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Q8R3N6

- THOC1_MOUSE

UniProt

Q8R3N6 - THOC1_MOUSE

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Protein
THO complex subunit 1
Gene
Thoc1, Hpr1
Organism
Mus musculus (Mouse)
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. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation By similarity.2 Publications
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.2 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW
  3. protein binding Source: MGI

GO - Biological processi

  1. RNA splicing Source: UniProtKB-KW
  2. apoptotic process Source: UniProtKB-KW
  3. mRNA export from nucleus Source: UniProtKB
  4. mRNA processing Source: UniProtKB-KW
  5. negative regulation of DNA damage checkpoint Source: UniProtKB
  6. negative regulation of isotype switching to IgA isotypes Source: UniProtKB
  7. positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  8. regulation of DNA recombination Source: UniProtKB
  9. replication fork processing Source: UniProtKB
  10. signal transduction Source: InterPro
  11. transcription, DNA-templated Source: UniProtKB-KW
  12. viral mRNA export from host cell nucleus Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Apoptosis, mRNA processing, mRNA splicing, mRNA transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
THO complex subunit 1
Short name:
Tho1
Alternative name(s):
Nuclear matrix protein p84
Gene namesi
Name:Thoc1
Synonyms:Hpr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1919668. Thoc1.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. THO complex part of transcription export complex Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
  3. nuclear matrix Source: UniProtKB-SubCell
  4. nuclear speck Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice show early embryonic lethality and severely diminished fertility.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657THO complex subunit 1
PRO_0000072521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei2 – 21Phosphoserine By similarity
Modified residuei133 – 1331N6-acetyllysine By similarity
Modified residuei300 – 3001N6-acetyllysine By similarity
Modified residuei560 – 5601Phosphoserine1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8R3N6.
PaxDbiQ8R3N6.
PRIDEiQ8R3N6.

PTM databases

PhosphoSiteiQ8R3N6.

Expressioni

Developmental stagei

Widely expressed during embryonic development.1 Publication

Gene expression databases

ArrayExpressiQ8R3N6.
BgeeiQ8R3N6.
CleanExiMM_THOC1.
GenevestigatoriQ8R3N6.

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. Binds to the hypophosphorylated form of RB1. Interacts with THOC2, THOC5, DDX39B and RNA polymerase II.1 Publication

Protein-protein interaction databases

IntActiQ8R3N6. 1 interaction.
MINTiMINT-4137684.

Structurei

3D structure databases

ProteinModelPortaliQ8R3N6.
SMRiQ8R3N6. Positions 558-657.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini570 – 65384Death
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 43017Nuclear localization signal By similarity
Add
BLAST

Domaini

An intact death domain is needed for apoptosis By similarity.

Sequence similaritiesi

Contains 1 death domain.

Phylogenomic databases

eggNOGiNOG275387.
GeneTreeiENSGT00390000016232.
HOGENOMiHOG000008123.
HOVERGENiHBG060294.
InParanoidiQ8R3N6.
KOiK12878.
OMAiACKSETR.
OrthoDBiEOG7R831Q.
PhylomeDBiQ8R3N6.
TreeFamiTF314796.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR021861. THO_THOC1.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF11957. efThoc1. 1 hit.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R3N6-1 [UniParc]FASTAAdd to Basket

« Hide

MSPTPALFSL PEARTRFTKS TREALNNKNI KPLLTAFSQL PGSENEKKCT    50
LDQAFRGVLE EEIINHSACE NVLAIISLAI GGVTESVCTA STPFVLLGDV 100
LDCLPLDQCD TIFTFVEKNV ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS 150
QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ FNLENVTVFN TNEQESTLGQ 200
KHTEDREEGM DVEEGEMGDD EAPTTCSIPI DYNLYRKFWS LQDYFRNPVQ 250
CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK 300
FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS 350
LWIEDTTKSV YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV 400
KERASDTKPT RVVRKRAAPE DFLGKGPNKK ILIGNEELTR LWNLCPDNME 450
ACKSETREYM PTLEEFFEEA IEQADPENMV ESEYKAVNNS NYGWRALRLL 500
ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI KTGEDEDEED 550
NDALLKENES PDVRRDKPIT GEQIESFANK LGEQWKILAP YLEIKDSDIR 600
QIECDSEDMK MRAKQLLVAW QDQEGVHATT DNLISALNKS GLSDLAESLT 650
NDTETNS 657
Length:657
Mass (Da):75,436
Last modified:June 1, 2002 - v1
Checksum:iE4235E395B5A82BC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK031785 mRNA. Translation: BAC27548.1.
AK032200 mRNA. Translation: BAC27754.1.
AK042867 mRNA. Translation: BAC31387.2.
BC024951 mRNA. Translation: AAH24951.1.
CCDSiCCDS37733.1.
RefSeqiNP_705780.1. NM_153552.3.
UniGeneiMm.219648.
Mm.329277.

Genome annotation databases

EnsembliENSMUST00000025137; ENSMUSP00000025137; ENSMUSG00000024287.
GeneIDi225160.
KEGGimmu:225160.
UCSCiuc008eal.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK031785 mRNA. Translation: BAC27548.1 .
AK032200 mRNA. Translation: BAC27754.1 .
AK042867 mRNA. Translation: BAC31387.2 .
BC024951 mRNA. Translation: AAH24951.1 .
CCDSi CCDS37733.1.
RefSeqi NP_705780.1. NM_153552.3.
UniGenei Mm.219648.
Mm.329277.

3D structure databases

ProteinModelPortali Q8R3N6.
SMRi Q8R3N6. Positions 558-657.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8R3N6. 1 interaction.
MINTi MINT-4137684.

PTM databases

PhosphoSitei Q8R3N6.

Proteomic databases

MaxQBi Q8R3N6.
PaxDbi Q8R3N6.
PRIDEi Q8R3N6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025137 ; ENSMUSP00000025137 ; ENSMUSG00000024287 .
GeneIDi 225160.
KEGGi mmu:225160.
UCSCi uc008eal.1. mouse.

Organism-specific databases

CTDi 9984.
MGIi MGI:1919668. Thoc1.

Phylogenomic databases

eggNOGi NOG275387.
GeneTreei ENSGT00390000016232.
HOGENOMi HOG000008123.
HOVERGENi HBG060294.
InParanoidi Q8R3N6.
KOi K12878.
OMAi ACKSETR.
OrthoDBi EOG7R831Q.
PhylomeDBi Q8R3N6.
TreeFami TF314796.

Miscellaneous databases

NextBioi 377554.
PROi Q8R3N6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8R3N6.
Bgeei Q8R3N6.
CleanExi MM_THOC1.
Genevestigatori Q8R3N6.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
InterProi IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR021861. THO_THOC1.
[Graphical view ]
Pfami PF00531. Death. 1 hit.
PF11957. efThoc1. 1 hit.
[Graphical view ]
SMARTi SM00005. DEATH. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiTHOC1_MOUSE
AccessioniPrimary (citable) accession number: Q8R3N6
Secondary accession number(s): Q8BWD5, Q8BXY3
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi