TBCB_MOUSE
ID TBCB_MOUSE Reviewed; 244 AA.
AC Q9D1E6; Q9CWR6; Q9DCZ6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tubulin-folding cofactor B;
DE AltName: Full=Cytoskeleton-associated protein 1;
DE AltName: Full=Cytoskeleton-associated protein CKAPI;
DE AltName: Full=Tubulin-specific chaperone B;
GN Name=Tbcb; Synonyms=Ckap1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH TBCE.
RX PubMed=17184771; DOI=10.1016/j.yexcr.2006.09.002;
RA Kortazar D., Fanarraga M.L., Carranza G., Bellido J., Villegas J.C.,
RA Avila J., Zabala J.C.;
RT "Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer
RT dissociation.";
RL Exp. Cell Res. 313:425-436(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17217416; DOI=10.1111/j.1471-4159.2006.04328.x;
RA Lopez-Fanarraga M., Carranza G., Bellido J., Kortazar D., Villegas J.C.,
RA Zabala J.C.;
RT "Tubulin cofactor B plays a role in the neuronal growth cone.";
RL J. Neurochem. 100:1680-1687(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP STRUCTURE BY NMR OF 11-92.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of a N-terminal ubiquitin-like domain in mouse tubulin-
RT specific chaperone B.";
RL Submitted (NOV-2003) to the PDB data bank.
RN [8]
RP STRUCTURE BY NMR OF 134-233.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CAP-Gly domain in mouse tubulin-specific
RT chaperone B.";
RL Submitted (NOV-2003) to the PDB data bank.
CC -!- FUNCTION: Binds to alpha-tubulin folding intermediates after their
CC interaction with cytosolic chaperonin in the pathway leading from newly
CC synthesized tubulin to properly folded heterodimer (By similarity).
CC Involved in regulation of tubulin heterodimer dissociation
CC (PubMed:17184771). May function as a negative regulator of axonal
CC growth (PubMed:17217416). {ECO:0000250|UniProtKB:Q99426,
CC ECO:0000269|PubMed:17184771, ECO:0000269|PubMed:17217416}.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state (By similarity).
CC Cofactors B and E can form a heterodimer which binds to alpha-tubulin
CC and enhances their ability to dissociate tubulin heterodimers
CC (PubMed:17184771). Interacts with GAN. Interacts with DCTN1 (By
CC similarity). {ECO:0000250|UniProtKB:Q99426,
CC ECO:0000269|PubMed:17184771}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17217416}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17217416}. Note=Colocalizes
CC with microtubules. In differentiated neurons, located in the cytoplasm.
CC In differentiating neurons, accumulates at the growth cone.
CC {ECO:0000269|PubMed:17217416}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain.
CC Broadly distributed throughout the neonate brain but restricted mainly
CC to ependymary cells in the adult brain where it is concentrated in the
CC cilia. {ECO:0000269|PubMed:17217416}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression increases at 12.5 dpc-
CC 14.5 dpc. Levels are highest in pre- and postnatal stages which
CC coincide with peaks of cerebral and cerebellar neurogenesis (at protein
CC level). {ECO:0000269|PubMed:17217416}.
CC -!- PTM: Phosphorylation by PAK1 is required for normal function.
CC {ECO:0000250|UniProtKB:Q99426}.
CC -!- PTM: Ubiquitinated in the presence of GAN which targets it for
CC degradation by the proteasome. {ECO:0000250|UniProtKB:Q99426}.
CC -!- DISRUPTION PHENOTYPE: Mice display significantly longer axons than
CC wild-type mice. Overexpression of Tbcb causes microtubule
CC depolymerization, growth cone retraction and axonal damage followed by
CC neuronal degeneration. {ECO:0000269|PubMed:17217416}.
CC -!- SIMILARITY: Belongs to the TBCB family. {ECO:0000305}.
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DR EMBL; AK002316; BAB22009.1; -; mRNA.
DR EMBL; AK003655; BAB22918.2; -; mRNA.
DR EMBL; AK010438; BAB26939.1; -; mRNA.
DR EMBL; BC010684; AAH10684.1; -; mRNA.
DR CCDS; CCDS21083.1; -.
DR RefSeq; NP_079824.2; NM_025548.3.
DR PDB; 1V6E; NMR; -; A=11-92.
DR PDB; 1WHG; NMR; -; A=134-233.
DR PDBsum; 1V6E; -.
DR PDBsum; 1WHG; -.
DR AlphaFoldDB; Q9D1E6; -.
DR BMRB; Q9D1E6; -.
DR SMR; Q9D1E6; -.
DR BioGRID; 211455; 18.
DR IntAct; Q9D1E6; 2.
DR MINT; Q9D1E6; -.
DR STRING; 10090.ENSMUSP00000006254; -.
DR iPTMnet; Q9D1E6; -.
DR PhosphoSitePlus; Q9D1E6; -.
DR EPD; Q9D1E6; -.
DR jPOST; Q9D1E6; -.
DR MaxQB; Q9D1E6; -.
DR PaxDb; Q9D1E6; -.
DR PeptideAtlas; Q9D1E6; -.
DR PRIDE; Q9D1E6; -.
DR ProteomicsDB; 263133; -.
DR Antibodypedia; 29702; 297 antibodies from 29 providers.
DR DNASU; 66411; -.
DR Ensembl; ENSMUST00000006254; ENSMUSP00000006254; ENSMUSG00000006095.
DR GeneID; 66411; -.
DR KEGG; mmu:66411; -.
DR UCSC; uc009gds.2; mouse.
DR CTD; 1155; -.
DR MGI; MGI:1913661; Tbcb.
DR VEuPathDB; HostDB:ENSMUSG00000006095; -.
DR eggNOG; KOG3206; Eukaryota.
DR GeneTree; ENSGT00940000156119; -.
DR HOGENOM; CLU_067577_0_0_1; -.
DR InParanoid; Q9D1E6; -.
DR OMA; IGVKYDE; -.
DR OrthoDB; 1550378at2759; -.
DR PhylomeDB; Q9D1E6; -.
DR TreeFam; TF313444; -.
DR BioGRID-ORCS; 66411; 28 hits in 77 CRISPR screens.
DR ChiTaRS; Tbcb; mouse.
DR EvolutionaryTrace; Q9D1E6; -.
DR PRO; PR:Q9D1E6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D1E6; protein.
DR Bgee; ENSMUSG00000006095; Expressed in facial nucleus and 258 other tissues.
DR Genevisible; Q9D1E6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd01789; Ubl_TBCB; 1.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR045172; TBCB_N_Ubl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Microtubule; Neurogenesis;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..244
FT /note="Tubulin-folding cofactor B"
FT /id="PRO_0000083535"
FT DOMAIN 183..225
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99426"
FT MOD_RES 65
FT /note="Phosphoserine; by PAK1"
FT /evidence="ECO:0000250|UniProtKB:Q99426"
FT MOD_RES 98
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 128
FT /note="Phosphoserine; by PAK1"
FT /evidence="ECO:0000250|UniProtKB:Q99426"
FT MOD_RES 219
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99426"
FT CONFLICT 84
FT /note="R -> S (in Ref. 1; BAB26939)"
FT /evidence="ECO:0000305"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:1V6E"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1V6E"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1V6E"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1V6E"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1V6E"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1V6E"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1V6E"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1V6E"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1V6E"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1V6E"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1V6E"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:1WHG"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:1WHG"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1WHG"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1WHG"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:1WHG"
FT STRAND 186..200
FT /evidence="ECO:0007829|PDB:1WHG"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1WHG"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1WHG"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:1WHG"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1WHG"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1WHG"
SQ SEQUENCE 244 AA; 27386 MW; 03BC7F0134F9289C CRC64;
MEVTGISAPT VMVFISSSLN SFRSEKRYSR SLTIAEFKCK LELVVGSPAS CMELELYGAD
DKFYSKLDQE DALLGSYPVD DGCRIHVIDH SGVRLGEYED VSKVEKYEIS PEAYERRQNT
VRSFMKRSKL GPYNEELRAQ QEAEAAQRLS EEKAQASAIS VGSRCEVRAP DHSLRRGTVM
YVGLTDFKPG YWVGVRYDEP LGKNDGSVNG KRYFECQAKY GAFVKPSAVT VGDFPEEDYG
LDEM
