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Protein

Pre-mRNA-splicing factor SLU7

Gene

SLU7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential protein involved in the second catalytic step of pre-mRNA splicing. Involved in the selection of 3'-type splice sites; this selection could be done via a 3'-splice site-binding factor, PRP16.9 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri120 – 13718CCHC-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29693-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor SLU7
Alternative name(s):
Synthetic lethal with U2 snRNA protein 17
Synthetic lethal with U5 snRNA protein 7
Gene namesi
Name:SLU7
Synonyms:SLT17
Ordered Locus Names:YDR088C
ORF Names:D4483
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR088C.
SGDiS000002495. SLU7.

Subcellular locationi

GO - Cellular componenti

  • spliceosomal complex Source: SGD
  • U2-type post-spliceosomal complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221C → A: Affects the ability to associate with the spliceosome. Loss of growth and in vitro splicing activity; when associated with 215-AAA-217. Cryo- and thermosensitivity; when associated with A-217. 1 Publication
Mutagenesisi130 – 1301H → A: Affects the ability to associate with the spliceosome. Loss of growth and in vitro splicing activity; when associated with 215-AAA-217. Cryo- and thermosensitivity; when associated with A-217. 1 Publication
Mutagenesisi135 – 1351C → A: Affects the ability to associate with the spliceosome. Loss of growth, spliceosome binding, and in vitro splicing activity; when associated with 215-AAA-217. Cryo- and thermosensitivity; when associated with A-217. 1 Publication
Mutagenesisi215 – 2173EIE → AAA: Abolishes the interaction with PRP18, and temperature sensitive growth defect. Loss of growth and in vitro splicing activity; when associated with A-122 or A-130 or A-135. 1 Publication
Mutagenesisi217 – 2171E → A: Abolishes the interaction with PRP18. Cryo- and thermosensitivity; when associated with A-122 or A-130 or A-135. 1 Publication
Mutagenesisi217 – 2171E → K: Abolishes the interaction with PRP18, and temperature sensitive growth defect. 1 Publication
Mutagenesisi221 – 2244LELY → AAAA: Abolishes the interaction with PRP18, and temperature sensitive growth defect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Pre-mRNA-splicing factor SLU7PRO_0000218554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei212 – 2121PhosphothreonineCombined sources

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ02775.

PTM databases

iPTMnetiQ02775.

Interactioni

Subunit structurei

Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with BRR2, ECM2, PRP18 and PRP22.8 Publications

Protein-protein interaction databases

BioGridi32144. 102 interactions.
DIPiDIP-220N.
IntActiQ02775. 10 interactions.
MINTiMINT-394061.

Structurei

3D structure databases

ProteinModelPortaliQ02775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 22425Interaction with PRP8Add
BLAST

Domaini

The CCHC-type zinc finger probably plays a role in the ability of SLU7 to bypass the requirement for PRP18.

Sequence similaritiesi

Belongs to the SLU7 family.Curated
Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri120 – 13718CCHC-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000154339.
InParanoidiQ02775.
KOiK12819.
OMAiWYGYSGK.
OrthoDBiEOG7RFTTM.

Family and domain databases

Gene3Di4.10.60.10. 1 hit.
InterProiIPR021715. Slu7.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF11708. Slu7. 1 hit.
[Graphical view]
SUPFAMiSSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNNSRNNEN RSTINRNKRQ LQQAKEKNEN IHIPRYIRNQ PWYYKDTPKE
60 70 80 90 100
QEGKKPGNDD TSTAEGGEKS DYLVHHRQKA KGGALDIDNN SEPKIGMGIK
110 120 130 140 150
DEFKLIRPQK MSVRDSHSLS FCRNCGEAGH KEKDCMEKPR KMQKLVPDLN
160 170 180 190 200
SQKNNGTVLV RATDDDWDSR KDRWYGYSGK EYNELISKWE RDKRNKIKGK
210 220 230 240 250
DKSQTDETLW DTDEEIELMK LELYKDSVGS LKKDDADNSQ LYRTSTRLRE
260 270 280 290 300
DKAAYLNDIN STESNYDPKS RLYKTETLGA VDEKSKMFRR HLTGEGLKLN
310 320 330 340 350
ELNQFARSHA KEMGIRDEIE DKEKVQHVLV ANPTKYEYLK KKREQEETKQ
360 370 380
PKIVSIGDLE ARKVDGTKQS EEQRNHLKDL YG
Length:382
Mass (Da):44,637
Last modified:July 1, 1993 - v1
Checksum:i6405458FC367A7D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351D → G in AAS56027 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67810 Genomic DNA. Translation: CAA48011.1.
X82086 Genomic DNA. Translation: CAA57617.1.
Z46796 Genomic DNA. Translation: CAA86810.1.
Z74384 Genomic DNA. Translation: CAA98908.1.
Z74385 Genomic DNA. Translation: CAA98909.1.
AY557701 Genomic DNA. Translation: AAS56027.1.
BK006938 Genomic DNA. Translation: DAA11935.1.
PIRiA46229.
RefSeqiNP_010373.3. NM_001180396.3.

Genome annotation databases

EnsemblFungiiYDR088C; YDR088C; YDR088C.
GeneIDi851661.
KEGGisce:YDR088C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67810 Genomic DNA. Translation: CAA48011.1.
X82086 Genomic DNA. Translation: CAA57617.1.
Z46796 Genomic DNA. Translation: CAA86810.1.
Z74384 Genomic DNA. Translation: CAA98908.1.
Z74385 Genomic DNA. Translation: CAA98909.1.
AY557701 Genomic DNA. Translation: AAS56027.1.
BK006938 Genomic DNA. Translation: DAA11935.1.
PIRiA46229.
RefSeqiNP_010373.3. NM_001180396.3.

3D structure databases

ProteinModelPortaliQ02775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32144. 102 interactions.
DIPiDIP-220N.
IntActiQ02775. 10 interactions.
MINTiMINT-394061.

PTM databases

iPTMnetiQ02775.

Proteomic databases

MaxQBiQ02775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR088C; YDR088C; YDR088C.
GeneIDi851661.
KEGGisce:YDR088C.

Organism-specific databases

EuPathDBiFungiDB:YDR088C.
SGDiS000002495. SLU7.

Phylogenomic databases

HOGENOMiHOG000154339.
InParanoidiQ02775.
KOiK12819.
OMAiWYGYSGK.
OrthoDBiEOG7RFTTM.

Enzyme and pathway databases

BioCyciYEAST:G3O-29693-MONOMER.

Miscellaneous databases

PROiQ02775.

Family and domain databases

Gene3Di4.10.60.10. 1 hit.
InterProiIPR021715. Slu7.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF11708. Slu7. 1 hit.
[Graphical view]
SUPFAMiSSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An essential splicing factor, SLU7, mediates 3' splice site choice in yeast."
    Frank D.N., Guthrie C.
    Genes Dev. 6:2112-2124(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Synthetic lethal mutations suggest interactions between U5 small nuclear RNA and four proteins required for the second step of splicing."
    Frank D.N., Patterson B., Guthrie C.
    Mol. Cell. Biol. 12:5197-5205(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of yeast pre-mRNA splicing."
    Ansari A., Schwer B.
    EMBO J. 14:4001-4009(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Characterization and functional ordering of Slu7p and Prp17p during the second step of pre-mRNA splicing in yeast."
    Jones M.H., Frank D.N., Guthrie C.
    Proc. Natl. Acad. Sci. U.S.A. 92:9687-9691(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Prp16p, Slu7p, and Prp8p interact with the 3' splice site in two distinct stages during the second catalytic step of pre-mRNA splicing."
    Umen J.G., Guthrie C.
    RNA 1:584-597(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE 3' SPLICE SITE.
  9. "Requirement for SLU7 in yeast pre-mRNA splicing is dictated by the distance between the branchpoint and the 3' splice site."
    Brys A., Schwer B.
    RNA 2:707-717(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE SPLICEOSOME.
  10. "Functional and physical interaction between the yeast splicing factors Slu7 and Prp18."
    Zhang X., Schwer B.
    Nucleic Acids Res. 25:2146-2152(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRP18.
  11. "Synthetic lethality of yeast slt mutations with U2 small nuclear RNA mutations suggests functional interactions between U2 and U5 snRNPs that are important for both steps of pre-mRNA splicing."
    Xu D., Field D.J., Tang S.-J., Moris A., Bobechko B.P., Friesen J.D.
    Mol. Cell. Biol. 18:2055-2066(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Crystal structure of the functional domain of the splicing factor Prp18."
    Jiang J., Horowitz D.S., Xu R.-M.
    Proc. Natl. Acad. Sci. U.S.A. 97:3022-3027(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRP18.
  13. "Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae."
    van Nues R.W., Beggs J.D.
    Genetics 157:1451-1467(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRR2; PRP18 AND PRP22.
  14. "Splicing factor slt11p and its involvement in formation of U2/U6 helix II in activation of the yeast spliceosome."
    Xu D., Friesen J.D.
    Mol. Cell. Biol. 21:1011-1023(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECM2, FUNCTION.
  15. "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.
  16. "How Slu7 and Prp18 cooperate in the second step of yeast pre-mRNA splicing."
    James S.-A., Turner W., Schwer B.
    RNA 8:1068-1077(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRP18, MUTAGENESIS OF CYS-122; HIS-130; CYS-135; 215-GLU--GLU-217; GLU-217 AND 221-LEU--TYR-224.
  17. "Mutational analysis identifies two separable roles of the Saccharomyces cerevisiae splicing factor Prp18."
    Bacikova D., Horowitz D.S.
    RNA 8:1280-1293(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRP18.
  18. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  19. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  20. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  21. "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-120 AND THR-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
    Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
    Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
  23. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSLU7_YEAST
AccessioniPrimary (citable) accession number: Q02775
Secondary accession number(s): D6VS75, P89902, Q6Q5U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 8, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1490 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.