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Q9ULC4

- MCTS1_HUMAN

UniProt

Q9ULC4 - MCTS1_HUMAN

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Protein

Malignant T-cell-amplified sequence 1

Gene

MCTS1

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

Functioni

Anti-oncogene that play 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

  1. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cellular response to DNA damage stimulus Source: UniProtKB-KW
  3. formation of translation preinitiation complex Source: UniProtKB
  4. IRES-dependent translational initiation Source: UniProtKB
  5. positive regulation of cell proliferation Source: ProtInc
  6. regulation of growth Source: UniProtKB-KW
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. ribosome disassembly Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

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

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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:23357. MCTS1.

Subcellular locationi

Cytoplasm 2 Publications
Note: Nuclear relocalization after DNA damage.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811T → A: No phosphorylation by MAPK1; decreased stability of MCTS1 protein; Significant cell growth reduction. 1 Publication
Mutagenesisi118 – 1181S → A: No phosphorylation by CDK1; No cell growth alteration. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA128394649.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Malignant T-cell-amplified sequence 1PRO_0000344786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811Phosphothreonine; by MAPK1 and MAPK31 Publication
Modified residuei118 – 1181Phosphoserine; by CDK11 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ULC4.
PaxDbiQ9ULC4.
PeptideAtlasiQ9ULC4.
PRIDEiQ9ULC4.

PTM databases

PhosphoSiteiQ9ULC4.

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

BgeeiQ9ULC4.
CleanExiHS_MCTS1.
GenevestigatoriQ9ULC4.

Organism-specific databases

HPAiHPA001045.

Interactioni

Subunit structurei

Interacts (via PUA domain) with DENR.1 Publication

Protein-protein interaction databases

BioGridi118806. 27 interactions.
IntActiQ9ULC4. 1 interaction.
MINTiMINT-1405141.
STRINGi9606.ENSP00000360365.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104Combined sources
Beta strandi11 – 166Combined sources
Helixi19 – 3214Combined sources
Helixi34 – 396Combined sources
Helixi40 – 434Combined sources
Beta strandi50 – 556Combined sources
Helixi56 – 583Combined sources
Beta strandi59 – 646Combined sources
Beta strandi67 – 737Combined sources
Helixi82 – 876Combined sources
Helixi89 – 913Combined sources
Beta strandi94 – 974Combined sources
Helixi99 – 1013Combined sources
Helixi102 – 1054Combined sources
Turni106 – 1083Combined sources
Helixi114 – 1174Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi143 – 1508Combined sources
Helixi152 – 1587Combined sources
Beta strandi161 – 1699Combined sources
Helixi173 – 1775Combined sources
Beta strandi179 – 1813Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R90X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L1-181[»]
ProteinModelPortaliQ9ULC4.
SMRiQ9ULC4. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 17180PUAPROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG2016.
GeneTreeiENSGT00550000074964.
HOGENOMiHOG000223988.
HOVERGENiHBG105551.
InParanoidiQ9ULC4.
KOiK07575.
OMAiGSNIMCP.
OrthoDBiEOG7S7SG1.
PhylomeDBiQ9ULC4.
TreeFamiTF315123.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
InterProiIPR002478. PUA.
IPR015947. PUA-like_domain.
IPR016437. Transl_RNA-bd_prd.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251I → L in AAH95461. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061L → H.
Corresponds to variant rs2233110 [ dbSNP | Ensembl ].
VAR_045632

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222MFKKF…KTSVI → MENYSFLDKE in isoform 2. 1 PublicationVSP_034856Add
BLAST
Alternative sequencei1 – 44MFKK → MGKGR in isoform 3. 1 PublicationVSP_041352

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [Q9ULC4-1]
uc011mub.2. human. [Q9ULC4-3]
uc022cdn.1. human. [Q9ULC4-2]

Polymorphism databases

DMDMi74735052.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14601.1. [Q9ULC4-1 ]
CCDS48160.1. [Q9ULC4-3 ]
RefSeqi NP_001131026.1. NM_001137554.1. [Q9ULC4-3 ]
NP_054779.1. NM_014060.2. [Q9ULC4-1 ]
UniGenei Hs.102696.
Hs.670803.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3R90 X-ray 1.70 A/B/C/D/E/F/G/H/I/J/K/L 1-181 [» ]
ProteinModelPortali Q9ULC4.
SMRi Q9ULC4. Positions 1-181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118806. 27 interactions.
IntActi Q9ULC4. 1 interaction.
MINTi MINT-1405141.
STRINGi 9606.ENSP00000360365.

PTM databases

PhosphoSitei Q9ULC4.

Polymorphism databases

DMDMi 74735052.

Proteomic databases

MaxQBi Q9ULC4.
PaxDbi Q9ULC4.
PeptideAtlasi Q9ULC4.
PRIDEi Q9ULC4.

Protocols and materials databases

DNASUi 28985.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371315 ; ENSP00000360365 ; ENSG00000232119 . [Q9ULC4-3 ]
ENST00000371317 ; ENSP00000360367 ; ENSG00000232119 . [Q9ULC4-1 ]
GeneIDi 28985.
KEGGi hsa:28985.
UCSCi uc004esx.3. human. [Q9ULC4-1 ]
uc011mub.2. human. [Q9ULC4-3 ]
uc022cdn.1. human. [Q9ULC4-2 ]

Organism-specific databases

CTDi 28985.
GeneCardsi GC0XP119727.
HGNCi HGNC:23357. MCTS1.
HPAi HPA001045.
MIMi 300587. gene.
neXtProti NX_Q9ULC4.
PharmGKBi PA128394649.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2016.
GeneTreei ENSGT00550000074964.
HOGENOMi HOG000223988.
HOVERGENi HBG105551.
InParanoidi Q9ULC4.
KOi K07575.
OMAi GSNIMCP.
OrthoDBi EOG7S7SG1.
PhylomeDBi Q9ULC4.
TreeFami TF315123.

Miscellaneous databases

GenomeRNAii 28985.
NextBioi 51887.
PROi Q9ULC4.
SOURCEi Search...

Gene expression databases

Bgeei Q9ULC4.
CleanExi HS_MCTS1.
Genevestigatori Q9ULC4.

Family and domain databases

Gene3Di 2.30.130.10. 1 hit.
InterProi IPR002478. PUA.
IPR015947. PUA-like_domain.
IPR016437. Transl_RNA-bd_prd.
IPR004521. Uncharacterised_CHP00451.
[Graphical view ]
PANTHERi PTHR22798. PTHR22798. 1 hit.
Pfami PF01472. PUA. 1 hit.
[Graphical view ]
PIRSFi PIRSF005067. Tma_RNA-bind_prd. 1 hit.
SMARTi SM00359. PUA. 1 hit.
[Graphical view ]
SUPFAMi SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR00451. unchar_dom_2. 1 hit.
PROSITEi PS50890. PUA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel candidate oncogene, MCT-1, is involved in cell cycle progression."
    Prosniak M., Dierov J., Okami K., Tilton B., Jameson B., Sawaya B.E., Gartenhaus R.B.
    Cancer Res. 58:4233-4237(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
    Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
    BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Brain.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2).
    Tissue: Chondrosarcoma and Eye.
  7. "Increased G1 cyclin/cdk activity in cells overexpressing the candidate oncogene, MCT-1."
    Dierov J., Prosniak M., Gallia G., Gartenhaus R.B.
    J. Cell. Biochem. 74:544-550(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Expression and stabilization of the MCT-1 protein by DNA damaging agents."
    Herbert G.B., Shi B., Gartenhaus R.B.
    Oncogene 20:6777-6783(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  9. "Expression of the candidate MCT-1 oncogene in B- and T-cell lymphoid malignancies."
    Shi B., Hsu H.-L., Evens A.M., Gordon L.I., Gartenhaus R.B.
    Blood 102:297-302(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "MCT-1 oncogene contributes to increased in vivo tumorigenicity of MCF7 cells by promotion of angiogenesis and inhibition of apoptosis."
    Levenson A.S., Thurn K.E., Simons L.A., Veliceasa D., Jarrett J., Osipo C., Jordan V.C., Volpert O.V., Satcher R.L. Jr., Gartenhaus R.B.
    Cancer Res. 65:10651-10656(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The MCT-1 oncogene product impairs cell cycle checkpoint control and transforms human mammary epithelial cells."
    Hsu H.-L., Shi B., Gartenhaus R.B.
    Oncogene 24:4956-4964(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "MCT-1 protein interacts with the cap complex and modulates messenger RNA translational profiles."
    Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M., Bachman K.E., He H., Gartenhaus R.B.
    Cancer Res. 66:8994-9001(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN PUA, INTERACTION WITH DENR.
  13. "MCT-1 oncogene downregulates p53 and destabilizes genome structure in the response to DNA double-strand damage."
    Hsu H.-L., Choy C.O., Kasiappan R., Shih H.-J., Sawyer J.R., Shu C.-L., Chu K.-L., Chen Y.-R., Hsu H.-F., Gartenhaus R.B.
    DNA Repair 6:1319-1332(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Phosphorylation of MCT-1 by p44/42 MAPK is required for its stabilization in response to DNA damage."
    Nandi S., Reinert L.S., Hachem A., Mazan-Mamczarz K., Hagner P., He H., Gartenhaus R.B.
    Oncogene 26:2283-2289(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-81 AND SER-118, MUTAGENESIS OF THR-81 AND SER-118.
  15. "Activities of ligatin and MCT-1/DENR in eukaryotic translation initiation and ribosomal recycling."
    Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U., Pestova T.V.
    Genes Dev. 24:1787-1801(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: October 29, 2014
This is version 119 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

External Data

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