TBB2_CHICK
ID TBB2_CHICK Reviewed; 445 AA.
AC P32882; P02555;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tubulin beta-2 chain;
DE AltName: Full=Beta-tubulin class-II;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7464932; DOI=10.1038/289650a0;
RA Valenzuela P., Quiroga M., Zaldivar J., Rutter W.J., Kirschner M.W.,
RA Cleveland D.W.;
RT "Nucleotide and corresponding amino acid sequences encoded by alpha and
RT beta tubulin mRNAs.";
RL Nature 289:650-655(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3837190; DOI=10.1128/mcb.5.9.2454-2465.1985;
RA Sullivan K.F., Lau J.T.Y., Cleveland D.W.;
RT "Apparent gene conversion between beta-tubulin genes yields multiple
RT regulatory pathways for a single beta-tubulin polypeptide isotype.";
RL Mol. Cell. Biol. 5:2454-2465(1985).
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 -!- TISSUE SPECIFICITY: Highly expressed in neuronal cells.
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. The precise function of polyglycylation is still unclear.
CC {ECO:0000250|UniProtKB:A2AQ07}.
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). {ECO:0000250|UniProtKB:A2AQ07,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; V00389; CAA23687.1; -; mRNA.
DR EMBL; M11443; AAA49125.1; -; Genomic_DNA.
DR PIR; A02974; UBCHB.
DR RefSeq; NP_001004400.1; NM_001004400.2.
DR PDB; 5CA1; X-ray; 2.40 A; B/D=1-445.
DR PDBsum; 5CA1; -.
DR AlphaFoldDB; P32882; -.
DR SMR; P32882; -.
DR IntAct; P32882; 1.
DR STRING; 9031.ENSGALP00000020884; -.
DR PRIDE; P32882; -.
DR Ensembl; ENSGALT00000020914; ENSGALP00000020884; ENSGALG00000012821.
DR GeneID; 420883; -.
DR KEGG; gga:420883; -.
DR CTD; 347733; -.
DR VEuPathDB; HostDB:geneid_420883; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000154150; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR OMA; SYVGNSH; -.
DR OrthoDB; 962471at2759; -.
DR Reactome; R-GGA-2467813; Separation of Sister Chromatids.
DR Reactome; R-GGA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-GGA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-GGA-5620924; Intraflagellar transport.
DR Reactome; R-GGA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-GGA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-9646399; Aggrephagy.
DR Reactome; R-GGA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-GGA-983189; Kinesins.
DR PRO; PR:P32882; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000012821; Expressed in brain and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IMP:CAFA.
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:0031115; P:negative regulation of microtubule polymerization; IMP:CAFA.
DR DisProt; DP00169; -.
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; Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond;
KW Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..445
FT /note="Tubulin beta-2 chain"
FT /id="PRO_0000048264"
FT REGION 424..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 431..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 438
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 10..27
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5CA1"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5CA1"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:5CA1"
FT STRAND 362..371
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 375..389
FT /evidence="ECO:0007829|PDB:5CA1"
FT TURN 390..395
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:5CA1"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:5CA1"
FT HELIX 405..426
FT /evidence="ECO:0007829|PDB:5CA1"
SQ SEQUENCE 445 AA; 49953 MW; 4DC3956EFCEB6746 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA DEQGEFEEEG EEDEA
