ID TBAL3_HUMAN Reviewed; 446 AA. AC A6NHL2; B4DKL2; Q4QQJ5; Q9H6Z0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 27-MAR-2024, entry version 141. DE RecName: Full=Tubulin alpha chain-like 3; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68363}; GN Name=TUBAL3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Colon; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 104-112; 147-163; 319-327 AND 402-408, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain; RA Lubec G., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder CC consisting of laterally associated linear protofilaments composed of CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to CC GTPase activity of alpha-tubulin. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a CC hollow water-filled tube with an outer diameter of 25 nm and an inner CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to CC form protofilaments running lengthwise along the microtubule wall with CC the beta-tubulin subunit facing the microtubule plus end conferring a CC structural polarity. Microtubules usually have 13 protofilaments but CC different protofilament numbers can be found in some organisms and CC specialized cells. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=A6NHL2-1; Sequence=Displayed; CC Name=2; CC IsoId=A6NHL2-2; Sequence=VSP_030108; CC -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation. CC {ECO:0000250|UniProtKB:P68363}. CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated, CC resulting in polyglutamate chains on the gamma-carboxyl group. CC Polyglutamylation plays a key role in microtubule severing by spastin CC (SPAST). SPAST preferentially recognizes and acts on microtubules CC decorated with short polyglutamate tails: severing activity by SPAST CC increases as the number of glutamates per tubulin rises from one to CC eight, but decreases beyond this glutamylation threshold. Glutamylation CC is also involved in cilia motility (By similarity). CC {ECO:0000250|UniProtKB:P99024, ECO:0000250|UniProtKB:Q71U36}. CC -!- PTM: Some glutamate residues at the C-terminus are monoglycylated but CC not polyglycylated due to the absence of functional TTLL10 in human. CC Monoglycylation is mainly limited to tubulin incorporated into cilia CC and flagella axonemes, which is required for their stability and CC maintenance. Flagella glycylation controls sperm motility. Both CC polyglutamylation and monoglycylation can coexist on the same protein CC on adjacent residues, and lowering glycylation levels increases CC polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P07437}. 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; AK025318; BAB15110.1; -; mRNA. DR EMBL; AK296616; BAG59224.1; -; mRNA. DR EMBL; AL683826; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86447.1; -; Genomic_DNA. DR EMBL; BC098247; AAH98247.1; -; mRNA. DR EMBL; BC099716; AAH99716.1; -; mRNA. DR EMBL; BC105634; AAI05635.1; -; mRNA. DR CCDS; CCDS53491.1; -. [A6NHL2-2] DR CCDS; CCDS7066.2; -. [A6NHL2-1] DR RefSeq; NP_001165335.1; NM_001171864.1. [A6NHL2-2] DR RefSeq; NP_079079.1; NM_024803.2. [A6NHL2-1] DR AlphaFoldDB; A6NHL2; -. DR SMR; A6NHL2; -. DR BioGRID; 122949; 58. DR IntAct; A6NHL2; 20. DR MINT; A6NHL2; -. DR STRING; 9606.ENSP00000369784; -. DR BindingDB; A6NHL2; -. DR ChEMBL; CHEMBL3832941; -. DR GlyGen; A6NHL2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; A6NHL2; -. DR MetOSite; A6NHL2; -. DR PhosphoSitePlus; A6NHL2; -. DR BioMuta; TUBAL3; -. DR EPD; A6NHL2; -. DR jPOST; A6NHL2; -. DR MassIVE; A6NHL2; -. DR MaxQB; A6NHL2; -. DR PaxDb; 9606-ENSP00000369784; -. DR PeptideAtlas; A6NHL2; -. DR PRIDE; A6NHL2; -. DR ProteomicsDB; 1205; -. [A6NHL2-1] DR ProteomicsDB; 1206; -. [A6NHL2-2] DR Pumba; A6NHL2; -. DR Antibodypedia; 24080; 253 antibodies from 15 providers. DR DNASU; 79861; -. DR Ensembl; ENST00000380419.8; ENSP00000369784.3; ENSG00000178462.12. [A6NHL2-1] DR Ensembl; ENST00000479328.1; ENSP00000418799.1; ENSG00000178462.12. [A6NHL2-2] DR GeneID; 79861; -. DR KEGG; hsa:79861; -. DR MANE-Select; ENST00000380419.8; ENSP00000369784.3; NM_024803.3; NP_079079.1. DR UCSC; uc001ihy.3; human. [A6NHL2-1] DR AGR; HGNC:23534; -. DR CTD; 79861; -. DR GeneCards; TUBAL3; -. DR HGNC; HGNC:23534; TUBAL3. DR HPA; ENSG00000178462; Tissue enriched (intestine). DR neXtProt; NX_A6NHL2; -. DR OpenTargets; ENSG00000178462; -. DR PharmGKB; PA134953102; -. DR VEuPathDB; HostDB:ENSG00000178462; -. DR eggNOG; KOG1376; Eukaryota. DR GeneTree; ENSGT00940000162594; -. DR HOGENOM; CLU_015718_0_0_1; -. DR InParanoid; A6NHL2; -. DR OMA; VYDICHH; -. DR OrthoDB; 899149at2759; -. DR PhylomeDB; A6NHL2; -. DR TreeFam; TF300314; -. DR PathwayCommons; A6NHL2; -. DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane. DR Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane. DR Reactome; R-HSA-190861; Gap junction assembly. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway. DR Reactome; R-HSA-437239; Recycling pathway of L1. DR Reactome; R-HSA-5617833; Cilium Assembly. DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors. DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs. DR Reactome; R-HSA-9646399; Aggrephagy. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III. DR Reactome; R-HSA-983189; Kinesins. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; A6NHL2; -. DR BioGRID-ORCS; 79861; 11 hits in 1157 CRISPR screens. DR GenomeRNAi; 79861; -. DR Pharos; A6NHL2; Tdark. DR PRO; PR:A6NHL2; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; A6NHL2; Protein. DR Bgee; ENSG00000178462; Expressed in jejunal mucosa and 83 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR CDD; cd02186; alpha_tubulin; 1. DR Gene3D; 1.10.287.600; Helix hairpin bin; 1. DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1. DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1. DR InterPro; IPR002452; Alpha_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR037103; Tubulin/FtsZ-like_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf. DR InterPro; IPR023123; Tubulin_C. DR InterPro; IPR017975; Tubulin_CS. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR PANTHER; PTHR11588; TUBULIN; 1. DR PANTHER; PTHR11588:SF278; TUBULIN ALPHA CHAIN-LIKE 3; 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; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. DR PROSITE; PS00227; TUBULIN; 1. DR Genevisible; A6NHL2; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW GTP-binding; Hydrolase; Magnesium; Metal-binding; Microtubule; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..446 FT /note="Tubulin alpha chain-like 3" FT /id="PRO_0000313709" FT MOTIF 1..4 FT /note="MREC motif" FT /evidence="ECO:0000250|UniProtKB:P68363" FT ACT_SITE 261 FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 11 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 78 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 78 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 147 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 151 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 152 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 186 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 213 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 235 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT VAR_SEQ 1..41 FT /note="MRECLSIHIGQAGIQIGDACWELYCLEHGIQPNGVVLDTQQ -> M (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_030108" FT VARIANT 135 FT /note="Q -> H (in dbSNP:rs11818372)" FT /id="VAR_037706" FT VARIANT 250 FT /note="R -> W (in dbSNP:rs34080891)" FT /id="VAR_037707" FT CONFLICT 128 FT /note="R -> G (in Ref. 1; BAG59224)" FT /evidence="ECO:0000305" FT CONFLICT 134 FT /note="E -> K (in Ref. 3; EAW86447)" FT /evidence="ECO:0000305" SQ SEQUENCE 446 AA; 49909 MW; D826240ACC90B6EC CRC64; MRECLSIHIG QAGIQIGDAC WELYCLEHGI QPNGVVLDTQ QDQLENAKME HTNASFDTFF CETRAGKHVP RALFVDLEPT VIDGIRTGQH RSLFHPEQLL SGKEDAANNY ARGRYSVGSE VIDLVLERTR KLAEQCGGLQ GFLIFRSFGG GTGSGFTSLL MERLTGEYSR KTKLEFSVYP APRISTAVVE PYNSVLTTHS TTEHTDCTFM VDNEAVYDIC HRKLGVECPS HASINRLVVQ VVSSITASLR FEGPLNVDLI EFQTNLVPYP RIHFPMTAFA PIVSADKAYH EQFSVSDITT ACFESSNQLV KCDPRLGKYM ACCLLYRGDV VPKEVNAAIA ATKSRHSVQF VDWCPTGFKV GINNRPPTVM PGGDLAKVHR SICMLSNTTA IVEAWARLDH KFDLMYAKRA FLHWYLREGM EEAEFLEARE DLAALERDYE EVAQSF //