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Protein

Malignant T-cell-amplified sequence 1

Gene

MCTS1

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

Functioni

Anti-oncogene that plays a role in cell cycle regulation; decreases cell doubling time and anchorage-dependent growth; shortens the duration of G1 transit time and G1/S transition. When constituvely expressed, increases CDK4 and CDK6 kinases activity and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex formation. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role as translation enhancer; recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, subsequently altering the mRNA translation profile; up-regulates protein levels of BCL2L2, TFDP1, MRE11A, CCND1 and E2F1, while mRNA levels remains constant. Hyperactivates DNA damage signaling pathway; increased gamma-irradiation-induced phosphorylation of histone H2AX, and induces damage foci formation. Increases the overall number of chromosomal abnormalities such as larger chromosomes formation and multiples chromosomal fusions when overexpressed in gamma-irradiated cells. May play a role in promoting lymphoid tumor development: lymphoid cell lines overexpressing MCTS1 exhibit increased growth rates and display increased protection against apoptosis. May contribute to the pathogenesis and progression of breast cancer via promotion of angiogenesis through the decline of inhibitory THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the process of proteasome degradation to down-regulate Tumor suppressor p53/TP53 in breast cancer cell; Positively regulates phosphorylation of MAPK1 and MAPK3. Involved in translation initiation; promotes aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits.10 Publications

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: UniProtKB-KW
  • formation of translation preinitiation complex Source: UniProtKB
  • IRES-dependent translational initiation Source: UniProtKB
  • positive regulation of cell proliferation Source: ProtInc
  • regulation of growth Source: UniProtKB-KW
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • ribosome disassembly Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • translation reinitiation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Cell cycle, DNA damage, Growth regulation, Protein biosynthesis, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101898-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Malignant T-cell-amplified sequence 1
Short name:
MCT-1
Alternative name(s):
Multiple copies T-cell malignancies
Gene namesi
Name:MCTS1
Synonyms:MCT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:23357. MCTS1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi81T → A: No phosphorylation by MAPK1; decreased stability of MCTS1 protein; Significant cell growth reduction. 1 Publication1
Mutagenesisi118S → A: No phosphorylation by CDK1; No cell growth alteration. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi28985.
OpenTargetsiENSG00000232119.
PharmGKBiPA128394649.

Polymorphism and mutation databases

BioMutaiMCTS1.
DMDMi74735052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003447861 – 181Malignant T-cell-amplified sequence 1Add BLAST181

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei81Phosphothreonine; by MAPK1 and MAPK31 Publication1
Modified residuei118Phosphoserine; by CDK11 Publication1

Post-translational modificationi

Phosphorylation is critical for stabilization and promotion of cell proliferation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9ULC4.
PaxDbiQ9ULC4.
PeptideAtlasiQ9ULC4.
PRIDEiQ9ULC4.

PTM databases

iPTMnetiQ9ULC4.
PhosphoSitePlusiQ9ULC4.

Expressioni

Tissue specificityi

Ubiquitous. Over-expressed in T-cell lymphoid cell lines and in non-Hodgkin lymphoma cell lines as well as in a subset of primary large B-cell lymphomas.1 Publication

Inductioni

By DNA damaging agents such as gamma irradiation, adriamycin or taxol in lymphoid cells, but not by stress stimuli such as heat shock. This induction of protein expression does not occur at the RNA level, and does not require new protein synthesis.1 Publication

Gene expression databases

BgeeiENSG00000232119.
CleanExiHS_MCTS1.
GenevisibleiQ9ULC4. HS.

Organism-specific databases

HPAiHPA001045.

Interactioni

Subunit structurei

Interacts (via PUA domain) with DENR.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DENRO435834EBI-716076,EBI-716083

Protein-protein interaction databases

BioGridi118806. 37 interactors.
IntActiQ9ULC4. 5 interactors.
MINTiMINT-1405141.
STRINGi9606.ENSP00000360365.

Structurei

Secondary structure

1181
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 10Combined sources4
Beta strandi11 – 16Combined sources6
Helixi19 – 32Combined sources14
Helixi34 – 39Combined sources6
Helixi40 – 43Combined sources4
Beta strandi50 – 55Combined sources6
Helixi56 – 58Combined sources3
Beta strandi59 – 64Combined sources6
Beta strandi67 – 73Combined sources7
Helixi82 – 87Combined sources6
Helixi89 – 91Combined sources3
Beta strandi94 – 97Combined sources4
Helixi99 – 101Combined sources3
Helixi102 – 105Combined sources4
Turni106 – 108Combined sources3
Helixi114 – 117Combined sources4
Beta strandi131 – 136Combined sources6
Beta strandi143 – 150Combined sources8
Helixi152 – 158Combined sources7
Beta strandi161 – 169Combined sources9
Helixi173 – 177Combined sources5
Beta strandi179 – 181Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3R90X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L1-181[»]
ProteinModelPortaliQ9ULC4.
SMRiQ9ULC4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini92 – 171PUAPROSITE-ProRule annotationAdd BLAST80

Domaini

The PUA RNA-binding domain is critical for cap binding, but not sufficient for translation enhancer function. MCT1 N-terminal region is required to enhance translation possibly through interaction with other proteins.1 Publication

Sequence similaritiesi

Belongs to the MCTS1 family.Curated
Contains 1 PUA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2523. Eukaryota.
COG2016. LUCA.
GeneTreeiENSGT00550000074964.
HOGENOMiHOG000223988.
HOVERGENiHBG105551.
InParanoidiQ9ULC4.
KOiK07575.
OMAiRGSNIMC.
OrthoDBiEOG091G0LZ0.
PhylomeDBiQ9ULC4.
TreeFamiTF315123.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
InterProiIPR016437. MCT-1/Tma20.
IPR002478. PUA.
IPR015947. PUA-like_domain.
IPR004521. Uncharacterised_CHP00451.
[Graphical view]
PANTHERiPTHR22798. PTHR22798. 1 hit.
PfamiPF01472. PUA. 1 hit.
[Graphical view]
PIRSFiPIRSF005067. Tma_RNA-bind_prd. 1 hit.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00451. unchar_dom_2. 1 hit.
PROSITEiPS50890. PUA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ULC4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MFKKFDEKEN VSNCIQLKTS VIKGIKNQLI EQFPGIEPWL NQIMPKKDPV
60 70 80 90 100
KIVRCHEHIE ILTVNGELLF FRQREGPFYP TLRLLHKYPF ILPHQQVDKG
110 120 130 140 150
AIKFVLSGAN IMCPGLTSPG AKLYPAAVDT IVAIMAEGKQ HALCVGVMKM
160 170 180
SAEDIEKVNK GIGIENIHYL NDGLWHMKTY K
Length:181
Mass (Da):20,555
Last modified:May 1, 2000 - v1
Checksum:i2FC00C7A992E24EB
GO
Isoform 2 (identifier: Q9ULC4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MFKKFDEKENVSNCIQLKTSVI → MENYSFLDKE

Show »
Length:169
Mass (Da):19,229
Checksum:i4EC881C03823737A
GO
Isoform 3 (identifier: Q9ULC4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MFKK → MGKGR

Show »
Length:182
Mass (Da):20,550
Checksum:i89F724E4C7657902
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25I → L in AAH95461 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_045632106L → H.Corresponds to variant rs2233110dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0348561 – 22MFKKF…KTSVI → MENYSFLDKE in isoform 2. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_0413521 – 4MFKK → MGKGR in isoform 3. 1 Publication4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034206 mRNA. Translation: BAA86055.1.
AY364258 mRNA. Translation: AAQ76817.1.
AK294834 mRNA. Translation: BAG57943.1.
AK311993 mRNA. Translation: BAG34931.1.
AC011890 Genomic DNA. No translation available.
CH471107 Genomic DNA. Translation: EAX11874.1.
BC001013 mRNA. Translation: AAH01013.1.
BC095461 mRNA. Translation: AAH95461.1.
CCDSiCCDS14601.1. [Q9ULC4-1]
CCDS48160.1. [Q9ULC4-3]
RefSeqiNP_001131026.1. NM_001137554.1. [Q9ULC4-3]
NP_054779.1. NM_014060.2. [Q9ULC4-1]
UniGeneiHs.102696.
Hs.670803.

Genome annotation databases

EnsembliENST00000371315; ENSP00000360365; ENSG00000232119. [Q9ULC4-3]
ENST00000371317; ENSP00000360367; ENSG00000232119. [Q9ULC4-1]
GeneIDi28985.
KEGGihsa:28985.
UCSCiuc004esx.4. human. [Q9ULC4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034206 mRNA. Translation: BAA86055.1.
AY364258 mRNA. Translation: AAQ76817.1.
AK294834 mRNA. Translation: BAG57943.1.
AK311993 mRNA. Translation: BAG34931.1.
AC011890 Genomic DNA. No translation available.
CH471107 Genomic DNA. Translation: EAX11874.1.
BC001013 mRNA. Translation: AAH01013.1.
BC095461 mRNA. Translation: AAH95461.1.
CCDSiCCDS14601.1. [Q9ULC4-1]
CCDS48160.1. [Q9ULC4-3]
RefSeqiNP_001131026.1. NM_001137554.1. [Q9ULC4-3]
NP_054779.1. NM_014060.2. [Q9ULC4-1]
UniGeneiHs.102696.
Hs.670803.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3R90X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L1-181[»]
ProteinModelPortaliQ9ULC4.
SMRiQ9ULC4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118806. 37 interactors.
IntActiQ9ULC4. 5 interactors.
MINTiMINT-1405141.
STRINGi9606.ENSP00000360365.

PTM databases

iPTMnetiQ9ULC4.
PhosphoSitePlusiQ9ULC4.

Polymorphism and mutation databases

BioMutaiMCTS1.
DMDMi74735052.

Proteomic databases

EPDiQ9ULC4.
PaxDbiQ9ULC4.
PeptideAtlasiQ9ULC4.
PRIDEiQ9ULC4.

Protocols and materials databases

DNASUi28985.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371315; ENSP00000360365; ENSG00000232119. [Q9ULC4-3]
ENST00000371317; ENSP00000360367; ENSG00000232119. [Q9ULC4-1]
GeneIDi28985.
KEGGihsa:28985.
UCSCiuc004esx.4. human. [Q9ULC4-1]

Organism-specific databases

CTDi28985.
DisGeNETi28985.
GeneCardsiMCTS1.
HGNCiHGNC:23357. MCTS1.
HPAiHPA001045.
MIMi300587. gene.
neXtProtiNX_Q9ULC4.
OpenTargetsiENSG00000232119.
PharmGKBiPA128394649.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2523. Eukaryota.
COG2016. LUCA.
GeneTreeiENSGT00550000074964.
HOGENOMiHOG000223988.
HOVERGENiHBG105551.
InParanoidiQ9ULC4.
KOiK07575.
OMAiRGSNIMC.
OrthoDBiEOG091G0LZ0.
PhylomeDBiQ9ULC4.
TreeFamiTF315123.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101898-MONOMER.

Miscellaneous databases

GenomeRNAii28985.
PROiQ9ULC4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000232119.
CleanExiHS_MCTS1.
GenevisibleiQ9ULC4. HS.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
InterProiIPR016437. MCT-1/Tma20.
IPR002478. PUA.
IPR015947. PUA-like_domain.
IPR004521. Uncharacterised_CHP00451.
[Graphical view]
PANTHERiPTHR22798. PTHR22798. 1 hit.
PfamiPF01472. PUA. 1 hit.
[Graphical view]
PIRSFiPIRSF005067. Tma_RNA-bind_prd. 1 hit.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00451. unchar_dom_2. 1 hit.
PROSITEiPS50890. PUA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCTS1_HUMAN
AccessioniPrimary (citable) accession number: Q9ULC4
Secondary accession number(s): B4DGY2, Q502X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 136 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 X
    Human chromosome X: 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

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.