TBA4B_HUMAN
ID TBA4B_HUMAN Reviewed; 241 AA.
AC Q9H853;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative tubulin-like protein alpha-4B;
DE AltName: Full=Alpha-tubulin 4B;
GN Name=TUBA4B; Synonyms=TUBA4;
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].
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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 -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AK024002; BAB14767.1; -; mRNA.
DR EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS86922.1; -.
DR AlphaFoldDB; Q9H853; -.
DR SMR; Q9H853; -.
DR IntAct; Q9H853; 8.
DR MINT; Q9H853; -.
DR ChEMBL; CHEMBL4295944; -.
DR DrugBank; DB05147; CYT997.
DR iPTMnet; Q9H853; -.
DR PhosphoSitePlus; Q9H853; -.
DR BioMuta; TUBA4B; -.
DR DMDM; 187663995; -.
DR jPOST; Q9H853; -.
DR MassIVE; Q9H853; -.
DR MaxQB; Q9H853; -.
DR PeptideAtlas; Q9H853; -.
DR PRIDE; Q9H853; -.
DR ProteomicsDB; 81178; -.
DR Ensembl; ENST00000490341.3; ENSP00000487719.1; ENSG00000243910.8.
DR MANE-Select; ENST00000490341.3; ENSP00000487719.1; NM_001355221.1; NP_001342150.1.
DR GeneCards; TUBA4B; -.
DR HGNC; HGNC:18637; TUBA4B.
DR HPA; ENSG00000243910; Tissue enriched (fallopian).
DR neXtProt; NX_Q9H853; -.
DR OpenTargets; ENSG00000243910; -.
DR VEuPathDB; HostDB:ENSG00000243910; -.
DR GeneTree; ENSGT00940000154457; -.
DR HOGENOM; CLU_015718_4_2_1; -.
DR InParanoid; Q9H853; -.
DR OMA; TTSSCWW; -.
DR PhylomeDB; Q9H853; -.
DR PathwayCommons; Q9H853; -.
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; Q9H853; -.
DR Pharos; Q9H853; Tdark.
DR PRO; PR:Q9H853; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H853; protein.
DR Bgee; ENSG00000243910; Expressed in right uterine tube and 153 other tissues.
DR Genevisible; Q9H853; 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; 3.40.50.1440; -; 1.
DR InterPro; IPR002452; Alpha_tubulin.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
PE 5: Uncertain;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..241
FT /note="Putative tubulin-like protein alpha-4B"
FT /id="PRO_0000331573"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 154
FT /note="C -> R (in Ref. 1; BAB14767)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="R -> K (in Ref. 1; BAB14767)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="W -> R (in Ref. 1; BAB14767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 27551 MW; 2CC581FEF7BF53BA CRC64;
MRHQQTERQD PSQPLSRQHG TYRQIFHPEQ LITGKEDAAN NYAWGHYTIG KEFIDLLLDR
IRKLADQCTG LQGFLVFHSL GRGTGSDVTS FLMEWLSVNY GKKSKLGFSI YPAPQVSTAM
VQPYNSILTT HTTLEHSDCA FMVDNKAIYD ICHCNLDIER PTYTNLNRLI SQIVSSITAS
LRFDGALNVD LTEFQTNLVS YLTSTSPWPP MHQSSLQKRY TTSSCWWQRL PMPALSLPTR
W
