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Q96FV9 (THOC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
Short name=p84N5
hTREX84
Gene names
Name:THOC1
Synonyms:HPR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.22 Ref.23

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.22 Ref.23

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.1 Ref.10 Ref.12 Ref.13 Ref.14

Subcellular location

Isoform 1: Nucleus speckle. Nucleusnucleoplasm. Nucleus matrix. Cytoplasm Ref.1 Ref.2 Ref.11. 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. Ref.1 Ref.2 Ref.11

Isoform 2: Cytoplasm Ref.1 Ref.2 Ref.11.

Tissue specificity

Ubiquitous. Expressed in various cancer cell lines. Expressed at very low levels in normal breast epithelial cells and highly expressed in breast tumors. Expression is strongly associated with an aggressive phenotype of breast tumors and expression correlates with tumor size and the metastatic state of the tumor progression. Ref.2 Ref.12

Induction

Up-regulated during cell proliferation. Ref.2

Domain

An intact death domain is needed for apoptosis. Ref.7

Post-translational modification

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

Polyubiquitinated, leading to proteasomal degradation; probably involves NEDD4.

Sequence similarities

Contains 1 death domain.

Ontologies

Keywords
   Biological processApoptosis
mRNA processing
mRNA splicing
mRNA transport
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
RNA-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Traceable author statement Ref.1. Source: ProtInc

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from direct assay Ref.7. Source: UniProtKB

mRNA export from nucleus

Inferred from direct assay Ref.15. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA damage checkpoint

Inferred from mutant phenotype Ref.22. Source: UniProtKB

negative regulation of isotype switching to IgA isotypes

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA-templated transcription, elongation

Inferred from mutant phenotype Ref.22. Source: UniProtKB

regulation of DNA recombination

Inferred from mutant phenotype Ref.22. Source: UniProtKB

regulation of DNA-templated transcription, elongation

Inferred from direct assay Ref.14. Source: UniProtKB

replication fork processing

Inferred from mutant phenotype Ref.22. 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 direct assay Ref.17. Source: UniProtKB

   Cellular_componentTHO complex

Inferred from direct assay Ref.13. Source: UniProtKB

THO complex part of transcription export complex

Inferred from direct assay Ref.13. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

intercellular bridge

Inferred from direct assay. Source: HPA

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

transcription export complex

Inferred from direct assay Ref.12Ref.13. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

THOC5Q137695EBI-1765605,EBI-5280316

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96FV9-1)

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.
Isoform 2 (identifier: Q96FV9-2)

Also known as: p84N5s;

The sequence of this isoform differs from the canonical sequence as follows:
     363-377: LLSENPPDGERFSKM → VSSTRNKPMIEKMEI
     378-657: Missing.
Note: May be due to an intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657THO complex subunit 1
PRO_0000072520

Regions

Domain570 – 65384Death
Motif414 – 43017Nuclear localization signal Ref.11

Amino acid modifications

Modified residue11N-acetylmethionine Ref.20
Modified residue21Phosphoserine Ref.18 Ref.20
Modified residue1331N6-acetyllysine Ref.19
Modified residue3001N6-acetyllysine Ref.19
Modified residue5601Phosphoserine Ref.20

Natural variations

Alternative sequence363 – 37715LLSEN…RFSKM → VSSTRNKPMIEKMEI in isoform 2.
VSP_038073
Alternative sequence378 – 657280Missing in isoform 2.
VSP_038074

Experimental info

Mutagenesis6171L → P: Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. Ref.7
Mutagenesis6201W → P or R: Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. Ref.7
Sequence conflict711N → H in AAT81408. Ref.2
Sequence conflict861G → A in AAT81408. Ref.2
Sequence conflict1301S → A in AAA53571. Ref.1
Sequence conflict1341N → S in BAG37293. Ref.3
Sequence conflict4331M → T in AAA53571. Ref.1
Sequence conflict4801V → A in AAA53571. Ref.1
Sequence conflict4871V → M in AAA53571. Ref.1
Sequence conflict4981R → K in AAA53571. Ref.1
Sequence conflict5191P → Q in AAA53571. Ref.1

Secondary structure

................. 657
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: DB7980BD0F252DAB

FASTA65775,666
        10         20         30         40         50         60 
MSPTPPLFSL PEARTRFTKS TREALNNKNI KPLLSTFSQV PGSENEKKCT LDQAFRGILE 

        70         80         90        100        110        120 
EEIINHSSCE NVLAIISLAI GGVTEGICTA STPFVLLGDV LDCLPLDQCD TIFTFVEKNV 

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

       190        200        210        220        230        240 
FNLENVTVFN TNEQESTLGQ KHTEDREEGM DVEEGEMGDE 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 KERTSDTKPT RIIRKRTAPE 

       430        440        450        460        470        480 
DFLGKGPTKK ILMGNEELTR LWNLCPDNME ACKSETREHM PTLEEFFEEA IEQADPENMV 

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

       550        560        570        580        590        600 
KTGEDEDEED NDALLKENES PDVRRDKPVT GEQIEVFANK LGEQWKILAP YLEMKDSEIR 

       610        620        630        640        650 
QIECDSEDMK MRAKQLLVAW QDQEGVHATP ENLINALNKS GLSDLAESLT NDNETNS 

« Hide

Isoform 2 (p84N5s) [UniParc].

Checksum: 313FCF7E19C03FFC
Show »

FASTA37743,359

References

« Hide 'large scale' references
[1]"The amino-terminal region of the retinoblastoma gene product binds a novel nuclear matrix protein that co-localizes to centers for RNA processing."
Durfee T., Mancini M.A., Jones D., Elledge S.J., Lee W.H.
J. Cell Biol. 127:609-622(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH RB1.
Tissue: Lymphocyte.
[2]"The death domain protein p84N5, but not the short isoform p84N5s, is cell cycle-regulated and shuttles between the nucleus and the cytoplasm."
Gasparri F., Sola F., Locatelli G., Muzio M.
FEBS Lett. 574:13-19(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-86 (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[3]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Uterus.
[4]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Bone marrow.
[7]"Apoptosis induced by the nuclear death domain protein p84N5 is inhibited by association with Rb protein."
Doostzadeh-Cizeron J., Evans R., Yin S., Goodrich D.W.
Mol. Biol. Cell 10:3251-3261(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PTM, DOMAIN, MUTAGENESIS OF LEU-617 AND TRP-620.
[8]"Apoptosis induced by the nuclear death domain protein p84N5 is associated with caspase-6 and NF-kappa B activation."
Doostzadeh-Cizeron J., Yin S., Goodrich D.W.
J. Biol. Chem. 275:25336-25341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The nuclear death domain protein p84N5 activates a G2/M cell cycle checkpoint prior to the onset of apoptosis."
Doostzadeh-Cizeron J., Terry N.H., Goodrich D.W.
J. Biol. Chem. 276:1127-1132(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"TREX is a conserved complex coupling transcription with messenger RNA export."
Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M., Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R., Hurt E.
Nature 417:304-308(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THE TREX COMPLEX.
[11]"Nuclear localization is required for induction of apoptotic cell death by the Rb-associated p84N5 death domain protein."
Evans R.L., Poe B.S., Goodrich D.W.
Oncogene 21:4691-4695(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
[12]"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, TISSUE SPECIFICITY.
[13]"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.
[14]"Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically links RNA polymerase II and RNA processing factors."
Li Y., Wang X., Zhang X., Goodrich D.W.
Mol. Cell. Biol. 25:4023-4033(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THOC2; DDX39B AND RNA POLYMERASE II.
[15]"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.
[16]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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-133 AND LYS-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Genome instability and transcription elongation impairment in human cells depleted of THO/TREX."
Dominguez-Sanchez M.S., Barroso S., Gomez-Gonzalez B., Luna R., Aguilera A.
PLoS Genet. 7:E1002386-E1002386(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"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.
[24]"The Thoc1 encoded ribonucleoprotein is a substrate for the NEDD4-1 E3 ubiquitin protein ligase."
Song F., Fan C., Wang X., Goodrich D.W.
PLoS ONE 8:E57995-E57995(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY NEDD4.
[25]"Solution structure of the death domain of nuclear matrix protein p84."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 561-657.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36529 mRNA. Translation: AAA53571.1.
AY573302 mRNA. Translation: AAT81408.1.
AY573303 mRNA. Translation: AAT81409.1.
AK314755 mRNA. Translation: BAG37293.1.
AP000845 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01732.1.
BC010381 mRNA. Translation: AAH10381.1.
PIRA53545.
RefSeqNP_005122.2. NM_005131.2.
UniGeneHs.712543.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXPNMR-A561-657[»]
ProteinModelPortalQ96FV9.
SMRQ96FV9. Positions 558-657.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115305. 32 interactions.
IntActQ96FV9. 16 interactions.
MINTMINT-4536762.
STRING9606.ENSP00000261600.

PTM databases

PhosphoSiteQ96FV9.

Polymorphism databases

DMDM37999906.

Proteomic databases

PaxDbQ96FV9.
PRIDEQ96FV9.

Protocols and materials databases

DNASU9984.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261600; ENSP00000261600; ENSG00000079134. [Q96FV9-1]
GeneID9984.
KEGGhsa:9984.
UCSCuc002kkj.4. human. [Q96FV9-1]
uc002kkl.2. human. [Q96FV9-2]

Organism-specific databases

CTD9984.
GeneCardsGC18M000204.
HGNCHGNC:19070. THOC1.
HPAHPA019096.
HPA019687.
MIM606930. gene.
neXtProtNX_Q96FV9.
PharmGKBPA134887435.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG275387.
HOGENOMHOG000008123.
HOVERGENHBG060294.
InParanoidQ96FV9.
KOK12878.
OMAACKSETR.
OrthoDBEOG7R831Q.
PhylomeDBQ96FV9.
TreeFamTF314796.

Gene expression databases

ArrayExpressQ96FV9.
BgeeQ96FV9.
CleanExHS_THOC1.
GenevestigatorQ96FV9.

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

ChiTaRSTHOC1. human.
EvolutionaryTraceQ96FV9.
GeneWikiTHOC1.
GenomeRNAi9984.
NextBio37696.
PROQ96FV9.
SOURCESearch...

Entry information

Entry nameTHOC1_HUMAN
AccessionPrimary (citable) accession number: Q96FV9
Secondary accession number(s): B2RBP6 expand/collapse secondary AC list , Q15219, Q64I72, Q64I73
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM