Q6I9Y2 (THOC7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
THO complex subunit 7 homolog

Alternative name(s):
Functional spliceosome-associated protein 24
Short name=fSAP24
Ngg1-interacting factor 3-like protein 1-binding protein 1
Short name=NIF3L1-binding protein 1
hTREX30

Gene names

Name:	THOC7
Synonyms:	NIF3L1BP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It 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. The recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. DDX39B functions as a bridge between ALYREF/THOC4 and the THO complex. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. The recruitment of the TREX complex to the intronless viral mRNA occurs via an interaction between KSHV ORF57 protein and ALYREF/THOC4. Ref.7 Ref.8 Ref.9 Ref.10
Subunit structure	Component of the THO complex, which is composed of THOC1, THOC2, THOC5, THOC6 and THOC7. Together with THOC3, ALYREF/THOC4 and DDX39B, THO forms the transcription/export (TREX) complex. Interacts with NIF3L1 and THOC5. Ref.6 Ref.7 Ref.8 Ref.11
Subcellular location	Cytoplasm. Nucleus. Note: Interaction with THOC5 is required for nuclear localization. Ref.6 Ref.11
Sequence similarities	Belongs to the THOC7 family.

Ontologies

Keywords
Biological process	Transport mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
Ligand	RNA-binding
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW intronless viral mRNA export from host nucleus Inferred from direct assay Ref.10. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	THO complex part of transcription export complex Inferred from direct assay Ref.8. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 204	204	THO complex subunit 7 homolog		PRO_0000310754
Regions
	Region	50 – 137	88	Interaction with THOC5
	Region	105 – 204	100	Interaction with NIF3L1
	Coiled coil	75 – 194	120	Potential
Amino acid modifications
	Modified residue	36	1	N6-acetyllysine Ref.12
Experimental info
	Sequence conflict	23	1	D → G in BAB15656. Ref.1
	Sequence conflict	187	1	L → P in CAG33654. Ref.2
	Sequence conflict	200	1	T → S in BAB15656. Ref.1
	Sequence conflict	200	1	T → S in CAG33654. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6I9Y2 [UniParc]. Last modified May 5, 2009. Version 3. Checksum: CB0D2608A23E5BFC	FASTA	204	23,743
	10 20 30 40 50 60 MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY QRMLSTLSQC 70 80 90 100 110 120 EFSMGKTLLV YDMNLREMEN YEKIYKEIEC SIAGAHEKIA ECKKQILQAK RIRKNRQEYD 130 140 150 160 170 180 ALAKVIQHHP DRHETLKELE ALGKELEHLS HIKESVEDKL ELRRKQFHVL LSTIHELQQT 190 200 LENDEKLSEV EEAQEASMET DPKP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]. Tissue: Small intestine.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Skin and Testis.
[6]	"Identification and characterization of NIF3L1 BP1, a novel cytoplasmic interaction partner of the NIF3L1 protein." Tascou S., Kang T.W., Trappe R., Engel W., Burfeind P. Biochem. Biophys. Res. Commun. 309:440-448(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NIF3L1, SUBCELLULAR LOCATION.
[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, 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, 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]	"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.
[11]	"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 THOC5.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, MASS SPECTROMETRY.
[13]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK027098 mRNA. Translation: BAB15656.1. CR457373 mRNA. Translation: CAG33654.1. AC104162 Genomic DNA. No translation available. CH471055 Genomic DNA. Translation: EAW65418.1. BC020599 mRNA. Translation: AAH20599.2. BC065012 mRNA. Translation: AAH65012.1.
IPI	IPI00291131.
RefSeq	NP_079351.2. NM_025075.2.
UniGene	Hs.288151.
3D structure databases
ProteinModelPortal	Q6I9Y2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6I9Y2. 4 interactions.
MINT	MINT-1374910.
STRING	9606.ENSP00000295899.
PTM databases
PhosphoSite	Q6I9Y2.
Polymorphism databases
DMDM	229462996.
Proteomic databases
PaxDb	Q6I9Y2.
PRIDE	Q6I9Y2.
Protocols and materials databases
DNASU	80145.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295899; ENSP00000295899; ENSG00000163634.
GeneID	80145.
KEGG	hsa:80145.
UCSC	uc003dlt.4. human.
Organism-specific databases
CTD	80145.
GeneCards	GC03M063795.
H-InvDB	HIX0003418.
HGNC	HGNC:29874. THOC7.
HPA	HPA044143.
MIM	611965. gene.
neXtProt	NX_Q6I9Y2.
PharmGKB	PA144596266.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG298141.
HOGENOM	HOG000044589.
HOVERGEN	HBG061300.
InParanoid	Q6I9Y2.
KO	K13176.
OMA	LRKKQFH.
OrthoDB	EOG4VX269.
PhylomeDB	Q6I9Y2.
Gene expression databases
Bgee	Q6I9Y2.
CleanEx	HS_THOC7.
Genevestigator	Q6I9Y2.
Family and domain databases
InterPro	IPR018018. THOC7. IPR008501. THOC7/Mft1. [Graphical view]
PANTHER	PTHR14854. PTHR14854. 1 hit.
Pfam	PF05615. THOC7. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	80145.
NextBio	70418.
SOURCE	Search...

Entry information

Entry name

THOC7_HUMAN

Accession

Primary (citable) accession number: Q6I9Y2
Secondary accession number(s): Q6P1L3, Q8WUF2, Q9H5H0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 5, 2009
Last modified:	April 3, 2013
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.