Q9Y6A5 (TACC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transforming acidic coiled-coil-containing protein 3

Alternative name(s):
ERIC-1

Gene names

Name:	TACC3
Synonyms:	ERIC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	838 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors By similarity. May be involved in the control of cell growth and differentiation. May contribute to cancer.
Subunit structure	Interacts with microtubules. Interacts with CCDC100/CEP120. The coiled coil C-terminus region interacts with AH receptor nuclear translocator protein (ARNT) and ARNT2 By similarity. Interacts with GCN5L2 and PCAF. Ref.4
Subcellular location	Cytoplasm By similarity Ref.4.
Induction	Up-regulated in various cancer cell lines.
Sequence similarities	Belongs to the TACC family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	centrosome Inferred from direct assay. Source: HPA
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 838	838	Transforming acidic coiled-coil-containing protein 3		PRO_0000179990
Regions
	Coiled coil	637 – 837	201	Potential
	Compositional bias	155 – 160	6	Poly-Ser
Amino acid modifications
	Modified residue	25	1	Phosphoserine Ref.6 Ref.8 Ref.9
	Modified residue	59	1	Phosphothreonine Ref.7
	Modified residue	71	1	Phosphoserine Ref.9
	Modified residue	175	1	Phosphoserine Ref.11
	Modified residue	317	1	Phosphoserine Ref.8 Ref.9 Ref.10
	Modified residue	434	1	Phosphoserine Ref.5 Ref.6 Ref.9 Ref.10
	Modified residue	558	1	Phosphoserine Ref.9
Natural variations
	Natural variant	143	1	E → K. Corresponds to variant rs34205238 [ dbSNP | Ensembl ].		VAR_053714
	Natural variant	275	1	C → Y. Ref.2 Corresponds to variant rs17132047 [ dbSNP | Ensembl ].		VAR_053715
	Natural variant	287	1	G → S. Ref.2 Corresponds to variant rs1063743 [ dbSNP | Ensembl ].		VAR_053716
	Natural variant	514	1	G → E. Ref.2 Corresponds to variant rs17680881 [ dbSNP | Ensembl ].		VAR_053717
Experimental info
	Sequence conflict	342	1	V → L in CAB53009. Ref.2
	Sequence conflict	406	1	D → G in CAB53009. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6A5 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 07F056678096775E	FASTA	838	90,360
	10 20 30 40 50 60 MSLQVLNDKN VSNEKNTENC DFLFSPPEVT GRSSVLRVSQ KENVPPKNLA KAMKVTFQTP 70 80 90 100 110 120 LRDPQTHRIL SPSMASKLEA PFTQDDTLGL ENSHPVWTQK ENQQLIKEVD AKTTHGILQK 130 140 150 160 170 180 PVEADTDLLG DASPAFGSGS SSESGPGALA DLDCSSSSQS PGSSENQMVS PGKVSGSPEQ 190 200 210 220 230 240 AVEENLSSYS LDRRVTPASE TLEDPCRTES QHKAETPHGA EEECKAETPH GAEEECRHGG 250 260 270 280 290 300 VCAPAAVATS PPGAIPKEAC GGAPLQGLPG EALGCPAGVG TPVPADGTQT LTCAHTSAPE 310 320 330 340 350 360 STAPTNHLVA GRAMTLSPQE EVAAGQMASS SRSGPVKLEF DVSDGATSKR APPPRRLGER 370 380 390 400 410 420 SGLKPPLRKA AVRQQKAPQE VEEDDGRSGA GEDPPMPASR GSYHLDWDKM DDPNFIPFGG 430 440 450 460 470 480 DTKSGCSEAQ PPESPETRLG QPAAEQLHAG PATEEPGPCL SQQLHSASAE DTPVVQLAAE 490 500 510 520 530 540 TPTAESKERA LNSASTSLPT SCPGSEPVPT HQQGQPALEL KEESFRDPAE VLGTGAEVDY 550 560 570 580 590 600 LEQFGTSSFK ESALRKQSLY LKFDPLLRDS PGRPVPVATE TSSMHGANET PSGRPREAKL 610 620 630 640 650 660 VEFDFLGALD IPVPGPPPGV PAPGGPPLST GPIVDLLQYS QKDLDAVVKA TQEENRELRS 670 680 690 700 710 720 RCEELHGKNL ELGKIMDRFE EVVYQAMEEV QKQKELSKAE IQKVLKEKDQ LTTDLNSMEK 730 740 750 760 770 780 SFSDLFKRFE KQKEVIEGYR KNEESLKKCV EDYLARITQE GQRYQALKAH AEEKLQLANE 790 800 810 820 830 EIAQVRSKAQ AEALALQASL RKEQMRIQSL EKTVEQKTKE NEELTRICDD LISKMEKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The third member of the transforming acidic coiled coil-containing gene family, TACC3, maps in 4p16, close to translocation breakpoints in multiple myeloma, and is upregulated in various cancer cell lines." Still I.H., Vince P., Cowell J.K. Genomics 58:165-170(1999) [PubMed: 10366448] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization and localization of expression of an erythropoietin-induced gene, ERIC-1/TACC3, identified in erythroid precursor cells." McKeveney P.J., Hodges V.M., Mullan R.N., Maxwell P., Simpson D., Thompson A., Winter P.C., Lappin T.R., Maxwell A.P. Br. J. Haematol. 112:1016-1024(2001) [PubMed: 11298601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TYR-275; SER-287 AND GLU-514.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[4]	"The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases." Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H. Oncogene 23:2559-2563(2004) [PubMed: 14767476] [Abstract] Cited for: INTERACTION WITH GCN5L2 AND PCAF, SUBCELLULAR LOCATION.
[5]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-434, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-317, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-71; SER-317; SER-434 AND SER-558, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-434, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF093543 mRNA. Translation: AAD25964.1. AJ243997 mRNA. Translation: CAB53009.1. BC106071 mRNA. Translation: AAI06072.1.
IPI	IPI00002135.
RefSeq	NP_006333.1. NM_006342.2.
UniGene	Hs.104019.
3D structure databases
ProteinModelPortal	Q9Y6A5.
SMR	Q9Y6A5. Positions 806-835.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y6A5. 4 interactions.
STRING	Q9Y6A5.
PTM databases
PhosphoSite	Q9Y6A5.
Polymorphism databases
DMDM	13431939.
Proteomic databases
PeptideAtlas	Q9Y6A5.
PRIDE	Q9Y6A5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000313288; ENSP00000326550; ENSG00000013810.
GeneID	10460.
KEGG	hsa:10460.
UCSC	uc003gdo.1. human.
Organism-specific databases
CTD	10460.
GeneCards	GC04P001690.
H-InvDB	HIX0031367.
HGNC	HGNC:11524. TACC3.
HPA	CAB010111. HPA005781. HPA022039.
MIM	605303. gene.
neXtProt	NX_Q9Y6A5.
PharmGKB	PA36301.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00530000063855.
HOGENOM	HBG713121.
HOVERGEN	HBG044999.
InParanoid	Q9Y6A5.
OrthoDB	EOG4H9XK8.
PhylomeDB	Q9Y6A5.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_a_pathway. Aurora A signaling.
Gene expression databases
ArrayExpress	Q9Y6A5.
Bgee	Q9Y6A5.
CleanEx	HS_TACC3.
Genevestigator	Q9Y6A5.
GermOnline	ENSG00000013810. Homo sapiens.
Family and domain databases
InterPro	IPR007707. TACC. [Graphical view]
KO	K14283.
PANTHER	PTHR13924. TACC. 1 hit.
Pfam	PF05010. TACC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	39663.
SOURCE	Search...

Entry information

Entry name

TACC3_HUMAN

Accession

Primary (citable) accession number: Q9Y6A5
Secondary accession number(s): Q3KQS5, Q9UMQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.