Reviewed,
UniProtKB/Swiss-Prot P56279 (TCL1A_HUMAN)
Last modified
November 25, 2008.
Version 75.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: T-cell leukemia/lymphoma protein 1A Alternative name(s): Protein p14 TCL1 Oncogene TCL1 Short name=TCL-1 | ||||
| Gene names |
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| 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 | 114 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Enhances the phosphorylation and activation of AKT1, AKT2 and AKT3. Promotes nuclear translocation of AKT1. Enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival. |
| Subunit structure | Homodimer. Interacts with AKT1, AKT2 and AKT3 (via PH domain). Interacts with PNPT1; the interaction has no effect on PNPT1 exonuclease activity. |
| Subcellular location | CytoplasmBy similarity. NucleusBy similarity. Microsome. Endoplasmic reticulum. Note= Microsomal fraction. |
| Tissue specificity | Restricted in the T-cell lineage to immature thymocytes and activated peripheral lymphocytes. Preferentially expressed early in T- and B-lymphocyte differentiation. |
| Involvement in disease | Chromosomal aberrations activating TCL1A are found in chronic T-cell leukemias (T-CLL). Translocation t(14;14)(q11;q32); translocation t(7;14)(q35;q32); inversion inv(14)(q11;q32) that involves the T-cell receptor alpha/delta locuses. |
| Sequence similarities | Belongs to the TCL1 family. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm Endoplasmic reticulum Microsome Nucleus |
| Coding sequence diversity | Chromosomal rearrangement |
| Disease | Proto-oncogene |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | multicellular organismal development Ref.1 Traceable author statement. Source: ProtInc |
| Cellular component | endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW microsomeInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 114 | 114 | T-cell leukemia/lymphoma protein 1A | PRO_0000184488 | |||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||
| Mutagenesis | 16 | 1 | D → G: Greatly reduced binding to AKT1, AKT2 and AKT3. Abolishes nuclear transport of AKT1 | ||||||||||||||||||||||||||
| Mutagenesis | 30 | 1 | K → M: Slightly reduced binding to AKT2 | ||||||||||||||||||||||||||
| Mutagenesis | 36 – 38 | 3 | PLT → AAA: Unable to homodimerize but has no effect on interaction with AKT1, AKT2 or AKT3 | ||||||||||||||||||||||||||
| Mutagenesis | 46 | 1 | Q → R: Slightly increased binding to AKT2 | ||||||||||||||||||||||||||
| Mutagenesis | 74 | 1 | I → V: Greatly reduced binding to AKT2. Abolishes nuclear transport of AKT1 | ||||||||||||||||||||||||||
| Mutagenesis | 106 | 1 | M → V: Slightly increased binding to AKT2 | ||||||||||||||||||||||||||
| Sequence conflict | 106 | 1 | M → V in CAG33077. Ref.2 | ||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||
| Beta strand | 8 – 10 | 3 | |||||||||||||||||||||||||||
| Beta strand | 16 – 22 | 7 | |||||||||||||||||||||||||||
| Beta strand | 25 – 28 | 4 | |||||||||||||||||||||||||||
| Beta strand | 33 – 42 | 10 | |||||||||||||||||||||||||||
| Turn | 43 – 45 | 3 | |||||||||||||||||||||||||||
| Beta strand | 46 – 53 | 8 | |||||||||||||||||||||||||||
| Helix | 64 – 67 | 4 | |||||||||||||||||||||||||||
| Beta strand | 74 – 78 | 5 | |||||||||||||||||||||||||||
| Beta strand | 84 – 86 | 3 | |||||||||||||||||||||||||||
| Beta strand | 91 – 100 | 10 | |||||||||||||||||||||||||||
| Beta strand | 103 – 111 | 9 | |||||||||||||||||||||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Identification of the TCL1 gene involved in T-cell malignancies." Virgilio L., Narducci M.G., Isobe M., Billips L.G., Cooper M.D., Croce C.M., Russo G. Proc. Natl. Acad. Sci. U.S.A. 91:12530-12534(1994) [PubMed: 7809072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [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: B-cell and Lymph. |
| [4] | "Characterization and localization of the TCL-1 oncogene product." Fu T.-B., Virgilio L., Narducci M.G., Facchiano A., Russo G., Croce C.M. Cancer Res. 54:6297-6301(1994) [PubMed: 7987816] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION. |
| [5] | "The protooncogene TCL1 is an Akt kinase coactivator." Laine J., Kuenstle G., Obata T., Sha M., Noguchi M. Mol. Cell 6:395-407(2000) [PubMed: 10983986] [Abstract] Cited for: FUNCTION, INTERACTION WITH AKT1 AND AKT2. |
| [6] | "Tcl1 enhances Akt kinase activity and mediates its nuclear translocation." Pekarsky Y., Koval A., Hallas C., Bichi R., Tresini M., Malstrom S., Russo G., Tsichlis P., Croce C.M. Proc. Natl. Acad. Sci. U.S.A. 97:3028-3033(2000) [PubMed: 10716693] [Abstract] Cited for: FUNCTION, INTERACTION WITH AKT1. |
| [7] | "Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family." Laine J., Kuenstle G., Obata T., Noguchi M. J. Biol. Chem. 277:3743-3751(2002) [PubMed: 11707444] [Abstract] Cited for: FUNCTION, INTERACTION WITH AKT3. |
| [8] | "Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1." Kuenstle G., Laine J., Pierron G., Kagami S., Nakajima H., Hoh F., Roumestand C., Stern M.H., Noguchi M. Mol. Cell. Biol. 22:1513-1525(2002) [PubMed: 11839817] [Abstract] Cited for: FUNCTION, INTERACTION WITH AKT1; AKT2 AND AKT3, MUTAGENESIS OF ASP-16; LYS-30; 36-PRO--THR-38; GLN-46; ILE-74 AND MET-106. |
| [9] | "The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity." French S.W., Dawson D.W., Chen H.-W., Rainey R.N., Sievers S.A., Balatoni C.E., Wong L., Troke J.J., Nguyen M.T.N., Koehler C.M., Teitell M.A. Cancer Lett. 248:198-210(2007) [PubMed: 16934922] [Abstract] Cited for: INTERACTION WITH PNPT1. |
| [10] | "Crystal structure of p14TCL1, an oncogene product involved in T-cell prolymphocytic leukemia, reveals a novel beta-barrel topology." Hoh F., Yang Y.-S., Guignard L., Padilla A., Stern M.-H., Lhoste J.-M., van Tilbourgh H. Structure 6:147-155(1998) [PubMed: 9519406] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X82240 mRNA. Translation: CAA57708.1. CR456796 mRNA. Translation: CAG33077.1. BC003574 mRNA. Translation: AAH03574.1. BC005831 mRNA. Translation: AAH05831.1. BC014024 mRNA. Translation: AAH14024.1. | |||||||||||||
| PIR | I38286. | ||||||||||||
| RefSeq | NP_001092195.1. NP_068801.1. | ||||||||||||
| UniGene | Hs.2484 | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P56279. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P56279. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000100721. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 8115. | ||||||||||||
| KEGG | hsa:8115. | ||||||||||||
Organism-specific databases | |||||||||||||
| H-InvDB | HIX0011943. | ||||||||||||
| HGNC | HGNC:11648. TCL1A. | ||||||||||||
| HPA | CAB004045. HPA016604. | ||||||||||||
| MIM | 186960. gene. | ||||||||||||
| Orphanet | 86872. T-cell large granular lymphocyte leukaemia. | ||||||||||||
| PharmGKB | PA36400. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
| GeneCards | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P56279. | ||||||||||||
| HOVERGEN | P56279. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P56279. | ||||||||||||
| CleanEx | HS_TCL1A. | ||||||||||||
| GermOnline | ENSG00000100721. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR004832. TCL1_MTCP1. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.40.15.10. TCL1_MTCP1. 1 hit. | ||||||||||||
| Pfam | PF01840. TCL1_MTCP1. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD015575. TCL1_MTCP1. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| LinkHub | P56279. | ||||||||||||
| NextBio | 30770. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | TCL1A_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P56279 Secondary accession number(s): Q6IBK7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 14 Human chromosome 14: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


