THO complex subunit THP2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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O13539 (THP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
THO complex subunit THP2

Gene names

Name:	THP2
Ordered Locus Names:	YHR167W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA. Ref.4 Ref.6 Ref.7 Ref.10
Subunit structure	Component of the THO complex, which is composed of HPR1, MFT1, THO2 and THP2. Together with SUB2, TEX1 and YRA1, THO forms the transcription/export (TREX) complex. THO associates with DNA and RNA in vitro. Ref.3 Ref.5
Subcellular location	Nucleus Ref.3 Ref.8.
Miscellaneous	Present with 2840 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from mutant phenotype Ref.3. Source: SGD mRNA export from nucleus Inferred from mutant phenotype Ref.5. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription elongation from RNA polymerase II promoter Inferred from mutant phenotype Ref.4. Source: SGD
Cellular_component	THO complex part of transcription export complex Inferred from physical interaction Ref.5. Source: SGD nucleoplasmic THO complex Inferred from physical interaction Ref.3. Source: SGD
Molecular_function	nucleic acid binding Inferred from direct assay Ref.4. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MFT1	P33441	4	EBI-30898,EBI-10841

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

THO complex subunit THP2

PRO_0000267642

Amino acid modifications

Modified residue

249

Phosphoserine Ref.11

Sequences

Sequence

Length

Mass (Da)

Tools

O13539 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 16EFA6F464507C57
Show »

FASTA

261

30,299

        10         20         30         40         50         60 
MTKEEGRTYF ESLCEEEQSL QESQTHLLNI LDILSVLADP RSSDDLLTES LKKLPDLHRE 

        70         80         90        100        110        120 
LINSSIRLRY DKYQTREAQL LEDTKTGRDV AAGVQNPKSI SEYYSTFEHL NRDTLRYINL 

       130        140        150        160        170        180 
LKRLSVDLAK QVEVSDPSVT VYEMDKWVPS EKLQGILEQY CAPDTDIRGV DAQIKNYLDQ 

       190        200        210        220        230        240 
IKMARAKFGL ENKYSLKERL STLTKELNHW RKEWDDIEML MFGDDAHSMK KMIQKIDSLK 

       250        260 
SEINAPSESY PVDKEGDIVL E

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M. Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae." Chavez S., Beilharz T., Rondon A.G., Erdjument-Bromage H., Tempst P., Svejstrup J.Q., Lithgow T., Aguilera A. EMBO J. 19:5824-5834(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THO COMPLEX, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[4]	"The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability." Jimeno S., Rondon A.G., Luna R., Aguilera A. EMBO J. 21:3526-3535(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"TREX is a conserved complex coupling transcription with messenger RNA export." Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M., Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R., Hurt E. Nature 417:304-308(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN TREX COMPLEX, MASS SPECTROMETRY.
[6]	"Molecular evidence that the eukaryotic THO/TREX complex is required for efficient transcription elongation." Rondon A.G., Jimeno S., Garcia-Rubio M., Aguilera A. J. Biol. Chem. 278:39037-39043(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination." Huertas P., Aguilera A. Mol. Cell 12:711-721(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes." Abruzzi K.C., Lacadie S., Rosbash M. EMBO J. 23:2620-2631(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00027 Genomic DNA. Translation: AAB68025.1. BK006934 Genomic DNA. Translation: DAA06860.1.
PIR	S52609.
RefSeq	NP_012037.1. NM_001179298.1.
3D structure databases
ProteinModelPortal	O13539.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4246N.
IntAct	O13539. 30 interactions.
MINT	MINT-473610.
STRING	4932.YHR167W.
Proteomic databases
PaxDb	O13539.
PeptideAtlas	O13539.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR167W; YHR167W; YHR167W.
GeneID	856572.
KEGG	sce:YHR167W.
Organism-specific databases
CYGD	YHR167w.
SGD	S000001210. THP2.
Phylogenomic databases
eggNOG	NOG72311.
HOGENOM	HOG000000890.
OMA	INSSEIR.
OrthoDB	EOG43JGF9.
Gene expression databases
Genevestigator	O13539.
GermOnline	YHR167W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR018557. THO_cplx_su_THP2. [Graphical view]
Pfam	PF09432. THP2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982420.

Entry information

Entry name

THP2_YEAST

Accession

Primary (citable) accession number: O13539
Secondary accession number(s): D3DLB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents