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 06-MAR-2013, entry version 130. 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; GN Name=Tuba1b; Synonyms=Tuba2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87064538; PubMed=3785200; 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 MASS SPECTROMETRY. RC STRAIN=C57BL/6, 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 MEDLINE=85289512; 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 POLYGLUTAMYLATION. 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 [7] RP POLYGLYCYLATION. 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). 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in CC spleen, thymus and immature brain. 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 (By similarity). CC -!- PTM: Some glutamate residues at the C-terminus are either CC polyglutamylated or polyglycylated. These 2 modifications occur CC exclusively on glutamate residues and result in either CC polyglutamate or 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 such CC modifications is still unclear but they are regulate the assembly CC and dynamics of axonemal microtubules. CC -!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules CC and affects affinity and processivity of microtubule motors. This CC modification has a role in multiple cellular functions, ranging CC from cell motility, cell cycle progression or cell differentiation CC to intracellular trafficking and signaling (By similarity). CC -!- SIMILARITY: Belongs to the tubulin family. 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 IPI; IPI00117348; -. DR PIR; I77425; I77425. DR PIR; S29013; A61275. DR RefSeq; NP_035784.1; NM_011654.2. DR UniGene; Mm.343377; -. DR UniGene; Mm.392113; -. DR UniGene; Mm.405359; -. DR ProteinModelPortal; P05213; -. DR SMR; P05213; 1-437. DR IntAct; P05213; 13. DR STRING; P05213; -. DR PhosphoSite; P05213; -. DR REPRODUCTION-2DPAGE; P05213; -. DR PaxDb; P05213; -. DR PRIDE; P05213; -. DR Ensembl; ENSMUST00000077577; ENSMUSP00000076777; ENSMUSG00000023004. DR GeneID; 22143; -. DR KEGG; mmu:22143; -. DR CTD; 10376; -. DR MGI; MGI:107804; Tuba1b. DR eggNOG; COG5023; -. DR GeneTree; ENSGT00690000101720; -. DR HOGENOM; HOG000165711; -. DR HOVERGEN; HBG000089; -. DR InParanoid; P05213; -. DR KO; K07374; -. DR OMA; KRATHES; -. DR OrthoDB; EOG44J2HZ; -. DR Reactome; REACT_147847; Translocation of Glut4 to the Plasma Membrane. DR Reactome; REACT_17056; Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding. DR Reactome; REACT_88307; Membrane Trafficking. DR Reactome; REACT_93132; Metabolism of proteins. DR NextBio; 302042; -. DR Bgee; P05213; -. DR CleanEx; MM_TUBA1B; -. DR Genevestigator; P05213; -. DR GermOnline; ENSMUSG00000023004; Mus musculus. DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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:0071353; P:cellular response to interleukin-4; IDA:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI. DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro. DR GO; GO:0006457; P:protein folding; TAS:Reactome. DR GO; GO:0051258; P:protein polymerization; IEA:InterPro. DR Gene3D; 1.10.287.600; -; 1. 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; IPR023123; Tubulin_C. 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; SSF55307; Tub_FtsZ_C; 1. DR SUPFAM; SSF52490; Tubulin_FtsZ; 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; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1 451 Tubulin alpha-1B chain. FT /FTId=PRO_0000048121. FT NP_BIND 142 148 GTP (Potential). FT SITE 451 451 Involved in polymerization. FT MOD_RES 40 40 N6-acetyllysine (By similarity). FT MOD_RES 41 41 Phosphothreonine (By similarity). FT MOD_RES 48 48 Phosphoserine (By similarity). FT MOD_RES 232 232 Phosphoserine (By similarity). FT MOD_RES 334 334 Phosphothreonine (By similarity). FT MOD_RES 339 339 Omega-N-methylarginine (By similarity). FT MOD_RES 340 340 Phosphoserine (By similarity). FT MOD_RES 432 432 Phosphotyrosine (By similarity). FT MOD_RES 439 439 Phosphoserine (By similarity). FT MOD_RES 451 451 Phosphotyrosine (By similarity). FT CROSSLNK 326 326 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT CROSSLNK 370 370 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT CONFLICT 55 55 E -> G (in Ref. 2; BAE30708/BAE31107). FT CONFLICT 114 114 I -> T (in Ref. 2; BAE34741). FT CONFLICT 119 119 L -> P (in Ref. 2; BAE29999/BAE30196). FT CONFLICT 135 136 FL -> LF (in Ref. 5; AAA40507). FT CONFLICT 340 340 S -> T (in Ref. 1 and 5; AAA40507). 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 //