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Q8R3N6 (THOC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
THO complex subunit 1

Short name=Tho1
Alternative name(s):
Nuclear matrix protein p84
Gene names
Name:Thoc1
Synonyms:Hpr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
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. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation By similarity. Ref.3 Ref.6

Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1 By similarity. Essential for early embryonic development. Required for normal gene expression during postnatal testis development. Ref.3 Ref.6

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. Binds to the hypophosphorylated form of RB1. Interacts with THOC2, THOC5, DDX39B and RNA polymerase II. Ref.4

Subcellular location

Nucleus speckle By similarity. Nucleusnucleoplasm. Nucleus matrix By similarity. Cytoplasm By similarity. Note: Can shuttle between the nucleus and cytoplasm. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase of apoptosis execution By similarity. Ref.3

Developmental stage

Widely expressed during embryonic development. Ref.3

Domain

An intact death domain is needed for apoptosis By similarity.

Post-translational modification

Expression is altered specifically during apoptosis and is accompanied by the appearance of novel forms with smaller apparent molecular mass By similarity.

Polyubiquitinated, leading to proteasomal degradation; probably involves NEDD4 By similarity.

Disruption phenotype

Mice show early embryonic lethality and severely diminished fertility. Ref.3 Ref.6

Sequence similarities

Contains 1 death domain.

Ontologies

Keywords
   Biological processApoptosis
mRNA processing
mRNA splicing
mRNA transport
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
RNA-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA export from nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of isotype switching to IgA isotypes

Inferred from mutant phenotype PubMed 22144908. Source: UniProtKB

positive regulation of DNA-templated transcription, elongation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA recombination

Inferred from sequence or structural similarity. Source: UniProtKB

replication fork processing

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral mRNA export from host cell nucleus

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentTHO complex part of transcription export complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 24315442. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657THO complex subunit 1
PRO_0000072521

Regions

Domain570 – 65384Death
Motif414 – 43017Nuclear localization signal By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21Phosphoserine By similarity
Modified residue1331N6-acetyllysine By similarity
Modified residue3001N6-acetyllysine By similarity
Modified residue5601Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8R3N6 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E4235E395B5A82BC

FASTA65775,436
        10         20         30         40         50         60 
MSPTPALFSL PEARTRFTKS TREALNNKNI KPLLTAFSQL PGSENEKKCT LDQAFRGVLE 

        70         80         90        100        110        120 
EEIINHSACE NVLAIISLAI GGVTESVCTA STPFVLLGDV LDCLPLDQCD TIFTFVEKNV 

       130        140        150        160        170        180 
ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ 

       190        200        210        220        230        240 
FNLENVTVFN TNEQESTLGQ KHTEDREEGM DVEEGEMGDD EAPTTCSIPI DYNLYRKFWS 

       250        260        270        280        290        300 
LQDYFRNPVQ CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK 

       310        320        330        340        350        360 
FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS LWIEDTTKSV 

       370        380        390        400        410        420 
YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV KERASDTKPT RVVRKRAAPE 

       430        440        450        460        470        480 
DFLGKGPNKK ILIGNEELTR LWNLCPDNME ACKSETREYM PTLEEFFEEA IEQADPENMV 

       490        500        510        520        530        540 
ESEYKAVNNS NYGWRALRLL ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI 

       550        560        570        580        590        600 
KTGEDEDEED NDALLKENES PDVRRDKPIT GEQIESFANK LGEQWKILAP YLEIKDSDIR 

       610        620        630        640        650 
QIECDSEDMK MRAKQLLVAW QDQEGVHATT DNLISALNKS GLSDLAESLT NDTETNS 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Head and Olfactory bulb.
[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].
Strain: Czech II.
Tissue: Mammary tumor.
[3]"Thoc1/Hpr1/p84 is essential for early embryonic development in the mouse."
Wang X., Chang Y., Li Y., Zhang X., Goodrich D.W.
Mol. Cell. Biol. 26:4362-4367(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[4]"FMIP controls the adipocyte lineage commitment of C2C12 cells by downmodulation of C/EBP alpha."
Mancini A., El Bounkari O., Norrenbrock A.-F., Scherr M., Schaefer D., Eder M., Banham A.H., Pulford K., Lyne L., Whetton A.D., Tamura T.
Oncogene 26:1020-1027(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THOC5.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Thoc1 deficiency compromises gene expression necessary for normal testis development in the mouse."
Wang X., Chinnam M., Wang J., Wang Y., Zhang X., Marcon E., Moens P., Goodrich D.W.
Mol. Cell. Biol. 29:2794-2803(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK031785 mRNA. Translation: BAC27548.1.
AK032200 mRNA. Translation: BAC27754.1.
AK042867 mRNA. Translation: BAC31387.2.
BC024951 mRNA. Translation: AAH24951.1.
CCDSCCDS37733.1.
RefSeqNP_705780.1. NM_153552.3.
UniGeneMm.219648.
Mm.329277.

3D structure databases

ProteinModelPortalQ8R3N6.
SMRQ8R3N6. Positions 558-657.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8R3N6. 1 interaction.
MINTMINT-4137684.

PTM databases

PhosphoSiteQ8R3N6.

Proteomic databases

MaxQBQ8R3N6.
PaxDbQ8R3N6.
PRIDEQ8R3N6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025137; ENSMUSP00000025137; ENSMUSG00000024287.
GeneID225160.
KEGGmmu:225160.
UCSCuc008eal.1. mouse.

Organism-specific databases

CTD9984.
MGIMGI:1919668. Thoc1.

Phylogenomic databases

eggNOGNOG275387.
GeneTreeENSGT00390000016232.
HOGENOMHOG000008123.
HOVERGENHBG060294.
InParanoidQ8R3N6.
KOK12878.
OMAACKSETR.
OrthoDBEOG7R831Q.
PhylomeDBQ8R3N6.
TreeFamTF314796.

Gene expression databases

ArrayExpressQ8R3N6.
BgeeQ8R3N6.
CleanExMM_THOC1.
GenevestigatorQ8R3N6.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR021861. THO_THOC1.
[Graphical view]
PfamPF00531. Death. 1 hit.
PF11957. efThoc1. 1 hit.
[Graphical view]
SMARTSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio377554.
PROQ8R3N6.
SOURCESearch...

Entry information

Entry nameTHOC1_MOUSE
AccessionPrimary (citable) accession number: Q8R3N6
Secondary accession number(s): Q8BWD5, Q8BXY3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot