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Q8R3N6

- THOC1_MOUSE

UniProt

Q8R3N6 - THOC1_MOUSE

Protein

THO complex subunit 1

Gene

Thoc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation By similarity.By similarity
    Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1 By similarity. Essential for early embryonic development. Required for normal gene expression during postnatal testis development.By similarity2 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. mRNA export from nucleus Source: UniProtKB
    3. mRNA processing Source: UniProtKB-KW
    4. negative regulation of DNA damage checkpoint Source: UniProtKB
    5. negative regulation of isotype switching to IgA isotypes Source: UniProtKB
    6. positive regulation of DNA-templated transcription, elongation Source: UniProtKB
    7. regulation of DNA recombination Source: UniProtKB
    8. replication fork processing Source: UniProtKB
    9. RNA splicing Source: UniProtKB-KW
    10. signal transduction Source: InterPro
    11. transcription, DNA-templated Source: UniProtKB-KW
    12. viral mRNA export from host cell nucleus Source: Ensembl

    Keywords - Biological processi

    Apoptosis, mRNA processing, mRNA splicing, mRNA transport, Transcription, Transcription regulation, Transport

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    THO complex subunit 1
    Short name:
    Tho1
    Alternative name(s):
    Nuclear matrix protein p84
    Gene namesi
    Name:Thoc1
    Synonyms:Hpr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1919668. Thoc1.

    Subcellular locationi

    Nucleus speckle By similarity. Nucleusnucleoplasm 1 Publication. Nucleus matrix By similarity. Cytoplasm By similarity
    Note: Can shuttle between the nucleus and cytoplasm. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase of apoptosis execution By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear matrix Source: UniProtKB-SubCell
    3. nuclear speck Source: UniProtKB-SubCell
    4. THO complex part of transcription export complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice show early embryonic lethality and severely diminished fertility.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 657657THO complex subunit 1PRO_0000072521Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei133 – 1331N6-acetyllysineBy similarity
    Modified residuei300 – 3001N6-acetyllysineBy similarity
    Modified residuei560 – 5601Phosphoserine1 Publication

    Post-translational modificationi

    Expression is altered specifically during apoptosis and is accompanied by the appearance of novel forms with smaller apparent molecular mass.By similarity
    Polyubiquitinated, leading to proteasomal degradation; probably involves NEDD4.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8R3N6.
    PaxDbiQ8R3N6.
    PRIDEiQ8R3N6.

    PTM databases

    PhosphoSiteiQ8R3N6.

    Expressioni

    Developmental stagei

    Widely expressed during embryonic development.1 Publication

    Gene expression databases

    ArrayExpressiQ8R3N6.
    BgeeiQ8R3N6.
    CleanExiMM_THOC1.
    GenevestigatoriQ8R3N6.

    Interactioni

    Subunit structurei

    Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. Binds to the hypophosphorylated form of RB1. Interacts with THOC2, THOC5, DDX39B and RNA polymerase II.1 Publication

    Protein-protein interaction databases

    IntActiQ8R3N6. 1 interaction.
    MINTiMINT-4137684.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R3N6.
    SMRiQ8R3N6. Positions 558-657.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini570 – 65384DeathPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi414 – 43017Nuclear localization signalBy similarityAdd
    BLAST

    Domaini

    An intact death domain is needed for apoptosis.By similarity

    Sequence similaritiesi

    Contains 1 death domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG275387.
    GeneTreeiENSGT00390000016232.
    HOGENOMiHOG000008123.
    HOVERGENiHBG060294.
    InParanoidiQ8R3N6.
    KOiK12878.
    OMAiACKSETR.
    OrthoDBiEOG7R831Q.
    PhylomeDBiQ8R3N6.
    TreeFamiTF314796.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR021861. THO_THOC1.
    [Graphical view]
    PfamiPF00531. Death. 1 hit.
    PF11957. efThoc1. 1 hit.
    [Graphical view]
    SMARTiSM00005. DEATH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8R3N6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPTPALFSL PEARTRFTKS TREALNNKNI KPLLTAFSQL PGSENEKKCT    50
    LDQAFRGVLE EEIINHSACE NVLAIISLAI GGVTESVCTA STPFVLLGDV 100
    LDCLPLDQCD TIFTFVEKNV ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS 150
    QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ FNLENVTVFN TNEQESTLGQ 200
    KHTEDREEGM DVEEGEMGDD EAPTTCSIPI DYNLYRKFWS LQDYFRNPVQ 250
    CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK 300
    FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS 350
    LWIEDTTKSV YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV 400
    KERASDTKPT RVVRKRAAPE DFLGKGPNKK ILIGNEELTR LWNLCPDNME 450
    ACKSETREYM PTLEEFFEEA IEQADPENMV ESEYKAVNNS NYGWRALRLL 500
    ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI KTGEDEDEED 550
    NDALLKENES PDVRRDKPIT GEQIESFANK LGEQWKILAP YLEIKDSDIR 600
    QIECDSEDMK MRAKQLLVAW QDQEGVHATT DNLISALNKS GLSDLAESLT 650
    NDTETNS 657
    Length:657
    Mass (Da):75,436
    Last modified:June 1, 2002 - v1
    Checksum:iE4235E395B5A82BC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK031785 mRNA. Translation: BAC27548.1.
    AK032200 mRNA. Translation: BAC27754.1.
    AK042867 mRNA. Translation: BAC31387.2.
    BC024951 mRNA. Translation: AAH24951.1.
    CCDSiCCDS37733.1.
    RefSeqiNP_705780.1. NM_153552.3.
    UniGeneiMm.219648.
    Mm.329277.

    Genome annotation databases

    EnsembliENSMUST00000025137; ENSMUSP00000025137; ENSMUSG00000024287.
    GeneIDi225160.
    KEGGimmu:225160.
    UCSCiuc008eal.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK031785 mRNA. Translation: BAC27548.1 .
    AK032200 mRNA. Translation: BAC27754.1 .
    AK042867 mRNA. Translation: BAC31387.2 .
    BC024951 mRNA. Translation: AAH24951.1 .
    CCDSi CCDS37733.1.
    RefSeqi NP_705780.1. NM_153552.3.
    UniGenei Mm.219648.
    Mm.329277.

    3D structure databases

    ProteinModelPortali Q8R3N6.
    SMRi Q8R3N6. Positions 558-657.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8R3N6. 1 interaction.
    MINTi MINT-4137684.

    PTM databases

    PhosphoSitei Q8R3N6.

    Proteomic databases

    MaxQBi Q8R3N6.
    PaxDbi Q8R3N6.
    PRIDEi Q8R3N6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025137 ; ENSMUSP00000025137 ; ENSMUSG00000024287 .
    GeneIDi 225160.
    KEGGi mmu:225160.
    UCSCi uc008eal.1. mouse.

    Organism-specific databases

    CTDi 9984.
    MGIi MGI:1919668. Thoc1.

    Phylogenomic databases

    eggNOGi NOG275387.
    GeneTreei ENSGT00390000016232.
    HOGENOMi HOG000008123.
    HOVERGENi HBG060294.
    InParanoidi Q8R3N6.
    KOi K12878.
    OMAi ACKSETR.
    OrthoDBi EOG7R831Q.
    PhylomeDBi Q8R3N6.
    TreeFami TF314796.

    Miscellaneous databases

    NextBioi 377554.
    PROi Q8R3N6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8R3N6.
    Bgeei Q8R3N6.
    CleanExi MM_THOC1.
    Genevestigatori Q8R3N6.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    InterProi IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR021861. THO_THOC1.
    [Graphical view ]
    Pfami PF00531. Death. 1 hit.
    PF11957. efThoc1. 1 hit.
    [Graphical view ]
    SMARTi SM00005. DEATH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum, Head and Olfactory bulb.
    2. "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].
      Strain: Czech II.
      Tissue: Mammary tumor.
    3. "Thoc1/Hpr1/p84 is essential for early embryonic development in the mouse."
      Wang X., Chang Y., Li Y., Zhang X., Goodrich D.W.
      Mol. Cell. Biol. 26:4362-4367(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    4. "FMIP controls the adipocyte lineage commitment of C2C12 cells by downmodulation of C/EBP alpha."
      Mancini A., El Bounkari O., Norrenbrock A.-F., Scherr M., Schaefer D., Eder M., Banham A.H., Pulford K., Lyne L., Whetton A.D., Tamura T.
      Oncogene 26:1020-1027(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THOC5.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Thoc1 deficiency compromises gene expression necessary for normal testis development in the mouse."
      Wang X., Chinnam M., Wang J., Wang Y., Zhang X., Marcon E., Moens P., Goodrich D.W.
      Mol. Cell. Biol. 29:2794-2803(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiTHOC1_MOUSE
    AccessioniPrimary (citable) accession number: Q8R3N6
    Secondary accession number(s): Q8BWD5, Q8BXY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3