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Q13769 (THOC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
THO complex subunit 5 homolog
Alternative name(s):
Functional spliceosome-associated protein 79
Short name=fSAP79
NF2/meningioma region protein pK1.3
Placental protein 39.2
Short name=PP39.2
hTREX90
Gene names
Name:THOC5
Synonyms:C22orf19, KIAA0983
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in transcription elongation and genome stability. Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probaly mediates association of the TREX and CFIm complexes. Ref.7 Ref.8 Ref.9 Ref.12 Ref.15 Ref.20 Ref.22 Ref.27

Regulates the expression of myeloid transcription factors CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol 3,4,5-trisphosphate. May be involved in the differentiation of granulocytes and adipocytes. Essential for hematopoietic primitive cell survival and plays an integral role in monocytic development. Ref.7 Ref.8 Ref.9 Ref.12 Ref.15 Ref.20 Ref.22 Ref.27

Subunit structure

Interacts with phosphorylated CSF1R. 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, ALYREF/THOC4, and THOC7. Interacts (via N-terminus) with the NTF2 domain of NXF1. Forms a complex with CEBPB. Interacts with CPSF6; indicative for an association with the cleavage factor Im (CFIm) complex. Ref.7 Ref.8 Ref.15 Ref.16 Ref.25 Ref.27

Subcellular location

Nucleus. Nucleus speckle Probable. Cytoplasm By similarity. Note: Shuttles between nucleus and cytoplasm. Ref.15 Ref.16

Tissue specificity

Ubiquitously expressed.

Post-translational modification

Phosphorylated on tyrosine upon binding to activated CSF1R; which causes a dissociation of the two proteins. Phosphorylation on Ser-5 and/or Ser-6 is required for nuclear export. Phosphorylated on Thr-328 in insulin-stimulated adipocytes By similarity. Phosphorylation at Tyr-225 modulates mRNA binding. Ref.11 Ref.26

Sequence similarities

Belongs to the THOC5 family.

Sequence caution

The sequence BAA76827.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDifferentiation
mRNA processing
mRNA splicing
mRNA transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA export from nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

monocyte differentiation

Inferred from direct assay PubMed 19015024. Source: UniProtKB

negative regulation of DNA damage checkpoint

Inferred from mutant phenotype Ref.20. Source: UniProtKB

negative regulation of macrophage differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA-templated transcription, elongation

Inferred from mutant phenotype Ref.20. Source: UniProtKB

primitive hemopoiesis

Inferred from sequence or structural similarity. Source: UniProtKB

viral mRNA export from host cell nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

   Cellular_componentTHO complex

Inferred from direct assay Ref.8. Source: UniProtKB

THO complex part of transcription export complex

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

transcription export complex

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.16Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.24
Chain2 – 683682THO complex subunit 5 homolog
PRO_0000079577

Regions

Region2 – 199198Interaction with THOC7
Region2 – 144143Interaction with CSF1R By similarity
Motif7 – 104Nuclear localization signal By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.24
Modified residue2251Phosphotyrosine; by SRC Ref.11 Ref.26
Modified residue3071Phosphoserine Ref.10 Ref.13 Ref.17 Ref.18 Ref.21
Modified residue3121Phosphoserine Ref.10 Ref.13 Ref.17 Ref.18 Ref.21
Modified residue3141Phosphoserine Ref.10 Ref.13 Ref.17 Ref.18 Ref.21
Modified residue3281Phosphothreonine Ref.18

Natural variations

Natural variant3801T → K in a breast cancer sample; somatic mutation. Ref.28
VAR_035692
Natural variant4751T → S.
Corresponds to variant rs8141153 [ dbSNP | Ensembl ].
VAR_037134
Natural variant4991G → S in a breast cancer sample; somatic mutation. Ref.28
VAR_035693
Natural variant5251V → I. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs737976 [ dbSNP | Ensembl ].
VAR_037135
Natural variant5791V → I. Ref.1 Ref.3 Ref.5
Corresponds to variant rs1049534 [ dbSNP | Ensembl ].
VAR_021410

Experimental info

Mutagenesis2251Y → F: Impairs mRNA binding, enhances CXCL12-dependent cell migration. Ref.26

Sequences

Sequence LengthMass (Da)Tools
Q13769 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 59550FA548835016

FASTA68378,508
        10         20         30         40         50         60 
MSSESSKKRK PKVIRSDGAP AEGKRNRSDT EQEGKYYSEE AEVDLRDPGR DYELYKYTCQ 

        70         80         90        100        110        120 
ELQRLMAEIQ DLKSRGGKDV AIEIEERRIQ SCVHFMTLKK LNRLAHIRLK KGRDQTHEAK 

       130        140        150        160        170        180 
QKVDAYHLQL QNLLYEVMHL QKEITKCLEF KSKHEEIDLV SLEEFYKEAP PDISKAEVTM 

       190        200        210        220        230        240 
GDPHQQTLAR LDWELEQRKR LAEKYRECLS NKEKILKEIE VKKEYLSSLQ PRLNSIMQAS 

       250        260        270        280        290        300 
LPVQEYLFMP FDQAHKQYET ARHLPPPLYV LFVQATAYGQ ACDKTLSVAI EGSVDEAKAL 

       310        320        330        340        350        360 
FKPPEDSQDD ESDSDAEEEQ TTKRRRPTLG VQLDDKRKEM LKRHPLSVML DLKCKDDSVL 

       370        380        390        400        410        420 
HLTFYYLMNL NIMTVKAKVT TAMELITPIS AGDLLSPDSV LSCLYPGDHG KKTPNPANQY 

       430        440        450        460        470        480 
QFDKVGILTL SDYVLELGHP YLWVQKLGGL HFPKEQPQQT VIADHSLSAS HMETTMKLLK 

       490        500        510        520        530        540 
TRVQSRLALH KQFASLEHGI VPVTSDCQYL FPAKVVSRLV KWVTVAHEDY MELHFTKDIV 

       550        560        570        580        590        600 
DAGLAGDTNL YYMALIERGT AKLQAAVVLN PGYSSIPPVF QLCLNWKGEK TNSNDDNIRA 

       610        620        630        640        650        660 
MEGEVNVCYK ELCGPWPSHQ LLTNQLQRLC VLLDVYLETE SHDDSVEGPK EFPQEKMCLR 

       670        680 
LFRGPSRMKP FKYNHPQGFF SHR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a novel, anonymous gene from a megabase-range YAC and cosmid contig in the neurofibromatosis type 2/meningioma region on human chromosome 22q12."
Xie Y.G., Han F.Y., Peyrard M., Ruttledge M.H., Fransson I., deJong P., Collins J., Dunham I., Nordenskjold M., Dumanski J.P.
Hum. Mol. Genet. 2:1361-1368(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-525 AND ILE-579.
Tissue: Fetus.
[2]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-525.
Tissue: Brain.
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ILE-525 AND ILE-579.
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANTS ILE-525 AND ILE-579.
Tissue: Colon.
[6]"Differential expression of placental genes."
Page N.M., Butlin D.J., Manyonda I., Bicknell A.B., Lowry P.J.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 548-650.
Tissue: Placenta.
[7]"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.
[8]"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.
[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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"THOC5 spliceosome protein: a target for leukaemogenic tyrosine kinases that affects inositol lipid turnover."
Pierce A., Carney L., Hamza H.G., Griffiths J.R., Zhang L., Whetton B.A., Gonzalez Sanchez M.B., Tamura T., Sternberg D., Whetton A.D.
Br. J. Haematol. 141:641-650(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-225, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"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.
[13]"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-307; SER-312 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA."
Katahira J., Inoue H., Hurt E., Yoneda Y.
EMBO J. 28:556-567(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALYREF/THOC4 AND NXF1.
[16]"Nuclear localization of the pre-mRNA associating protein THOC7 depends upon its direct interaction with Fms tyrosine kinase interacting protein (FMIP)."
El Bounkari O., Guria A., Klebba-Faerber S., Claussen M., Pieler T., Griffiths J.R., Whetton A.D., Koch A., Tamura T.
FEBS Lett. 583:13-18(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH THOC7.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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 SER-307; SER-312; SER-314 AND THR-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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.
[21]"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-307; SER-312 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export."
Viphakone N., Hautbergue G.M., Walsh M., Chang C.T., Holland A., Folco E.G., Reed R., Wilson S.A.
Nat. Commun. 3:1006-1006(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]Erratum
Viphakone N., Hautbergue G.M., Walsh M., Chang C.T., Holland A., Folco E.G., Reed R., Wilson S.A.
Nat. Commun. 4:2377-2377(2013)
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[25]"Chtop is a component of the dynamic TREX mRNA export complex."
Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B., Philipsen S., Wilson S.A.
EMBO J. 32:473-486(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NXF1.
[26]"A pathway from leukemogenic oncogenes and stem cell chemokines to RNA processing via THOC5."
Griaud F., Pierce A., Gonzalez Sanchez M.B., Scott M., Abraham S.A., Holyoake T.L., Tran D.D., Tamura T., Whetton A.D.
Leukemia 27:932-940(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-225 BY SRC, MUTAGENESIS OF TYR-225, RNA-BINDING.
[27]"Human TREX component Thoc5 affects alternative polyadenylation site choice by recruiting mammalian cleavage factor I."
Katahira J., Okuzaki D., Inoue H., Yoneda Y., Maehara K., Ohkawa Y.
Nucleic Acids Res. 41:7060-7072(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CPSF6.
[28]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-380 AND SER-499.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18972 Genomic DNA. Translation: AAC26837.1.
AB023200 mRNA. Translation: BAA76827.2. Different initiation.
CR456542 mRNA. Translation: CAG30428.1.
AC005529 Genomic DNA. No translation available.
BC003615 mRNA. Translation: AAH03615.1.
AJ006069 mRNA. Translation: CAA06841.1.
CCDSCCDS13859.1.
PIRI39463.
RefSeqNP_001002877.1. NM_001002877.1.
NP_001002878.1. NM_001002878.1.
NP_001002879.1. NM_001002879.1.
NP_003669.4. NM_003678.4.
UniGeneHs.75361.

3D structure databases

ProteinModelPortalQ13769.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114132. 28 interactions.
IntActQ13769. 10 interactions.
MINTMINT-4532759.
STRING9606.ENSP00000380969.

PTM databases

PhosphoSiteQ13769.

Polymorphism databases

DMDM259016156.

Proteomic databases

MaxQBQ13769.
PaxDbQ13769.
PRIDEQ13769.

Protocols and materials databases

DNASU8563.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397871; ENSP00000380969; ENSG00000100296.
ENST00000397872; ENSP00000380970; ENSG00000100296.
ENST00000397873; ENSP00000380971; ENSG00000100296.
ENST00000490103; ENSP00000420306; ENSG00000100296.
GeneID8563.
KEGGhsa:8563.
UCSCuc003afq.3. human.

Organism-specific databases

CTD8563.
GeneCardsGC22M029901.
HGNCHGNC:19074. THOC5.
HPAHPA029812.
HPA048402.
MIM612733. gene.
neXtProtNX_Q13769.
PharmGKBPA38188.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266546.
HOGENOMHOG000007514.
HOVERGENHBG051271.
InParanoidQ13769.
KOK13174.
OMAYYMALVE.
OrthoDBEOG7XPZ5G.
PhylomeDBQ13769.
TreeFamTF314812.

Gene expression databases

ArrayExpressQ13769.
BgeeQ13769.
CleanExHS_THOC5.
GenevestigatorQ13769.

Family and domain databases

InterProIPR019163. THO_Thoc5.
[Graphical view]
PfamPF09766. FimP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTHOC5.
GenomeRNAi8563.
NextBio32099.
PROQ13769.
SOURCESearch...

Entry information

Entry nameTHOC5_HUMAN
AccessionPrimary (citable) accession number: Q13769
Secondary accession number(s): O60839, Q9UPZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 116 of the entry and version 2 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM