Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9ULC4

- MCTS1_HUMAN

UniProt

Q9ULC4 - MCTS1_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. RNA binding Source: InterPro

    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

    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

    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. 25 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 – 104
    Beta strandi11 – 166
    Helixi19 – 3214
    Helixi34 – 396
    Helixi40 – 434
    Beta strandi50 – 556
    Helixi56 – 583
    Beta strandi59 – 646
    Beta strandi67 – 737
    Helixi82 – 876
    Helixi89 – 913
    Beta strandi94 – 974
    Helixi99 – 1013
    Helixi102 – 1054
    Turni106 – 1083
    Helixi114 – 1174
    Beta strandi131 – 1366
    Beta strandi143 – 1508
    Helixi152 – 1587
    Beta strandi161 – 1699
    Helixi173 – 1775
    Beta strandi179 – 1813

    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.
    HOGENOMiHOG000223988.
    HOVERGENiHBG105551.
    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

    MFKKFDEKEN VSNCIQLKTS VIKGIKNQLI EQFPGIEPWL NQIMPKKDPV    50
    KIVRCHEHIE ILTVNGELLF FRQREGPFYP TLRLLHKYPF ILPHQQVDKG 100
    AIKFVLSGAN IMCPGLTSPG AKLYPAAVDT IVAIMAEGKQ HALCVGVMKM 150
    SAEDIEKVNK GIGIENIHYL NDGLWHMKTY K 181
    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. 25 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.
    HOGENOMi HOG000223988.
    HOVERGENi HBG105551.
    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

    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 1, 2014
    This is version 118 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

    Dasty 3