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P56279

- TCL1A_HUMAN

UniProt

P56279 - TCL1A_HUMAN

Protein

T-cell leukemia/lymphoma protein 1A

Gene

TCL1A

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

    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.4 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. multicellular organismal development Source: ProtInc
    2. stem cell maintenance Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    T-cell leukemia/lymphoma protein 1A
    Alternative name(s):
    Oncogene TCL-1
    Short name:
    Oncogene TCL1
    Protein p14 TCL1
    Gene namesi
    Name:TCL1A
    Synonyms:TCL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:11648. TCL1A.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Microsome 1 Publication. Endoplasmic reticulum 1 Publication
    Note: Microsomal fraction.

    GO - Cellular componenti

    1. cell cortex Source: Ensembl
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    3. pronucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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 loci.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161D → G: Greatly reduced binding to AKT1, AKT2 and AKT3. Abolishes nuclear transport of AKT1. 1 Publication
    Mutagenesisi30 – 301K → M: Slightly reduced binding to AKT2. 1 Publication
    Mutagenesisi36 – 383PLT → AAA: Unable to homodimerize but has no effect on interaction with AKT1, AKT2 or AKT3.
    Mutagenesisi46 – 461Q → R: Slightly increased binding to AKT2. 1 Publication
    Mutagenesisi74 – 741I → V: Greatly reduced binding to AKT2. Abolishes nuclear transport of AKT1. 1 Publication
    Mutagenesisi106 – 1061M → V: Slightly increased binding to AKT2. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBiPA36400.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 114114T-cell leukemia/lymphoma protein 1APRO_0000184488Add
    BLAST

    Proteomic databases

    MaxQBiP56279.
    PaxDbiP56279.
    PRIDEiP56279.

    PTM databases

    PhosphoSiteiP56279.

    Expressioni

    Tissue specificityi

    Restricted in the T-cell lineage to immature thymocytes and activated peripheral lymphocytes. Preferentially expressed early in T- and B-lymphocyte differentiation.

    Gene expression databases

    ArrayExpressiP56279.
    BgeeiP56279.
    CleanExiHS_TCL1A.
    GenevestigatoriP56279.

    Organism-specific databases

    HPAiCAB004045.
    HPA016604.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with AKT1, AKT2 and AKT3 (via PH domain). Interacts with PNPT1; the interaction has no effect on PNPT1 exonuclease activity.5 Publications

    Protein-protein interaction databases

    BioGridi113783. 11 interactions.
    DIPiDIP-60787N.
    IntActiP56279. 2 interactions.
    MINTiMINT-1454936.
    STRINGi9606.ENSP00000216612.

    Structurei

    Secondary structure

    1
    114
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Beta strandi16 – 227
    Beta strandi25 – 284
    Beta strandi33 – 4210
    Turni43 – 453
    Beta strandi46 – 538
    Helixi64 – 674
    Beta strandi74 – 785
    Beta strandi84 – 863
    Beta strandi91 – 10010
    Beta strandi103 – 1119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JSGX-ray2.50A1-114[»]
    ProteinModelPortaliP56279.
    SMRiP56279. Positions 4-114.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56279.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TCL1 family.Curated

    Phylogenomic databases

    eggNOGiNOG42423.
    HOGENOMiHOG000037945.
    HOVERGENiHBG052523.
    InParanoidiP56279.
    KOiK10167.
    OMAiKITFATH.
    OrthoDBiEOG7MD4S1.
    PhylomeDBiP56279.
    TreeFamiTF337903.

    Family and domain databases

    Gene3Di2.40.15.10. 1 hit.
    InterProiIPR004832. TCL1_MTCP1.
    [Graphical view]
    PfamiPF01840. TCL1_MTCP1. 1 hit.
    [Graphical view]
    ProDomiPD015575. TCL1_MTCP1. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF50904. SSF50904. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P56279-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAECPTLGEA VTDHPDRLWA WEKFVYLDEK QHAWLPLTIE IKDRLQLRVL    50
    LRREDVVLGR PMTPTQIGPS LLPIMWQLYP DGRYRSSDSS FWRLVYHIKI 100
    DGVEDMLLEL LPDD 114
    Length:114
    Mass (Da):13,460
    Last modified:July 15, 1998 - v1
    Checksum:i90D55ABC97C36D04
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061M → V in CAG33077. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561V → I.
    Corresponds to variant rs17093294 [ dbSNP | Ensembl ].
    VAR_053718

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS9941.1.
    PIRiI38286.
    RefSeqiNP_001092195.1. NM_001098725.1.
    NP_068801.1. NM_021966.2.
    UniGeneiHs.2484.

    Genome annotation databases

    EnsembliENST00000402399; ENSP00000385036; ENSG00000100721.
    ENST00000554012; ENSP00000451506; ENSG00000100721.
    ENST00000555202; ENSP00000450496; ENSG00000100721.
    ENST00000556450; ENSP00000450701; ENSG00000100721.
    GeneIDi8115.
    KEGGihsa:8115.
    UCSCiuc001yfb.4. human.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS9941.1.
    PIRi I38286.
    RefSeqi NP_001092195.1. NM_001098725.1.
    NP_068801.1. NM_021966.2.
    UniGenei Hs.2484.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JSG X-ray 2.50 A 1-114 [» ]
    ProteinModelPortali P56279.
    SMRi P56279. Positions 4-114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113783. 11 interactions.
    DIPi DIP-60787N.
    IntActi P56279. 2 interactions.
    MINTi MINT-1454936.
    STRINGi 9606.ENSP00000216612.

    PTM databases

    PhosphoSitei P56279.

    Proteomic databases

    MaxQBi P56279.
    PaxDbi P56279.
    PRIDEi P56279.

    Protocols and materials databases

    DNASUi 8115.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000402399 ; ENSP00000385036 ; ENSG00000100721 .
    ENST00000554012 ; ENSP00000451506 ; ENSG00000100721 .
    ENST00000555202 ; ENSP00000450496 ; ENSG00000100721 .
    ENST00000556450 ; ENSP00000450701 ; ENSG00000100721 .
    GeneIDi 8115.
    KEGGi hsa:8115.
    UCSCi uc001yfb.4. human.

    Organism-specific databases

    CTDi 8115.
    GeneCardsi GC14M096177.
    HGNCi HGNC:11648. TCL1A.
    HPAi CAB004045.
    HPA016604.
    MIMi 186960. gene.
    neXtProti NX_P56279.
    Orphaneti 99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBi PA36400.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42423.
    HOGENOMi HOG000037945.
    HOVERGENi HBG052523.
    InParanoidi P56279.
    KOi K10167.
    OMAi KITFATH.
    OrthoDBi EOG7MD4S1.
    PhylomeDBi P56279.
    TreeFami TF337903.

    Miscellaneous databases

    EvolutionaryTracei P56279.
    GeneWikii TCL1A.
    GenomeRNAii 8115.
    NextBioi 30770.
    PROi P56279.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56279.
    Bgeei P56279.
    CleanExi HS_TCL1A.
    Genevestigatori P56279.

    Family and domain databases

    Gene3Di 2.40.15.10. 1 hit.
    InterProi IPR004832. TCL1_MTCP1.
    [Graphical view ]
    Pfami PF01840. TCL1_MTCP1. 1 hit.
    [Graphical view ]
    ProDomi PD015575. TCL1_MTCP1. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF50904. SSF50904. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AKT1 AND AKT2.
    6. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiTCL1A_HUMAN
    AccessioniPrimary (citable) accession number: P56279
    Secondary accession number(s): Q6IBK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 132 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3