TBB8_PANTR
ID TBB8_PANTR Reviewed; 444 AA.
AC Q8WP14;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Tubulin beta-8 chain;
GN Name=TUBB8;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11731935; DOI=10.1086/338307;
RA van Geel M., Eichler E.E., Beck A.F., Shan Z., Haaf T.,
RA van der Maarel S.M., Frants R.R., de Jong P.J.;
RT "A cascade of complex subtelomeric duplications during the evolution of the
RT hominoid and Old World monkey genomes.";
RL Am. J. Hum. Genet. 70:269-278(2002).
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). Has a
CC key role in meiotic spindle assembly and oocyte maturation (By
CC similarity). {ECO:0000250|UniProtKB:Q3ZCM7}.
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 {ECO:0000250|UniProtKB:Q3ZCM7}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q3ZCM7}.
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:Q922F4}.
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:Q71U36,
CC ECO:0000250|UniProtKB:Q922F4}.
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:Q3ZCM7}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AF355128; AAL32435.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WP14; -.
DR SMR; Q8WP14; -.
DR STRING; 9598.ENSPTRP00000050906; -.
DR PaxDb; Q8WP14; -.
DR eggNOG; KOG1375; Eukaryota.
DR InParanoid; Q8WP14; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0072687; C:meiotic spindle; ISS:UniProtKB.
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 GO; GO:0001556; P:oocyte maturation; ISS:UniProtKB.
DR GO; GO:0007056; P:spindle assembly involved in female meiosis; ISS:UniProtKB.
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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..444
FT /note="Tubulin beta-8 chain"
FT /id="PRO_0000048259"
FT REGION 423..444
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 427..444
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 172
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q3ZCM7"
FT MOD_RES 436
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
SQ SEQUENCE 444 AA; 49791 MW; 9A557A92E6C4FCCA CRC64;
MREIVLTQIG QCGNQIGAKF WEVISDEHAI NSAGTYHGDS HLQLERINVY YNEASGGRYV
PRAVLVDLEP GTMDSVRSGP FGQVFRPDNF IFGQCGAGNN WAKGHYTEGA ELMESVMDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LLSKIREEYP DRIINTFSIL PSPKVSDTVV
EPYNATLSVH QLIENADETF CIDNEALYDI CSKTLKLPTP TYGDLNHLVC ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVAELT QQMFDAKNMM
AACDPRHGRY LTAAAIFRGR MPMREVDEQM FNIQDKNSSY FADWLPNNVK TAVCDIPPRG
LKMSATFIGN NTAIQELFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEEDEEYAE EEVA
