomics; P05213; -. DR Ensembl; ENSMUST00000077577; ENSMUSP00000076777; ENSMUSG00000023004. DR GeneID; 22143; -. DR KEGG; mmu:22143; -. DR UCSC; uc007xoj.1; mouse. DR CTD; 10376; -. DR MGI; MGI:107804; Tuba1b. DR eggNOG; KOG1376; Eukaryota. DR eggNOG; COG5023; LUCA. DR GeneTree; ENSGT00870000136497; -. DR HOGENOM; HOG000165711; -. DR HOVERGEN; HBG000089; -. DR InParanoid; P05213; -. DR KO; K07374; -. DR OMA; WARTRNT; -. DR OrthoDB; EOG091G0736; -. DR PhylomeDB; P05213; -. DR TreeFam; TF300314; -. DR Reactome; R-MMU-1445148; Translocation of GLUT4 to the plasma membrane. DR Reactome; R-MMU-389967; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-MMU-5610787; Hedgehog 'off' state. DR Reactome; R-MMU-5620924; Intraflagellar transport. DR PRO; PR:P05213; -. DR Proteomes; UP000000589; Chromosome 15. DR Bgee; ENSMUSG00000023004; -. DR CleanEx; MM_TUBA1B; -. DR Genevisible; P05213; MM. DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0045121; C:membrane raft; IEA:Ensembl. DR GO; GO:0005874; C:microtubule; IDA:MGI. DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI. DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB. DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI. DR GO; GO:0006457; P:protein folding; TAS:Reactome. DR Gene3D; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 1. DR InterPro; IPR002452; Alpha_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR017975; Tubulin_CS. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR PANTHER; PTHR11588; PTHR11588; 1. DR Pfam; PF00091; Tubulin; 1. DR Pfam; PF03953; Tubulin_C; 1. DR PRINTS; PR01162; ALPHATUBULIN. DR PRINTS; PR01161; TUBULIN. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR SUPFAM; SSF55307; SSF55307; 1. DR PROSITE; PS00227; TUBULIN; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation; KW Microtubule; Nitration; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1 451 Tubulin alpha-1B chain. FT /FTId=PRO_0000048121. FT CHAIN 1 450 Detyrosinated tubulin alpha-1B chain. FT {ECO:0000305|PubMed:26446751, FT ECO:0000305|PubMed:27102488}. FT /FTId=PRO_0000437387. FT NP_BIND 142 148 GTP. {ECO:0000255}. FT SITE 451 451 Involved in polymerization. FT MOD_RES 40 40 N6,N6,N6-trimethyllysine; alternate. FT {ECO:0000250|UniProtKB:P68363}. FT MOD_RES 40 40 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P68363}. FT MOD_RES 48 48 Phosphoserine. FT {ECO:0000250|UniProtKB:P68363}. FT MOD_RES 232 232 Phosphoserine. FT {ECO:0000250|UniProtKB:P68363}. FT MOD_RES 282 282 Nitrated tyrosine. FT {ECO:0000250|UniProtKB:P68373}. FT MOD_RES 339 339 Omega-N-methylarginine. FT {ECO:0000250|UniProtKB:P68363}. FT MOD_RES 439 439 Phosphoserine. FT {ECO:0000250|UniProtKB:P68373}. FT MOD_RES 445 445 5-glutamyl polyglutamate. FT {ECO:0000269|PubMed:1967194}. FT MOD_RES 451 451 3'-nitrotyrosine. FT {ECO:0000250|UniProtKB:Q71U36}. FT CROSSLNK 326 326 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P68363}. FT CROSSLNK 370 370 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P68363}. FT CONFLICT 55 55 E -> G (in Ref. 2; BAE30708/BAE31107). FT {ECO:0000305}. FT CONFLICT 114 114 I -> T (in Ref. 2; BAE34741). FT {ECO:0000305}. FT CONFLICT 119 119 L -> P (in Ref. 2; BAE29999/BAE30196). FT {ECO:0000305}. FT CONFLICT 135 136 FL -> LF (in Ref. 5; AAA40507). FT {ECO:0000305}. FT CONFLICT 340 340 S -> T (in Ref. 1 and 5; AAA40507). FT {ECO:0000305}. SQ 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 //