O95359 (TACC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 101.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Transforming acidic coiled-coil-containing protein 2 Alternative name(s): Anti-Zuai-1 Short name=AZU-1 | ||
| Gene names |
| ||
| 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 | 2948 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 play a role in organizing centrosomal microtubules. May act as a tumor suppressor protein. May represent a tumor progression marker. Ref.1 |
| Subunit structure | Interacts with CCDC100/CEP120 By similarity. Interacts with microtubules. Interacts with YEATS4, GCN5L2 and PCAF. Ref.3 Ref.9 |
| Subcellular location | Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › centrosome Ref.1 Ref.8 Ref.9. |
| Tissue specificity | Strongly expressed in heart, skeletal muscle, brain, prostate, thyroid and trachea. Ref.3 Ref.6 |
| Developmental stage | Expressed in fetal brain, lung, liver and kidney. Ref.3 |
| Post-translational modification | Phosphorylated by TTK; which is required for localization in centrosome. Ref.8 Ref.10 Ref.11 Ref.12 |
| Sequence similarities | Belongs to the TACC family. Contains 1 SPAZ (Ser/Pro-rich AZU-1) domain. |
| Sequence caution | The sequence AAF29537.2 differs from that shown. Reason: Intron retention. The sequence AAF63433.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton Nucleus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Coiled coil |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | Golgi apparatus Inferred from direct assay. Source: HPA microtubule organizing centerInferred from electronic annotation. Source: UniProtKB-SubCell nucleolusInferred from direct assay. Source: HPA |
| Molecular function | nuclear hormone receptor binding Inferred from direct assay. Source: MGI |
| Complete GO annotation... | |
Alternative products
| This entry describes 6 isoforms produced by alternative splicing. [Align] [Select] Note: Experimental confirmation may be lacking for some isoforms. | ||||||
| Isoform 4 (identifier: O95359-4) Also known as: Long; TACC2s; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 1 (identifier: O95359-1) Also known as: Short; The sequence of this isoform differs from the canonical sequence as follows: 1-1922: Missing. 1923-1945: APAGDRVEASTPSCPDPAKDLSR → MGGSQSLQPAPASDLNLEASEAM | ||||||
| Isoform 2 (identifier: O95359-2) The sequence of this isoform differs from the canonical sequence as follows: 1-2296: Missing. 2429-2432: Missing. 2633-2709: Missing. | ||||||
| Isoform 3 (identifier: O95359-3) Also known as: ECTACC; The sequence of this isoform differs from the canonical sequence as follows: 2633-2709: Missing. | ||||||
| Isoform 5 (identifier: O95359-5) Also known as: TACC21; The sequence of this isoform differs from the canonical sequence as follows: 49-1857: Missing. 1900-1944: Missing. | ||||||
| Isoform 6 (identifier: O95359-6) The sequence of this isoform differs from the canonical sequence as follows: 1-1922: Missing. 1923-1945: APAGDRVEASTPSCPDPAKDLSR → MGGSQSLQPAPASDLNLEASEAM 2680-2709: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2948 | 2948 | Transforming acidic coiled-coil-containing protein 2 | PRO_0000179988 | |||||
Regions | |||||||||
| Domain | 2315 – 2403 | 89 | SPAZ | ||||||
| Coiled coil | 2675 – 2703 | 29 | Potential | ||||||
| Coiled coil | 2746 – 2947 | 202 | Potential | ||||||
| Compositional bias | 482 – 549 | 68 | Pro-rich | ||||||
| Compositional bias | 1956 – 2016 | 61 | Pro-rich | ||||||
| Compositional bias | 2420 – 2423 | 4 | Poly-Lys | ||||||
Amino acid modifications | |||||||||
| Modified residue | 197 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 201 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 493 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 571 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 575 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 758 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 962 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1025 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1267 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1313 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1426 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 1562 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1946 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1949 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2072 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2073 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 2226 | 1 | Phosphoserine Ref.11 Ref.12 | ||||||
| Modified residue | 2246 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 2256 | 1 | Phosphoserine Ref.10 Ref.11 | ||||||
| Modified residue | 2317 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2321 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2359 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2389 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2390 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2392 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2394 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2403 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2512 | 1 | Phosphoserine Ref.10 Ref.11 | ||||||
| Modified residue | 2884 | 1 | N6-acetyllysine Ref.13 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 2296 | 2296 | Missing in isoform 2. | VSP_022151 | |||||
| Alternative sequence | 1 – 1922 | 1922 | Missing in isoform 1 and isoform 6. | VSP_022153 | |||||
| Alternative sequence | 49 – 1857 | 1809 | Missing in isoform 5. | VSP_022154 | |||||
| Alternative sequence | 1900 – 1944 | 45 | Missing in isoform 5. | VSP_022155 | |||||
| Alternative sequence | 1923 – 1945 | 23 | APAGD…KDLSR → MGGSQSLQPAPASDLNLEAS EAM in isoform 1 and isoform 6. | VSP_022156 | |||||
| Alternative sequence | 2429 – 2432 | 4 | Missing in isoform 2. | VSP_006368 | |||||
| Alternative sequence | 2633 – 2709 | 77 | Missing in isoform 2 and isoform 3. | VSP_006369 | |||||
| Alternative sequence | 2680 – 2709 | 30 | Missing in isoform 6. | VSP_022158 | |||||
| Natural variant | 170 | 1 | V → I. Corresponds to variant rs11200385 [ dbSNP | Ensembl ]. | VAR_053706 | |||||
| Natural variant | 798 | 1 | L → V in a breast cancer sample; somatic mutation. Ref.14 | VAR_036381 | |||||
| Natural variant | 830 | 1 | L → F. Ref.3 Corresponds to variant rs10887063 [ dbSNP | Ensembl ]. | VAR_053707 | |||||
| Natural variant | 1103 | 1 | W → R. Ref.3 Corresponds to variant rs7073433 [ dbSNP | Ensembl ]. | VAR_053708 | |||||
| Natural variant | 1347 | 1 | A → S in a breast cancer sample; somatic mutation. Ref.14 | VAR_036382 | |||||
| Natural variant | 1425 | 1 | A → T. Corresponds to variant rs4752642 [ dbSNP | Ensembl ]. | VAR_053709 | |||||
| Natural variant | 1492 | 1 | P → L. Corresponds to variant rs7920896 [ dbSNP | Ensembl ]. | VAR_053710 | |||||
| Natural variant | 1916 | 1 | E → K. Corresponds to variant rs12765679 [ dbSNP | Ensembl ]. | VAR_053711 | |||||
| Natural variant | 2078 | 1 | I → T. Corresponds to variant rs7083331 [ dbSNP | Ensembl ]. | VAR_029803 | |||||
| Natural variant | 2102 | 1 | N → S. Corresponds to variant rs3750843 [ dbSNP | Ensembl ]. | VAR_020478 | |||||
| Natural variant | 2197 | 1 | V → A. Corresponds to variant rs2295873 [ dbSNP | Ensembl ]. | VAR_020479 | |||||
| Natural variant | 2210 | 1 | A → V. Corresponds to variant rs2295874 [ dbSNP | Ensembl ]. | VAR_029804 | |||||
| Natural variant | 2216 | 1 | P → L. Corresponds to variant rs2295875 [ dbSNP | Ensembl ]. | VAR_053712 | |||||
| Natural variant | 2261 | 1 | L → H. Corresponds to variant rs2295876 [ dbSNP | Ensembl ]. | VAR_020480 | |||||
| Natural variant | 2271 | 1 | E → D. Corresponds to variant rs11200483 [ dbSNP | Ensembl ]. | VAR_053713 | |||||
| Natural variant | 2718 | 1 | V → I. Corresponds to variant rs2295878 [ dbSNP | Ensembl ]. | VAR_020481 | |||||
| Natural variant | 2732 | 1 | A → T. Ref.7 Corresponds to variant rs2295879 [ dbSNP | Ensembl ]. | VAR_020482 | |||||
| Natural variant | 2900 | 1 | Q → K. Ref.3 Corresponds to variant rs1063627 [ dbSNP | Ensembl ]. | VAR_029805 | |||||
Experimental info | |||||||||
| Sequence conflict | 2896 | 1 | R → Q in AAO62629. Ref.3 | ||||||
| Sequence conflict | 2896 | 1 | R → Q in AAO62630. Ref.3 | ||||||
| Sequence conflict | 2909 | 1 | S → T in AAH39311. Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "AZU-1: a candidate breast tumor suppressor and biomarker for tumor progression." Chen H.-M., Schmeichel K.L., Mian I.S., Lelievre S., Petersen O.W., Bissell M.J. Mol. Biol. Cell 11:1357-1367(2000) [PubMed: 10749935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION. |
| [2] | "The TACC domain identifies a family of centrosomal proteins that can interact with microtubules." Gergely F., Karlsson C., Still I.H., Cowell J.K., Kilmartin J., Raff J.W. Proc. Natl. Acad. Sci. U.S.A. 97:14352-14357(2000) [PubMed: 11121038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain, Fetal brain and Skeletal muscle. |
| [3] | "Molecular cloning, genomic structure and interactions of the putative breast tumor suppressor TACC2." Lauffart B., Gangisetty O., Still I.H. Genomics 81:192-201(2003) [PubMed: 12620397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH YEATS4, VARIANTS PHE-830; ARG-1103 AND LYS-2900. |
| [4] | "The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. Rogers J.Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "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] (ISOFORM 6). Tissue: Placenta and Testis. |
| [6] | "Cloning and structural characterization of ECTACC, a new member of the transforming acidic coiled coil (TACC) gene family: cDNA sequence and expression analysis in human microvascular endothelial cells." Pu J.J., Li C., Rodriguez M., Banerjee D. Cytokine 13:129-137(2001) [PubMed: 11161455] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1990-2948 (ISOFORM 3), TISSUE SPECIFICITY. Tissue: Endothelial cell. |
| [7] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2065-2948 (ISOFORM 3), VARIANT THR-2732. Tissue: Brain. |
| [8] | "TTK kinase is essential for the centrosomal localization of TACC2." Dou Z., Ding X., Zereshki A., Zhang Y., Zhang J., Wang F., Sun J., Huang H., Yao X. FEBS Lett. 572:51-56(2004) [PubMed: 15304323] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION. |
| [9] | "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. |
| [10] | "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-2256 AND SER-2512, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [11] | "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-197; SER-201; SER-493; SER-571; SER-575; SER-758; SER-962; SER-1025; SER-1267; SER-1313; THR-1426; SER-1562; SER-2072; THR-2073; SER-2226; THR-2246; SER-2256; SER-2317; SER-2321; SER-2359; SER-2389; SER-2390; SER-2392; SER-2394; SER-2403 AND SER-2512, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "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-2226, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [13] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2884, MASS SPECTROMETRY. |
| [14] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-798 AND SER-1347. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF176646 mRNA. Translation: AAF63433.1. Different initiation. AF095791 mRNA. Translation: AAC64968.2. AF528098 mRNA. Translation: AAO62629.1. AF528099 mRNA. Translation: AAO62630.1. AL135793, AC063960 Genomic DNA. Translation: CAI95127.1. AL135793 Genomic DNA. Translation: CAI95128.1. AL135793 Genomic DNA. Translation: CAI95131.1. AL135793, AC063960 Genomic DNA. Translation: CAI95134.1. BC000999 mRNA. Translation: AAH00999.1. BC039311 mRNA. Translation: AAH39311.1. AF220152 mRNA. Translation: AAF29537.2. Sequence problems. AL713712 mRNA. Translation: CAD28509.1. |
| IPI | IPI00030033. IPI00384450. IPI00410127. IPI00642773. IPI00643465. IPI00935164. |
| RefSeq | NP_008928.1. NM_006997.2. NP_996742.1. NM_206860.1. NP_996743.1. NM_206861.1. NP_996744.2. NM_206862.2. |
| UniGene | Hs.501252. Hs.713875. |
3D structure databases | |
| ProteinModelPortal | O95359. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O95359. 2 interactions. |
| MINT | MINT-1203853. |
| STRING | O95359. |
PTM databases | |
| PhosphoSite | O95359. |
Proteomic databases | |
| PRIDE | O95359. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000334433; ENSP00000334280; ENSG00000138162. ENST00000369005; ENSP00000358001; ENSG00000138162. |
| GeneID | 10579. |
| KEGG | hsa:10579. |
| UCSC | uc001lfv.1. human. uc001lfw.1. human. uc001lfy.1. human. uc001lfz.1. human. uc001lga.1. human. uc001lgb.1. human. |
Organism-specific databases | |
| CTD | 10579. |
| GeneCards | GC10P123738. |
| HGNC | HGNC:11523. TACC2. |
| HPA | HPA031020. |
| MIM | 605302. gene. |
| neXtProt | NX_O95359. |
| PharmGKB | PA36300. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG14226. |
| HOVERGEN | HBG093142. |
| InParanoid | O95359. |
| OMA | QVVCVAA. |
| OrthoDB | EOG44QT02. |
| PhylomeDB | O95359. |
Gene expression databases | |
| ArrayExpress | O95359. |
| Bgee | O95359. |
| Genevestigator | O95359. |
| GermOnline | ENSG00000138162. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR007707. TACC. [Graphical view] |
| KO | K14282. |
| PANTHER | PTHR13924. TACC. 1 hit. |
| Pfam | PF05010. TACC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 40155. |
| SOURCE | Search... |
Entry information
| Entry name | TACC2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O95359 Secondary accession number(s): Q4VXL0 Q9NZR5 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with