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Protein

THO complex subunit 3

Gene

THOC3

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 and spliced mRNA. 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

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

Enzyme and pathway databases

SignaLinkiQ96J01.

Names & Taxonomyi

Protein namesi
Recommended name:
THO complex subunit 3
Short name:
Tho3
Alternative name(s):
TEX1 homolog
hTREX45
Gene namesi
Name:THOC3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:19072. THOC3.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134893535.

Polymorphism and mutation databases

DMDMi48474597.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 351350THO complex subunit 3PRO_0000051273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ96J01.
MaxQBiQ96J01.
PaxDbiQ96J01.
PRIDEiQ96J01.

PTM databases

iPTMnetiQ96J01.
PhosphoSiteiQ96J01.

Expressioni

Gene expression databases

BgeeiQ96J01.
CleanExiHS_THOC3.
ExpressionAtlasiQ96J01. baseline and differential.
GenevisibleiQ96J01. HS.

Organism-specific databases

HPAiHPA042764.
HPA044009.
HPA045071.

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.3 Publications

Protein-protein interaction databases

BioGridi124047. 32 interactions.
IntActiQ96J01. 11 interactions.
MINTiMINT-2814144.
STRINGi9606.ENSP00000265097.

Structurei

3D structure databases

ProteinModelPortaliQ96J01.
SMRiQ96J01. Positions 19-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati53 – 9442WD 1Add
BLAST
Repeati97 – 13741WD 2Add
BLAST
Repeati139 – 17840WD 3Add
BLAST
Repeati180 – 22142WD 4Add
BLAST
Repeati222 – 26140WD 5Add
BLAST
Repeati264 – 30340WD 6Add
BLAST

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1407. Eukaryota.
ENOG410XPZJ. LUCA.
GeneTreeiENSGT00750000117536.
HOGENOMiHOG000264781.
HOVERGENiHBG059732.
InParanoidiQ96J01.
KOiK12880.
OMAiYACDDKE.
PhylomeDBiQ96J01.
TreeFamiTF314069.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR024977. Apc4_WD40_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF08662. eIF2A. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96J01-1) [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

        10         20         30         40         50
MAVPAAAMGP SALGQSGPGS MAPWCSVSSG PSRYVLGMQE LFRGHSKTRE
60 70 80 90 100
FLAHSAKVHS VAWSCDGRRL ASGSFDKTAS VFLLEKDRLV KENNYRGHGD
110 120 130 140 150
SVDQLCWHPS NPDLFVTASG DKTIRIWDVR TTKCIATVNT KGENINICWS
160 170 180 190 200
PDGQTIAVGN KDDVVTFIDA KTHRSKAEEQ FKFEVNEISW NNDNNMFFLT
210 220 230 240 250
NGNGCINILS YPELKPVQSI NAHPSNCICI KFDPMGKYFA TGSADALVSL
260 270 280 290 300
WDVDELVCVR CFSRLDWPVR TLSFSHDGKM LASASEDHFI DIAEVETGDK
310 320 330 340 350
LWEVQCESPT FTVAWHPKRP LLAFACDDKD GKYDSSREAG TVKLFGLPND

S
Length:351
Mass (Da):38,772
Last modified:December 1, 2001 - v1
Checksum:i9BA03D9D5571E424
GO
Isoform 2 (identifier: Q96J01-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     299-351: DKLWEVQCES...VKLFGLPNDS → NFMRIYRLSPLAVRTSLVISSLHVTTSPA

Note: No experimental confirmation available.
Show »
Length:327
Mass (Da):36,032
Checksum:iA0975A5DE8E4E830
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei299 – 35153DKLWE…LPNDS → NFMRIYRLSPLAVRTSLVIS SLHVTTSPA in isoform 2. 1 PublicationVSP_056173Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC138965 Genomic DNA. No translation available.
AC139491 Genomic DNA. No translation available.
BC006849 mRNA. Translation: AAH06849.1.
BC066325 mRNA. Translation: AAH66325.1.
BC068499 mRNA. Translation: AAH68499.1.
CCDSiCCDS4397.1. [Q96J01-1]
RefSeqiNP_115737.1. NM_032361.3. [Q96J01-1]
UniGeneiHs.484227.
Hs.535769.
Hs.715943.

Genome annotation databases

EnsembliENST00000265097; ENSP00000265097; ENSG00000051596. [Q96J01-1]
ENST00000513482; ENSP00000422243; ENSG00000051596. [Q96J01-2]
GeneIDi84321.
KEGGihsa:84321.
UCSCiuc003mdg.6. human. [Q96J01-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC138965 Genomic DNA. No translation available.
AC139491 Genomic DNA. No translation available.
BC006849 mRNA. Translation: AAH06849.1.
BC066325 mRNA. Translation: AAH66325.1.
BC068499 mRNA. Translation: AAH68499.1.
CCDSiCCDS4397.1. [Q96J01-1]
RefSeqiNP_115737.1. NM_032361.3. [Q96J01-1]
UniGeneiHs.484227.
Hs.535769.
Hs.715943.

3D structure databases

ProteinModelPortaliQ96J01.
SMRiQ96J01. Positions 19-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124047. 32 interactions.
IntActiQ96J01. 11 interactions.
MINTiMINT-2814144.
STRINGi9606.ENSP00000265097.

PTM databases

iPTMnetiQ96J01.
PhosphoSiteiQ96J01.

Polymorphism and mutation databases

DMDMi48474597.

Proteomic databases

EPDiQ96J01.
MaxQBiQ96J01.
PaxDbiQ96J01.
PRIDEiQ96J01.

Protocols and materials databases

DNASUi84321.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265097; ENSP00000265097; ENSG00000051596. [Q96J01-1]
ENST00000513482; ENSP00000422243; ENSG00000051596. [Q96J01-2]
GeneIDi84321.
KEGGihsa:84321.
UCSCiuc003mdg.6. human. [Q96J01-1]

Organism-specific databases

CTDi84321.
GeneCardsiTHOC3.
HGNCiHGNC:19072. THOC3.
HPAiHPA042764.
HPA044009.
HPA045071.
MIMi606929. gene.
neXtProtiNX_Q96J01.
PharmGKBiPA134893535.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1407. Eukaryota.
ENOG410XPZJ. LUCA.
GeneTreeiENSGT00750000117536.
HOGENOMiHOG000264781.
HOVERGENiHBG059732.
InParanoidiQ96J01.
KOiK12880.
OMAiYACDDKE.
PhylomeDBiQ96J01.
TreeFamiTF314069.

Enzyme and pathway databases

SignaLinkiQ96J01.

Miscellaneous databases

ChiTaRSiTHOC3. human.
GenomeRNAii84321.
NextBioi74048.
PROiQ96J01.
SOURCEiSearch...

Gene expression databases

BgeeiQ96J01.
CleanExiHS_THOC3.
ExpressionAtlasiQ96J01. baseline and differential.
GenevisibleiQ96J01. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR024977. Apc4_WD40_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF08662. eIF2A. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Placenta.
  3. Cited for: FUNCTION, INTERACTION WITH THE TREX COMPLEX.
  4. "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.
  5. "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 TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "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.
  7. "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.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION IN THE THO COMLEX.

Entry informationi

Entry nameiTHOC3_HUMAN
AccessioniPrimary (citable) accession number: Q96J01
Secondary accession number(s): Q6NZ53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 124 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

Caution

There are two almost identical copies of this gene on chromosome 5q35. One copy is frameshifted and unlikely to encode a functional protein.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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 one 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.