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Q03654 (CEF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-mRNA-splicing factor CEF1
Alternative name(s):
PRP nineteen-associated complex protein 85
PRP19-associated complex protein 85
Gene names
Name:CEF1
Synonyms:NTC85
Ordered Locus Names:YMR213W
ORF Names:YM8261.07
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in pre-mRNA splicing and cell cycle control. Required for the binding of the NTC complex (or PRP19-associated complex) components to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. Its absence leads to an arrest of the cell cycle, possibly due to the inefficient splicing of TUB1. Ref.4 Ref.5 Ref.7 Ref.8

Subunit structure

Belongs to the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CLF1, ISY1, NTC20, PRP19, PRP46, SYF1 and SYF2. Ref.4 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleus Ref.13.

Miscellaneous

Present with 784 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the CEF1 family.

Contains 2 HTH myb-type DNA-binding domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 590590Pre-mRNA-splicing factor CEF1
PRO_0000197107

Regions

Domain1 – 6060HTH myb-type 1
Domain63 – 11048HTH myb-type 2
DNA binding33 – 5624H-T-H motif By similarity
DNA binding84 – 10623H-T-H motif By similarity
Region460 – 49031Interaction with PRP19 and self-interaction
Compositional bias238 – 32184Lys-rich

Experimental info

Mutagenesis331W → G: No effect. Slower growth and thermosensitivity; when associated with G-84. Complete loss of function; when associated with G-52 and G-84. Complete loss of function; when associated with G-52; G-84 and G-102. Ref.7
Mutagenesis521W → G: No effect. Slower growth and thermosensitivity; when associated with G-84. Complete loss of function; when associated with G-33 and G-84. Complete loss of function; when associated with G-33; G-84 and G-102. Ref.5 Ref.7
Mutagenesis841W → G: No effect. Slower growth and thermosensitivity; when associated with G-33 or G-52. Complete loss of function; when associated with G-33 and G-52 or G-52 and Y-102. Complete loss of function; when associated with G-33; G-52 and G-102. Ref.5 Ref.7
Mutagenesis1021Y → G: No effect. Slower growth and thermosensitivity; when associated with G-52 or G-84. Complete loss of function; when associated with G-33; G-52 and G-84. Ref.7
Sequence conflict111G → E AA sequence Ref.4
Sequence conflict1921K → E in AAT93161. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q03654 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A4C417A8B330EA9C

FASTA59067,731
        10         20         30         40         50         60 
MPPVPIYVKG GVWTNVEDQI LKAAVQKYGT HQWSKVASLL QKKTARQSEL RWNEYLNPKL 

        70         80         90        100        110        120 
NFTEFSKEED AQLLDLAREL PNQWRTIADM MARPAQVCVE RYNRLLESED SGGAALSTGV 

       130        140        150        160        170        180 
TDLKAGDINP NAETQMARPD NGDLEDEEKE MLAEARARLL NTQGKKATRK IRERMLEESK 

       190        200        210        220        230        240 
RIAELQKRRE LKQAGINVAI KKPKKKYGTD IDYNEDIVYE QAPMPGIYDT STEDRQIKKK 

       250        260        270        280        290        300 
FEQFERKVNR KGLDGNKDKP SKKNKDKKRK HDENEHVEKA ALGESTTLTD EYKKPKLILS 

       310        320        330        340        350        360 
APGTKQGKVT YKKKLESKRQ KLIEAQATGT VLTPKELLPH DSGQEDNERS NIKSGKQLKS 

       370        380        390        400        410        420 
RIRKFLVQMF ASLPSPKNDF EIVLSEDEKE EDAEIAEYEK EFENERAMNE EDNFIEPPSQ 

       430        440        450        460        470        480 
NDAPRVSLVA VPLAYSTLPI PEFKNNPQSA IDNKYNLLVA NAINKEPHMV PEDTVDFLKE 

       490        500        510        520        530        540 
VESRMQHITQ GRTSMKIQFK TAMPPTEVLL ESIQSKVESI EQLQRKLQHV QPLEQQNNEM 

       550        560        570        580        590 
CSTLCHHSLP ALIEGQRKYY ADYYAYRQEI RSLEGRRKRL QAMLNSSSSI 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Cef1p is a component of the Prp19p-associated complex and essential for pre-mRNA splicing."
Tsai W.-Y., Chow Y.-T., Chen H.-R., Huang K.-T., Hong R.-I., Jan S.-P., Kuo N.-Y., Tsao T.Y., Chen C.-H., Cheng S.-C.
J. Biol. Chem. 274:9455-9462(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-16, FUNCTION, DOMAIN, IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
[5]"Removal of a single alpha-tubulin gene intron suppresses cell cycle arrest phenotypes of splicing factor mutations in Saccharomyces cerevisiae."
Burns C.G., Ohi R., Mehta S., O'Toole E.T., Winey M., Clark T.A., Sugnet C.W., Ares M. Jr., Gould K.L.
Mol. Cell. Biol. 22:801-815(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-52 AND TRP-84.
[6]"Snt309p, a component of the Prp19p-associated complex that interacts with Prp19p and associates with the spliceosome simultaneously with or immediately after dissociation of U4 in the same manner as Prp19p."
Chen H.-R., Jan S.-P., Tsao T.Y., Sheu Y.-J., Banroques J., Cheng S.-C.
Mol. Cell. Biol. 18:2196-2204(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRP19, IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
[7]"Myb-related Schizosaccharomyces pombe cdc5p is structurally and functionally conserved in eukaryotes."
Ohi R., Feoktistova A., McCann S., Valentine V., Look A.T., Lipsick J.S., Gould K.L.
Mol. Cell. Biol. 18:4097-4108(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-33; TRP-52; TRP-84 AND TYR-102.
[8]"Evidence that Myb-related CDC5 proteins are required for pre-mRNA splicing."
Burns C.G., Ohi R., Krainer A.R., Gould K.L.
Proc. Natl. Acad. Sci. U.S.A. 96:13789-13794(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Genetic and physical interactions between factors involved in both cell cycle progression and pre-mRNA splicing in Saccharomyces cerevisiae."
Ben-Yehuda S., Dix I., Russell C.S., McGarvey M., Beggs J.D., Kupiec M.
Genetics 156:1503-1517(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLF1; ISY1; NTC20; SYF1 AND SYF2.
[10]"Identification and characterization of two novel components of the Prp19p-associated complex, Ntc30p and Ntc20p."
Chen C.-H., Tsai W.-Y., Chen H.-R., Wang C.-H., Cheng S.-C.
J. Biol. Chem. 276:488-494(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ISY1; NTC20 AND PRP19.
[11]"Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs."
Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.
Mol. Cell. Biol. 22:2011-2024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CWC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Characterization of interactions among the Cef1p-Prp19p-associated splicing complex."
Ohi M.D., Gould K.L.
RNA 8:798-815(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRP19; PRP46 AND SYF1.
[13]"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].
[14]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49809 Genomic DNA. Translation: CAA89928.1.
AY693142 Genomic DNA. Translation: AAT93161.1.
BK006946 Genomic DNA. Translation: DAA10112.1.
PIRS55095.
RefSeqNP_013940.1. NM_001182720.1.

3D structure databases

ProteinModelPortalQ03654.
SMRQ03654. Positions 12-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35391. 72 interactions.
DIPDIP-1113N.
IntActQ03654. 51 interactions.
MINTMINT-517325.
STRING4932.YMR213W.

Proteomic databases

MaxQBQ03654.
PaxDbQ03654.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR213W; YMR213W; YMR213W.
GeneID855253.
KEGGsce:YMR213W.

Organism-specific databases

CYGDYMR213w.
SGDS000004826. CEF1.

Phylogenomic databases

eggNOGCOG5147.
GeneTreeENSGT00550000074922.
HOGENOMHOG000111535.
KOK12860.
OMAWNEYLNP.
OrthoDBEOG78SQWR.

Enzyme and pathway databases

BioCycYEAST:G3O-32896-MONOMER.

Gene expression databases

GenevestigatorQ03654.

Family and domain databases

Gene3D1.10.10.60. 2 hits.
InterProIPR021786. DUF3351.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamPF11831. Myb_Cef. 1 hit.
PF00249. Myb_DNA-binding. 2 hits.
[Graphical view]
SMARTSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS51294. HTH_MYB. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio978831.
PROQ03654.

Entry information

Entry nameCEF1_YEAST
AccessionPrimary (citable) accession number: Q03654
Secondary accession number(s): D6W038, Q6B1D8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families