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Q6I9Y2

- THOC7_HUMAN

UniProt

Q6I9Y2 - THOC7_HUMAN

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Protein
THO complex subunit 7 homolog
Gene
THOC7, NIF3L1BP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

GO - Biological processi

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

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 Inferred
Note: Interaction with THOC5 is required for nuclear localization.2 Publications

GO - Cellular componenti

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

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 homolog
PRO_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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 13788Interaction with THOC5
Add
BLAST
Regioni105 – 204100Interaction with NIF3L1
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili75 – 194120 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the THOC7 family.

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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 79 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

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