TACC1_MOUSE
ID TACC1_MOUSE Reviewed; 774 AA.
AC Q6Y685; Q05A66; Q6Y686;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Transforming acidic coiled-coil-containing protein 1;
GN Name=Tacc1;
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 [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=15207008; DOI=10.1186/1471-2148-4-16;
RA Still I.H., Vettaikkorumakankauv A.K., DiMatteo A., Liang P.;
RT "Structure-function evolution of the transforming acidic coiled coil genes
RT revealed by analysis of phylogenetically diverse organisms.";
RL BMC Evol. Biol. 4:16-16(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP INTERACTION WITH RARA AND THRA, AND SUBCELLULAR LOCATION.
RX PubMed=20078863; DOI=10.1186/1471-2199-11-3;
RA Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
RT "The transforming acidic coiled coil (TACC1) protein modulates the
RT transcriptional activity of the nuclear receptors TR and RAR.";
RL BMC Mol. Biol. 11:3-3(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-480 AND SER-560, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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).
CC -!- FUNCTION: Involved in transcription regulation induced by nuclear
CC receptors, including in T3 thyroid hormone and all-trans retinoic acid
CC pathways. Might promote the nuclear localization of the receptors (By
CC similarity). Likely involved in the processes that promote cell
CC division prior to the formation of differentiated tissues.
CC {ECO:0000250|UniProtKB:O75410}.
CC -!- SUBUNIT: Interacts with CH-TOG and YEATS4. Interacts with the AURKA and
CC AURKB and AURKC. Interacts with LSM7, TDRD7 and SNRPG. Interacts with
CC GCN5L2 and PCAF (By similarity). Interacts with the thyroid hormone
CC receptors THRB and THRA, predominantly with isoform alpha-2. The
CC interaction with THRA isoform alpha-1 and THRB is decreased in the
CC presence of thyroid hormone T3 (PubMed:20078863). Interacts with RARA
CC in the nucleus (PubMed:20078863). Also interacts with other nuclear
CC receptors, including ESR1, NR3C1, PPARG and RXRA, preferentially in the
CC absence of their hormonal ligands (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O75410, ECO:0000269|PubMed:20078863}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75410}. Nucleus
CC {ECO:0000269|PubMed:20078863}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O75410}. Midbody
CC {ECO:0000250|UniProtKB:O75410}. Note=Nucleus during interphase. Weakly
CC concentrated at centrosomes during mitosis and colocalizes with AURKC
CC at the midbody during cytokinesis. {ECO:0000250|UniProtKB:O75410}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q6Y685-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q6Y685-2; Sequence=VSP_012650, VSP_012651;
CC -!- SIMILARITY: Belongs to the TACC 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; AY177412; AAO53447.1; -; mRNA.
DR EMBL; AY177413; AAO53448.1; -; mRNA.
DR EMBL; BC125389; AAI25390.1; -; mRNA.
DR EMBL; BC145709; AAI45710.1; -; mRNA.
DR CCDS; CCDS40302.1; -. [Q6Y685-2]
DR RefSeq; NP_796063.3; NM_177089.5.
DR RefSeq; NP_955355.1; NM_199323.3. [Q6Y685-2]
DR AlphaFoldDB; Q6Y685; -.
DR SMR; Q6Y685; -.
DR BioGRID; 235809; 1.
DR IntAct; Q6Y685; 2.
DR STRING; 10090.ENSMUSP00000081043; -.
DR iPTMnet; Q6Y685; -.
DR PhosphoSitePlus; Q6Y685; -.
DR EPD; Q6Y685; -.
DR jPOST; Q6Y685; -.
DR MaxQB; Q6Y685; -.
DR PaxDb; Q6Y685; -.
DR PeptideAtlas; Q6Y685; -.
DR PRIDE; Q6Y685; -.
DR ProteomicsDB; 254489; -. [Q6Y685-1]
DR ProteomicsDB; 254490; -. [Q6Y685-2]
DR Antibodypedia; 4470; 244 antibodies from 32 providers.
DR DNASU; 320165; -.
DR Ensembl; ENSMUST00000084512; ENSMUSP00000081560; ENSMUSG00000065954. [Q6Y685-2]
DR GeneID; 320165; -.
DR KEGG; mmu:320165; -.
DR UCSC; uc009lft.2; mouse. [Q6Y685-2]
DR CTD; 6867; -.
DR MGI; MGI:2443510; Tacc1.
DR VEuPathDB; HostDB:ENSMUSG00000065954; -.
DR eggNOG; ENOG502QUCC; Eukaryota.
DR GeneTree; ENSGT00940000156991; -.
DR HOGENOM; CLU_005375_2_1_1; -.
DR InParanoid; Q6Y685; -.
DR PhylomeDB; Q6Y685; -.
DR BioGRID-ORCS; 320165; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Tacc1; mouse.
DR PRO; PR:Q6Y685; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6Y685; protein.
DR Bgee; ENSMUSG00000065954; Expressed in gastrula and 218 other tissues.
DR ExpressionAtlas; Q6Y685; baseline and differential.
DR Genevisible; Q6Y685; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISS:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IDA:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IDA:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0022027; P:interkinetic nuclear migration; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR InterPro; IPR039915; TACC.
DR InterPro; IPR007707; TACC_C.
DR PANTHER; PTHR13924; PTHR13924; 1.
DR Pfam; PF05010; TACC_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75410"
FT CHAIN 2..774
FT /note="Transforming acidic coiled-coil-containing protein
FT 1"
FT /id="PRO_0000179987"
FT DOMAIN 216..294
FT /note="SPAZ 1"
FT DOMAIN 354..504
FT /note="SPAZ 2"
FT REGION 2..56
FT /note="Interaction with LSM7 and SNRPG"
FT /evidence="ECO:0000250"
FT REGION 21..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..255
FT /note="Interaction with TDRD7"
FT /evidence="ECO:0000250"
FT REGION 207..424
FT /note="Interaction with YEATS4"
FT /evidence="ECO:0000250"
FT REGION 214..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..774
FT /note="Interaction with CH-TOG"
FT /evidence="ECO:0000250"
FT COILED 579..774
FT MOTIF 452..468
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75410"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75410"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75410"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75410"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75410"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75410"
FT MOD_RES 228
FT /note="Phosphoserine; by AURKC"
FT /evidence="ECO:0000250|UniProtKB:O75410"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 55
FT /note="S -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15207008,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012650"
FT VAR_SEQ 56..461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15207008,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012651"
SQ SEQUENCE 774 AA; 83952 MW; AE9D412E63180976 CRC64;
MAFSPWQILS PVQWAKWTWS AVRGSGAGED EAGGPEGDPE EEEDSQAETK SLSFSSDSEG
NFETPEAETP IRSPLKESCD SSPGLAEPEA KPQESREADE QLVAEVIEKC SPDTCSRSSE
NEAPQATVDS HPVKDVRGKA EHDVSKISVV RPFSIETRNC TDDPAALGTA AAHGCVPVLP
GMALPSTTPE ATQDEPVMDR GMGVTLEAFT EASLKTGGPC PEPVASRSKL RKPKPVSLRK
KMAPEPEMLM EGSPLPKASS PWLPDGLDQN ANPSVLRGSG AQRSPLNLKE TAGVLSNDTS
DSGVEVAPGS PPLQLEDDFT EDGENVKIRS ALPKQSGRKP SNKLAPSIRK DGVSKPVGVE
QPSDPTVQDA LLDQMSPKLD PSKRSHPPAN FFGSGPILQN SPPLSSKCSH HFDPNNINTD
DSGDPCKPTP ALTSSGFCPA TGNHVNEILD SPKKAKSRLI TSGCKVKKYE AQPLDLDACS
QDEGAVISKI SEIPNRDGHA TDEEKLASTS SCAQKSAGAG VKGIEKETCQ KMEKEELAVH
GLLESSSEKA PVSVACGGES PLDGICLSEA DKTAVLTLIR EEIITKEIEA NEWKKKYEET
REEVLEMRKI VAEYEKTIAQ MIEDEQRTSM SSQKSFQQLT MEKEQALADL NSVERSLSDL
FRRYENLKGV LEGFKKNEEA LKKCAQDYLA RVKQEEQRYQ ALKVHAEEKL DRANEEIAQV
RSKAKAESAA LHAGLRKEQM KVESLERALQ QKNQEIEELT KICDELIAKL GKTD
