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Q05776 (UPS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein UPS1, mitochondrial
Alternative name(s):
Unprocessed MGM1 protein 1
Gene names
Name:UPS1
Ordered Locus Names:YLR193C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for maintenance of normal mitochondrial morphology as well as PCP1-dependent processing of MGM1. With UPS2, controls the level of cardiolipin in mitochondria. Cardiolipin is a unique phospholipid with four fatty acid chains and is present mainly in the mitochondrial inner membrane where it stabilizes the electron transport chain supercomplex between complexes III and IV through direct interaction of their subunits. Ref.5 Ref.6 Ref.7 Ref.8

Subunit structure

Interacts with MDM35. Found associated with a 170 kDa complex. Ref.5 Ref.8 Ref.9

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Mitochondrion intermembrane space. Note: Lacks the two major intermembrane space-targeting signals, bipartite presequences and cysteine motifs, and import is mediated by another IMS protein, MDM35. Ref.3 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Disruption phenotype

Cells show slow growth, fragmented mitochondria and have a 50-fold reduced level of s-MGM1. These defects can be complemented by human PRELI or bypassed by growth on a nonfermentable carbon source. Ref.5

Miscellaneous

Present with 704 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the slowmo family.

Contains 1 PRELI/MSF1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 175175Protein UPS1, mitochondrial
PRO_0000271269

Regions

Domain2 – 172171PRELI/MSF1
Region1 – 8080Required for mitochondrial targeting Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q05776 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5B9003B6A2323109

FASTA17520,108
        10         20         30         40         50         60 
MVLLHKSTHI FPTDFASVSR AFFNRYPNPY SPHVLSIDTI SRNVDQEGNL RTTRLLKKSG 

        70         80         90        100        110        120 
KLPTWVKPFL RGITETWIIE VSVVNPANST MKTYTRNLDH TGIMKVEEYT TYQFDSATSS 

       130        140        150        160        170 
TIADSRVKFS SGFNMGIKSK VEDWSRTKFD ENVKKSRMGM AFVIQKLEEA RNPQF 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [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]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p."
Sesaki H., Dunn C.D., Iijima M., Shepard K.A., Yaffe M.P., Machamer C.E., Jensen R.E.
J. Cell Biol. 173:651-658(2006) [PubMed: 16754953] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[6]"The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria."
Osman C., Haag M., Potting C., Rodenfels J., Dip P.V., Wieland F.T., Brugger B., Westermann B., Langer T.
J. Cell Biol. 184:583-596(2009) [PubMed: 19221197] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria."
Tamura Y., Endo T., Iijima M., Sesaki H.
J. Cell Biol. 185:1029-1045(2009) [PubMed: 19506038] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation."
Tamura Y., Iijima M., Sesaki H.
EMBO J. 29:2875-2887(2010) [PubMed: 20622808] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION MDM35.
[9]"Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35."
Potting C., Wilmes C., Engmann T., Osman C., Langer T.
EMBO J. 29:2888-2898(2010) [PubMed: 20657548] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MDM35.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14913 Genomic DNA. Translation: AAB67434.1.
BK006945 Genomic DNA. Translation: DAA09512.1.
PIRS48546.
RefSeqNP_013294.1. NM_001182080.1.

3D structure databases

ProteinModelPortalQ05776.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4798N.
MINTMINT-494469.
STRINGQ05776.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR193C; YLR193C; YLR193C.
GeneID850890.
KEGGsce:YLR193C.
NMPDRfig|4932.3.peg.4304.

Organism-specific databases

CYGDYLR193c.
SGDS000004183. UPS1.

Phylogenomic databases

eggNOGfuNOG10656.
GeneTreeEFGT00050000003515.
HOGENOMHBG398237.
OMARISESWV.
OrthoDBEOG47WRZ5.

Gene expression databases

ArrayExpressQ05776.
GenevestigatorQ05776.

Family and domain databases

InterProIPR006797. PRELI/MSF1.
[Graphical view]
PfamPF04707. PRELI. 1 hit.
[Graphical view]
PROSITEPS50904. PRELI_MSF1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967260.

Entry information

Entry nameUPS1_YEAST
AccessionPrimary (citable) accession number: Q05776
Secondary accession number(s): D6VYJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

SIMILARITY comments

Index of protein domains and families