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Protein

THO complex subunit 2

Gene

THOC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for efficient export of polyadenylated RNA and spliced mRNA. 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. THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. Required for NXF1 localization to the nuclear rim. Plays a role for proper neuronal development.8 Publications

GO - Molecular functioni

GO - Biological processi

  • generation of neurons Source: UniProtKB
  • mRNA 3'-end processing Source: Reactome
  • mRNA export from nucleus Source: UniProtKB
  • neuron development Source: UniProtKB
  • poly(A)+ mRNA export from nucleus Source: UniProtKB
  • RNA export from nucleus Source: Reactome
  • RNA splicing Source: UniProtKB-KW
  • termination of RNA polymerase II transcription Source: Reactome
  • viral mRNA export from host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
THO complex subunit 2
Short name:
Tho2
Alternative name(s):
hTREX120
Gene namesi
Name:THOC2
Synonyms:CXorf3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:19073. THOC2.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • THO complex Source: UniProtKB
  • THO complex part of transcription export complex Source: UniProtKB
  • transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 12 (MRX12)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX12 patients manifest variable degrees of intellectual disability. Commonly observed features included speech delay, elevated BMI, short stature, seizure disorders, gait disturbance, and tremors.
See also OMIM:300957
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti313 – 3131L → F in MRX12. 1 Publication
VAR_075718
Natural varianti438 – 4381L → P in MRX12; reduced amounts of protein; reduced amounts of other THO complex subunits; the mutant protein has a significantly shorter half-life. 1 Publication
VAR_075719
Natural varianti800 – 8001I → T in MRX12; reduced amounts of mutant protein; reduced amounts of other THO complex subunits; the mutant protein has a significantly shorter half-life. 1 Publication
VAR_075720
Natural varianti1012 – 10121S → P in MRX12; normal amounts of mutant protein; normal amounts of other THO complex subunits. 1 Publication
VAR_075721

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300957. phenotype.
PharmGKBiPA128395788.

Polymorphism and mutation databases

BioMutaiTHOC2.
DMDMi259016155.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15931593THO complex subunit 2PRO_0000072523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1222 – 12221PhosphoserineBy similarity
Modified residuei1385 – 13851PhosphothreonineCombined sources
Modified residuei1393 – 13931PhosphoserineCombined sources
Modified residuei1417 – 14171PhosphoserineCombined sources
Modified residuei1443 – 14431PhosphothreonineCombined sources
Modified residuei1486 – 14861PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8NI27.
MaxQBiQ8NI27.
PaxDbiQ8NI27.
PRIDEiQ8NI27.

PTM databases

iPTMnetiQ8NI27.
PhosphoSiteiQ8NI27.

Expressioni

Tissue specificityi

Expressed in the hippocampus and the cerebral cortex.1 Publication

Gene expression databases

BgeeiQ8NI27.
CleanExiHS_THOC2.
ExpressionAtlasiQ8NI27. baseline and differential.
GenevisibleiQ8NI27. HS.

Organism-specific databases

HPAiHPA047921.

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. Interacts with THOC1, POLDIP3 and ZC3H11A.5 Publications

Protein-protein interaction databases

BioGridi121436. 103 interactions.
IntActiQ8NI27. 79 interactions.
MINTiMINT-2811626.
STRINGi9606.ENSP00000245838.

Structurei

3D structure databases

ProteinModelPortaliQ8NI27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili293 – 33947Sequence analysisAdd
BLAST
Coiled coili896 – 96570Sequence analysisAdd
BLAST
Coiled coili1464 – 149128Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi923 – 9286Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1264 – 1591328Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the THOC2 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1874. Eukaryota.
ENOG410XQ2A. LUCA.
GeneTreeiENSGT00710000106792.
HOGENOMiHOG000048227.
HOVERGENiHBG104451.
InParanoidiQ8NI27.
KOiK12879.
OMAiHLPKVWD.
OrthoDBiEOG73803R.
PhylomeDBiQ8NI27.
TreeFamiTF313127.

Family and domain databases

InterProiIPR021418. THO_THOC2_C.
IPR021726. THO_THOC2_N.
IPR032302. THOC2_N.
[Graphical view]
PfamiPF11262. Tho2. 1 hit.
PF11732. Thoc2. 1 hit.
PF16134. THOC2_N. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NI27-1) [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
MAAAAVVVPA EWIKNWEKSG RGEFLHLCRI LSENKSHDSS TYRDFQQALY
60 70 80 90 100
ELSYHVIKGN LKHEQASNVL SDISEFREDM PSILADVFCI LDIETNCLEE
110 120 130 140 150
KSKRDYFTQL VLACLYLVSD TVLKERLDPE TLESLGLIKQ SQQFNQKSVK
160 170 180 190 200
IKTKLFYKQQ KFNLLREENE GYAKLIAELG QDLSGSITSD LILENIKSLI
210 220 230 240 250
GCFNLDPNRV LDVILEVFEC RPEHDDFFIS LLESYMSMCE PQTLCHILGF
260 270 280 290 300
KFKFYQEPNG ETPSSLYRVA AVLLQFNLID LDDLYVHLLP ADNCIMDEHK
310 320 330 340 350
REIAEAKQIV RKLTMVVLSS EKMDEREKEK EKEEEKVEKP PDNQKLGLLE
360 370 380 390 400
ALLKIGDWQH AQNIMDQMPP YYAASHKLIA LAICKLIHIT IEPLYRRVGV
410 420 430 440 450
PKGAKGSPVN ALQNKRAPKQ AESFEDLRRD VFNMFCYLGP HLSHDPILFA
460 470 480 490 500
KVVRIGKSFM KEFQSDGSKQ EDKEKTEVIL SCLLSITDQV LLPSLSLMDC
510 520 530 540 550
NACMSEELWG MFKTFPYQHR YRLYGQWKNE TYNSHPLLVK VKAQTIDRAK
560 570 580 590 600
YIMKRLTKEN VKPSGRQIGK LSHSNPTILF DYILSQIQKY DNLITPVVDS
610 620 630 640 650
LKYLTSLNYD VLAYCIIEAL ANPEKERMKH DDTTISSWLQ SLASFCGAVF
660 670 680 690 700
RKYPIDLAGL LQYVANQLKA GKSFDLLILK EVVQKMAGIE ITEEMTMEQL
710 720 730 740 750
EAMTGGEQLK AEGGYFGQIR NTKKSSQRLK DALLDHDLAL PLCLLMAQQR
760 770 780 790 800
NGVIFQEGGE KHLKLVGKLY DQCHDTLVQF GGFLASNLST EDYIKRVPSI
810 820 830 840 850
DVLCNEFHTP HDAAFFLSRP MYAHHISSKY DELKKSEKGS KQQHKVHKYI
860 870 880 890 900
TSCEMVMAPV HEAVVSLHVS KVWDDISPQF YATFWSLTMY DLAVPHTSYE
910 920 930 940 950
REVNKLKVQM KAIDDNQEMP PNKKKKEKER CTALQDKLLE EEKKQMEHVQ
960 970 980 990 1000
RVLQRLKLEK DNWLLAKSTK NETITKFLQL CIFPRCIFSA IDAVYCARFV
1010 1020 1030 1040 1050
ELVHQQKTPN FSTLLCYDRV FSDIIYTVAS CTENEASRYG RFLCCMLETV
1060 1070 1080 1090 1100
TRWHSDRATY EKECGNYPGF LTILRATGFD GGNKADQLDY ENFRHVVHKW
1110 1120 1130 1140 1150
HYKLTKASVH CLETGEYTHI RNILIVLTKI LPWYPKVLNL GQALERRVHK
1160 1170 1180 1190 1200
ICQEEKEKRP DLYALAMGYS GQLKSRKSYM IPENEFHHKD PPPRNAVASV
1210 1220 1230 1240 1250
QNGPGGGPSS SSIGSASKSD ESSTEETDKS RERSQCGVKA VNKASSTTPK
1260 1270 1280 1290 1300
GNSSNGNSGS NSNKAVKEND KEKGKEKEKE KKEKTPATTP EARVLGKDGK
1310 1320 1330 1340 1350
EKPKEERPNK DEKARETKER TPKSDKEKEK FKKEEKAKDE KFKTTVPNAE
1360 1370 1380 1390 1400
SKSTQERERE KEPSRERDIA KEMKSKENVK GGEKTPVSGS LKSPVPRSDI
1410 1420 1430 1440 1450
PEPEREQKRR KIDTHPSPSH SSTVKDSLIE LKESSAKLYI NHTPPPLSKS
1460 1470 1480 1490 1500
KEREMDKKDL DKSRERSRER EKKDEKDRKE RKRDHSNNDR EVPPDLTKRR
1510 1520 1530 1540 1550
KEENGTMGVS KHKSESPCES PYPNEKDKEK NKSKSSGKEK GSDSFKSEKM
1560 1570 1580 1590
DKISSGGKKE SRHDKEKIEK KEKRDSSGGK EEKKHHKSSD KHR
Length:1,593
Mass (Da):182,775
Last modified:September 22, 2009 - v2
Checksum:iA869B3E412CA4356
GO
Isoform 2 (identifier: Q8NI27-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1179: Missing.

Note: No experimental confirmation available.
Show »
Length:414
Mass (Da):46,812
Checksum:i2ECC3FEF7EE2607D
GO

Sequence cautioni

The sequence AAM28436.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence BAB14630.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti807 – 8071F → S in BAB14630 (PubMed:14702039).Curated
Sequence conflicti1276 – 12761E → G in CAE46196 (PubMed:17974005).Curated
Sequence conflicti1356 – 13561E → K in CAE46196 (PubMed:17974005).Curated
Sequence conflicti1426 – 14294DSLI → VSIA in CAE46196 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti313 – 3131L → F in MRX12. 1 Publication
VAR_075718
Natural varianti438 – 4381L → P in MRX12; reduced amounts of protein; reduced amounts of other THO complex subunits; the mutant protein has a significantly shorter half-life. 1 Publication
VAR_075719
Natural varianti800 – 8001I → T in MRX12; reduced amounts of mutant protein; reduced amounts of other THO complex subunits; the mutant protein has a significantly shorter half-life. 1 Publication
VAR_075720
Natural varianti1012 – 10121S → P in MRX12; normal amounts of mutant protein; normal amounts of other THO complex subunits. 1 Publication
VAR_075721

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11791179Missing in isoform 2. 1 PublicationVSP_008588Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL030996, AL023575, Z82901 Genomic DNA. Translation: CAI42271.2.
Z82901, AL023575, AL030996 Genomic DNA. Translation: CAI42864.2.
AL023575, AL030996, Z82901 Genomic DNA. Translation: CAO03594.1.
BC072400 mRNA. Translation: AAH72400.1.
AF441770 mRNA. Translation: AAM28436.1. Sequence problems.
AK023659 mRNA. Translation: BAB14630.1. Different initiation.
BX648654 mRNA. Translation: CAE46196.1.
CCDSiCCDS43988.1. [Q8NI27-1]
RefSeqiNP_001075019.1. NM_001081550.1. [Q8NI27-1]
UniGeneiHs.149991.

Genome annotation databases

EnsembliENST00000245838; ENSP00000245838; ENSG00000125676. [Q8NI27-1]
ENST00000355725; ENSP00000347959; ENSG00000125676. [Q8NI27-1]
ENST00000618150; ENSP00000480478; ENSG00000125676. [Q8NI27-2]
GeneIDi57187.
KEGGihsa:57187.
UCSCiuc004etu.4. human. [Q8NI27-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL030996, AL023575, Z82901 Genomic DNA. Translation: CAI42271.2.
Z82901, AL023575, AL030996 Genomic DNA. Translation: CAI42864.2.
AL023575, AL030996, Z82901 Genomic DNA. Translation: CAO03594.1.
BC072400 mRNA. Translation: AAH72400.1.
AF441770 mRNA. Translation: AAM28436.1. Sequence problems.
AK023659 mRNA. Translation: BAB14630.1. Different initiation.
BX648654 mRNA. Translation: CAE46196.1.
CCDSiCCDS43988.1. [Q8NI27-1]
RefSeqiNP_001075019.1. NM_001081550.1. [Q8NI27-1]
UniGeneiHs.149991.

3D structure databases

ProteinModelPortaliQ8NI27.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121436. 103 interactions.
IntActiQ8NI27. 79 interactions.
MINTiMINT-2811626.
STRINGi9606.ENSP00000245838.

PTM databases

iPTMnetiQ8NI27.
PhosphoSiteiQ8NI27.

Polymorphism and mutation databases

BioMutaiTHOC2.
DMDMi259016155.

Proteomic databases

EPDiQ8NI27.
MaxQBiQ8NI27.
PaxDbiQ8NI27.
PRIDEiQ8NI27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245838; ENSP00000245838; ENSG00000125676. [Q8NI27-1]
ENST00000355725; ENSP00000347959; ENSG00000125676. [Q8NI27-1]
ENST00000618150; ENSP00000480478; ENSG00000125676. [Q8NI27-2]
GeneIDi57187.
KEGGihsa:57187.
UCSCiuc004etu.4. human. [Q8NI27-1]

Organism-specific databases

CTDi57187.
GeneCardsiTHOC2.
H-InvDBHIX0017032.
HGNCiHGNC:19073. THOC2.
HPAiHPA047921.
MIMi300395. gene.
300957. phenotype.
neXtProtiNX_Q8NI27.
PharmGKBiPA128395788.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1874. Eukaryota.
ENOG410XQ2A. LUCA.
GeneTreeiENSGT00710000106792.
HOGENOMiHOG000048227.
HOVERGENiHBG104451.
InParanoidiQ8NI27.
KOiK12879.
OMAiHLPKVWD.
OrthoDBiEOG73803R.
PhylomeDBiQ8NI27.
TreeFamiTF313127.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72187. mRNA 3'-end processing.

Miscellaneous databases

ChiTaRSiTHOC2. human.
GeneWikiiTHOC2.
GenomeRNAii57187.
PROiQ8NI27.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NI27.
CleanExiHS_THOC2.
ExpressionAtlasiQ8NI27. baseline and differential.
GenevisibleiQ8NI27. HS.

Family and domain databases

InterProiIPR021418. THO_THOC2_C.
IPR021726. THO_THOC2_N.
IPR032302. THOC2_N.
[Graphical view]
PfamiPF11262. Tho2. 1 hit.
PF11732. Thoc2. 1 hit.
PF16134. THOC2_N. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 2).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 233-1593 (ISOFORM 1), FUNCTION, INTERACTION WITH THE TREX COMPLEX.
  4. "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] OF 559-1277 (ISOFORM 1).
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1266-1593 (ISOFORM 1).
    Tissue: Salivary gland.
  6. "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.
  7. "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.
  8. "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: INTERACTION WITH THOC1.
  9. "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.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1385; SER-1393; SER-1417; THR-1443 AND SER-1486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1385; SER-1393 AND SER-1417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1417 AND SER-1486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: FUNCTION.
  18. "The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export."
    Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.
    PLoS ONE 7:E43804-E43804(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLDIP3 AND ZC3H11A.
  19. "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.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. Cited for: FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN MRX12, VARIANTS MRX12 PHE-313; PRO-438; THR-800 AND PRO-1012, CHARACTERIZATION OF VARIANTS MRX12 PRO-438; THR-800 AND PRO-1012.

Entry informationi

Entry nameiTHOC2_HUMAN
AccessioniPrimary (citable) accession number: Q8NI27
Secondary accession number(s): A6NM50
, Q5JZ12, Q6IN92, Q9H8I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: September 22, 2009
Last modified: June 8, 2016
This is version 121 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.