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Q13769

- THOC5_HUMAN

UniProt

Q13769 - THOC5_HUMAN

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Protein

THO complex subunit 5 homolog

Gene
THOC5, C22orf19, KIAA0983
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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; probably mediates association of the TREX and CFIm complexes.8 Publications
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.8 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. monocyte differentiation 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 macrophage differentiation Source: Ensembl
  6. positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  7. primitive hemopoiesis Source: UniProtKB
  8. RNA splicing Source: UniProtKB-KW
  9. viral mRNA export from host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation, mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:THOC5
Synonyms:C22orf19, KIAA0983
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:19074. THOC5.

Subcellular locationi

Nucleus. Nucleus speckle Inferred. Cytoplasm By similarity
Note: Shuttles between nucleus and cytoplasm.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nuclear speck Source: UniProtKB-SubCell
  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
Mutagenesisi225 – 2251Y → F: Impairs mRNA binding, enhances CXCL12-dependent cell migration. 1 Publication

Organism-specific databases

PharmGKBiPA38188.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 683682THO complex subunit 5 homologPRO_0000079577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei225 – 2251Phosphotyrosine; by SRC2 Publications
Modified residuei307 – 3071Phosphoserine5 Publications
Modified residuei312 – 3121Phosphoserine5 Publications
Modified residuei314 – 3141Phosphoserine5 Publications
Modified residuei328 – 3281Phosphothreonine1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13769.
PaxDbiQ13769.
PRIDEiQ13769.

PTM databases

PhosphoSiteiQ13769.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

ArrayExpressiQ13769.
BgeeiQ13769.
CleanExiHS_THOC5.
GenevestigatoriQ13769.

Organism-specific databases

HPAiHPA029812.
HPA048402.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TAP1Q035184EBI-5280316,EBI-747259
THOC1Q96FV95EBI-5280316,EBI-1765605
THOC7Q6I9Y27EBI-5280316,EBI-716286

Protein-protein interaction databases

BioGridi114132. 28 interactions.
IntActiQ13769. 10 interactions.
MINTiMINT-4532759.
STRINGi9606.ENSP00000380969.

Structurei

3D structure databases

ProteinModelPortaliQ13769.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 199198Interaction with THOC7Add
BLAST
Regioni2 – 144143Interaction with CSF1R By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi7 – 104Nuclear localization signal By similarity

Sequence similaritiesi

Belongs to the THOC5 family.

Phylogenomic databases

eggNOGiNOG266546.
HOGENOMiHOG000007514.
HOVERGENiHBG051271.
InParanoidiQ13769.
KOiK13174.
OMAiYYMALVE.
OrthoDBiEOG7XPZ5G.
PhylomeDBiQ13769.
TreeFamiTF314812.

Family and domain databases

InterProiIPR019163. THO_Thoc5.
[Graphical view]
PfamiPF09766. FimP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13769-1 [UniParc]FASTAAdd to Basket

« Hide

MSSESSKKRK PKVIRSDGAP AEGKRNRSDT EQEGKYYSEE AEVDLRDPGR    50
DYELYKYTCQ ELQRLMAEIQ DLKSRGGKDV AIEIEERRIQ SCVHFMTLKK 100
LNRLAHIRLK KGRDQTHEAK QKVDAYHLQL QNLLYEVMHL QKEITKCLEF 150
KSKHEEIDLV SLEEFYKEAP PDISKAEVTM GDPHQQTLAR LDWELEQRKR 200
LAEKYRECLS NKEKILKEIE VKKEYLSSLQ PRLNSIMQAS LPVQEYLFMP 250
FDQAHKQYET ARHLPPPLYV LFVQATAYGQ ACDKTLSVAI EGSVDEAKAL 300
FKPPEDSQDD ESDSDAEEEQ TTKRRRPTLG VQLDDKRKEM LKRHPLSVML 350
DLKCKDDSVL HLTFYYLMNL NIMTVKAKVT TAMELITPIS AGDLLSPDSV 400
LSCLYPGDHG KKTPNPANQY QFDKVGILTL SDYVLELGHP YLWVQKLGGL 450
HFPKEQPQQT VIADHSLSAS HMETTMKLLK TRVQSRLALH KQFASLEHGI 500
VPVTSDCQYL FPAKVVSRLV KWVTVAHEDY MELHFTKDIV DAGLAGDTNL 550
YYMALIERGT AKLQAAVVLN PGYSSIPPVF QLCLNWKGEK TNSNDDNIRA 600
MEGEVNVCYK ELCGPWPSHQ LLTNQLQRLC VLLDVYLETE SHDDSVEGPK 650
EFPQEKMCLR LFRGPSRMKP FKYNHPQGFF SHR 683
Length:683
Mass (Da):78,508
Last modified:September 22, 2009 - v2
Checksum:i59550FA548835016
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti380 – 3801T → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035692
Natural varianti475 – 4751T → S.
Corresponds to variant rs8141153 [ dbSNP | Ensembl ].
VAR_037134
Natural varianti499 – 4991G → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_035693
Natural varianti525 – 5251V → I.4 Publications
Corresponds to variant rs737976 [ dbSNP | Ensembl ].
VAR_037135
Natural varianti579 – 5791V → I.3 Publications
Corresponds to variant rs1049534 [ dbSNP | Ensembl ].
VAR_021410

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13859.1.
PIRiI39463.
RefSeqiNP_001002877.1. NM_001002877.1.
NP_001002878.1. NM_001002878.1.
NP_001002879.1. NM_001002879.1.
NP_003669.4. NM_003678.4.
UniGeneiHs.75361.

Genome annotation databases

EnsembliENST00000397871; ENSP00000380969; ENSG00000100296.
ENST00000397872; ENSP00000380970; ENSG00000100296.
ENST00000397873; ENSP00000380971; ENSG00000100296.
ENST00000490103; ENSP00000420306; ENSG00000100296.
GeneIDi8563.
KEGGihsa:8563.
UCSCiuc003afq.3. human.

Polymorphism databases

DMDMi259016156.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13859.1.
PIRi I39463.
RefSeqi NP_001002877.1. NM_001002877.1.
NP_001002878.1. NM_001002878.1.
NP_001002879.1. NM_001002879.1.
NP_003669.4. NM_003678.4.
UniGenei Hs.75361.

3D structure databases

ProteinModelPortali Q13769.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114132. 28 interactions.
IntActi Q13769. 10 interactions.
MINTi MINT-4532759.
STRINGi 9606.ENSP00000380969.

PTM databases

PhosphoSitei Q13769.

Polymorphism databases

DMDMi 259016156.

Proteomic databases

MaxQBi Q13769.
PaxDbi Q13769.
PRIDEi Q13769.

Protocols and materials databases

DNASUi 8563.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000397871 ; ENSP00000380969 ; ENSG00000100296 .
ENST00000397872 ; ENSP00000380970 ; ENSG00000100296 .
ENST00000397873 ; ENSP00000380971 ; ENSG00000100296 .
ENST00000490103 ; ENSP00000420306 ; ENSG00000100296 .
GeneIDi 8563.
KEGGi hsa:8563.
UCSCi uc003afq.3. human.

Organism-specific databases

CTDi 8563.
GeneCardsi GC22M029901.
HGNCi HGNC:19074. THOC5.
HPAi HPA029812.
HPA048402.
MIMi 612733. gene.
neXtProti NX_Q13769.
PharmGKBi PA38188.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266546.
HOGENOMi HOG000007514.
HOVERGENi HBG051271.
InParanoidi Q13769.
KOi K13174.
OMAi YYMALVE.
OrthoDBi EOG7XPZ5G.
PhylomeDBi Q13769.
TreeFami TF314812.

Miscellaneous databases

GeneWikii THOC5.
GenomeRNAii 8563.
NextBioi 32099.
PROi Q13769.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13769.
Bgeei Q13769.
CleanExi HS_THOC5.
Genevestigatori Q13769.

Family and domain databases

InterProi IPR019163. THO_Thoc5.
[Graphical view ]
Pfami PF09766. FimP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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. 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. Cited for: FUNCTION.
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  24. Cited for: INTERACTION WITH NXF1.
  25. "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.
  26. "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.
  27. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-380 AND SER-499.

Entry informationi

Entry nameiTHOC5_HUMAN
AccessioniPrimary (citable) accession number: Q13769
Secondary accession number(s): O60839, Q9UPZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: September 22, 2009
Last modified: September 3, 2014
This is version 117 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 22
    Human chromosome 22: 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

External Data

Dasty 3

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