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Database: UniProt
Entry: TBB2A_RAT
LinkDB: TBB2A_RAT
Original site: TBB2A_RAT 
ID   TBB2A_RAT               Reviewed;         445 AA.
AC   P85108;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Tubulin beta-2A chain;
GN   Name=Tubb2a {ECO:0000250|UniProtKB:Q7TMM9};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 3-19; 47-58; 104-121 AND 242-251, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Chen W.-Q., Afjehi-Sadat L.;
RL   Submitted (DEC-2006) to UniProtKB.
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC       consisting of laterally associated linear protofilaments composed of
CC       alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC       of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC       forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC       GTPase activity of alpha-tubulin.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC   -!- SUBUNIT: Part of complex consisting of SFPQ, NONO and MATR3. Interacts
CC       with AGO1 and AGO2 (By similarity). Part of a complex composed at least
CC       of ASH2L, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5
CC       and ZNF335; this complex may have a histone H3-specific
CC       methyltransferase activity (By similarity). Dimer of alpha and beta
CC       chains. A typical microtubule is a hollow water-filled tube with an
CC       outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta
CC       heterodimers associate head-to-tail to form protofilaments running
CC       lengthwise along the microtubule wall with the beta-tubulin subunit
CC       facing the microtubule plus end conferring a structural polarity.
CC       Microtubules usually have 13 protofilaments but different protofilament
CC       numbers can be found in some organisms and specialized cells. Interacts
CC       with TFCB. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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:Q7TMM9}.
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:Q7TMM9}.
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:Q13885}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000255}.
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DR   EMBL; AC112857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001102589.1; NM_001109119.1.
DR   AlphaFoldDB; P85108; -.
DR   SMR; P85108; -.
DR   BioGRID; 270046; 8.
DR   IntAct; P85108; 5.
DR   MINT; P85108; -.
DR   STRING; 10116.ENSRNOP00000071729; -.
DR   GlyGen; P85108; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P85108; -.
DR   PhosphoSitePlus; P85108; -.
DR   SwissPalm; P85108; -.
DR   jPOST; P85108; -.
DR   PaxDb; 10116-ENSRNOP00000023611; -.
DR   Ensembl; ENSRNOT00055024356; ENSRNOP00055019908; ENSRNOG00055014170.
DR   Ensembl; ENSRNOT00060034947; ENSRNOP00060028702; ENSRNOG00060020190.
DR   GeneID; 498736; -.
DR   KEGG; rno:498736; -.
DR   UCSC; RGD:1588452; rat.
DR   AGR; RGD:1588452; -.
DR   CTD; 7280; -.
DR   RGD; 1588452; Tubb2a.
DR   VEuPathDB; HostDB:ENSRNOG00000017558; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   InParanoid; P85108; -.
DR   OrthoDB; 3124041at2759; -.
DR   PhylomeDB; P85108; -.
DR   TreeFam; TF300298; -.
DR   Reactome; R-RNO-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR   Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-RNO-437239; Recycling pathway of L1.
DR   Reactome; R-RNO-5610787; Hedgehog 'off' state.
DR   Reactome; R-RNO-5617833; Cilium Assembly.
DR   Reactome; R-RNO-5620924; Intraflagellar transport.
DR   Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-RNO-68877; Mitotic Prometaphase.
DR   Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-RNO-8955332; Carboxyterminal post-translational modifications of tubulin.
DR   Reactome; R-RNO-9646399; Aggrephagy.
DR   Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-RNO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   Reactome; R-RNO-983189; Kinesins.
DR   Reactome; R-RNO-9833482; PKR-mediated signaling.
DR   PRO; PR:P85108; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000017558; Expressed in Ammon's horn and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; ISO:RGD.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd02187; beta_tubulin; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF488; TUBULIN BETA-2A CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Isopeptide bond; Magnesium; Metal-binding; Methylation;
KW   Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..445
FT                   /note="Tubulin beta-2A chain"
FT                   /id="PRO_0000283741"
FT   REGION          422..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         11
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q13509"
FT   BINDING         69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q13509"
FT   BINDING         142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q13509"
FT   BINDING         143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q13509"
FT   BINDING         144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q13509"
FT   BINDING         204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q13509"
FT   BINDING         226
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q13509"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P99024"
FT   MOD_RES         58
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P07437"
FT   MOD_RES         58
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P99024"
FT   MOD_RES         172
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13885"
FT   MOD_RES         285
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07437"
FT   MOD_RES         290
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07437"
FT   MOD_RES         318
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P07437"
FT   MOD_RES         438
FT                   /note="5-glutamyl polyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT   CROSSLNK        58
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P07437"
FT   CROSSLNK        324
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P07437"
SQ   SEQUENCE   445 AA;  49907 MW;  93B3213EB2A9367B CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV
     PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV
     EPYNATLSVH QLVENTDETY SIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
     AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA DEQGEFEEEE GEDEA
//
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