TBCE_HUMAN
ID TBCE_HUMAN Reviewed; 527 AA.
AC Q15813; A8K8C2; B7Z3P1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Tubulin-specific chaperone E;
DE AltName: Full=Tubulin-folding cofactor E;
GN Name=TBCE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8706133; DOI=10.1016/s0092-8674(00)80100-2;
RA Tian G., Huang Y., Rommelaere H., Vandekerckhove J., Ampe C., Cowan N.J.;
RT "Pathway leading to correctly folded beta-tubulin.";
RL Cell 86:287-296(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP FUNCTION.
RX PubMed=11847227; DOI=10.1074/jbc.m200128200;
RA Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A.,
RA Cowan N.J.;
RT "Functional overlap between retinitis pigmentosa 2 protein and the tubulin-
RT specific chaperone cofactor C.";
RL J. Biol. Chem. 277:14629-14634(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-463, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INTERACTION WITH TBCD.
RX PubMed=27666374; DOI=10.1016/j.ajhg.2016.08.005;
RA Miyake N., Fukai R., Ohba C., Chihara T., Miura M., Shimizu H., Kakita A.,
RA Imagawa E., Shiina M., Ogata K., Okuno-Yuguchi J., Fueki N., Ogiso Y.,
RA Suzumura H., Watabe Y., Imataka G., Leong H.Y., Fattal-Valevski A.,
RA Kramer U., Miyatake S., Kato M., Okamoto N., Sato Y., Mitsuhashi S.,
RA Nishino I., Kaneko N., Nishiyama A., Tamura T., Mizuguchi T., Nakashima M.,
RA Tanaka F., Saitsu H., Matsumoto N.;
RT "Biallelic TBCD mutations cause early-onset neurodegenerative
RT encephalopathy.";
RL Am. J. Hum. Genet. 99:950-961(2016).
RN [15]
RP FUNCTION, INVOLVEMENT IN PEAMO, VARIANT PEAMO ASN-155, AND CHARACTERIZATION
RP OF VARIANT PEAMO ASN-155.
RX PubMed=27666369; DOI=10.1016/j.ajhg.2016.08.006;
RA Sferra A., Baillat G., Rizza T., Barresi S., Flex E., Tasca G., D'Amico A.,
RA Bellacchio E., Ciolfi A., Caputo V., Cecchetti S., Torella A., Zanni G.,
RA Diodato D., Piermarini E., Niceta M., Coppola A., Tedeschi E.,
RA Martinelli D., Dionisi-Vici C., Nigro V., Dallapiccola B., Compagnucci C.,
RA Tartaglia M., Haase G., Bertini E.;
RT "TBCE mutations cause early-onset progressive encephalopathy with distal
RT spinal muscular atrophy.";
RL Am. J. Hum. Genet. 99:974-983(2016).
RN [16]
RP VARIANT HRDS 52-SER--GLY-55 DEL, AND VARIANT KCS1 52-SER--GLY-55 DEL.
RX PubMed=12389028; DOI=10.1038/ng1012;
RA Parvari R., Hershkovitz E., Grossman N., Gorodischer R., Loeys B.,
RA Zecic A., Mortier G., Gregory S., Sharony R., Kambouris M., Sakati N.,
RA Meyer B.F., Al-Aqeel A.I., Al-Humaidan A.K., Al-Zanhrani F., Al-Swaid A.,
RA Al Othman J., Diaz G.A., Weiner R., Khan K.T.S., Gordon R., Gelb B.D.;
RT "Mutation of TBCE causes hypoparathyroidism-retardation-dysmorphism and
RT autosomal recessive Kenny-Caffey syndrome.";
RL Nat. Genet. 32:448-452(2002).
CC -!- FUNCTION: Tubulin-folding protein; involved in the second step of the
CC tubulin folding pathway and in the regulation of tubulin heterodimer
CC dissociation. Required for correct organization of microtubule
CC cytoskeleton and mitotic splindle, and maintenance of the neuronal
CC microtubule network. {ECO:0000269|PubMed:11847227,
CC ECO:0000269|PubMed:27666369}.
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. Cofactors B and E
CC can form a heterodimer which binds to alpha-tubulin and enhances their
CC ability to dissociate tubulin heterodimers (By similarity). Interacts
CC with TBCD (PubMed:27666374). {ECO:0000250|UniProtKB:Q8CIV8,
CC ECO:0000269|PubMed:27666374}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15813-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15813-2; Sequence=VSP_053870;
CC -!- DISEASE: Hypoparathyroidism-retardation-dysmorphism syndrome (HRDS)
CC [MIM:241410]: An autosomal recessive multisystem disorder characterized
CC by hypoparathyroidism, intrauterine and postnatal growth retardation,
CC psychomotor retardation, epilepsy, microcephaly, and facial
CC dysmorphism. {ECO:0000269|PubMed:12389028}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Kenny-Caffey syndrome 1 (KCS1) [MIM:244460]: An autosomal
CC recessive form of Kenny-Caffey syndrome, a disorder characterized by
CC impaired skeletal development with small and dense bones, short
CC stature, and primary hypoparathyroidism with hypocalcemia. Clinical
CC features include cortical thickening and medullary stenosis of the
CC tubular bones, delayed closure of fontanels, defective dentition, small
CC eyes with hypermetropia, and frontal bossing with a triangular face.
CC {ECO:0000269|PubMed:12389028}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Encephalopathy, progressive, with amyotrophy and optic atrophy
CC (PEAMO) [MIM:617207]: An autosomal recessive, progressive,
CC neurodegenerative encephalopathy with onset in infancy. Affected
CC individuals manifest delayed psychomotor development, severe hypotonia,
CC motor regression, spinal muscular atrophy, distal amyotrophy and
CC weakness of all limbs, and intellectual disability of variable
CC severity. Additional features include optic atrophy, thin corpus
CC callosum, and cerebellar atrophy. {ECO:0000269|PubMed:27666369}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the TBCE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U61232; AAB17538.1; -; mRNA.
DR EMBL; BT007086; AAP35749.1; -; mRNA.
DR EMBL; AK292287; BAF84976.1; -; mRNA.
DR EMBL; AK296185; BAH12277.1; -; mRNA.
DR EMBL; AL357556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO393422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008654; AAH08654.1; -; mRNA.
DR CCDS; CCDS1605.1; -. [Q15813-1]
DR CCDS; CCDS73052.1; -. [Q15813-2]
DR RefSeq; NP_001072983.1; NM_001079515.2. [Q15813-1]
DR RefSeq; NP_001274730.1; NM_001287801.1. [Q15813-2]
DR RefSeq; NP_001274731.1; NM_001287802.1.
DR RefSeq; NP_003184.1; NM_003193.4. [Q15813-1]
DR PDB; 4ICU; X-ray; 2.40 A; A/B/C/D=443-527.
DR PDB; 4ICV; X-ray; 1.45 A; A=443-527.
DR PDBsum; 4ICU; -.
DR PDBsum; 4ICV; -.
DR AlphaFoldDB; Q15813; -.
DR SMR; Q15813; -.
DR BioGRID; 112768; 55.
DR CORUM; Q15813; -.
DR IntAct; Q15813; 13.
DR GlyGen; Q15813; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15813; -.
DR MetOSite; Q15813; -.
DR PhosphoSitePlus; Q15813; -.
DR BioMuta; TBCE; -.
DR DMDM; 74762146; -.
DR EPD; Q15813; -.
DR jPOST; Q15813; -.
DR MassIVE; Q15813; -.
DR MaxQB; Q15813; -.
DR PaxDb; Q15813; -.
DR PeptideAtlas; Q15813; -.
DR PRIDE; Q15813; -.
DR ProteomicsDB; 60772; -. [Q15813-1]
DR ProteomicsDB; 6536; -.
DR Antibodypedia; 79050; 194 antibodies from 26 providers.
DR Antibodypedia; 81226; 3 antibodies from 1 providers.
DR DNASU; 6905; -.
DR Ensembl; ENST00000406207.5; ENSP00000384571.1; ENSG00000284770.2. [Q15813-1]
DR Ensembl; ENST00000543662.4; ENSP00000439170.1; ENSG00000284770.2. [Q15813-2]
DR Ensembl; ENST00000634751.2; ENSP00000489110.1; ENSG00000282984.2. [Q15813-1]
DR Ensembl; ENST00000634780.2; ENSP00000488933.1; ENSG00000282984.2. [Q15813-1]
DR Ensembl; ENST00000635692.2; ENSP00000489157.2; ENSG00000282984.2. [Q15813-1]
DR Ensembl; ENST00000642284.1; ENSP00000494585.1; ENSG00000282984.2. [Q15813-1]
DR Ensembl; ENST00000642610.2; ENSP00000494796.1; ENSG00000284770.2. [Q15813-1]
DR Ensembl; ENST00000644604.1; ENSP00000495961.1; ENSG00000285053.1. [Q15813-1]
DR Ensembl; ENST00000645205.1; ENSP00000495823.1; ENSG00000285053.1. [Q15813-1]
DR Ensembl; ENST00000645351.1; ENSP00000494319.1; ENSG00000285053.1. [Q15813-1]
DR Ensembl; ENST00000645655.1; ENSP00000495202.1; ENSG00000285053.1. [Q15813-1]
DR Ensembl; ENST00000646624.1; ENSP00000494575.1; ENSG00000285053.1. [Q15813-1]
DR Ensembl; ENST00000646802.1; ENSP00000496170.1; ENSG00000282984.2. [Q15813-1]
DR Ensembl; ENST00000646934.1; ENSP00000494500.1; ENSG00000282984.2. [Q15813-1]
DR Ensembl; ENST00000647186.1; ENSP00000494775.1; ENSG00000285053.1. [Q15813-1]
DR GeneID; 6905; -.
DR KEGG; hsa:6905; -.
DR MANE-Select; ENST00000642610.2; ENSP00000494796.1; NM_003193.5; NP_003184.1.
DR UCSC; uc001hwz.2; human. [Q15813-1]
DR CTD; 6905; -.
DR DisGeNET; 6905; -.
DR GeneCards; TBCE; -.
DR HGNC; HGNC:11582; TBCE.
DR HPA; ENSG00000284770; Low tissue specificity.
DR HPA; ENSG00000285053; Low tissue specificity.
DR MalaCards; TBCE; -.
DR MIM; 241410; phenotype.
DR MIM; 244460; phenotype.
DR MIM; 604934; gene.
DR MIM; 617207; phenotype.
DR neXtProt; NX_Q15813; -.
DR Orphanet; 93324; Autosomal recessive Kenny-Caffey syndrome.
DR Orphanet; 496756; Early-onset progressive encephalopathy-spastic ataxia-distal spinal muscular atrophy syndrome.
DR Orphanet; 2323; Sanjad-Sakati syndrome.
DR PharmGKB; PA36346; -.
DR VEuPathDB; HostDB:ENSG00000284770; -.
DR VEuPathDB; HostDB:ENSG00000285053; -.
DR eggNOG; KOG3207; Eukaryota.
DR GeneTree; ENSGT00530000063405; -.
DR HOGENOM; CLU_017716_5_0_1; -.
DR InParanoid; Q15813; -.
DR OMA; KKYALDW; -.
DR OrthoDB; 1596773at2759; -.
DR PhylomeDB; Q15813; -.
DR TreeFam; TF313455; -.
DR PathwayCommons; Q15813; -.
DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
DR SignaLink; Q15813; -.
DR BioGRID-ORCS; 6905; 380 hits in 1070 CRISPR screens.
DR ChiTaRS; TBCE; human.
DR GeneWiki; TBCE; -.
DR GenomeRNAi; 6905; -.
DR Pharos; Q15813; Tbio.
DR PRO; PR:Q15813; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15813; protein.
DR Bgee; ENSG00000284770; Expressed in ventricular zone and 95 other tissues.
DR ExpressionAtlas; Q15813; baseline and differential.
DR Genevisible; Q15813; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; TAS:ProtInc.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; TAS:ProtInc.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0014889; P:muscle atrophy; IEA:Ensembl.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IEA:Ensembl.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IDA:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; TAS:UniProtKB.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR CDD; cd17044; Ubl_TBCE; 1.
DR Gene3D; 2.30.30.190; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044079; Ubl_TBCE.
DR PANTHER; PTHR15140; PTHR15140; 1.
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; Alternative splicing; Chaperone; Cytoplasm;
KW Cytoskeleton; Disease variant; Dwarfism; Intellectual disability;
KW Leucine-rich repeat; Neurodegeneration; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..527
FT /note="Tubulin-specific chaperone E"
FT /id="PRO_0000083538"
FT DOMAIN 27..71
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REPEAT 154..175
FT /note="LRR 1"
FT REPEAT 180..200
FT /note="LRR 2"
FT REPEAT 205..226
FT /note="LRR 3"
FT REPEAT 230..252
FT /note="LRR 4"
FT REPEAT 253..274
FT /note="LRR 5"
FT REPEAT 278..299
FT /note="LRR 6"
FT REPEAT 308..329
FT /note="LRR 7"
FT DOMAIN 342..384
FT /note="LRRCT"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 463
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 220
FT /note="E -> EAHAQCGGSRHGLDMQKDASKFVDLCVLQKCSTSNCIISAKDHTSMR
FT MNVAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053870"
FT VARIANT 52..55
FT /note="Missing (in HRDS and KCS1)"
FT /evidence="ECO:0000269|PubMed:12389028"
FT /id="VAR_032920"
FT VARIANT 155
FT /note="I -> N (in PEAMO; decreased function in the
FT organization of microtubule cytoskeleton and mitotic
FT splindle; dbSNP:rs780472451)"
FT /evidence="ECO:0000269|PubMed:27666369"
FT /id="VAR_077878"
FT VARIANT 205
FT /note="V -> A (in dbSNP:rs16832611)"
FT /id="VAR_032921"
FT VARIANT 333
FT /note="S -> T (in dbSNP:rs35579976)"
FT /id="VAR_032922"
FT VARIANT 409
FT /note="E -> G (in dbSNP:rs16832619)"
FT /id="VAR_032923"
FT CONFLICT 450
FT /note="I -> V (in Ref. 3; BAF84976)"
FT /evidence="ECO:0000305"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:4ICV"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:4ICU"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:4ICV"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:4ICV"
FT HELIX 471..482
FT /evidence="ECO:0007829|PDB:4ICV"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:4ICV"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:4ICV"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:4ICV"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:4ICV"
SQ SEQUENCE 527 AA; 59346 MW; C919052D2D463BA1 CRC64;
MSDTLTADVI GRRVEVNGEH ATVRFAGVVP PVAGPWLGVE WDNPERGKHD GSHEGTVYFK
CRHPTGGSFI RPNKVNFGTD FLTAIKNRYV LEDGPEEDRK EQIVTIGNKP VETIGFDSIM
KQQSQLSKLQ EVSLRNCAVS CAGEKGGVAE ACPNIRKVDL SKNLLSSWDE VIHIADQLRH
LEVLNVSENK LKFPSGSVLT GTLSVLKVLV LNQTGITWAE VLRCVAGCPG LEELYLESNN
IFISERPTDV LQTVKLLDLS SNQLIDENQL YLIAHLPRLE QLILSDTGIS SLHFPDAGIG
CKTSMFPSLK YLVVNDNQIS QWSFFNELEK LPSLRALSCL RNPLTKEDKE AETARLLIIA
SIGQLKTLNK CEILPEERRR AELDYRKAFG NEWKQAGGHK DPEKNRLSEE FLTAHPRYQF
LCLKYGAPED WELKTQQPLM LKNQLLTLKI KYPHQLDQKV LEKQLPGSMT IQKVKGLLSR
LLKVPVSDLL LSYESPKKPG REIELENDLK SLQFYSVENG DCLLVRW
