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 22-JUL-2008, entry version 85. DE RecName: Full=Tubulin alpha-1B chain; DE AltName: Full=Tubulin alpha-2 chain; DE AltName: Full=Alpha-tubulin 2; DE AltName: Full=Alpha-tubulin isotype M-alpha-2; 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. 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; 85-96; 112-121; 216-280; 327-336; RP 340-370; 374-390; 395-401 AND 403-432, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP PROTEIN SEQUENCE OF 65-79; 113-121; 216-280; 340-352 AND 403-422, AND RP MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [6] 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). 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 -!- 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 -!- 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 PIR; I77425; I77425. DR PIR; S29013; A61275. DR RefSeq; NP_035784.1; -. DR UniGene; Mm.392113; -. DR UniGene; Mm.456836; -. DR HSSP; P02550; 1FFX. DR SMR; P05213; 2-439. DR PhosphoSite; P05213; -. DR REPRODUCTION-2DPAGE; P05213; -. DR Ensembl; ENSMUSG00000023004; Mus musculus. DR GeneID; 22143; -. DR KEGG; mmu:22143; -. DR MGI; MGI:107804; Tuba1b. DR HOGENOM; P05213; -. DR HOVERGEN; P05213; -. DR CleanEx; MM_TUBA1B; -. DR GermOnline; ENSMUSG00000023004; Mus musculus. DR GO; GO:0005874; C:microtubule; IDA:MGI. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization and b...; IDA:MGI. DR InterPro; IPR002452; Alpha_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1. DR PANTHER; PTHR11588:SF10; Alpha_tubulin; 1. DR PANTHER; PTHR11588; Tubulin; 1. DR Pfam; PF00091; Tubulin; 1. DR Pfam; PF03953; Tubulin_C; 1. DR PRINTS; PR01162; ALPHATUBULIN. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; GTP-binding; Microtubule; KW Nucleotide-binding. 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 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. 6; AAA40507). FT CONFLICT 340 340 S -> T (in Ref. 1 and 6). 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 //