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Protein

T-cell leukemia/lymphoma protein 1A

Gene

TCL1A

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

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

  • identical protein binding Source: IntAct

GO - Biological processi

  • multicellular organism development Source: ProtInc

Enzyme and pathway databases

SIGNORiP56279.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:11648. TCL1A.

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi16D → G: Greatly reduced binding to AKT1, AKT2 and AKT3. Abolishes nuclear transport of AKT1. 1 Publication1
Mutagenesisi30K → M: Slightly reduced binding to AKT2. 1 Publication1
Mutagenesisi36 – 38PLT → AAA: Unable to homodimerize but has no effect on interaction with AKT1, AKT2 or AKT3. 1 Publication3
Mutagenesisi46Q → R: Slightly increased binding to AKT2. 1 Publication1
Mutagenesisi74I → V: Greatly reduced binding to AKT2. Abolishes nuclear transport of AKT1. 1 Publication1
Mutagenesisi106M → V: Slightly increased binding to AKT2. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi8115.
MalaCardsiTCL1A.
OpenTargetsiENSG00000100721.
Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA36400.

Polymorphism and mutation databases

BioMutaiTCL1A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001844881 – 114T-cell leukemia/lymphoma protein 1AAdd BLAST114

Proteomic databases

EPDiP56279.
MaxQBiP56279.
PaxDbiP56279.
PeptideAtlasiP56279.
PRIDEiP56279.

PTM databases

iPTMnetiP56279.
PhosphoSitePlusiP56279.

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

BgeeiENSG00000100721.
CleanExiHS_TCL1A.
ExpressionAtlasiP56279. baseline and differential.
GenevisibleiP56279. HS.

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

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi113783. 26 interactors.
DIPiDIP-60787N.
IntActiP56279. 35 interactors.
MINTiMINT-1454936.
STRINGi9606.ENSP00000385036.

Structurei

Secondary structure

1114
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Beta strandi16 – 22Combined sources7
Beta strandi25 – 28Combined sources4
Beta strandi33 – 42Combined sources10
Turni43 – 45Combined sources3
Beta strandi46 – 53Combined sources8
Helixi64 – 67Combined sources4
Beta strandi74 – 78Combined sources5
Beta strandi84 – 86Combined sources3
Beta strandi91 – 100Combined sources10
Beta strandi103 – 111Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JSGX-ray2.50A1-114[»]
ProteinModelPortaliP56279.
SMRiP56279.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56279.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCL1 family.Curated

Phylogenomic databases

eggNOGiENOG410JEFE. Eukaryota.
ENOG4111B9D. LUCA.
GeneTreeiENSGT00390000006885.
HOGENOMiHOG000037945.
HOVERGENiHBG052523.
InParanoidiP56279.
KOiK10167.
OMAiNQRTWLP.
OrthoDBiEOG091G0ZI2.
PhylomeDBiP56279.
TreeFamiTF337903.

Family and domain databases

Gene3Di2.40.15.10. 1 hit.
InterProiView protein in InterPro
IPR004832. TCL1_MTCP1.
PfamiView protein in Pfam
PF01840. TCL1_MTCP1. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD015575. TCL1_MTCP1. 1 hit.
SUPFAMiSSF50904. SSF50904. 1 hit.

Sequencei

Sequence statusi: Complete.

P56279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAECPTLGEA VTDHPDRLWA WEKFVYLDEK QHAWLPLTIE IKDRLQLRVL
60 70 80 90 100
LRREDVVLGR PMTPTQIGPS LLPIMWQLYP DGRYRSSDSS FWRLVYHIKI
110
DGVEDMLLEL LPDD
Length:114
Mass (Da):13,460
Last modified:July 15, 1998 - v1
Checksum:i90D55ABC97C36D04
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti106M → V in CAG33077 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05371856V → I. Corresponds to variant dbSNP:rs17093294Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_016877165.1. XM_017021676.1.
XP_016877166.1. XM_017021677.1.
UniGeneiHs.2484.

Genome annotation databases

EnsembliENST00000402399; ENSP00000385036; ENSG00000100721.
ENST00000554012; ENSP00000451506; ENSG00000100721.
ENST00000555202; ENSP00000450496; ENSG00000100721.
ENST00000556450; ENSP00000450701; ENSG00000100721.
GeneIDi8115.
KEGGihsa:8115.
UCSCiuc001yfb.5. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

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.

Entry informationi

Entry nameiTCL1A_HUMAN
AccessioniPrimary (citable) accession number: P56279
Secondary accession number(s): Q6IBK7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: March 15, 2017
This is version 157 of the entry and version 1 of the sequence. See 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