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Q96FV9

- THOC1_HUMAN

UniProt

Q96FV9 - THOC1_HUMAN

Protein

THO complex subunit 1

Gene

THOC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation.
    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.

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    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. regulation of DNA-templated transcription, elongation Source: UniProtKB
    9. replication fork processing Source: UniProtKB
    10. RNA processing Source: ProtInc
    11. RNA splicing Source: UniProtKB-KW
    12. signal transduction Source: InterPro
    13. transcription, DNA-templated Source: UniProtKB-KW
    14. viral mRNA export from host cell nucleus Source: UniProtKB

    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
    Short name:
    p84N5
    hTREX84
    Gene namesi
    Name:THOC1
    Synonyms:HPR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:19070. THOC1.

    Subcellular locationi

    Isoform 1 : Nucleus speckle. Nucleusnucleoplasm. Nucleus matrix. Cytoplasm
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. intercellular bridge Source: HPA
    3. nuclear matrix Source: UniProtKB-SubCell
    4. nuclear speck Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB
    6. THO complex Source: UniProtKB
    7. THO complex part of transcription export complex Source: UniProtKB
    8. transcription export complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi617 – 6171L → P: Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. 1 Publication
    Mutagenesisi620 – 6201W → P or R: Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. 1 Publication

    Organism-specific databases

    PharmGKBiPA134887435.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 657657THO complex subunit 1PRO_0000072520Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21Phosphoserine2 Publications
    Modified residuei133 – 1331N6-acetyllysine1 Publication
    Modified residuei300 – 3001N6-acetyllysine1 Publication
    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.
    Polyubiquitinated, leading to proteasomal degradation; probably involves NEDD4.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96FV9.
    PaxDbiQ96FV9.
    PRIDEiQ96FV9.

    PTM databases

    PhosphoSiteiQ96FV9.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expressed in various cancer cell lines. Expressed at very low levels in normal breast epithelial cells and highly expressed in breast tumors. Expression is strongly associated with an aggressive phenotype of breast tumors and expression correlates with tumor size and the metastatic state of the tumor progression.2 Publications

    Inductioni

    Up-regulated during cell proliferation.1 Publication

    Gene expression databases

    ArrayExpressiQ96FV9.
    BgeeiQ96FV9.
    CleanExiHS_THOC1.
    GenevestigatoriQ96FV9.

    Organism-specific databases

    HPAiHPA019096.
    HPA019687.

    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.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    THOC5Q137697EBI-1765605,EBI-5280316

    Protein-protein interaction databases

    BioGridi115305. 37 interactions.
    IntActiQ96FV9. 19 interactions.
    MINTiMINT-4536762.
    STRINGi9606.ENSP00000261600.

    Structurei

    Secondary structure

    1
    657
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi565 – 5673
    Helixi571 – 58111
    Turni582 – 5843
    Helixi585 – 5884
    Turni589 – 5935
    Helixi596 – 60510
    Helixi609 – 62416
    Helixi625 – 6273
    Helixi630 – 63910
    Helixi643 – 6508

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WXPNMR-A561-657[»]
    ProteinModelPortaliQ96FV9.
    SMRiQ96FV9. Positions 558-657.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96FV9.

    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 signal1 PublicationAdd
    BLAST

    Domaini

    An intact death domain is needed for apoptosis.1 Publication

    Sequence similaritiesi

    Contains 1 death domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG275387.
    HOGENOMiHOG000008123.
    HOVERGENiHBG060294.
    InParanoidiQ96FV9.
    KOiK12878.
    OMAiACKSETR.
    OrthoDBiEOG7R831Q.
    PhylomeDBiQ96FV9.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96FV9-1) [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

    MSPTPPLFSL PEARTRFTKS TREALNNKNI KPLLSTFSQV PGSENEKKCT    50
    LDQAFRGILE EEIINHSSCE NVLAIISLAI GGVTEGICTA STPFVLLGDV 100
    LDCLPLDQCD TIFTFVEKNV ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS 150
    QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ FNLENVTVFN TNEQESTLGQ 200
    KHTEDREEGM DVEEGEMGDE EAPTTCSIPI DYNLYRKFWS LQDYFRNPVQ 250
    CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK 300
    FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS 350
    LWIEDTTKSV YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV 400
    KERTSDTKPT RIIRKRTAPE DFLGKGPTKK ILMGNEELTR LWNLCPDNME 450
    ACKSETREHM PTLEEFFEEA IEQADPENMV ENEYKAVNNS NYGWRALRLL 500
    ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI KTGEDEDEED 550
    NDALLKENES PDVRRDKPVT GEQIEVFANK LGEQWKILAP YLEMKDSEIR 600
    QIECDSEDMK MRAKQLLVAW QDQEGVHATP ENLINALNKS GLSDLAESLT 650
    NDNETNS 657
    Length:657
    Mass (Da):75,666
    Last modified:December 1, 2001 - v1
    Checksum:iDB7980BD0F252DAB
    GO
    Isoform 2 (identifier: Q96FV9-2) [UniParc]FASTAAdd to Basket

    Also known as: p84N5s

    The sequence of this isoform differs from the canonical sequence as follows:
         363-377: LLSENPPDGERFSKM → VSSTRNKPMIEKMEI
         378-657: Missing.

    Note: May be due to an intron retention.

    Show »
    Length:377
    Mass (Da):43,359
    Checksum:i313FCF7E19C03FFC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711N → H in AAT81408. (PubMed:15358532)Curated
    Sequence conflicti86 – 861G → A in AAT81408. (PubMed:15358532)Curated
    Sequence conflicti130 – 1301S → A in AAA53571. (PubMed:7525595)Curated
    Sequence conflicti134 – 1341N → S in BAG37293. (PubMed:14702039)Curated
    Sequence conflicti433 – 4331M → T in AAA53571. (PubMed:7525595)Curated
    Sequence conflicti480 – 4801V → A in AAA53571. (PubMed:7525595)Curated
    Sequence conflicti487 – 4871V → M in AAA53571. (PubMed:7525595)Curated
    Sequence conflicti498 – 4981R → K in AAA53571. (PubMed:7525595)Curated
    Sequence conflicti519 – 5191P → Q in AAA53571. (PubMed:7525595)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei363 – 37715LLSEN…RFSKM → VSSTRNKPMIEKMEI in isoform 2. 1 PublicationVSP_038073Add
    BLAST
    Alternative sequencei378 – 657280Missing in isoform 2. 1 PublicationVSP_038074Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36529 mRNA. Translation: AAA53571.1.
    AY573302 mRNA. Translation: AAT81408.1.
    AY573303 mRNA. Translation: AAT81409.1.
    AK314755 mRNA. Translation: BAG37293.1.
    AP000845 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01732.1.
    BC010381 mRNA. Translation: AAH10381.1.
    CCDSiCCDS45820.1. [Q96FV9-1]
    PIRiA53545.
    RefSeqiNP_005122.2. NM_005131.2. [Q96FV9-1]
    UniGeneiHs.712543.

    Genome annotation databases

    EnsembliENST00000261600; ENSP00000261600; ENSG00000079134. [Q96FV9-1]
    GeneIDi9984.
    KEGGihsa:9984.
    UCSCiuc002kkj.4. human. [Q96FV9-1]
    uc002kkl.2. human. [Q96FV9-2]

    Polymorphism databases

    DMDMi37999906.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36529 mRNA. Translation: AAA53571.1 .
    AY573302 mRNA. Translation: AAT81408.1 .
    AY573303 mRNA. Translation: AAT81409.1 .
    AK314755 mRNA. Translation: BAG37293.1 .
    AP000845 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01732.1 .
    BC010381 mRNA. Translation: AAH10381.1 .
    CCDSi CCDS45820.1. [Q96FV9-1 ]
    PIRi A53545.
    RefSeqi NP_005122.2. NM_005131.2. [Q96FV9-1 ]
    UniGenei Hs.712543.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WXP NMR - A 561-657 [» ]
    ProteinModelPortali Q96FV9.
    SMRi Q96FV9. Positions 558-657.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115305. 37 interactions.
    IntActi Q96FV9. 19 interactions.
    MINTi MINT-4536762.
    STRINGi 9606.ENSP00000261600.

    PTM databases

    PhosphoSitei Q96FV9.

    Polymorphism databases

    DMDMi 37999906.

    Proteomic databases

    MaxQBi Q96FV9.
    PaxDbi Q96FV9.
    PRIDEi Q96FV9.

    Protocols and materials databases

    DNASUi 9984.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261600 ; ENSP00000261600 ; ENSG00000079134 . [Q96FV9-1 ]
    GeneIDi 9984.
    KEGGi hsa:9984.
    UCSCi uc002kkj.4. human. [Q96FV9-1 ]
    uc002kkl.2. human. [Q96FV9-2 ]

    Organism-specific databases

    CTDi 9984.
    GeneCardsi GC18M000204.
    HGNCi HGNC:19070. THOC1.
    HPAi HPA019096.
    HPA019687.
    MIMi 606930. gene.
    neXtProti NX_Q96FV9.
    PharmGKBi PA134887435.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG275387.
    HOGENOMi HOG000008123.
    HOVERGENi HBG060294.
    InParanoidi Q96FV9.
    KOi K12878.
    OMAi ACKSETR.
    OrthoDBi EOG7R831Q.
    PhylomeDBi Q96FV9.
    TreeFami TF314796.

    Miscellaneous databases

    ChiTaRSi THOC1. human.
    EvolutionaryTracei Q96FV9.
    GeneWikii THOC1.
    GenomeRNAii 9984.
    NextBioi 37696.
    PROi Q96FV9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96FV9.
    Bgeei Q96FV9.
    CleanExi HS_THOC1.
    Genevestigatori Q96FV9.

    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 amino-terminal region of the retinoblastoma gene product binds a novel nuclear matrix protein that co-localizes to centers for RNA processing."
      Durfee T., Mancini M.A., Jones D., Elledge S.J., Lee W.H.
      J. Cell Biol. 127:609-622(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH RB1.
      Tissue: Lymphocyte.
    2. "The death domain protein p84N5, but not the short isoform p84N5s, is cell cycle-regulated and shuttles between the nucleus and the cytoplasm."
      Gasparri F., Sola F., Locatelli G., Muzio M.
      FEBS Lett. 574:13-19(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-86 (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    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] (ISOFORM 1).
      Tissue: Uterus.
    4. 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] (ISOFORM 1).
      Tissue: Bone marrow.
    7. "Apoptosis induced by the nuclear death domain protein p84N5 is inhibited by association with Rb protein."
      Doostzadeh-Cizeron J., Evans R., Yin S., Goodrich D.W.
      Mol. Biol. Cell 10:3251-3261(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PTM, DOMAIN, MUTAGENESIS OF LEU-617 AND TRP-620.
    8. "Apoptosis induced by the nuclear death domain protein p84N5 is associated with caspase-6 and NF-kappa B activation."
      Doostzadeh-Cizeron J., Yin S., Goodrich D.W.
      J. Biol. Chem. 275:25336-25341(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The nuclear death domain protein p84N5 activates a G2/M cell cycle checkpoint prior to the onset of apoptosis."
      Doostzadeh-Cizeron J., Terry N.H., Goodrich D.W.
      J. Biol. Chem. 276:1127-1132(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: FUNCTION, INTERACTION WITH THE TREX COMPLEX.
    11. "Nuclear localization is required for induction of apoptotic cell death by the Rb-associated p84N5 death domain protein."
      Evans R.L., Poe B.S., Goodrich D.W.
      Oncogene 21:4691-4695(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
    12. "Linking transcriptional elongation and messenger RNA export to metastatic breast cancers."
      Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J., Cooch N.S., Godwin A.K., Shiekhattar R.
      Cancer Res. 65:3011-3016(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
    13. "Recruitment of the human TREX complex to mRNA during splicing."
      Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.
      Genes Dev. 19:1512-1517(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE THO AND TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically links RNA polymerase II and RNA processing factors."
      Li Y., Wang X., Zhang X., Goodrich D.W.
      Mol. Cell. Biol. 25:4023-4033(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THOC2; DDX39B AND RNA POLYMERASE II.
    15. "Human mRNA export machinery recruited to the 5' end of mRNA."
      Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.
      Cell 127:1389-1400(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE TREX COMPLEX.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication."
      Boyne J.R., Colgan K.J., Whitehouse A.
      PLoS Pathog. 4:E1000194-E1000194(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE TREX COMPLEX.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133 AND LYS-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Genome instability and transcription elongation impairment in human cells depleted of THO/TREX."
      Dominguez-Sanchez M.S., Barroso S., Gomez-Gonzalez B., Luna R., Aguilera A.
      PLoS Genet. 7:E1002386-E1002386(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Aly and THO are required for assembly of the human TREX complex and association of TREX components with the spliced mRNA."
      Chi B., Wang Q., Wu G., Tan M., Wang L., Shi M., Chang X., Cheng H.
      Nucleic Acids Res. 41:1294-1306(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "The Thoc1 encoded ribonucleoprotein is a substrate for the NEDD4-1 E3 ubiquitin protein ligase."
      Song F., Fan C., Wang X., Goodrich D.W.
      PLoS ONE 8:E57995-E57995(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY NEDD4.
    25. "Solution structure of the death domain of nuclear matrix protein p84."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 561-657.

    Entry informationi

    Entry nameiTHOC1_HUMAN
    AccessioniPrimary (citable) accession number: Q96FV9
    Secondary accession number(s): B2RBP6
    , Q15219, Q64I72, Q64I73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 122 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 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3