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Protein

Tubulin-specific chaperone D

Gene

Tbcd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Tubulin-folding protein; involved in the first step of the tubulin folding pathway. Modulates microtubule dynamics by capturing GTP-bound beta-tubulin (TUBB). Acts as a GTPase-activating protein (GAP) for ARL2. Its ability to interact with beta tubulin is regulated via its interaction with 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin-specific chaperone D
Alternative name(s):
Beta-tubulin cofactor D
Tubulin-folding cofactor D
Gene namesi
Name:Tbcd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1919686. Tbcd.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11961196Tubulin-specific chaperone DPRO_0000080050Add
BLAST

Proteomic databases

EPDiQ8BYA0.
MaxQBiQ8BYA0.
PaxDbiQ8BYA0.
PRIDEiQ8BYA0.

PTM databases

iPTMnetiQ8BYA0.
PhosphoSiteiQ8BYA0.
SwissPalmiQ8BYA0.

Expressioni

Gene expression databases

BgeeiQ8BYA0.
CleanExiMM_TBCD.
ExpressionAtlasiQ8BYA0. baseline and differential.
GenevisibleiQ8BYA0. MM.

Interactioni

Subunit structurei

Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with PPP2CB. Interacts with ARL2. 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. Interacts with ARL2; interaction is enhanced with the GDP-bound form of ARL2. Does not interact with ARL3, ARL4A and ARL4D. Interacts with beta tubulin (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi224462. 1 interaction.
STRINGi10090.ENSMUSP00000099302.

Structurei

3D structure databases

ProteinModelPortaliQ8BYA0.
SMRiQ8BYA0. Positions 357-430, 576-627.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati363 – 40139HEAT 1Add
BLAST
Repeati599 – 63436HEAT 2Add
BLAST
Repeati752 – 78837HEAT 3Add
BLAST
Repeati1106 – 114237HEAT 4Add
BLAST

Sequence similaritiesi

Belongs to the TBCD family.Curated
Contains 4 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1943. Eukaryota.
COG5234. LUCA.
GeneTreeiENSGT00390000017103.
HOGENOMiHOG000231203.
HOVERGENiHBG053297.
InParanoidiQ8BYA0.
OMAiIVNAADY.
OrthoDBiEOG78D7JC.
PhylomeDBiQ8BYA0.
TreeFamiTF105754.

Family and domain databases

Gene3Di1.25.10.10. 5 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR033162. TBCD.
IPR022577. Tubulin_specific_chaperoneD_C.
[Graphical view]
PANTHERiPTHR12658:SF0. PTHR12658:SF0. 1 hit.
PfamiPF12612. TFCD_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

Q8BYA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSNEPAAS AAEEEVEDDA LVRASALEAF GESAETRALL RSLPAVHRER
60 70 80 90 100
ASREVAEERF RVIMDKYQEQ PHLLDPHLEW MMNSLLDLVQ DETSLPDLVH
110 120 130 140 150
LAFKFLYIIT KVRGYKVFLR LFPHEVANVQ PVLDMFTGQN PKDHETWETR
160 170 180 190 200
YMLLLWLSVT CLIPFDFSRL DGNLSTQTGE TRVPTMDRIL QIAESYLVVS
210 220 230 240 250
DKARDAAAVL VSKFITRPDV KQRKMASFLD WSLCTLAHSS FQTIEGVITM
260 270 280 290 300
DGMLQALAQI FKHGKREDCL PYANTVLQCL DGCRLPESSH TSLRKLGVKL
310 320 330 340 350
VQRLGLTFLK PKVATWRYQR GCRSLAANLK LCAPGKSDQK LLSDSLTSDG
360 370 380 390 400
DEDYDVPEGV ETVIEQLLVG LKDKDTVVRW SAAKGIGRMA GRLPRELADD
410 420 430 440 450
VVGSVLDCFS FQETDKAWHG GCLALAELGR RGLLLPSRLS EVVTVILKAL
460 470 480 490 500
TYDEKRGACS VGANVRDAAC YVCWAFARAY EPQELTPFVT AISSALVIAA
510 520 530 540 550
VFDRNVNCRR AASAAFQENV GRQGTFPHGI DILTTADYFA VGNISNCFLI
560 570 580 590 600
ISVFIAGFQE YTKPMIDHLV SMKINHWDGA IRELSAKALH NLTPQVPEYI
610 620 630 640 650
AMHVFPALLL MTQSPDLHTR HGAILACAEV TYALYKLATQ SNRLVTDYLD
660 670 680 690 700
EKAVQSLKQI HQQLCDRHLY RGLGGELMRQ AVCILIEKLS LSRMPFKGDA
710 720 730 740 750
TVEGWQWLIN DTLRSLHLVS SHSRQQIKEV AVSALTALCS EYYVKEPGEA
760 770 780 790 800
GSSIAKELIP QYLAELQSPE EMARCGFSSA LGALPGFLLR GHLQQVLSGL
810 820 830 840 850
RRVTCISPND VSFAEARRDG LKAISRICQT VGVNTRGPPD EVICKENISE
860 870 880 890 900
VYAALLGCMS DYTTDSRGDV GAWVREAAMT SLMDLMLLLA RTEPVLIEAH
910 920 930 940 950
ICERVMCCVA QQASEKIDRF RAHAARVFLT LLHFDSPPIP HVPHRQELES
960 970 980 990 1000
LFPRSDVATV NWNAPSQAFP LITQLLGLPT YRYHVLLGLA VSVGGLTEST
1010 1020 1030 1040 1050
VRHSTQSLFE YMKGIQKDAQ VLQSFSETLL KVFEDNLLND RVSVSLLKML
1060 1070 1080 1090 1100
DQLLANGCFD IFTAEENHPF CVKLLTLCKE EIKKSKDIQK LRSSIAVLCG
1110 1120 1130 1140 1150
MVQFNGDVRK KILLQLFLLL GHPFPVIRKS TASQVYEMVL TYSDLVDAEV
1160 1170 1180 1190
LDEVMSVLSD TAWDAELPVV REQRNRLCDL LGVPRPQLVP KPIPGS
Length:1,196
Mass (Da):133,321
Last modified:March 1, 2003 - v1
Checksum:i5439133B4CD54938
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK041464 mRNA. Translation: BAC30951.1.
BC059843 mRNA. Translation: AAH59843.1.
CCDSiCCDS25778.1.
RefSeqiNP_084154.1. NM_029878.3.
UniGeneiMm.23686.
Mm.386847.

Genome annotation databases

EnsembliENSMUST00000103013; ENSMUSP00000099302; ENSMUSG00000039230.
GeneIDi108903.
KEGGimmu:108903.
UCSCiuc007mvy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK041464 mRNA. Translation: BAC30951.1.
BC059843 mRNA. Translation: AAH59843.1.
CCDSiCCDS25778.1.
RefSeqiNP_084154.1. NM_029878.3.
UniGeneiMm.23686.
Mm.386847.

3D structure databases

ProteinModelPortaliQ8BYA0.
SMRiQ8BYA0. Positions 357-430, 576-627.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224462. 1 interaction.
STRINGi10090.ENSMUSP00000099302.

PTM databases

iPTMnetiQ8BYA0.
PhosphoSiteiQ8BYA0.
SwissPalmiQ8BYA0.

Proteomic databases

EPDiQ8BYA0.
MaxQBiQ8BYA0.
PaxDbiQ8BYA0.
PRIDEiQ8BYA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103013; ENSMUSP00000099302; ENSMUSG00000039230.
GeneIDi108903.
KEGGimmu:108903.
UCSCiuc007mvy.2. mouse.

Organism-specific databases

CTDi6904.
MGIiMGI:1919686. Tbcd.

Phylogenomic databases

eggNOGiKOG1943. Eukaryota.
COG5234. LUCA.
GeneTreeiENSGT00390000017103.
HOGENOMiHOG000231203.
HOVERGENiHBG053297.
InParanoidiQ8BYA0.
OMAiIVNAADY.
OrthoDBiEOG78D7JC.
PhylomeDBiQ8BYA0.
TreeFamiTF105754.

Miscellaneous databases

ChiTaRSiTbcd. mouse.
NextBioi361437.
PROiQ8BYA0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BYA0.
CleanExiMM_TBCD.
ExpressionAtlasiQ8BYA0. baseline and differential.
GenevisibleiQ8BYA0. MM.

Family and domain databases

Gene3Di1.25.10.10. 5 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR033162. TBCD.
IPR022577. Tubulin_specific_chaperoneD_C.
[Graphical view]
PANTHERiPTHR12658:SF0. PTHR12658:SF0. 1 hit.
PfamiPF12612. TFCD_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTBCD_MOUSE
AccessioniPrimary (citable) accession number: Q8BYA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.