Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Tubulin-specific chaperone D (Beta-tubulin cofactor D) (tfcD) (SSD-1) (Tubulin-folding cofactor D)

 TBCD_HUMAN              Reviewed;        1192 AA.
Q9BTW9; O95458; Q7L8K1; Q8IXP6; Q8NAX0; Q8WYH4; Q96E74; Q9UF82;
Q9UG46; Q9Y2J3;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
25-APR-2018, entry version 148.
RecName: Full=Tubulin-specific chaperone D;
AltName: Full=Beta-tubulin cofactor D;
Short=tfcD;
AltName: Full=SSD-1;
AltName: Full=Tubulin-folding cofactor D;
Name=TBCD; Synonyms=KIAA0988, SSD1, TFCD; ORFNames=PP1096;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, AND
INDUCTION.
PubMed=11110777; DOI=10.1161/01.RES.87.12.1188;
Schubert A., Cattaruzza M., Hecker M., Darmer D., Holtz J.,
Morawietz H.;
"Shear stress-dependent regulation of the human beta-tubulin folding
cofactor D gene.";
Circ. Res. 87:1188-1194(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[4]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 143-1192 (ISOFORM 1).
TISSUE=Testis, and Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-617.
TISSUE=Brain, Colon, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION.
PubMed=10722852; DOI=10.1016/S0014-5793(00)01293-X;
Martin L., Fanarraga M.L., Aloria K., Zabala J.C.;
"Tubulin folding cofactor D is a microtubule destabilizing protein.";
FEBS Lett. 470:93-95(2000).
[10]
FUNCTION, INTERACTION WITH BETA TUBULIN AND ARL2, AND ABSENCE OF
INTERACTION WITH ARL3; ARL4A AND ARL4D.
PubMed=10831612; DOI=10.1083/jcb.149.5.1087;
Bhamidipati A., Lewis S.A., Cowan N.J.;
"ADP ribosylation factor-like protein 2 (Arl2) regulates the
interaction of tubulin-folding cofactor D with native tubulin.";
J. Cell Biol. 149:1087-1096(2000).
[11]
FUNCTION.
PubMed=11847227; DOI=10.1074/jbc.M200128200;
Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A.,
Cowan N.J.;
"Functional overlap between retinitis pigmentosa 2 protein and the
tubulin-specific chaperone cofactor C.";
J. Biol. Chem. 277:14629-14634(2002).
[12]
FUNCTION.
PubMed=20740604; DOI=10.1002/cm.20480;
Tian G., Thomas S., Cowan N.J.;
"Effect of TBCD and its regulatory interactor Arl2 on tubulin and
microtubule integrity.";
Cytoskeleton 67:706-714(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
FUNCTION, INTERACTION WITH ARL2; TBCE AND BETA TUBULIN, INVOLVEMENT IN
PEBAT, VARIANTS PEBAT ARG-387; CYS-772; THR-921; ARG-937 AND LEU-1122,
AND CHARACTERIZATION OF VARIANTS PEBAT ARG-387; CYS-772; THR-921;
ARG-937 AND LEU-1122.
PubMed=27666374; DOI=10.1016/j.ajhg.2016.08.005;
Miyake N., Fukai R., Ohba C., Chihara T., Miura M., Shimizu H.,
Kakita A., Imagawa E., Shiina M., Ogata K., Okuno-Yuguchi J.,
Fueki N., Ogiso Y., Suzumura H., Watabe Y., Imataka G., Leong H.Y.,
Fattal-Valevski A., Kramer U., Miyatake S., Kato M., Okamoto N.,
Sato Y., Mitsuhashi S., Nishino I., Kaneko N., Nishiyama A.,
Tamura T., Mizuguchi T., Nakashima M., Tanaka F., Saitsu H.,
Matsumoto N.;
"Biallelic TBCD mutations cause early-onset neurodegenerative
encephalopathy.";
Am. J. Hum. Genet. 99:950-961(2016).
[15]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BETA TUBULIN,
INVOLVEMENT IN PEBAT, VARIANTS PEBAT ARG-229; MET-374; GLN-377;
THR-626; MET-994; MET-1105 AND LEU-1122, AND CHARACTERIZATION OF
VARIANTS PEBAT MET-374; GLN-377; THR-626 AND LEU-1122.
PubMed=27666370; DOI=10.1016/j.ajhg.2016.08.003;
Flex E., Niceta M., Cecchetti S., Thiffault I., Au M.G., Capuano A.,
Piermarini E., Ivanova A.A., Francis J.W., Chillemi G.,
Chandramouli B., Carpentieri G., Haaxma C.A., Ciolfi A., Pizzi S.,
Douglas G.V., Levine K., Sferra A., Dentici M.L., Pfundt R.R.,
Le Pichon J.B., Farrow E., Baas F., Piemonte F., Dallapiccola B.,
Graham J.M. Jr., Saunders C.J., Bertini E., Kahn R.A., Koolen D.A.,
Tartaglia M.;
"Biallelic mutations in TBCD, encoding the tubulin folding cofactor D,
perturb microtubule dynamics and cause early-onset encephalopathy.";
Am. J. Hum. Genet. 99:962-973(2016).
[16]
FUNCTION, VARIANTS PEBAT THR-475 AND VAL-586, AND CHARACTERIZATION OF
VARIANTS PEBAT THR-475 AND VAL-586.
PubMed=28158450; DOI=10.1093/hmg/ddw292;
Edvardson S., Tian G., Cullen H., Vanyai H., Ngo L., Bhat S., Aran A.,
Daana M., Da'amseh N., Abu-Libdeh B., Cowan N.J., Heng J., Elpeleg O.;
"Infantile neurodegenerative disorder associated with mutations in
TBCD, an essential gene in the tubulin heterodimer assembly pathway.";
Hum. Mol. Genet. 25:4635-4648(2016).
[17]
VARIANTS PEBAT THR-475; VAL-586 AND ARG-937.
PubMed=27807845; DOI=10.1111/cge.12914;
Pode-Shakked B., Barash H., Ziv L., Gripp K.W., Flex E., Barel O.,
Carvalho K.S., Scavina M., Chillemi G., Niceta M., Eyal E., Kol N.,
Ben-Zeev B., Bar-Yosef O., Marek-Yagel D., Bertini E., Duker A.L.,
Anikster Y., Tartaglia M., Raas-Rothschild A.;
"Microcephaly, intractable seizures and developmental delay caused by
biallelic variants in TBCD: further delineation of a new chaperone-
mediated tubulinopathy.";
Clin. Genet. 91:725-738(2017).
-!- FUNCTION: Tubulin-folding protein implicated in the first step of
the tubulin folding pathway and required for tubulin complex
assembly. Involved in the regulation of microtubule polymerization
or depolymerization, it modulates microtubule dynamics by
capturing GTP-bound beta-tubulin (TUBB). Its ability to interact
with beta tubulin is regulated via its interaction with ARL2. Acts
as a GTPase-activating protein (GAP) for ARL2. Induces microtubule
disruption in absence of ARL2. Increases degradation of beta
tubulin, when overexpressed in polarized cells. Promotes
epithelial cell detachment, a process antagonized by ARL2. Induces
tight adherens and tight junctions disassembly at the lateral cell
membrane (PubMed:10722852, PubMed:10831612, PubMed:11847227,
PubMed:20740604, PubMed:27666370, PubMed:28158450). Required for
correct assembly and maintenance of the mitotic spindle, and
proper progression of mitosis (PubMed:27666370). Involved in
neuron morphogenesis (PubMed:27666374).
{ECO:0000269|PubMed:10722852, ECO:0000269|PubMed:10831612,
ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:20740604,
ECO:0000269|PubMed:27666370, ECO:0000269|PubMed:27666374,
ECO:0000269|PubMed:28158450}.
-!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
PPP2R2A, PPP2R5E and TBCD. Interacts with PPP2CB (By similarity).
Part of a supercomplex made of cofactors A to E. Cofactors A and D
function by capturing and stabilizing tubulin in a quasi-native
conformation. Cofactor E binds to the cofactor D-tubulin complex;
interaction with cofactor C then causes the release of tubulin
polypeptides that are committed to the native state
(PubMed:10831612). Interacts with ARL2; interaction is enhanced
with the GDP-bound form of ARL2 (PubMed:10831612,
PubMed:27666374). Does not interact with ARL3, ARL4A and ARL4D
(PubMed:10831612). Interacts with beta tubulin (PubMed:10831612,
PubMed:27666370, PubMed:27666374). Interacts with TBCE
(PubMed:27666374). {ECO:0000250|UniProtKB:Q28205,
ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:27666370,
ECO:0000269|PubMed:27666374}.
-!- INTERACTION:
Q96AP0:ACD; NbExp=2; IntAct=EBI-356005, EBI-717666;
-!- SUBCELLULAR LOCATION: Cell junction, tight junction
{ECO:0000250|UniProtKB:Q28205}. Lateral cell membrane
{ECO:0000250|UniProtKB:Q28205}. Cytoplasm
{ECO:0000250|UniProtKB:Q28205}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:Q28205}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:27666370}. Note=Localized in cell-cell
contacts. {ECO:0000250|UniProtKB:Q28205}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9BTW9-1; Sequence=Displayed;
Name=2;
IsoId=Q9BTW9-2; Sequence=VSP_017210;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9BTW9-3; Sequence=VSP_017211, VSP_017215, VSP_017213,
VSP_017214;
Name=4;
IsoId=Q9BTW9-4; Sequence=VSP_017217, VSP_017218;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9BTW9-5; Sequence=VSP_017212, VSP_017216;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10231032, ECO:0000269|PubMed:11110777}.
-!- INDUCTION: Down-regulated by shear stress.
{ECO:0000269|PubMed:11110777}.
-!- DISEASE: Encephalopathy, progressive, early-onset, with brain
atrophy and thin corpus callosum (PEBAT) [MIM:617193]: An
autosomal recessive disease with neurodevelopmental and
neurodegenerative features. PEBAT is characterized by early-onset
cortical atrophy, hypomyelination, microcephaly, thin corpus
callosum, delayed psychomotor development, developmental
regression, intellectual disability, seizures, optic atrophy,
muscle weakness and atrophy, spastic quadriplegia, and respiratory
insufficiency due to hypotonia. {ECO:0000269|PubMed:27666370,
ECO:0000269|PubMed:27666374, ECO:0000269|PubMed:27807845,
ECO:0000269|PubMed:28158450}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TBCD family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH39654.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA76832.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ006417; CAA07022.1; -; mRNA.
EMBL; AF193042; AAG22470.1; -; mRNA.
EMBL; AB023205; BAA76832.2; ALT_INIT; mRNA.
EMBL; AK091959; BAC03777.1; -; mRNA.
EMBL; AL133562; CAB63716.1; -; mRNA.
EMBL; AL096745; CAB62532.2; -; mRNA.
EMBL; AC024361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC130371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003094; AAH03094.1; -; mRNA.
EMBL; BC012824; AAH12824.2; -; mRNA.
EMBL; BC039654; AAH39654.1; ALT_INIT; mRNA.
CCDS; CCDS45818.1; -. [Q9BTW9-1]
PIR; T12548; T12548.
PIR; T43482; T43482.
RefSeq; NP_005984.3; NM_005993.4. [Q9BTW9-1]
UniGene; Hs.464391; -.
ProteinModelPortal; Q9BTW9; -.
BioGrid; 112767; 60.
CORUM; Q9BTW9; -.
IntAct; Q9BTW9; 18.
MINT; Q9BTW9; -.
STRING; 9606.ENSP00000347719; -.
iPTMnet; Q9BTW9; -.
PhosphoSitePlus; Q9BTW9; -.
SwissPalm; Q9BTW9; -.
BioMuta; TBCD; -.
DMDM; 296452924; -.
EPD; Q9BTW9; -.
MaxQB; Q9BTW9; -.
PaxDb; Q9BTW9; -.
PeptideAtlas; Q9BTW9; -.
PRIDE; Q9BTW9; -.
DNASU; 6904; -.
Ensembl; ENST00000355528; ENSP00000347719; ENSG00000141556. [Q9BTW9-1]
GeneID; 6904; -.
KEGG; hsa:6904; -.
UCSC; uc002kfz.4; human. [Q9BTW9-1]
CTD; 6904; -.
DisGeNET; 6904; -.
EuPathDB; HostDB:ENSG00000141556.20; -.
GeneCards; TBCD; -.
H-InvDB; HIX0021105; -.
HGNC; HGNC:11581; TBCD.
HPA; HPA045200; -.
MalaCards; TBCD; -.
MIM; 604649; gene.
MIM; 617193; phenotype.
neXtProt; NX_Q9BTW9; -.
OpenTargets; ENSG00000141556; -.
PharmGKB; PA36345; -.
eggNOG; KOG1943; Eukaryota.
eggNOG; COG5234; LUCA.
GeneTree; ENSGT00390000017103; -.
HOVERGEN; HBG053297; -.
InParanoid; Q9BTW9; -.
KO; K21767; -.
PhylomeDB; Q9BTW9; -.
TreeFam; TF105754; -.
Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
ChiTaRS; TBCD; human.
GeneWiki; TBCD; -.
GenomeRNAi; 6904; -.
PRO; PR:Q9BTW9; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141556; -.
ExpressionAtlas; Q9BTW9; baseline and differential.
Genevisible; Q9BTW9; HS.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
GO; GO:0005874; C:microtubule; TAS:ProtInc.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; TAS:ProtInc.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISS:UniProtKB.
GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IDA:UniProtKB.
GO; GO:0006457; P:protein folding; IDA:UniProtKB.
GO; GO:0007021; P:tubulin complex assembly; IDA:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR033162; TBCD.
InterPro; IPR022577; Tubulin_specific_chaperoneD_C.
PANTHER; PTHR12658; PTHR12658; 1.
Pfam; PF12612; TFCD_C; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Chaperone;
Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
GTPase activation; Membrane; Neurodegeneration; Polymorphism;
Reference proteome; Repeat; Tight junction.
CHAIN 1 1192 Tubulin-specific chaperone D.
/FTId=PRO_0000080049.
REPEAT 361 399 HEAT 1.
REPEAT 557 594 HEAT 2.
REPEAT 596 632 HEAT 3.
VAR_SEQ 1 1008 Missing (in isoform 2).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_017210.
VAR_SEQ 1 546 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_017211.
VAR_SEQ 62 78 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_017212.
VAR_SEQ 547 549 LVI -> MFN (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_017215.
VAR_SEQ 662 697 LYDRQLYRGLGGQLMRQAVCVLIEKLSLSKMPFRGD -> P
CICSWGLMSPESKAEFCVCVCRISLGRQCVHLSGL (in
isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_017213.
VAR_SEQ 698 1192 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_017214.
VAR_SEQ 739 1156 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_017216.
VAR_SEQ 1094 1094 V -> VDFPSATLVCVGTVQMYAHTHLRLGAPGPHCAHGSA
MPR (in isoform 4).
{ECO:0000303|PubMed:11110777}.
/FTId=VSP_017217.
VAR_SEQ 1182 1192 RPQLVPQPGAC -> SPTWCPAWCLLKPVLEPIPHPCLVRM
SCS (in isoform 4).
{ECO:0000303|PubMed:11110777}.
/FTId=VSP_017218.
VARIANT 229 229 L -> R (in PEBAT; dbSNP:rs778417127).
{ECO:0000269|PubMed:27666370}.
/FTId=VAR_077968.
VARIANT 374 374 T -> M (in PEBAT; severely decreased
interaction with beta tubulin; does not
affect localization to centrosome;
dbSNP:rs953299085).
{ECO:0000269|PubMed:27666370}.
/FTId=VAR_077969.
VARIANT 377 377 R -> Q (in PEBAT; decreased protein
abundance; severely decreased interaction
with beta tubulin; does not affect
localization to centrosome;
dbSNP:rs764085684).
{ECO:0000269|PubMed:27666370}.
/FTId=VAR_077970.
VARIANT 387 387 M -> R (in PEBAT; decreased function in
neuron morphogenesis; severely decreased
interaction with ARL2; decreased
interaction with TBCE; decreased
interaction with beta tubulin;
dbSNP:rs886041086).
{ECO:0000269|PubMed:27666374}.
/FTId=VAR_077971.
VARIANT 475 475 A -> T (in PEBAT; decreased function in
tubulin complex assembly; increased
protein degradation; dbSNP:rs775014444).
{ECO:0000269|PubMed:27807845,
ECO:0000269|PubMed:28158450}.
/FTId=VAR_077972.
VARIANT 586 586 A -> V (in PEBAT; decreased function in
tubulin complex assembly).
{ECO:0000269|PubMed:27807845,
ECO:0000269|PubMed:28158450}.
/FTId=VAR_077973.
VARIANT 617 617 M -> T (in dbSNP:rs2292971).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_057264.
VARIANT 626 626 A -> T (in PEBAT; decreased protein
abundance; does not affect localization
to centrosome; dbSNP:rs749225304).
{ECO:0000269|PubMed:27666370}.
/FTId=VAR_077974.
VARIANT 772 772 R -> C (in PEBAT; decreased function in
neuron morphogenesis; decreased
interaction with ARL2; decreased
interaction with TBCE; decreased
interaction with beta tubulin;
dbSNP:rs181969865).
{ECO:0000269|PubMed:27666374}.
/FTId=VAR_077975.
VARIANT 921 921 A -> T (in PEBAT; decreased interaction
with ARL2; decreased interaction with
TBCE; decreased interaction with beta
tubulin; dbSNP:rs886041085).
{ECO:0000269|PubMed:27666374}.
/FTId=VAR_077976.
VARIANT 923 923 S -> N (in dbSNP:rs3214033).
/FTId=VAR_057265.
VARIANT 937 937 P -> R (in PEBAT; decreased interaction
with TBCE; decreased interaction with
beta tubulin; does not affect interaction
with ARL2; dbSNP:rs886041087).
{ECO:0000269|PubMed:27666374,
ECO:0000269|PubMed:27807845}.
/FTId=VAR_077977.
VARIANT 943 943 G -> V (in dbSNP:rs8072406).
/FTId=VAR_057266.
VARIANT 994 994 T -> M (in PEBAT; unknown pathological
significance; dbSNP:rs867484272).
{ECO:0000269|PubMed:27666370}.
/FTId=VAR_077978.
VARIANT 1105 1105 V -> M (in PEBAT; unknown pathological
significance; dbSNP:rs764003906).
{ECO:0000269|PubMed:27666370}.
/FTId=VAR_077979.
VARIANT 1122 1122 P -> L (in PEBAT; severely decreased
protein abundance; does not affect
localization to centrosome; decreased
interaction with ARL2; decreased
interaction with TBCE; decreased
interaction with beta tubulin;
dbSNP:rs755177846).
{ECO:0000269|PubMed:27666370,
ECO:0000269|PubMed:27666374}.
/FTId=VAR_077980.
VARIANT 1185 1185 L -> P (in dbSNP:rs2292969).
/FTId=VAR_057267.
CONFLICT 31 31 G -> S (in Ref. 1; CAA07022).
{ECO:0000305}.
CONFLICT 472 472 W -> C (in Ref. 3; BAA76832).
{ECO:0000305}.
CONFLICT 799 801 RAV -> GAL (in Ref. 1; CAA07022).
{ECO:0000305}.
CONFLICT 985 985 G -> R (in Ref. 1; CAA07022).
{ECO:0000305}.
CONFLICT 1068 1068 A -> S (in Ref. 8; AAH12824).
{ECO:0000305}.
CONFLICT 1075 1075 C -> V (in Ref. 1; CAA07022).
{ECO:0000305}.
CONFLICT 1097 1097 E -> G (in Ref. 1; CAA07022, 3; BAA76832
and 8; AAH03094). {ECO:0000305}.
SEQUENCE 1192 AA; 132600 MW; C46BE2048A5FEBC2 CRC64;
MALSDEPAAG GPEEEAEDET LAFGAALEAF GESAETRALL GRLREVHGGG AEREVALERF
RVIMDKYQEQ PHLLDPHLEW MMNLLLDIVQ DQTSPASLVH LAFKFLYIIT KVRGYKTFLR
LFPHEVADVE PVLDLVTIQN PKDHEAWETR YMLLLWLSVT CLIPFDFSRL DGNLLTQPGQ
ARMSIMDRIL QIAESYLIVS DKARDAAAVL VSRFITRPDV KQSKMAEFLD WSLCNLARSS
FQTMQGVITM DGTLQALAQI FKHGKREDCL PYAATVLRCL DGCRLPESNQ TLLRKLGVKL
VQRLGLTFLK PKVAAWRYQR GCRSLAANLQ LLTQGQSEQK PLILTEDDDE DDDVPEGVER
VIEQLLVGLK DKDTVVRWSA AKGIGRMAGR LPRALADDVV GSVLDCFSFQ ETDKAWHGGC
LALAELGRRG LLLPSRLVDV VAVILKALTY DEKRGACSVG TNVRDAACYV CWAFARAYEP
QELKPFVTAI SSALVIAAVF DRDINCRRAA SAAFQENVGR QGTFPHGIDI LTTADYFAVG
NRSNCFLVIS VFIAGFPEYT QPMIDHLVTM KISHWDGVIR ELAARALHNL AQQAPEFSAT
QVFPRLLSMT LSPDLHMRHG SILACAEVAY ALYKLAAQEN RPVTDHLDEQ AVQGLKQIHQ
QLYDRQLYRG LGGQLMRQAV CVLIEKLSLS KMPFRGDTVI DGWQWLINDT LRHLHLISSH
SRQQMKDAAV SALAALCSEY YMKEPGEADP AIQEELITQY LAELRNPEEM TRCGFSLALG
ALPGFLLKGR LQQVLTGLRA VTHTSPEDVS FAESRRDGLK AIARICQTVG VKAGAPDEAV
CGENVSQIYC ALLGCMDDYT TDSRGDVGTW VRKAAMTSLM DLTLLLARSQ PELIEAHTCE
RIMCCVAQQA SEKIDRFRAH AASVFLTLLH FDSPPIPHVP HRGELEKLFP RSDVASVNWS
APSQAFPRIT QLLGLPTYRY HVLLGLVVSL GGLTESTIRH STQSLFEYMK GIQSDPQALG
SFSGTLLQIF EDNLLNERVS VPLLKTLDHV LTHGCFDIFT TEEDHPFAVK LLALCKKEIK
NSKDIQKLLS GIAVFCEMVQ FPGDVRRQAL LQLCLLLCHR FPLIRKTTAS QVYETLLTYS
DVVGADVLDE VVTVLSDTAW DAELAVVREQ RNRLCDLLGV PRPQLVPQPG AC


Related products :

Catalog number Product name Quantity
EIAAB41533 Beta-tubulin cofactor D,Homo sapiens,Human,KIAA0988,PP1096,SSD1,SSD-1,TBCD,tfcD,TFCD,Tubulin-folding cofactor D,Tubulin-specific chaperone D
EIAAB41531 Beta-tubulin cofactor D,Bos taurus,Bovine,TBCD,Tubulin-folding cofactor D,Tubulin-specific chaperone D
EIAAB41530 Beta-tubulin cofactor D,Mouse,Mus musculus,Tbcd,Tubulin-folding cofactor D,Tubulin-specific chaperone D
EIAAB41532 Beta-tubulin cofactor D,Chicken,Gallus gallus,RCJMB04_29e8,TBCD,Tubulin-folding cofactor D,Tubulin-specific chaperone D
EIAAB41513 CFA,Rat,Rattus norvegicus,Tbca,TCP1-chaperonin cofactor A,Tubulin-folding cofactor A,Tubulin-specific chaperone A
EIAAB41515 Bos taurus,Bovine,CFA,TBCA,TCP1-chaperonin cofactor A,Tubulin-folding cofactor A,Tubulin-specific chaperone A
EIAAB41516 CFA,Mouse,Mus musculus,Tbca,TCP1-chaperonin cofactor A,Tubulin-folding cofactor A,Tubulin-specific chaperone A
EIAAB41518 CFA,Oryctolagus cuniculus,Rabbit,TBCA,TCP1-chaperonin cofactor A,Tubulin-folding cofactor A,Tubulin-specific chaperone A
EIAAB41514 CFA,Homo sapiens,Human,TBCA,TCP1-chaperonin cofactor A,Tubulin-folding cofactor A,Tubulin-specific chaperone A
EIAAB41517 CFA,Chicken,Gallus gallus,TBCA,TCP1-chaperonin cofactor A,Tubulin-folding cofactor A,Tubulin-specific chaperone A
EIAAB41524 CFC,Mouse,Mus musculus,Tbcc,Tubulin-folding cofactor C,Tubulin-specific chaperone C
EIAAB41523 Bos taurus,Bovine,CFC,TBCC,Tubulin-folding cofactor C,Tubulin-specific chaperone C
EIAAB41548 Mouse,Mus musculus,Tbce,Tubulin-folding cofactor E,Tubulin-specific chaperone E
EIAAB41551 Rat,Rattus norvegicus,Tbce,Tubulin-folding cofactor E,Tubulin-specific chaperone E
EIAAB41550 Bos taurus,Bovine,TBCE,Tubulin-folding cofactor E,Tubulin-specific chaperone E
EIAAB41522 CFC,Homo sapiens,Human,TBCC,Tubulin-folding cofactor C,Tubulin-specific chaperone C
EIAAB41549 Homo sapiens,Human,TBCE,Tubulin-folding cofactor E,Tubulin-specific chaperone E
EIAAB41520 Bos taurus,Bovine,CKAP1,Cytoskeleton-associated protein 1,Cytoskeleton-associated protein CKAPI,TBCB,Tubulin-folding cofactor B,Tubulin-specific chaperone B
EIAAB41519 Ckap1,Cytoskeleton-associated protein 1,Cytoskeleton-associated protein CKAPI,Mouse,Mus musculus,Tbcb,Tubulin-folding cofactor B,Tubulin-specific chaperone B
EIAAB41521 CG22,CKAP1,Cytoskeleton-associated protein 1,Cytoskeleton-associated protein CKAPI,Homo sapiens,Human,TBCB,Tubulin-folding cofactor B,Tubulin-specific chaperone B
TBCEL_MOUSE Mouse ELISA Kit FOR Tubulin-specific chaperone cofactor E-like protein 96T
abx109387 Polyclonal Rabbit Tubulin-specific chaperone cofactor E-like Antibody 100 μg
abx108854 Polyclonal Rabbit Tubulin-specific chaperone cofactor E-like Antibody (HRP) 100 μg
H9274 Tubulin-specific chaperone cofactor E-like protein (TBCEL), Rat, ELISA Kit 96T
E11644h Human ELISA Kit FOR Tubulin-specific chaperone cofactor E-like protein 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur