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Protein

THO complex subunit 1

Gene

Thoc1

Organism
Mus musculus (Mouse)
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. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation (By similarity).By similarity
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.By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

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 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1919668. Thoc1.

Subcellular locationi

  • Nucleus speckle By similarity
  • Nucleusnucleoplasm 1 Publication
  • 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).By similarity

GO - Cellular componenti

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 1PRO_0000072521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei133 – 1331N6-acetyllysineBy similarity
Modified residuei300 – 3001N6-acetyllysineBy 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

BgeeiQ8R3N6.
CleanExiMM_THOC1.
ExpressionAtlasiQ8R3N6. baseline and differential.
GenevisibleiQ8R3N6. MM.

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, DDX39B and RNA polymerase II (By similarity). Interacts with THOC5 (PubMed:16909111). Interacts with LUZP4 (By similarity).By similarity1 Publication

Protein-protein interaction databases

IntActiQ8R3N6. 2 interactions.
MINTiMINT-4137684.
STRINGi10090.ENSMUSP00000025137.

Structurei

3D structure databases

ProteinModelPortaliQ8R3N6.
SMRiQ8R3N6. Positions 558-657.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini570 – 65384DeathPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 43017Nuclear localization signalBy similarityAdd
BLAST

Domaini

An intact death domain is needed for apoptosis.By similarity

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG275387.
GeneTreeiENSGT00390000016232.
HOGENOMiHOG000008123.
HOVERGENiHBG060294.
InParanoidiQ8R3N6.
KOiK12878.
OMAiPTSCSIP.
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

        10         20         30         40         50
MSPTPALFSL PEARTRFTKS TREALNNKNI KPLLTAFSQL PGSENEKKCT
60 70 80 90 100
LDQAFRGVLE EEIINHSACE NVLAIISLAI GGVTESVCTA STPFVLLGDV
110 120 130 140 150
LDCLPLDQCD TIFTFVEKNV ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS
160 170 180 190 200
QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ FNLENVTVFN TNEQESTLGQ
210 220 230 240 250
KHTEDREEGM DVEEGEMGDD EAPTTCSIPI DYNLYRKFWS LQDYFRNPVQ
260 270 280 290 300
CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK
310 320 330 340 350
FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS
360 370 380 390 400
LWIEDTTKSV YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV
410 420 430 440 450
KERASDTKPT RVVRKRAAPE DFLGKGPNKK ILIGNEELTR LWNLCPDNME
460 470 480 490 500
ACKSETREYM PTLEEFFEEA IEQADPENMV ESEYKAVNNS NYGWRALRLL
510 520 530 540 550
ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI KTGEDEDEED
560 570 580 590 600
NDALLKENES PDVRRDKPIT GEQIESFANK LGEQWKILAP YLEIKDSDIR
610 620 630 640 650
QIECDSEDMK MRAKQLLVAW QDQEGVHATT DNLISALNKS GLSDLAESLT

NDTETNS
Length:657
Mass (Da):75,436
Last modified:June 1, 2002 - v1
Checksum:iE4235E395B5A82BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ8R3N6.
SMRiQ8R3N6. Positions 558-657.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R3N6. 2 interactions.
MINTiMINT-4137684.
STRINGi10090.ENSMUSP00000025137.

PTM databases

PhosphoSiteiQ8R3N6.

Proteomic databases

MaxQBiQ8R3N6.
PaxDbiQ8R3N6.
PRIDEiQ8R3N6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9984.
MGIiMGI:1919668. Thoc1.

Phylogenomic databases

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

Miscellaneous databases

NextBioi377554.
PROiQ8R3N6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R3N6.
CleanExiMM_THOC1.
ExpressionAtlasiQ8R3N6. baseline and differential.
GenevisibleiQ8R3N6. MM.

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]
ProtoNetiSearch...

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 22, 2015
This is version 115 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

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.