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Q6I9Y2 (THOC7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:THOC7
Synonyms:NIF3L1BP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.15

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.12

Subcellular location

Cytoplasm. Nucleus. Nucleus speckle Probable. Note: Interaction with THOC5 is required for nuclear localization. Ref.6 Ref.12

Sequence similarities

Belongs to the THOC7 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

THOC5Q137697EBI-716286,EBI-5280316

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 204203THO complex subunit 7 homolog
PRO_0000310754

Regions

Region50 – 13788Interaction with THOC5
Region105 – 204100Interaction with NIF3L1
Coiled coil75 – 194120 Potential

Amino acid modifications

Modified residue21N-acetylglycine Ref.11
Modified residue361N6-acetyllysine Ref.13

Experimental info

Sequence conflict231D → G in BAB15656. Ref.1
Sequence conflict1871L → P in CAG33654. Ref.2
Sequence conflict2001T → S in BAB15656. Ref.1
Sequence conflict2001T → S in CAG33654. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6I9Y2 [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: CB0D2608A23E5BFC

FASTA20423,743
        10         20         30         40         50         60 
MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY QRMLSTLSQC 

        70         80         90        100        110        120 
EFSMGKTLLV YDMNLREMEN YEKIYKEIEC SIAGAHEKIA ECKKQILQAK RIRKNRQEYD 

       130        140        150        160        170        180 
ALAKVIQHHP DRHETLKELE ALGKELEHLS HIKESVEDKL ELRRKQFHVL LSTIHELQQT 

       190        200 
LENDEKLSEV EEAQEASMET DPKP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2900.1.
RefSeqNP_001272333.1. NM_001285404.1.
NP_079351.2. NM_025075.3.
UniGeneHs.288151.

3D structure databases

ProteinModelPortalQ6I9Y2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123138. 29 interactions.
IntActQ6I9Y2. 7 interactions.
MINTMINT-1374910.
STRING9606.ENSP00000295899.

PTM databases

PhosphoSiteQ6I9Y2.

Polymorphism databases

DMDM229462996.

Proteomic databases

MaxQBQ6I9Y2.
PaxDbQ6I9Y2.
PRIDEQ6I9Y2.

Protocols and materials databases

DNASU80145.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295899; ENSP00000295899; ENSG00000163634.
GeneID80145.
KEGGhsa:80145.
UCSCuc003dlt.4. human.

Organism-specific databases

CTD80145.
GeneCardsGC03M063795.
H-InvDBHIX0003418.
HGNCHGNC:29874. THOC7.
HPAHPA044143.
MIM611965. gene.
neXtProtNX_Q6I9Y2.
PharmGKBPA144596266.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298141.
HOGENOMHOG000044589.
HOVERGENHBG061300.
InParanoidQ6I9Y2.
KOK13176.
OMALRKKQFH.
OrthoDBEOG776SRR.
PhylomeDBQ6I9Y2.
TreeFamTF319308.

Gene expression databases

BgeeQ6I9Y2.
CleanExHS_THOC7.
GenevestigatorQ6I9Y2.

Family and domain databases

InterProIPR008501. THOC7/Mft1.
[Graphical view]
PANTHERPTHR14854. PTHR14854. 1 hit.
PfamPF05615. THOC7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi80145.
NextBio70418.
PROQ6I9Y2.
SOURCESearch...

Entry information

Entry nameTHOC7_HUMAN
AccessionPrimary (citable) accession number: Q6I9Y2
Secondary accession number(s): Q6P1L3, Q8WUF2, Q9H5H0
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM