TBD_HUMAN
ID TBD_HUMAN Reviewed; 453 AA.
AC Q9UJT1; B4DPT8; B4DW01; D3DU02; E9PCA7; E9PCQ8; Q5KU36; Q9BWG9; Q9H7Z8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Tubulin delta chain;
DE AltName: Full=Delta-tubulin;
GN Name=TUBD1; Synonyms=TUBD;
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), AND VARIANT THR-76.
RX PubMed=10620804; DOI=10.1038/71350;
RA Chang P., Stearns T.;
RT "Delta-tubulin and epsilon-tubulin: two new human centrosomal tubulins
RT reveal new aspects of centrosome structure and function.";
RL Nat. Cell Biol. 2:30-35(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), AND VARIANT THR-76.
RX PubMed=15081367; DOI=10.1016/j.ydbio.2004.01.026;
RA Kato A., Nagata Y., Todokoro K.;
RT "Delta-tubulin is a component of intercellular bridges and both the early
RT and mature perinuclear rings during spermatogenesis.";
RL Dev. Biol. 269:196-205(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC TISSUE=Embryo, Mammary gland, and Stomach;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC -!- FUNCTION: Acts as a positive regulator of hedgehog signaling and
CC regulates ciliary function. {ECO:0000250|UniProtKB:Q9R1K7}.
CC -!- SUBUNIT: Found in a complex with TEDC1, TEDC2, TUBE1 and TUBD1.
CC {ECO:0000250|UniProtKB:Q9R1K7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9R1K7}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9R1K7}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9R1K7}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9R1K7}. Note=Associated with centrioles. Both
CC cytoplasmic and nuclear. In the elongating spermatid it is associated
CC with the manchette, a specialized microtubule system present during
CC reshaping of the sperm head. {ECO:0000250|UniProtKB:Q9R1K7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9UJT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJT1-2; Sequence=VSP_006681;
CC Name=3;
CC IsoId=Q9UJT1-3; Sequence=VSP_006680;
CC Name=4;
CC IsoId=Q9UJT1-4; Sequence=VSP_045196;
CC Name=5;
CC IsoId=Q9UJT1-5; Sequence=VSP_046950;
CC Name=6;
CC IsoId=Q9UJT1-6; Sequence=VSP_046949;
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AF201333; AAF09584.1; -; mRNA.
DR EMBL; AB030837; BAD16590.1; -; mRNA.
DR EMBL; AB031045; BAD83581.1; -; mRNA.
DR EMBL; AK024096; BAB14825.1; -; mRNA.
DR EMBL; AK298492; BAG60700.1; -; mRNA.
DR EMBL; AK301312; BAG62863.1; -; mRNA.
DR EMBL; AC004686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94385.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94387.1; -; Genomic_DNA.
DR EMBL; BC000258; AAH00258.1; -; mRNA.
DR CCDS; CCDS11620.1; -. [Q9UJT1-1]
DR CCDS; CCDS54151.1; -. [Q9UJT1-4]
DR CCDS; CCDS54152.1; -. [Q9UJT1-6]
DR CCDS; CCDS54153.1; -. [Q9UJT1-2]
DR CCDS; CCDS54154.1; -. [Q9UJT1-5]
DR RefSeq; NP_001180538.1; NM_001193609.1. [Q9UJT1-2]
DR RefSeq; NP_001180539.1; NM_001193610.1. [Q9UJT1-5]
DR RefSeq; NP_001180540.1; NM_001193611.1. [Q9UJT1-6]
DR RefSeq; NP_001180541.1; NM_001193612.1.
DR RefSeq; NP_001180542.1; NM_001193613.1. [Q9UJT1-4]
DR RefSeq; NP_057345.2; NM_016261.3. [Q9UJT1-1]
DR AlphaFoldDB; Q9UJT1; -.
DR SMR; Q9UJT1; -.
DR BioGRID; 119352; 28.
DR IntAct; Q9UJT1; 5.
DR STRING; 9606.ENSP00000320797; -.
DR DrugBank; DB00570; Vinblastine.
DR iPTMnet; Q9UJT1; -.
DR PhosphoSitePlus; Q9UJT1; -.
DR BioMuta; TUBD1; -.
DR DMDM; 124056483; -.
DR EPD; Q9UJT1; -.
DR jPOST; Q9UJT1; -.
DR MassIVE; Q9UJT1; -.
DR MaxQB; Q9UJT1; -.
DR PaxDb; Q9UJT1; -.
DR PeptideAtlas; Q9UJT1; -.
DR PRIDE; Q9UJT1; -.
DR ProteomicsDB; 19408; -.
DR ProteomicsDB; 19495; -.
DR ProteomicsDB; 5305; -.
DR ProteomicsDB; 84644; -. [Q9UJT1-1]
DR ProteomicsDB; 84645; -. [Q9UJT1-2]
DR ProteomicsDB; 84646; -. [Q9UJT1-3]
DR Antibodypedia; 3899; 136 antibodies from 25 providers.
DR DNASU; 51174; -.
DR Ensembl; ENST00000325752.8; ENSP00000320797.3; ENSG00000108423.15. [Q9UJT1-1]
DR Ensembl; ENST00000340993.10; ENSP00000342399.5; ENSG00000108423.15. [Q9UJT1-2]
DR Ensembl; ENST00000346141.10; ENSP00000342561.5; ENSG00000108423.15. [Q9UJT1-3]
DR Ensembl; ENST00000376094.8; ENSP00000365262.4; ENSG00000108423.15. [Q9UJT1-6]
DR Ensembl; ENST00000394239.7; ENSP00000377785.3; ENSG00000108423.15. [Q9UJT1-5]
DR Ensembl; ENST00000539018.5; ENSP00000441757.1; ENSG00000108423.15. [Q9UJT1-4]
DR Ensembl; ENST00000592426.5; ENSP00000468518.1; ENSG00000108423.15. [Q9UJT1-1]
DR Ensembl; ENST00000613721.4; ENSP00000480387.1; ENSG00000108423.15. [Q9UJT1-6]
DR GeneID; 51174; -.
DR KEGG; hsa:51174; -.
DR MANE-Select; ENST00000325752.8; ENSP00000320797.3; NM_016261.4; NP_057345.2.
DR UCSC; uc002ixw.3; human. [Q9UJT1-1]
DR CTD; 51174; -.
DR DisGeNET; 51174; -.
DR GeneCards; TUBD1; -.
DR HGNC; HGNC:16811; TUBD1.
DR HPA; ENSG00000108423; Low tissue specificity.
DR MIM; 607344; gene.
DR neXtProt; NX_Q9UJT1; -.
DR OpenTargets; ENSG00000108423; -.
DR PharmGKB; PA134909953; -.
DR VEuPathDB; HostDB:ENSG00000108423; -.
DR eggNOG; KOG1374; Eukaryota.
DR GeneTree; ENSGT00940000157069; -.
DR HOGENOM; CLU_1371783_0_0_1; -.
DR InParanoid; Q9UJT1; -.
DR OMA; ACHPEYK; -.
DR OrthoDB; 1166669at2759; -.
DR PhylomeDB; Q9UJT1; -.
DR TreeFam; TF329833; -.
DR PathwayCommons; Q9UJT1; -.
DR SignaLink; Q9UJT1; -.
DR SIGNOR; Q9UJT1; -.
DR BioGRID-ORCS; 51174; 203 hits in 1084 CRISPR screens.
DR ChiTaRS; TUBD1; human.
DR GeneWiki; TUBD1; -.
DR GenomeRNAi; 51174; -.
DR Pharos; Q9UJT1; Tbio.
DR PRO; PR:Q9UJT1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UJT1; protein.
DR Bgee; ENSG00000108423; Expressed in secondary oocyte and 174 other tissues.
DR ExpressionAtlas; Q9UJT1; baseline and differential.
DR Genevisible; Q9UJT1; HS.
DR GO; GO:0005814; C:centriole; TAS:ProtInc.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002967; Delta_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
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; PTHR11588; 1.
DR PANTHER; PTHR11588:SF4; PTHR11588:SF4; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR01224; DELTATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Developmental protein; GTP-binding; Microtubule;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..453
FT /note="Tubulin delta chain"
FT /id="PRO_0000048484"
FT BINDING 143..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045196"
FT VAR_SEQ 58..311
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_006680"
FT VAR_SEQ 257..358
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15081367"
FT /id="VSP_046949"
FT VAR_SEQ 257..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006681"
FT VAR_SEQ 358..420
FT /note="VEGFKDPALYTSWLKPVNAFNVWKTQRAFSKYEKSAVLVSNSQFLVKPLDMI
FT VGKAWNMFASK -> VGKKFR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046950"
FT VARIANT 76
FT /note="M -> T (in dbSNP:rs1292053)"
FT /evidence="ECO:0000269|PubMed:10620804,
FT ECO:0000269|PubMed:15081367"
FT /id="VAR_030000"
FT CONFLICT 130
FT /note="C -> R (in Ref. 3; BAG60700)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="K -> R (in Ref. 3; BAG60700)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="N -> D (in Ref. 3; BAB14825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 51034 MW; 2D78AB3D9EEB9158 CRC64;
MSIVTVQLGQ CGNQIGFEVF DALLSDSHSS QGLCSMRENE AYQASCKERF FSEEENGVPI
ARAVLVDMEP KVINQMLSKA AQSGQWKYGQ HACFCQKQGS GNNWAYGYSV HGPRHEESIM
NIIRKEVEKC DSFSGFFIIM SMAGGTGSGL GAFVTQNLED QYSNSLKMNQ IIWPYGTGEV
IVQNYNSILT LSHLYRSSDA LLLHENDAIH KICAKLMNIK QISFSDINQV LAHQLGSVFQ
PTYSAESSFH YRRNPLGDLM EHLVPHPEFK MLSVRNIPHM SENSLAYTTF TWAGLLKHLR
QMLISNAKME EGIDRHVWPP LSGLPPLSKM SLNKDLHFNT SIANLVILRG KDVQSADVEG
FKDPALYTSW LKPVNAFNVW KTQRAFSKYE KSAVLVSNSQ FLVKPLDMIV GKAWNMFASK
AYIHQYTKFG IEEEDFLDSF TSLEQVVASY CNL
