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Protein

Nuclear mRNA export protein SAC3

Gene

SAC3

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

Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket.2 Publications

GO - Biological processi

  • actin filament-based process Source: SGD
  • mitotic nuclear division Source: SGD
  • mRNA 3'-end processing Source: SGD
  • mRNA export from nucleus Source: SGD
  • nuclear retention of pre-mRNA at the site of transcription Source: SGD
  • posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
  • protein export from nucleus Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • ribosomal small subunit biogenesis Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
  • transcription-coupled nucleotide-excision repair Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29749-MONOMER.

Protein family/group databases

TCDBi3.A.22.1.1. the transcription-coupled trex/tap nuclear mrna export complex (trex) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear mRNA export protein SAC3
Alternative name(s):
Leucine permease transcriptional regulator
Gene namesi
Name:SAC3
Synonyms:LEP1
Ordered Locus Names:YDR159W
ORF Names:YD8358.13
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR159W.
SGDiS000002566. SAC3.

Subcellular locationi

GO - Cellular componenti

  • nuclear envelope Source: UniProtKB-SubCell
  • transcription export complex 2 Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13011301Nuclear mRNA export protein SAC3PRO_0000097562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei568 – 5681PhosphoserineCombined sources
Modified residuei748 – 7481N6-acetyllysine1 Publication
Modified residuei866 – 8661PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP46674.

PTM databases

iPTMnetiP46674.

Interactioni

Subunit structurei

Heterodimer with THP1. The SAC3-THP1 complex interacts with CDC31 and SUS1, and with the mRNA export factor MEX67-MTR2, the TREX complex component SUB2, and the nucleoporin NUP1. SAC3 directly interacts with MEX67, NUP1 and SUB2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC31P0670410EBI-16425,EBI-4259
SUS1Q6WNK711EBI-16425,EBI-1251050

Protein-protein interaction databases

BioGridi32210. 452 interactions.
DIPiDIP-2444N.
IntActiP46674. 13 interactions.
MINTiMINT-596858.

Structurei

Secondary structure

1
1301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi258 – 27114Combined sources
Helixi273 – 2753Combined sources
Turni276 – 2783Combined sources
Helixi280 – 29617Combined sources
Helixi302 – 32423Combined sources
Helixi331 – 35424Combined sources
Helixi362 – 37211Combined sources
Helixi378 – 3836Combined sources
Helixi388 – 3914Combined sources
Helixi394 – 40613Combined sources
Helixi426 – 4338Combined sources
Helixi440 – 4467Combined sources
Helixi447 – 4493Combined sources
Helixi450 – 46415Combined sources
Helixi474 – 4807Combined sources
Helixi486 – 49510Combined sources
Turni502 – 5043Combined sources
Helixi508 – 5103Combined sources
Beta strandi514 – 5174Combined sources
Helixi530 – 5378Combined sources
Helixi541 – 5455Combined sources
Helixi753 – 80351Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FWBX-ray2.50B752-805[»]
3FWCX-ray2.70B/F/J/N723-805[»]
3T5VX-ray2.90A/D250-563[»]
4C31X-ray3.00A/D757-787[»]
4MBEX-ray2.61B/E753-805[»]
4TRQX-ray3.10A/D253-551[»]
ProteinModelPortaliP46674.
SMRiP46674. Positions 252-550, 723-805.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46674.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 572572Required for interaction with MEX67, SUB2 and THP1Add
BLAST
Regioni573 – 1301729Required for targeting SAC3 to the nuclear poreAdd
BLAST
Regioni733 – 860128Interaction with CDC31Add
BLAST

Sequence similaritiesi

Belongs to the SAC3 family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063781.
HOGENOMiHOG000065955.
InParanoidiP46674.
OMAiYAHLESH.
OrthoDBiEOG7VDXXJ.

Family and domain databases

InterProiIPR017173. Sac3.
IPR005062. SAC3/GANP/THP3.
IPR024293. SAC3_helical.
[Graphical view]
PfamiPF12209. SAC3. 1 hit.
PF03399. SAC3_GANP. 1 hit.
[Graphical view]
PIRSFiPIRSF037320. mRNA_export_factor_Sac3. 1 hit.

Sequencei

Sequence statusi: Complete.

P46674-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTSFGSVVP STNFNFFKGH GNNDNTSANS TVNNSNFFLN SNETKPSKNV
60 70 80 90 100
FMVHSTSQKK SQQPLQNLSH SPSYTENKPD KKKKYMINDA KTIQLVGPLI
110 120 130 140 150
SSPDNLGFQK RSHKARELPR FLINQEPQLE KRAFVQDPWD KANQEKMISL
160 170 180 190 200
EESIDDLNEL YETLKKMRNT ERSIMEEKGL VDKADSAKDL YDAIVFQGTC
210 220 230 240 250
LDMCPTFERS RRNVEYTVYS YEKNQPNDKK ASRTKALKVF ARPAAAAAPP
260 270 280 290 300
LPSDVRPPHI LVKTLDYIVD NLLTTLPESE GFLWDRMRSI RQDFTYQNYS
310 320 330 340 350
GPEAVDCNER IVRIHLLILH IMVKSNVEFS LQQELEQLHK SLITLSEIYD
360 370 380 390 400
DVRSSGGTCP NEAEFRAYAL LSKIRDPQYD ENIQRLPKHI FQDKLVQMAL
410 420 430 440 450
CFRRVISNSA YTERGFVKTE NCLNFYARFF QLMQSPSLPL LMGFFLQMHL
460 470 480 490 500
TDIRFYALRA LSHTLNKKHK PIPFIYLENM LLFNNRQEII EFCNYYSIEI
510 520 530 540 550
INGDAADLKT LQHYSHKLSE TQPLKKTYLT CLERRLQKTT YKGLINGGED
560 570 580 590 600
NLASSVYVKD PKKDRIPSIA DQSFLMENFQ NNYNEKLNQN SSVKPQINTS
610 620 630 640 650
PKRVATRPNH FPFSQESKQL PQISQSHTLS TNPLLTPQVH GDLSEQKQQQ
660 670 680 690 700
IKTVTDGGSP FVFDQSAQNS TVEASKAHMI STTSNGAYDE KLSSEQEEMR
710 720 730 740 750
KKEEQRIEEE KTQLKKKQEN ADKQVITEQI ANDLVKEVVN SSVISIVKRE
760 770 780 790 800
FSEANYRKDF IDTMTRELYD AFLHERLYLI YMDSRAELKR NSTLKKKFFE
810 820 830 840 850
KWQASYSQAK KNRILEEKKR EEIKLVSHQL GVPGFKKSTC LFRTPYKGNV
860 870 880 890 900
NSSFMLSSSD KNLIFSPVND EFNKFATHLT KISKLWRPLE MQSIYYDNLT
910 920 930 940 950
KKFPSNSLTP ANLFIYAKDW TSLSNRWILS KFNLQTAQDS KKFSNNIISS
960 970 980 990 1000
RIICIDDEYE PSDFSDLQLL IFNTGVTNPD IFDLEMKLKD DGEELIKLIT
1010 1020 1030 1040 1050
GISLNTNICF SLLIIYWESA ENTLSESTIK HLLKLNRISK NYSSVIERID
1060 1070 1080 1090 1100
LMNLTEESPH KCLEDKLSEI SHSYVYKLTE RGKYDKTLRQ KRSLAGIHSR
1110 1120 1130 1140 1150
STQLQTTKDI DQKMKKMLEK EKNKYQQQIG ERNTYAHLES HIDASPRSKK
1160 1170 1180 1190 1200
RKLPILLSTS HSSQFKTPLA SRLNTSGSST SPPLPSHLAM KFRKNSRVTS
1210 1220 1230 1240 1250
LHTVLPVSTP SHSNNIPAAS FSGNNTTDIQ SQQLIENQKS TSVYLNNVSE
1260 1270 1280 1290 1300
RILGNQEICQ TPINPVTPVL DGADQGKEDI PDSILELKIL IDSVKKKVNN

D
Length:1,301
Mass (Da):149,569
Last modified:October 1, 1996 - v2
Checksum:i0679DB1673DDACEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47805 Genomic DNA. Translation: CAA87767.1.
Z50046 Genomic DNA. Translation: CAA90379.1.
U35227 Genomic DNA. Translation: AAA79056.1.
BK006938 Genomic DNA. Translation: DAA11999.1.
PIRiS51323.
RefSeqiNP_010443.3. NM_001180466.3.

Genome annotation databases

EnsemblFungiiYDR159W; YDR159W; YDR159W.
GeneIDi851737.
KEGGisce:YDR159W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47805 Genomic DNA. Translation: CAA87767.1.
Z50046 Genomic DNA. Translation: CAA90379.1.
U35227 Genomic DNA. Translation: AAA79056.1.
BK006938 Genomic DNA. Translation: DAA11999.1.
PIRiS51323.
RefSeqiNP_010443.3. NM_001180466.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FWBX-ray2.50B752-805[»]
3FWCX-ray2.70B/F/J/N723-805[»]
3T5VX-ray2.90A/D250-563[»]
4C31X-ray3.00A/D757-787[»]
4MBEX-ray2.61B/E753-805[»]
4TRQX-ray3.10A/D253-551[»]
ProteinModelPortaliP46674.
SMRiP46674. Positions 252-550, 723-805.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32210. 452 interactions.
DIPiDIP-2444N.
IntActiP46674. 13 interactions.
MINTiMINT-596858.

Protein family/group databases

TCDBi3.A.22.1.1. the transcription-coupled trex/tap nuclear mrna export complex (trex) family.

PTM databases

iPTMnetiP46674.

Proteomic databases

MaxQBiP46674.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR159W; YDR159W; YDR159W.
GeneIDi851737.
KEGGisce:YDR159W.

Organism-specific databases

EuPathDBiFungiDB:YDR159W.
SGDiS000002566. SAC3.

Phylogenomic databases

GeneTreeiENSGT00530000063781.
HOGENOMiHOG000065955.
InParanoidiP46674.
OMAiYAHLESH.
OrthoDBiEOG7VDXXJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29749-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP46674.
PROiP46674.

Family and domain databases

InterProiIPR017173. Sac3.
IPR005062. SAC3/GANP/THP3.
IPR024293. SAC3_helical.
[Graphical view]
PfamiPF12209. SAC3. 1 hit.
PF03399. SAC3_GANP. 1 hit.
[Graphical view]
PIRSFiPIRSF037320. mRNA_export_factor_Sac3. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the SAC3 gene of Saccharomyces cerevisiae."
    Bauer A., Koelling R.
    Yeast 12:965-975(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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. "The Saccharomyces cerevisiae LEP1/SAC3 gene is associated with leucine transport."
    Stella C.A., Korch C., Ramos E.H., Bauer A., Koelling R., Mattoon J.R.
    Mol. Gen. Genet. 262:332-341(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-1301.
    Strain: DBY939.
  5. "The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores."
    Fischer T., Straesser K., Racz A., Rodriguez-Navarro S., Oppizzi M., Ihrig P., Lechner J., Hurt E.
    EMBO J. 21:5843-5852(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MEX67, NUP1, SUB2 AND THP1, SUBCELLULAR LOCATION.
  6. "Nab2p and the Thp1p-Sac3p complex functionally interact at the interface between transcription and mRNA metabolism."
    Gallardo M., Luna R., Erdjument-Bromage H., Tempst P., Aguilera A.
    J. Biol. Chem. 278:24225-24232(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery."
    Rodriguez-Navarro S., Fischer T., Luo M.-J., Antunez O., Brettschneider S., Lechner J., Perez-Ortin J.E., Reed R., Hurt E.C.
    Cell 116:75-86(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUS1, ACETYLATION AT LYS-748.
  10. "Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery."
    Fischer T., Rodriguez-Navarro S., Pereira G., Racz A., Schiebel E., Hurt E.C.
    Nat. Cell Biol. 6:840-848(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC31.
  11. "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 SER-866, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "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-866, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 SER-568 AND SER-866, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSAC3_YEAST
AccessioniPrimary (citable) accession number: P46674
Secondary accession number(s): D6VSD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 339 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. 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.