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Protein

Transforming acidic coiled-coil-containing protein 3

Gene

TACC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming acidic coiled-coil-containing protein 3
Alternative name(s):
ERIC-1
Gene namesi
Name:TACC3
Synonyms:ERIC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:11524. TACC3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

MalaCardsiTACC3.
Orphaneti251579. Giant cell glioblastoma.
251576. Gliosarcoma.
PharmGKBiPA36301.

Polymorphism and mutation databases

BioMutaiTACC3.
DMDMi13431939.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 838837Transforming acidic coiled-coil-containing protein 3PRO_0000179990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei39 – 391PhosphoserineCombined sources
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei175 – 1751PhosphoserineCombined sources
Modified residuei177 – 1771PhosphoserineCombined sources
Modified residuei250 – 2501PhosphoserineCombined sources
Modified residuei317 – 3171PhosphoserineCombined sources
Modified residuei402 – 4021PhosphoserineCombined sources
Modified residuei434 – 4341PhosphoserineCombined sources
Modified residuei558 – 5581PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y6A5.
MaxQBiQ9Y6A5.
PaxDbiQ9Y6A5.
PeptideAtlasiQ9Y6A5.
PRIDEiQ9Y6A5.

PTM databases

iPTMnetiQ9Y6A5.
PhosphoSiteiQ9Y6A5.

Expressioni

Inductioni

Up-regulated in various cancer cell lines.

Gene expression databases

BgeeiQ9Y6A5.
CleanExiHS_TACC3.
ExpressionAtlasiQ9Y6A5. baseline and differential.
GenevisibleiQ9Y6A5. HS.

Organism-specific databases

HPAiCAB010111.
HPA005781.
HPA022039.

Interactioni

Subunit structurei

Interacts with microtubules. Interacts with CCDC100/CEP120. The coiled coil C-terminal region interacts with AH receptor nuclear translocator protein (ARNT) and ARNT2 (By similarity). Interacts with GCN5L2 and PCAF.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ASPSCR1Q9BZE93EBI-2554984,EBI-1993677
CIB3Q96Q773EBI-2554984,EBI-10292696
CKAP5Q140087EBI-2554984,EBI-310585
CLTAP094963EBI-2554984,EBI-1171169
KIZQ2M2Z53EBI-2554984,EBI-2554344
SNX20Q7Z6143EBI-2554984,EBI-744896
TBC1D22BQ9NU193EBI-2554984,EBI-8787464
VPS37CA5D8V63EBI-2554984,EBI-2559305

Protein-protein interaction databases

BioGridi115723. 77 interactions.
IntActiQ9Y6A5. 43 interactions.
MINTiMINT-8144915.
STRINGi9606.ENSP00000326550.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6A5.
SMRiQ9Y6A5. Positions 792-838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili637 – 837201Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi155 – 1606Poly-Ser

Sequence similaritiesi

Belongs to the TACC family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IIVK. Eukaryota.
ENOG410YMFS. LUCA.
GeneTreeiENSGT00530000063855.
HOGENOMiHOG000294059.
HOVERGENiHBG044999.
InParanoidiQ9Y6A5.
KOiK14283.
OMAiSMHGANE.
OrthoDBiEOG7HB58V.
PhylomeDBiQ9Y6A5.
TreeFamiTF333149.

Family and domain databases

InterProiIPR007707. TACC.
[Graphical view]
PfamiPF05010. TACC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y6A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQVLNDKN VSNEKNTENC DFLFSPPEVT GRSSVLRVSQ KENVPPKNLA
60 70 80 90 100
KAMKVTFQTP LRDPQTHRIL SPSMASKLEA PFTQDDTLGL ENSHPVWTQK
110 120 130 140 150
ENQQLIKEVD AKTTHGILQK PVEADTDLLG DASPAFGSGS SSESGPGALA
160 170 180 190 200
DLDCSSSSQS PGSSENQMVS PGKVSGSPEQ AVEENLSSYS LDRRVTPASE
210 220 230 240 250
TLEDPCRTES QHKAETPHGA EEECKAETPH GAEEECRHGG VCAPAAVATS
260 270 280 290 300
PPGAIPKEAC GGAPLQGLPG EALGCPAGVG TPVPADGTQT LTCAHTSAPE
310 320 330 340 350
STAPTNHLVA GRAMTLSPQE EVAAGQMASS SRSGPVKLEF DVSDGATSKR
360 370 380 390 400
APPPRRLGER SGLKPPLRKA AVRQQKAPQE VEEDDGRSGA GEDPPMPASR
410 420 430 440 450
GSYHLDWDKM DDPNFIPFGG DTKSGCSEAQ PPESPETRLG QPAAEQLHAG
460 470 480 490 500
PATEEPGPCL SQQLHSASAE DTPVVQLAAE TPTAESKERA LNSASTSLPT
510 520 530 540 550
SCPGSEPVPT HQQGQPALEL KEESFRDPAE VLGTGAEVDY LEQFGTSSFK
560 570 580 590 600
ESALRKQSLY LKFDPLLRDS PGRPVPVATE TSSMHGANET PSGRPREAKL
610 620 630 640 650
VEFDFLGALD IPVPGPPPGV PAPGGPPLST GPIVDLLQYS QKDLDAVVKA
660 670 680 690 700
TQEENRELRS RCEELHGKNL ELGKIMDRFE EVVYQAMEEV QKQKELSKAE
710 720 730 740 750
IQKVLKEKDQ LTTDLNSMEK SFSDLFKRFE KQKEVIEGYR KNEESLKKCV
760 770 780 790 800
EDYLARITQE GQRYQALKAH AEEKLQLANE EIAQVRSKAQ AEALALQASL
810 820 830
RKEQMRIQSL EKTVEQKTKE NEELTRICDD LISKMEKI
Length:838
Mass (Da):90,360
Last modified:November 1, 1999 - v1
Checksum:i07F056678096775E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3421V → L in CAB53009 (PubMed:11298601).Curated
Sequence conflicti406 – 4061D → G in CAB53009 (PubMed:11298601).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431E → K.
Corresponds to variant rs34205238 [ dbSNP | Ensembl ].
VAR_053714
Natural varianti275 – 2751C → Y.2 Publications
Corresponds to variant rs17132047 [ dbSNP | Ensembl ].
VAR_053715
Natural varianti287 – 2871G → S.2 Publications
Corresponds to variant rs1063743 [ dbSNP | Ensembl ].
VAR_053716
Natural varianti514 – 5141G → E.2 Publications
Corresponds to variant rs17680881 [ dbSNP | Ensembl ].
VAR_053717

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093543 mRNA. Translation: AAD25964.1.
AJ243997 mRNA. Translation: CAB53009.1.
BC106071 mRNA. Translation: AAI06072.1.
BC111771 mRNA. Translation: AAI11772.1.
CCDSiCCDS3352.1.
RefSeqiNP_006333.1. NM_006342.2.
UniGeneiHs.104019.

Genome annotation databases

EnsembliENST00000313288; ENSP00000326550; ENSG00000013810.
GeneIDi10460.
KEGGihsa:10460.
UCSCiuc003gdo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093543 mRNA. Translation: AAD25964.1.
AJ243997 mRNA. Translation: CAB53009.1.
BC106071 mRNA. Translation: AAI06072.1.
BC111771 mRNA. Translation: AAI11772.1.
CCDSiCCDS3352.1.
RefSeqiNP_006333.1. NM_006342.2.
UniGeneiHs.104019.

3D structure databases

ProteinModelPortaliQ9Y6A5.
SMRiQ9Y6A5. Positions 792-838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115723. 77 interactions.
IntActiQ9Y6A5. 43 interactions.
MINTiMINT-8144915.
STRINGi9606.ENSP00000326550.

PTM databases

iPTMnetiQ9Y6A5.
PhosphoSiteiQ9Y6A5.

Polymorphism and mutation databases

BioMutaiTACC3.
DMDMi13431939.

Proteomic databases

EPDiQ9Y6A5.
MaxQBiQ9Y6A5.
PaxDbiQ9Y6A5.
PeptideAtlasiQ9Y6A5.
PRIDEiQ9Y6A5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313288; ENSP00000326550; ENSG00000013810.
GeneIDi10460.
KEGGihsa:10460.
UCSCiuc003gdo.4. human.

Organism-specific databases

CTDi10460.
GeneCardsiTACC3.
HGNCiHGNC:11524. TACC3.
HPAiCAB010111.
HPA005781.
HPA022039.
MalaCardsiTACC3.
MIMi605303. gene.
neXtProtiNX_Q9Y6A5.
Orphaneti251579. Giant cell glioblastoma.
251576. Gliosarcoma.
PharmGKBiPA36301.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIVK. Eukaryota.
ENOG410YMFS. LUCA.
GeneTreeiENSGT00530000063855.
HOGENOMiHOG000294059.
HOVERGENiHBG044999.
InParanoidiQ9Y6A5.
KOiK14283.
OMAiSMHGANE.
OrthoDBiEOG7HB58V.
PhylomeDBiQ9Y6A5.
TreeFamiTF333149.

Miscellaneous databases

GeneWikiiTACC3.
GenomeRNAii10460.
PROiQ9Y6A5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y6A5.
CleanExiHS_TACC3.
ExpressionAtlasiQ9Y6A5. baseline and differential.
GenevisibleiQ9Y6A5. HS.

Family and domain databases

InterProiIPR007707. TACC.
[Graphical view]
PfamiPF05010. TACC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS TYR-275; SER-287 AND GLU-514.
    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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCN5L2 AND PCAF, SUBCELLULAR LOCATION.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-71; SER-317; SER-434 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-71; SER-317 AND SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-39; SER-71; SER-177; SER-250; SER-317; SER-434 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiTACC3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6A5
Secondary accession number(s): Q2NKK4, Q3KQS5, Q9UMQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.