TBAL3_HUMAN
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 03-AUG-2022, entry version 132.
DE RecName: Full=Tubulin alpha chain-like 3;
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. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain (By similarity).
CC {ECO:0000250}.
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}.
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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; 50.
DR IntAct; A6NHL2; 19.
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; A6NHL2; -.
DR PeptideAtlas; A6NHL2; -.
DR PRIDE; A6NHL2; -.
DR ProteomicsDB; 1205; -. [A6NHL2-1]
DR ProteomicsDB; 1206; -. [A6NHL2-2]
DR Antibodypedia; 24080; 220 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 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; FEFSNQL; -.
DR OrthoDB; 514396at2759; -.
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 SignaLink; A6NHL2; -.
DR BioGRID-ORCS; 79861; 10 hits in 1078 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 tissues.
DR Genevisible; A6NHL2; HS.
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:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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; 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; 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 Alternative splicing; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW GTP-binding; Microtubule; 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 BINDING 149..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
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
