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Protein

THO complex subunit 7 homolog

Gene

THOC7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.4 Publications
The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production.1 Publication

GO - Molecular functioni

GO - Biological processi

  • mRNA export from nucleus Source: UniProtKB
  • mRNA processing Source: UniProtKB-KW
  • RNA splicing Source: UniProtKB-KW
  • 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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:29874. THOC7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • THO complex Source: UniProtKB
  • THO complex part of transcription export complex Source: UniProtKB
  • transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA144596266.

Polymorphism and mutation databases

DMDMi229462996.

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.
ExpressionAtlasiQ6I9Y2. baseline and differential.
GenevisibleiQ6I9Y2. HS.

Organism-specific databases

HPAiHPA044143.
HPA060806.

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. 35 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 THOC51 PublicationAdd
BLAST
Regioni105 – 204100Interaction with NIF3L11 PublicationAdd
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.
GeneTreeiENSGT00390000002873.
HOGENOMiHOG000044589.
HOVERGENiHBG061300.
InParanoidiQ6I9Y2.
OMAiRKKQFHV.
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

        10         20         30         40         50
MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY
60 70 80 90 100
QRMLSTLSQC EFSMGKTLLV YDMNLREMEN YEKIYKEIEC SIAGAHEKIA
110 120 130 140 150
ECKKQILQAK RIRKNRQEYD ALAKVIQHHP DRHETLKELE ALGKELEHLS
160 170 180 190 200
HIKESVEDKL ELRRKQFHVL LSTIHELQQT LENDEKLSEV EEAQEASMET

DPKP
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 (Ref. 2) Curated
Sequence conflicti200 – 2001T → S in BAB15656 (PubMed:14702039).Curated
Sequence conflicti200 – 2001T → S in CAG33654 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UCSCiuc003dlt.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ6I9Y2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123138. 35 interactions.
IntActiQ6I9Y2. 7 interactions.
MINTiMINT-1374910.
STRINGi9606.ENSP00000295899.

PTM databases

PhosphoSiteiQ6I9Y2.

Polymorphism and mutation databases

DMDMi229462996.

Proteomic databases

MaxQBiQ6I9Y2.
PaxDbiQ6I9Y2.
PRIDEiQ6I9Y2.

Protocols and materials databases

DNASUi80145.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295899; ENSP00000295899; ENSG00000163634.
GeneIDi80145.
UCSCiuc003dlt.4. human.

Organism-specific databases

CTDi80145.
GeneCardsiGC03M063795.
H-InvDBHIX0003418.
HGNCiHGNC:29874. THOC7.
HPAiHPA044143.
HPA060806.
MIMi611965. gene.
neXtProtiNX_Q6I9Y2.
PharmGKBiPA144596266.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG298141.
GeneTreeiENSGT00390000002873.
HOGENOMiHOG000044589.
HOVERGENiHBG061300.
InParanoidiQ6I9Y2.
OMAiRKKQFHV.
OrthoDBiEOG776SRR.
PhylomeDBiQ6I9Y2.
TreeFamiTF319308.

Miscellaneous databases

GenomeRNAii80145.
NextBioi70418.
PROiQ6I9Y2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6I9Y2.
CleanExiHS_THOC7.
ExpressionAtlasiQ6I9Y2. baseline and differential.
GenevisibleiQ6I9Y2. HS.

Family and domain databases

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

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, REGION, 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 22, 2015
This is version 87 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.