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Q6I9Y2

- THOC7_HUMAN

UniProt

Q6I9Y2 - THOC7_HUMAN

Protein

THO complex subunit 7 homolog

Gene

THOC7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 3 (05 May 2009)
      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.5 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. mRNA export from nucleus Source: UniProtKB
    2. mRNA processing Source: UniProtKB-KW
    3. RNA splicing Source: UniProtKB-KW
    4. viral mRNA export from host cell nucleus Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing, mRNA transport, Transport

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    THO complex subunit 7 homolog
    Alternative name(s):
    Functional spliceosome-associated protein 24
    Short name:
    fSAP24
    Ngg1-interacting factor 3-like protein 1-binding protein 1
    Short name:
    NIF3L1-binding protein 1
    hTREX30
    Gene namesi
    Name:THOC7
    Synonyms:NIF3L1BP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:29874. THOC7.

    Subcellular locationi

    Cytoplasm. Nucleus. Nucleus speckle Curated
    Note: Interaction with THOC5 is required for nuclear localization.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA144596266.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 204203THO complex subunit 7 homologPRO_0000310754Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Modified residuei36 – 361N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ6I9Y2.
    PaxDbiQ6I9Y2.
    PRIDEiQ6I9Y2.

    PTM databases

    PhosphoSiteiQ6I9Y2.

    Expressioni

    Gene expression databases

    BgeeiQ6I9Y2.
    CleanExiHS_THOC7.
    GenevestigatoriQ6I9Y2.

    Organism-specific databases

    HPAiHPA044143.

    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. Interacts with NIF3L1 and THOC5.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    THOC5Q137697EBI-716286,EBI-5280316

    Protein-protein interaction databases

    BioGridi123138. 29 interactions.
    IntActiQ6I9Y2. 7 interactions.
    MINTiMINT-1374910.
    STRINGi9606.ENSP00000295899.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6I9Y2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 13788Interaction with THOC5Add
    BLAST
    Regioni105 – 204100Interaction with NIF3L1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili75 – 194120Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the THOC7 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG298141.
    HOGENOMiHOG000044589.
    HOVERGENiHBG061300.
    InParanoidiQ6I9Y2.
    KOiK13176.
    OMAiLRKKQFH.
    OrthoDBiEOG776SRR.
    PhylomeDBiQ6I9Y2.
    TreeFamiTF319308.

    Family and domain databases

    InterProiIPR008501. THOC7/Mft1.
    [Graphical view]
    PANTHERiPTHR14854. PTHR14854. 1 hit.
    PfamiPF05615. THOC7. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6I9Y2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY    50
    QRMLSTLSQC EFSMGKTLLV YDMNLREMEN YEKIYKEIEC SIAGAHEKIA 100
    ECKKQILQAK RIRKNRQEYD ALAKVIQHHP DRHETLKELE ALGKELEHLS 150
    HIKESVEDKL ELRRKQFHVL LSTIHELQQT LENDEKLSEV EEAQEASMET 200
    DPKP 204
    Length:204
    Mass (Da):23,743
    Last modified:May 5, 2009 - v3
    Checksum:iCB0D2608A23E5BFC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231D → G in BAB15656. (PubMed:14702039)Curated
    Sequence conflicti187 – 1871L → P in CAG33654. 1 PublicationCurated
    Sequence conflicti200 – 2001T → S in BAB15656. (PubMed:14702039)Curated
    Sequence conflicti200 – 2001T → S in CAG33654. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027098 mRNA. Translation: BAB15656.1.
    CR457373 mRNA. Translation: CAG33654.1.
    AC104162 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65418.1.
    BC020599 mRNA. Translation: AAH20599.2.
    BC065012 mRNA. Translation: AAH65012.1.
    CCDSiCCDS2900.1.
    RefSeqiNP_001272333.1. NM_001285404.1.
    NP_079351.2. NM_025075.3.
    UniGeneiHs.288151.

    Genome annotation databases

    EnsembliENST00000295899; ENSP00000295899; ENSG00000163634.
    GeneIDi80145.
    KEGGihsa:80145.
    UCSCiuc003dlt.4. human.

    Polymorphism databases

    DMDMi229462996.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027098 mRNA. Translation: BAB15656.1 .
    CR457373 mRNA. Translation: CAG33654.1 .
    AC104162 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65418.1 .
    BC020599 mRNA. Translation: AAH20599.2 .
    BC065012 mRNA. Translation: AAH65012.1 .
    CCDSi CCDS2900.1.
    RefSeqi NP_001272333.1. NM_001285404.1.
    NP_079351.2. NM_025075.3.
    UniGenei Hs.288151.

    3D structure databases

    ProteinModelPortali Q6I9Y2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123138. 29 interactions.
    IntActi Q6I9Y2. 7 interactions.
    MINTi MINT-1374910.
    STRINGi 9606.ENSP00000295899.

    PTM databases

    PhosphoSitei Q6I9Y2.

    Polymorphism databases

    DMDMi 229462996.

    Proteomic databases

    MaxQBi Q6I9Y2.
    PaxDbi Q6I9Y2.
    PRIDEi Q6I9Y2.

    Protocols and materials databases

    DNASUi 80145.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295899 ; ENSP00000295899 ; ENSG00000163634 .
    GeneIDi 80145.
    KEGGi hsa:80145.
    UCSCi uc003dlt.4. human.

    Organism-specific databases

    CTDi 80145.
    GeneCardsi GC03M063795.
    H-InvDB HIX0003418.
    HGNCi HGNC:29874. THOC7.
    HPAi HPA044143.
    MIMi 611965. gene.
    neXtProti NX_Q6I9Y2.
    PharmGKBi PA144596266.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298141.
    HOGENOMi HOG000044589.
    HOVERGENi HBG061300.
    InParanoidi Q6I9Y2.
    KOi K13176.
    OMAi LRKKQFH.
    OrthoDBi EOG776SRR.
    PhylomeDBi Q6I9Y2.
    TreeFami TF319308.

    Miscellaneous databases

    GenomeRNAii 80145.
    NextBioi 70418.
    PROi Q6I9Y2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6I9Y2.
    CleanExi HS_THOC7.
    Genevestigatori Q6I9Y2.

    Family and domain databases

    InterProi IPR008501. THOC7/Mft1.
    [Graphical view ]
    PANTHERi PTHR14854. PTHR14854. 1 hit.
    Pfami PF05615. THOC7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Small intestine.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Skin and Testis.
    6. "Identification and characterization of NIF3L1 BP1, a novel cytoplasmic interaction partner of the NIF3L1 protein."
      Tascou S., Kang T.W., Trappe R., Engel W., Burfeind P.
      Biochem. Biophys. Res. Commun. 309:440-448(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIF3L1, SUBCELLULAR LOCATION.
    7. "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.
    8. "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.
    9. "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.
    10. "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.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "Nuclear localization of the pre-mRNA associating protein THOC7 depends upon its direct interaction with Fms tyrosine kinase interacting protein (FMIP)."
      El Bounkari O., Guria A., Klebba-Faerber S., Claussen M., Pieler T., Griffiths J.R., Whetton A.D., Koch A., Tamura T.
      FEBS Lett. 583:13-18(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH THOC5.
    13. "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-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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.

    Entry informationi

    Entry nameiTHOC7_HUMAN
    AccessioniPrimary (citable) accession number: Q6I9Y2
    Secondary accession number(s): Q6P1L3, Q8WUF2, Q9H5H0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 80 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3