Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96FV9

- THOC1_HUMAN

UniProt

Q96FV9 - THOC1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

THO complex subunit 1

Gene

THOC1

Organism
Homo sapiens (Human)
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. 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.
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.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. mRNA export from nucleus Source: UniProtKB
  3. mRNA processing Source: UniProtKB-KW
  4. negative regulation of DNA damage checkpoint Source: UniProtKB
  5. negative regulation of isotype switching to IgA isotypes Source: UniProtKB
  6. positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  7. regulation of DNA recombination Source: UniProtKB
  8. regulation of DNA-templated transcription, elongation Source: UniProtKB
  9. replication fork processing Source: UniProtKB
  10. RNA processing Source: ProtInc
  11. RNA splicing Source: UniProtKB-KW
  12. signal transduction Source: InterPro
  13. transcription, DNA-templated Source: UniProtKB-KW
  14. viral mRNA export from host cell nucleus Source: UniProtKB
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
Short name:
p84N5
hTREX84
Gene namesi
Name:THOC1
Synonyms:HPR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:19070. THOC1.

Subcellular locationi

Isoform 1 : Nucleus speckle. Nucleusnucleoplasm. Nucleus matrix. Cytoplasm
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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. intercellular bridge Source: HPA
  3. nucleus Source: UniProtKB
  4. THO complex Source: UniProtKB
  5. THO complex part of transcription export complex Source: UniProtKB
  6. transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi617 – 6171L → P: Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. 1 Publication
Mutagenesisi620 – 6201W → P or R: Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. 1 Publication

Organism-specific databases

PharmGKBiPA134887435.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657THO complex subunit 1PRO_0000072520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21Phosphoserine2 Publications
Modified residuei133 – 1331N6-acetyllysine1 Publication
Modified residuei300 – 3001N6-acetyllysine1 Publication
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.
Polyubiquitinated, leading to proteasomal degradation; probably involves NEDD4.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96FV9.
PaxDbiQ96FV9.
PRIDEiQ96FV9.

PTM databases

PhosphoSiteiQ96FV9.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

Up-regulated during cell proliferation.1 Publication

Gene expression databases

BgeeiQ96FV9.
CleanExiHS_THOC1.
ExpressionAtlasiQ96FV9. baseline and differential.
GenevestigatoriQ96FV9.

Organism-specific databases

HPAiHPA019096.
HPA019687.

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
THOC5Q137697EBI-1765605,EBI-5280316

Protein-protein interaction databases

BioGridi115305. 37 interactions.
IntActiQ96FV9. 19 interactions.
MINTiMINT-4536762.
STRINGi9606.ENSP00000261600.

Structurei

Secondary structure

1
657
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi565 – 5673Combined sources
Helixi571 – 58111Combined sources
Turni582 – 5843Combined sources
Helixi585 – 5884Combined sources
Turni589 – 5935Combined sources
Helixi596 – 60510Combined sources
Helixi609 – 62416Combined sources
Helixi625 – 6273Combined sources
Helixi630 – 63910Combined sources
Helixi643 – 6508Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXPNMR-A561-657[»]
ProteinModelPortaliQ96FV9.
SMRiQ96FV9. Positions 558-657.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96FV9.

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 signal1 PublicationAdd
BLAST

Domaini

An intact death domain is needed for apoptosis.1 Publication

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG275387.
GeneTreeiENSGT00390000016232.
HOGENOMiHOG000008123.
HOVERGENiHBG060294.
InParanoidiQ96FV9.
KOiK12878.
OMAiACKSETR.
OrthoDBiEOG7R831Q.
PhylomeDBiQ96FV9.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96FV9-1) [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
MSPTPPLFSL PEARTRFTKS TREALNNKNI KPLLSTFSQV PGSENEKKCT
60 70 80 90 100
LDQAFRGILE EEIINHSSCE NVLAIISLAI GGVTEGICTA 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 DVEEGEMGDE 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
KERTSDTKPT RIIRKRTAPE DFLGKGPTKK ILMGNEELTR LWNLCPDNME
460 470 480 490 500
ACKSETREHM PTLEEFFEEA IEQADPENMV ENEYKAVNNS NYGWRALRLL
510 520 530 540 550
ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI KTGEDEDEED
560 570 580 590 600
NDALLKENES PDVRRDKPVT GEQIEVFANK LGEQWKILAP YLEMKDSEIR
610 620 630 640 650
QIECDSEDMK MRAKQLLVAW QDQEGVHATP ENLINALNKS GLSDLAESLT

NDNETNS
Length:657
Mass (Da):75,666
Last modified:December 1, 2001 - v1
Checksum:iDB7980BD0F252DAB
GO
Isoform 2 (identifier: Q96FV9-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:377
Mass (Da):43,359
Checksum:i313FCF7E19C03FFC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711N → H in AAT81408. (PubMed:15358532)Curated
Sequence conflicti86 – 861G → A in AAT81408. (PubMed:15358532)Curated
Sequence conflicti130 – 1301S → A in AAA53571. (PubMed:7525595)Curated
Sequence conflicti134 – 1341N → S in BAG37293. (PubMed:14702039)Curated
Sequence conflicti433 – 4331M → T in AAA53571. (PubMed:7525595)Curated
Sequence conflicti480 – 4801V → A in AAA53571. (PubMed:7525595)Curated
Sequence conflicti487 – 4871V → M in AAA53571. (PubMed:7525595)Curated
Sequence conflicti498 – 4981R → K in AAA53571. (PubMed:7525595)Curated
Sequence conflicti519 – 5191P → Q in AAA53571. (PubMed:7525595)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei363 – 37715LLSEN…RFSKM → VSSTRNKPMIEKMEI in isoform 2. 1 PublicationVSP_038073Add
BLAST
Alternative sequencei378 – 657280Missing in isoform 2. 1 PublicationVSP_038074Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45820.1. [Q96FV9-1]
PIRiA53545.
RefSeqiNP_005122.2. NM_005131.2. [Q96FV9-1]
UniGeneiHs.712543.

Genome annotation databases

EnsembliENST00000261600; ENSP00000261600; ENSG00000079134. [Q96FV9-1]
GeneIDi9984.
KEGGihsa:9984.
UCSCiuc002kkj.4. human. [Q96FV9-1]
uc002kkl.2. human. [Q96FV9-2]

Polymorphism databases

DMDMi37999906.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS45820.1. [Q96FV9-1 ]
PIRi A53545.
RefSeqi NP_005122.2. NM_005131.2. [Q96FV9-1 ]
UniGenei Hs.712543.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WXP NMR - A 561-657 [» ]
ProteinModelPortali Q96FV9.
SMRi Q96FV9. Positions 558-657.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115305. 37 interactions.
IntActi Q96FV9. 19 interactions.
MINTi MINT-4536762.
STRINGi 9606.ENSP00000261600.

PTM databases

PhosphoSitei Q96FV9.

Polymorphism databases

DMDMi 37999906.

Proteomic databases

MaxQBi Q96FV9.
PaxDbi Q96FV9.
PRIDEi Q96FV9.

Protocols and materials databases

DNASUi 9984.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261600 ; ENSP00000261600 ; ENSG00000079134 . [Q96FV9-1 ]
GeneIDi 9984.
KEGGi hsa:9984.
UCSCi uc002kkj.4. human. [Q96FV9-1 ]
uc002kkl.2. human. [Q96FV9-2 ]

Organism-specific databases

CTDi 9984.
GeneCardsi GC18M000204.
HGNCi HGNC:19070. THOC1.
HPAi HPA019096.
HPA019687.
MIMi 606930. gene.
neXtProti NX_Q96FV9.
PharmGKBi PA134887435.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG275387.
GeneTreei ENSGT00390000016232.
HOGENOMi HOG000008123.
HOVERGENi HBG060294.
InParanoidi Q96FV9.
KOi K12878.
OMAi ACKSETR.
OrthoDBi EOG7R831Q.
PhylomeDBi Q96FV9.
TreeFami TF314796.

Miscellaneous databases

ChiTaRSi THOC1. human.
EvolutionaryTracei Q96FV9.
GeneWikii THOC1.
GenomeRNAii 9984.
NextBioi 37696.
PROi Q96FV9.
SOURCEi Search...

Gene expression databases

Bgeei Q96FV9.
CleanExi HS_THOC1.
ExpressionAtlasi Q96FV9. baseline and differential.
Genevestigatori Q96FV9.

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 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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. 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. 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. 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.

Entry informationi

Entry nameiTHOC1_HUMAN
AccessioniPrimary (citable) accession number: Q96FV9
Secondary accession number(s): B2RBP6
, Q15219, Q64I72, Q64I73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: December 1, 2001
Last modified: November 26, 2014
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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3