TBB4B_BOVIN
ID TBB4B_BOVIN Reviewed; 445 AA.
AC Q3MHM5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Tubulin beta-4B chain;
DE AltName: Full=Tubulin beta-2C chain;
GN Name=TUBB4B; Synonyms=TUBB2C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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.
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.
CC -!- DOMAIN: The highly acidic C-terminal region may bind cations such as
CC calcium.
CC -!- DOMAIN: The MREI motif is common among all beta-tubulin isoforms and
CC may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P07437}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC resulting in polyglycine chains on the gamma-carboxyl group.
CC Glycylation is mainly limited to tubulin incorporated into axonemes
CC (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC cells, centrioles, axonemes, and the mitotic spindle. Both
CC modifications can coexist on the same protein on adjacent residues, and
CC lowering polyglycylation levels increases polyglutamylation, and
CC reciprocally. Cilia and flagella glycylation is required for their
CC stability and maintenance. Flagella glycylation controls sperm
CC motility. {ECO:0000250|UniProtKB:P68372}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group (By
CC similarity). Polyglutamylation plays a key role in microtubule severing
CC by spastin (SPAST). SPAST preferentially recognizes and acts on
CC microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (By similarity). Glutamylation is also involved in cilia
CC motility (By similarity). {ECO:0000250|UniProtKB:P68372,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
CC metaphase to telophase, but not in interphase. This phosphorylation
CC inhibits tubulin incorporation into microtubules.
CC {ECO:0000250|UniProtKB:P68371}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; BC105181; AAI05182.1; -; mRNA.
DR RefSeq; NP_001029835.1; NM_001034663.2.
DR PDB; 7RRO; EM; 3.40 A; AB/AD/AF/AH/AJ/AL/BB/BD/BF/BH/BJ/BL/CB/CD/CF/CH/CJ/CL/DB/DD/DF/DH/DJ/DL/DN/EB/ED/EF/EH/EJ=1-445.
DR PDBsum; 7RRO; -.
DR AlphaFoldDB; Q3MHM5; -.
DR SMR; Q3MHM5; -.
DR STRING; 9913.ENSBTAP00000008372; -.
DR iPTMnet; Q3MHM5; -.
DR PaxDb; Q3MHM5; -.
DR PeptideAtlas; Q3MHM5; -.
DR PRIDE; Q3MHM5; -.
DR Ensembl; ENSBTAT00000074704; ENSBTAP00000064454; ENSBTAG00000052518.
DR GeneID; 539149; -.
DR KEGG; bta:539149; -.
DR CTD; 10383; -.
DR VEuPathDB; HostDB:ENSBTAG00000052518; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000154394; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q3MHM5; -.
DR OMA; VCSVAPK; -.
DR OrthoDB; 962471at2759; -.
DR TreeFam; TF300298; -.
DR Reactome; R-BTA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-BTA-5610787; Hedgehog 'off' state.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-BTA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-BTA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-BTA-983189; Kinesins.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000052518; Expressed in retina and 108 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; 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; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_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; PR01163; BETATUBULIN.
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.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; GTP-binding;
KW Isopeptide bond; Microtubule; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..445
FT /note="Tubulin beta-4B chain"
FT /id="PRO_0000233028"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..4
FT /note="MREI motif"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT COMPBIAS 428..445
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68371"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68371"
FT MOD_RES 172
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P68371"
FT MOD_RES 438
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
SQ SEQUENCE 445 AA; 49831 MW; A552C52822AFA072 CRC64;
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGKYV
PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEFEEEA EEEVA
