Protein PTI1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P39927 (PTI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 112. History...

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

Documents (2) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Protein PTI1

Gene names

Name:	PTI1
Ordered Locus Names:	YGR156W
ORF Names:	G6670

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	425 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. PTI1 is required for 3'-end formation of snoRNAs. Ref.6
Subunit structure	Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Component of the APT complex, which is a subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2. Ref.8
Subcellular location	Nucleus Ref.8.
Miscellaneous	Present with 937 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA cleavage Inferred from mutant phenotype PubMed 12504017. Source: SGD mRNA polyadenylation Inferred from mutant phenotype PubMed 12504017. Source: SGD snoRNA 3'-end processing Inferred from mutant phenotype Ref.6. Source: SGD termination of RNA polymerase II transcription, exosome-dependent Inferred from mutant phenotype Ref.6. Source: SGD termination of RNA polymerase II transcription, poly(A)-coupled Inferred from physical interaction Ref.8. Source: SGD
Cellular_component	mRNA cleavage and polyadenylation specificity factor complex Inferred from direct assay Ref.8. Source: SGD
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 425

425

Protein PTI1

PRO_0000076294

Amino acid modifications

Modified residue

177

Phosphoserine Ref.10

Modified residue

268

Phosphoserine Ref.10

Modified residue

271

Phosphothreonine Ref.10

Modified residue

272

Phosphoserine Ref.10

Modified residue

274

Phosphoserine Ref.10

Modified residue

276

Phosphothreonine Ref.9

Experimental info

Sequence conflict

300

N → Y in BAA03953. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P39927 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: F6564311A2B1F240
Show »

FASTA

425

46,983

        10         20         30         40         50         60 
MTDPRRRTGR HFLTPENLSS TLQITNLPPE WNQDIITSVV AGSGPVIDIK AKNDPRTGKL 

        70         80         90        100        110        120 
TGVLFDYLTS KDCKRAWEIL NRIENFPVKI EQIIPPNYKD HLRETANKNS QKQVLQLNRD 

       130        140        150        160        170        180 
SYPFEAGLEL PFEMVTEVPI PRRPPPPQAA NNTNSVSNNT NIQFPDILSK ASKHLPSFQD 

       190        200        210        220        230        240 
GSIIAPDKIS QNLSKIPPLQ LIEIISNLKI LSNQENIQKS QLESFLDTNS DITISVTQAL 

       250        260        270        280        290        300 
LEMGFIDYSV VTKVLKSQVG EAPSLLSSNN TSNSNTPVSV IRNNTPLHVP SNEVSNNPNN 

       310        320        330        340        350        360 
MPLNVAMPMP MSTPPFIPLP LQQQPFGFAP PGPFMPPAQG PSMGQPVLAN QLGQVQQQNI 

       370        380        390        400        410        420 
SSTEGPSNAN KANDSGTINM AKLQLLPENQ QDMIKQVLTL TPAQIQSLPS DQQLMVENFR 


KEYII

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Ono B., Inoue T., Kijima K., Matsuda A., Negishi K., Shinoda S. Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A5-8-1A.
[2]	"The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames." Skala J., Nawrocki A., Goffeau A. Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Pti1p and Ref2p found in association with the mRNA 3' end formation complex direct snoRNA maturation." Dheur S., Vo le T.A., Voisinet-Hakil F., Minet M., Schmitter J.-M., Lacroute F., Wyers F., Minvielle-Sebastia L. EMBO J. 22:2831-2840(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SNORNA 3-END FORMATION.
[7]	"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].
[8]	"Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends." Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T., Buratowski S., Moore C.L., Greenblatt J. J. Biol. Chem. 278:33000-33010(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CPF COMPLEX, COMPOSITION OF THE APT COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"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-177; SER-268; THR-271; SER-272 AND SER-274, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16502 Genomic DNA. Translation: BAA03953.1. X85807 Genomic DNA. Translation: CAA59813.1. Z72941 Genomic DNA. Translation: CAA97170.1. AY557841 Genomic DNA. Translation: AAS56167.1. BK006941 Genomic DNA. Translation: DAA08247.1.
PIR	S60446.
RefSeq	NP_011672.1. NM_001181285.1.
3D structure databases
ProteinModelPortal	P39927.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4402N.
IntAct	P39927. 14 interactions.
MINT	MINT-562054.
STRING	4932.YGR156W.
Proteomic databases
PaxDb	P39927.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR156W; YGR156W; YGR156W.
GeneID	853060.
KEGG	sce:YGR156W.
Organism-specific databases
CYGD	YGR156w.
SGD	S000003388. PTI1.
Phylogenomic databases
eggNOG	NOG148794.
HOGENOM	HOG000000936.
KO	K14407.
OMA	LLMGFID.
OrthoDB	EOG4V72S0.
Enzyme and pathway databases
BioCyc	YEAST:G3O-30857-MONOMER.
Gene expression databases
Genevestigator	P39927.
GermOnline	YGR156W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR025742. CSTF2_hinge. IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF14327. CSTF2_hinge. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972995.

Entry information

Entry name

PTI1_YEAST

Accession

Primary (citable) accession number: P39927
Secondary accession number(s): D6VUT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1996
Last modified:	May 29, 2013
This is version 112 of the entry and version 2 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 VII

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

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents