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Protein

Mitofusin FZO1

Gene

FZO1

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 transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondrial morphology, which is balanced between fusion and fission, mediated by FZO1 and DNM1, respectively. Functions antagonistically with DNM1. May act by forming membrane contact sites that mediate mitochondrial fusion. Mitochondrial fusion promotes also increased lifespan.11 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi194 – 2018GTPCurated
Nucleotide bindingi313 – 3175GTPCurated
Nucleotide bindingi370 – 3734GTPCurated

GO - Molecular functioni

  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB-KW
  • protein homodimerization activity Source: SGD

GO - Biological processi

  • mitochondrial fusion Source: SGD
  • mitochondrion localization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29123-MONOMER.

Protein family/group databases

TCDBi9.B.25.1.1. the mitochondrial inner/outer membrane fusion (mmf) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitofusin FZO1 (EC:3.6.5.-)
Alternative name(s):
Transmembrane GTPase FZO1
Gene namesi
Name:FZO1
Ordered Locus Names:YBR179C
ORF Names:YBR1241
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR179C.
SGDiS000000383. FZO1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 705705Cytoplasmic1 PublicationAdd
BLAST
Transmembranei706 – 72621Helical; Name=1Add
BLAST
Topological domaini727 – 73610Mitochondrial intermembrane1 Publication
Transmembranei737 – 75721Helical; Name=2Add
BLAST
Topological domaini758 – 85598Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • integral component of mitochondrial outer membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi172 – 1721V → P: Abolishes fusion function. 1 Publication
Mutagenesisi195 – 1951D → A: Abolishes fusion function. 1 Publication
Mutagenesisi196 – 1961V → M: Leads to an unusual intermediate mitochondrial morphology described as disorganized tubules in which mitochondria are tubular, distorted, less branched, and poorly distributed throughout the cell. 1 Publication
Mutagenesisi197 – 1971N → A: Abolishes fusion function. 1 Publication
Mutagenesisi200 – 2001K → A: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination. No effect on localization or interaction with UGO1. 4 Publications
Mutagenesisi201 – 2011S → N: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination, but not localization to mitochondrial outer membrane. 4 Publications
Mutagenesisi221 – 2211T → A: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination, but not localization to mitochondrial outer membrane. 4 Publications
Mutagenesisi320 – 3201D → A: Loss of mitochondrial fusion. 1 Publication
Mutagenesisi327 – 3271V → T: Impairs GTP Hydrolysis and abolishes fusion function. 1 Publication
Mutagenesisi371 – 3711K → A: No effect. 1 Publication
Mutagenesisi398 – 3981K → R: Leads to accelerated proteolysis. 1 Publication
Mutagenesisi464 – 4641K → R: Abolishes fusion function. 1 Publication
Mutagenesisi490 – 4901Y → P: Abolishes fusion function. 1 Publication
Mutagenesisi501 – 5011L → A: Abolishes fusion function; when associated with Ala-504. 1 Publication
Mutagenesisi504 – 5041L → A: Abolishes fusion function; when associated with Ala-501. 1 Publication
Mutagenesisi518 – 5181L → P: Abolishes fusion function. 1 Publication
Mutagenesisi538 – 5381K → P: Abolishes fusion function. 1 Publication
Mutagenesisi769 – 7691Y → P: Abolishes fusion function. 1 Publication
Mutagenesisi773 – 7731L → P: Abolishes fusion function. 1 Publication
Mutagenesisi819 – 8191L → P: Abolishes fusion function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 855855Mitofusin FZO1PRO_0000127682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki398 – 398Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki464 – 464Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated at Lys-398 and Lys-464. MDM30 and UGO1 are involved in ubiquitination. Deubiquitinated by UBP2 and UBP12. UBP2 and UBP12 recognize distinct ubiquitin chains on FZO1 that have opposing effects on mitochondrial fusion. UBP2 removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit fusion. UBP12 recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization.5 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP38297.
TopDownProteomicsiP38297.

PTM databases

iPTMnetiP38297.

Interactioni

Subunit structurei

Honodimer. Dimerization depends on GTP binding. Binds the cytoplasmic domain of UGO1 which binds MGM1 through its intermembrane space domain. Interacts with MDM30, UBP2 and UBP12. Component of a large multiprotein complex of 800 kDa.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MGM1P322662EBI-20900,EBI-10865
UGO1Q033272EBI-20900,EBI-32955

GO - Molecular functioni

  • protein homodimerization activity Source: SGD

Protein-protein interaction databases

BioGridi32877. 50 interactions.
DIPiDIP-5581N.
IntActiP38297. 3 interactions.
MINTiMINT-527599.

Structurei

3D structure databases

ProteinModelPortaliP38297.
SMRiP38297. Positions 309-392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini184 – 467284Dynamin-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni91 – 190100HRNAdd
BLAST
Regioni484 – 54764HR1Add
BLAST
Regioni630 – 843214Required for interaction with UGO1Add
BLAST
Regioni769 – 83163HR2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili798 – 82528Sequence analysisAdd
BLAST

Domaini

The GTPase domain may regulate the interaction with UGO1 since FZO1 lacking the GTPase domain binds 5-fold higher amount of UGO1 than full length FZO1. The HRN, HR1 and HR2 domains are required for the oligomerization and function in mitochondrial fusion.1 Publication

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000177197.
InParanoidiP38297.
KOiK06030.
OMAiIVVNGFD.
OrthoDBiEOG779P6J.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022812. Dynamin_SF.
IPR030381. G_DYNAMIN_dom.
IPR027091. GTPase_Fzo/Fzo1.
IPR027094. Mitofusin_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10465. PTHR10465. 1 hit.
PTHR10465:SF0. PTHR10465:SF0. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEGKQQFKD SNKPHKDSTD QDDDAATIVP QTLTYSRNEG HFLGSNFHGV
60 70 80 90 100
TDDRTTLFDG EEGRREDDLL PSLRSSNSKA HLISSQLSQW NYNNNRVLLK
110 120 130 140 150
RSILKTQAFM DQLQEENNIR PIFIAANDER EKLHVLQLNI KLDGQYNTKE
160 170 180 190 200
KNGFNIEKKA LSKLFHSQIV SVTNHLNALK KRVDDVSSKV FITGDVNTGK
210 220 230 240 250
SALCNSLLKQ RLLPEDQLPC TNVFSEILEA RENDGIEEVH AIPLNIAPTL
260 270 280 290 300
KEAIDMYSIQ NPKTYEIHTL KELPDLVPQN GKYALLKIYI KDDKRPASTS
310 320 330 340 350
LLRNGTVDIS LIDSPGLNMD SLQTAEVMSR QEEIDLVIFV VNAENQLTLS
360 370 380 390 400
AKEFISLASR EKKLMFFVVK KFDKIRDKQR CKELILKQIR DLSPETYKRA
410 420 430 440 450
ADFVHFVSKN GDELPHYHNE NDNEDHGDRK PDDDPYSSSD PDPDFDSLED
460 470 480 490 500
SLRNFVLKKR SLSKLLPAKT YLSKLLSDII MISKSNMKMY SEEEIKINEQ
510 520 530 540 550
LETLRPEILS ARAKCNDLTT SVDQMAEQTI TMTYNNTKEA LLNALDVPLH
560 570 580 590 600
EYPKYQGLGQ IYDFIFSTEA FIANQIDESI GSSELFAKQK TDLLVKKIYE
610 620 630 640 650
IGKNELGDDF MCERVFRSEL MFRKRKHLIG KRLKVSLSIT DLFAPTWKGF
660 670 680 690 700
LSYLSWQKPV TAPLPDIEGQ TNEGQIGLMK YLGLKNYPLT QYWSRPSLLF
710 720 730 740 750
TSKIPTLTLY FLGSTKVVGN IILNGIKLSS WSSLKKLSVP VIVVGSLLGL
760 770 780 790 800
TYLIHDLPRA LPMNLSIKYK RKLQELDYIH LNAQRTSNEV RDVLRVPTRE
810 820 830 840 850
ILRSCEIIMD KKQITKKELE NKKESNLLSI KFFQSLYEGT VAQKLMVEEI

NLDID
Length:855
Mass (Da):97,808
Last modified:October 1, 1994 - v1
Checksum:iD796DA455E2AE28B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36048 Genomic DNA. Translation: CAA85140.1.
BK006936 Genomic DNA. Translation: DAA07293.1.
PIRiS46050.
RefSeqiNP_009738.1. NM_001178527.1.

Genome annotation databases

EnsemblFungiiYBR179C; YBR179C; YBR179C.
GeneIDi852477.
KEGGisce:YBR179C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36048 Genomic DNA. Translation: CAA85140.1.
BK006936 Genomic DNA. Translation: DAA07293.1.
PIRiS46050.
RefSeqiNP_009738.1. NM_001178527.1.

3D structure databases

ProteinModelPortaliP38297.
SMRiP38297. Positions 309-392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32877. 50 interactions.
DIPiDIP-5581N.
IntActiP38297. 3 interactions.
MINTiMINT-527599.

Protein family/group databases

TCDBi9.B.25.1.1. the mitochondrial inner/outer membrane fusion (mmf) family.

PTM databases

iPTMnetiP38297.

Proteomic databases

MaxQBiP38297.
TopDownProteomicsiP38297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR179C; YBR179C; YBR179C.
GeneIDi852477.
KEGGisce:YBR179C.

Organism-specific databases

EuPathDBiFungiDB:YBR179C.
SGDiS000000383. FZO1.

Phylogenomic databases

HOGENOMiHOG000177197.
InParanoidiP38297.
KOiK06030.
OMAiIVVNGFD.
OrthoDBiEOG779P6J.

Enzyme and pathway databases

BioCyciYEAST:G3O-29123-MONOMER.

Miscellaneous databases

PROiP38297.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022812. Dynamin_SF.
IPR030381. G_DYNAMIN_dom.
IPR027091. GTPase_Fzo/Fzo1.
IPR027094. Mitofusin_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10465. PTHR10465. 1 hit.
PTHR10465:SF0. PTHR10465:SF0. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae."
    Rapaport D., Brunner M., Neupert W., Westermann B.
    J. Biol. Chem. 273:20150-20155(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  4. "Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p."
    Hermann G.J., Thatcher J.W., Mills J.P., Hales K.G., Fuller M.T., Nunnari J., Shaw J.M.
    J. Cell Biol. 143:359-373(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-200; SER-201; THR-221 AND LYS-371.
  5. "Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape."
    Sesaki H., Jensen R.E.
    J. Cell Biol. 147:699-706(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion."
    Fritz S., Rapaport D., Klanner E., Neupert W., Westermann B.
    J. Cell Biol. 152:683-692(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY.
  7. "Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane."
    Sesaki H., Southard S.M., Yaffe M.P., Jensen R.E.
    Mol. Biol. Cell 14:2342-2356(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MGM1 AND UGO1.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion."
    Sesaki H., Jensen R.E.
    J. Biol. Chem. 279:28298-28303(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UGO1 AND MGM1.
  11. "Mitochondrial fusion intermediates revealed in vitro."
    Meeusen S., McCaffery J.M., Nunnari J.
    Science 305:1747-1752(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Instability of the mitofusin Fzo1 regulates mitochondrial morphology during the mating response of the yeast Saccharomyces cerevisiae."
    Neutzner A., Youle R.J.
    J. Biol. Chem. 280:18598-18603(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEIN DEGRADATION.
  13. "Domain interactions within Fzo1 oligomers are essential for mitochondrial fusion."
    Griffin E.E., Chan D.C.
    J. Biol. Chem. 281:16599-16606(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, SUBUNIT, MUTAGENESIS OF VAL-172; LYS-200; SER-201; THR-221; TYR-490; LEU-501; LEU-504; LEU-518; LYS-538; TYR-769; LEU-773 AND LEU-819.
  14. "Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1."
    Escobar-Henriques M., Westermann B., Langer T.
    J. Cell Biol. 173:645-650(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MDM30.
  15. "Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical regulator of mitochondrial fusion."
    Cohen M.M., Leboucher G.P., Livnat-Levanon N., Glickman M.H., Weissman A.M.
    Mol. Biol. Cell 19:2457-2464(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY MDM30.
  16. "A mutation associated with CMT2A neuropathy causes defects in Fzo1 GTP hydrolysis, ubiquitylation, and protein turnover."
    Amiott E.A., Cohen M.M., Saint-Georges Y., Weissman A.M., Shaw J.M.
    Mol. Biol. Cell 20:5026-5035(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, UBIQUITINATION, MUTAGENESIS OF VAL-196 AND VAL-327.
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Acetyl-L-carnitine protects yeast cells from apoptosis and aging and inhibits mitochondrial fission."
    Palermo V., Falcone C., Calvani M., Mazzoni C.
    Aging Cell 9:570-579(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Mdm36 is a mitochondrial fission-promoting protein in Saccharomyces cerevisiae."
    Hammermeister M., Schodel K., Westermann B.
    Mol. Biol. Cell 21:2443-2452(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Ugo1 and Mdm30 act sequentially during Fzo1-mediated mitochondrial outer membrane fusion."
    Anton F., Fres J.M., Schauss A., Pinson B., Praefcke G.J., Langer T., Escobar-Henriques M.
    J. Cell Sci. 124:1126-1135(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, FUNCTION, MUTAGENESIS OF ASP-195; ASN-197; LYS-200; SER-201; THR-221 AND ASP-320, INTERACTION WITH MDM30, UBIQUITINATION.
  21. "Sequential requirements for the GTPase domain of the mitofusin Fzo1 and the ubiquitin ligase SCFMdm30 in mitochondrial outer membrane fusion."
    Cohen M.M., Amiott E.A., Day A.R., Leboucher G.P., Pryce E.N., Glickman M.H., McCaffery J.M., Shaw J.M., Weissman A.M.
    J. Cell Sci. 124:1403-1410(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-200; SER-201 AND THR-221, INTERACTION WITH MDM30, UBIQUITINATION BY MDM30.
  22. "Glucose levels regulate the nucleo-mitochondrial distribution of Mig2."
    Fernandez-Cid A., Riera A., Herrero P., Moreno F.
    Mitochondrion 12:370-380(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Two deubiquitylases act on mitofusin and regulate mitochondrial fusion along independent pathways."
    Anton F., Dittmar G., Langer T., Escobar-Henriques M.
    Mol. Cell 49:487-498(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-398 AND LYS-464, INTERACTION WITH UBP2 AND UBP12, DEUBIQUITINATION BY UBP2 AND UBP12, MUTAGENESIS OF LYS-398 AND LYS-464.

Entry informationi

Entry nameiFZO1_YEAST
AccessioniPrimary (citable) accession number: P38297
Secondary accession number(s): D6VQH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 8, 2016
This is version 127 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 1000 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.