Skip Header

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

THO complex subunit 6 homolog

Gene

THOC6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Plays a role in apoptosis negative control involved in brain development.5 Publications

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • central nervous system development Source: UniProtKB
  • mRNA 3'-end processing Source: Reactome
  • mRNA export from nucleus Source: UniProtKB
  • negative regulation of apoptotic process 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 - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, 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.
SignaLinkiQ86W42.

Names & Taxonomyi

Protein namesi
Recommended name:
THO complex subunit 6 homolog
Alternative name(s):
Functional spliceosome-associated protein 35
Short name:
fSAP35
WD repeat-containing protein 58
Gene namesi
Name:THOC6
Synonyms:WDR58
ORF Names:PSEC0006
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:28369. THOC6.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • 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

Beaulieu-Boycott-Innes syndrome (BBIS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive neurodevelopmental disorder characterized by delayed development, moderate intellectual disability, and dysmorphic facial features. Other developmental anomalies, such as cardiac and renal defects, may also occur.
See also OMIM:613680
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461G → R in BBIS; localizes to the cytoplasm and not to the nucleus. 1 Publication
Corresponds to variant rs587777030 [ dbSNP | Ensembl ].
VAR_069779

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiTHOC6.
MIMi613680. phenotype.
Orphaneti363444. Developmental delay-microcephaly-facial dysmorphism syndrome, Hutterite type.
PharmGKBiPA142670592.

Polymorphism and mutation databases

BioMutaiTHOC6.
DMDMi74759455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341THO complex subunit 6 homologPRO_0000233158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ86W42.
MaxQBiQ86W42.
PaxDbiQ86W42.
PeptideAtlasiQ86W42.
PRIDEiQ86W42.

PTM databases

iPTMnetiQ86W42.
PhosphoSiteiQ86W42.

Expressioni

Gene expression databases

BgeeiQ86W42.
CleanExiHS_THOC6.
GenevisibleiQ86W42. HS.

Organism-specific databases

HPAiHPA052953.

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.2 Publications

Protein-protein interaction databases

BioGridi122605. 43 interactions.
IntActiQ86W42. 17 interactions.
MINTiMINT-4994871.
STRINGi9606.ENSP00000326531.

Structurei

3D structure databases

ProteinModelPortaliQ86W42.
SMRiQ86W42. Positions 22-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati22 – 6140WD 1Add
BLAST
Repeati74 – 11239WD 2Add
BLAST
Repeati124 – 16542WD 3Add
BLAST
Repeati166 – 20540WD 4Add
BLAST
Repeati215 – 25440WD 5Add
BLAST
Repeati256 – 29338WD 6Add
BLAST
Repeati295 – 33945WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat THOC6 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0649. Eukaryota.
ENOG410XTCD. LUCA.
GeneTreeiENSGT00390000015278.
HOGENOMiHOG000008085.
HOVERGENiHBG079643.
InParanoidiQ86W42.
KOiK13175.
OMAiGRCVNQW.
OrthoDBiEOG7Z69CM.
PhylomeDBiQ86W42.
TreeFamiTF324760.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86W42-1) [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
MERAVPLAVP LGQTEVFQAL QRLHMTIFSQ SVSPCGKFLA AGNNYGQIAI
60 70 80 90 100
FSLSSALSSE AKEESKKPVV TFQAHDGPVY SMVSTDRHLL SAGDGEVKAW
110 120 130 140 150
LWAEMLKKGC KELWRRQPPY RTSLEVPEIN ALLLVPKENS LILAGGDCQL
160 170 180 190 200
HTMDLETGTF TRVLRGHTDY IHCLALRERS PEVLSGGEDG AVRLWDLRTA
210 220 230 240 250
KEVQTIEVYK HEECSRPHNG RWIGCLATDS DWMVCGGGPA LTLWHLRSST
260 270 280 290 300
PTTIFPIRAP QKHVTFYQDL ILSAGQGRCV NQWQLSGELK AQVPGSSPGL
310 320 330 340
LSLSLNQQPA APECKVLTAA GNSCRVDVFT NLGYRAFSLS F
Length:341
Mass (Da):37,535
Last modified:June 1, 2003 - v1
Checksum:iE854A8959F245FA9
GO
Isoform 2 (identifier: Q86W42-2) [UniParc]FASTAAdd to basket

Also known as: hTREX40

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.

Note: No experimental confirmation available.
Show »
Length:317
Mass (Da):34,849
Checksum:i1773CC1DBB1D65D9
GO
Isoform 3 (identifier: Q86W42-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     271-315: Missing.

Note: No experimental confirmation available.
Show »
Length:296
Mass (Da):32,891
Checksum:iC5B89BE0F3BC0B96
GO

Sequence cautioni

The sequence BAG36782.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971V → E in BAC11552 (PubMed:14702039).Curated
Sequence conflicti121 – 1211R → S in BAG36782 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461G → R in BBIS; localizes to the cytoplasm and not to the nucleus. 1 Publication
Corresponds to variant rs587777030 [ dbSNP | Ensembl ].
VAR_069779

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424Missing in isoform 2. 1 PublicationVSP_018079Add
BLAST
Alternative sequencei271 – 31545Missing in isoform 3. 1 PublicationVSP_018078Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075330 mRNA. Translation: BAC11552.1.
AK314086 mRNA. Translation: BAG36782.1. Different initiation.
BC003118 mRNA. Translation: AAH03118.1.
BC050674 mRNA. Translation: AAH50674.1.
CCDSiCCDS10491.1. [Q86W42-1]
CCDS45392.1. [Q86W42-3]
RefSeqiNP_001135822.1. NM_001142350.1. [Q86W42-3]
NP_077315.2. NM_024339.3. [Q86W42-1]
UniGeneiHs.412304.

Genome annotation databases

EnsembliENST00000253952; ENSP00000253952; ENSG00000131652. [Q86W42-3]
ENST00000326266; ENSP00000326531; ENSG00000131652. [Q86W42-1]
ENST00000574549; ENSP00000458295; ENSG00000131652. [Q86W42-2]
ENST00000575576; ENSP00000460015; ENSG00000131652. [Q86W42-2]
GeneIDi79228.
KEGGihsa:79228.
UCSCiuc002cta.2. human. [Q86W42-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075330 mRNA. Translation: BAC11552.1.
AK314086 mRNA. Translation: BAG36782.1. Different initiation.
BC003118 mRNA. Translation: AAH03118.1.
BC050674 mRNA. Translation: AAH50674.1.
CCDSiCCDS10491.1. [Q86W42-1]
CCDS45392.1. [Q86W42-3]
RefSeqiNP_001135822.1. NM_001142350.1. [Q86W42-3]
NP_077315.2. NM_024339.3. [Q86W42-1]
UniGeneiHs.412304.

3D structure databases

ProteinModelPortaliQ86W42.
SMRiQ86W42. Positions 22-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122605. 43 interactions.
IntActiQ86W42. 17 interactions.
MINTiMINT-4994871.
STRINGi9606.ENSP00000326531.

PTM databases

iPTMnetiQ86W42.
PhosphoSiteiQ86W42.

Polymorphism and mutation databases

BioMutaiTHOC6.
DMDMi74759455.

Proteomic databases

EPDiQ86W42.
MaxQBiQ86W42.
PaxDbiQ86W42.
PeptideAtlasiQ86W42.
PRIDEiQ86W42.

Protocols and materials databases

DNASUi79228.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000253952; ENSP00000253952; ENSG00000131652. [Q86W42-3]
ENST00000326266; ENSP00000326531; ENSG00000131652. [Q86W42-1]
ENST00000574549; ENSP00000458295; ENSG00000131652. [Q86W42-2]
ENST00000575576; ENSP00000460015; ENSG00000131652. [Q86W42-2]
GeneIDi79228.
KEGGihsa:79228.
UCSCiuc002cta.2. human. [Q86W42-1]

Organism-specific databases

CTDi79228.
GeneCardsiTHOC6.
H-InvDBHIX0012753.
HGNCiHGNC:28369. THOC6.
HPAiHPA052953.
MalaCardsiTHOC6.
MIMi613680. phenotype.
615403. gene.
neXtProtiNX_Q86W42.
Orphaneti363444. Developmental delay-microcephaly-facial dysmorphism syndrome, Hutterite type.
PharmGKBiPA142670592.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0649. Eukaryota.
ENOG410XTCD. LUCA.
GeneTreeiENSGT00390000015278.
HOGENOMiHOG000008085.
HOVERGENiHBG079643.
InParanoidiQ86W42.
KOiK13175.
OMAiGRCVNQW.
OrthoDBiEOG7Z69CM.
PhylomeDBiQ86W42.
TreeFamiTF324760.

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.
SignaLinkiQ86W42.

Miscellaneous databases

ChiTaRSiTHOC6. human.
GenomeRNAii79228.
PROiQ86W42.
SOURCEiSearch...

Gene expression databases

BgeeiQ86W42.
CleanExiHS_THOC6.
GenevisibleiQ86W42. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 3).
    Tissue: Neuroblastoma and Teratocarcinoma.
  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] (ISOFORMS 1 AND 2).
    Tissue: Lung and Testis.
  3. "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.
  4. "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.
  5. "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.
  6. "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.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  9. Cited for: FUNCTION, SUBCELLULAR LOCATION, VARIANT BBIS ARG-46, CHARACTERIZATION OF VARIANT BBIS ARG-46.

Entry informationi

Entry nameiTHOC6_HUMAN
AccessioniPrimary (citable) accession number: Q86W42
Secondary accession number(s): B2RA85, Q8NBR1, Q9BTV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 125 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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.