Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 157 (16 Oct 2019)
Sequence version 1 (01 Oct 1994)
Previous versions | rss
Help videoAdd a publicationFeedback
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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Essential transmembrane GTPase, which mediates mitochondrial fusion (PubMed:9685359, PubMed:9786948, PubMed:10562274, PubMed:11266460, PubMed:15297626, PubMed:15760898, PubMed:16624808, PubMed:19812251, PubMed:21385840, PubMed:21502136, PubMed:23317502, PubMed:27253069). Fusion proceeds through several steps; first mitochondria are tethered together, then brought into close contact, followed by the formation of a docking ring around contact areas, and finally membrane fusion (PubMed:27253069). 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 (PubMed:10562274). Functions antagonistically with DNM1 (PubMed:10562274). Probably acts by forming membrane contact sites that mediate mitochondrial membrane fusion (PubMed:27253069). Mitochondrial docking and fusion requires GTP hydrolysis (PubMed:15297626, PubMed:19812251, PubMed:27253069). Mitochondrial fusion promotes also increased lifespan.12 Publications

Miscellaneous

Present with 1000 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei408GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi197 – 202GTPBy similarity6
Nucleotide bindingi370 – 373GTPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29123-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-983231 Factors involved in megakaryocyte development and platelet production

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.N.6.1.1 the mitochondrial inner/outer membrane fusion (mmf) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Mitofusin FZO1 (EC:3.6.5.-1 Publication)
Alternative name(s):
Transmembrane GTPase FZO1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FZO1
Ordered Locus Names:YBR179C
ORF Names:YBR1241
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome II

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YBR179C

Saccharomyces Genome Database

More...
SGDi
S000000383 FZO1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 705Cytoplasmic1 PublicationAdd BLAST705
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei706 – 726Helical; Name=11 PublicationAdd BLAST21
Topological domaini727 – 736Mitochondrial intermembrane1 Publication10
Transmembranei737 – 757Helical; Name=21 PublicationAdd BLAST21
Topological domaini758 – 855Cytoplasmic1 PublicationAdd BLAST98

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi172V → P: Abolishes fusion function. 1 Publication1
Mutagenesisi195D → A: Abolishes fusion function. 1 Publication1
Mutagenesisi196V → 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 Publication1
Mutagenesisi197N → A: Abolishes fusion function. 1 Publication1
Mutagenesisi200K → A: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination. No effect on localization or interaction with UGO1. 5 Publications1
Mutagenesisi200K → D: Abolishes respiratory growth. 1 Publication1
Mutagenesisi200K → R: No effect. 1 Publication1
Mutagenesisi201S → N: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination, but not localization to mitochondrial outer membrane. 4 Publications1
Mutagenesisi221T → A: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination, but not localization to mitochondrial outer membrane. 4 Publications1
Mutagenesisi313D → K: Abolishes respiratory growth. 1 Publication1
Mutagenesisi320D → A: Loss of mitochondrial fusion. 1 Publication1
Mutagenesisi327V → T: Impairs GTP Hydrolysis and abolishes fusion function. 1 Publication1
Mutagenesisi335D → K: Abolishes respiratory growth. Restores respiratory growth; when associated with D-464. 1 Publication1
Mutagenesisi371K → A: No effect. 1 Publication1
Mutagenesisi398K → R: Leads to accelerated proteolysis. 1 Publication1
Mutagenesisi464K → D: Abolishes respiratory growth. Restores respiratory growth; when associated with K-335. 1 Publication1
Mutagenesisi464K → R: Abolishes fusion function. 1 Publication1
Mutagenesisi490Y → A or K: No effect. 1 Publication1
Mutagenesisi490Y → P: Abolishes fusion function. 1 Publication1
Mutagenesisi501L → A: Abolishes fusion function; when associated with Ala-504. 1 Publication1
Mutagenesisi504L → A: Abolishes fusion function; when associated with Ala-501. 1 Publication1
Mutagenesisi518L → P: Abolishes fusion function. 1 Publication1
Mutagenesisi523D → H: Abolishes respiratory growth. Restores respiratory growth; when associated with D-780. 1 Publication1
Mutagenesisi538K → P: Abolishes fusion function. 1 Publication1
Mutagenesisi769Y → P: Abolishes fusion function. 1 Publication1
Mutagenesisi773L → P: Abolishes fusion function. 1 Publication1
Mutagenesisi780H → D: No effect. Restores respiratory growth; when associated with H-523. 1 Publication1
Mutagenesisi818E → A or R: No effect. 1 Publication1
Mutagenesisi818E → P: Abolishes respiratory growth. 1 Publication1
Mutagenesisi819L → A: No effect. 1 Publication1
Mutagenesisi819L → P or E: Abolishes fusion function. 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001276821 – 855Mitofusin FZO1Add BLAST855

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki398Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki464Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated at Lys-398 and Lys-464 (PubMed:19812251, PubMed:23317502, PubMed:27044889). MDM30 and UGO1 are involved in ubiquitination (PubMed:18353967, PubMed:21385840, PubMed:21502136). Deubiquitinated by UBP2 and UBP12 (PubMed:23317502). UBP2 and UBP12 recognize distinct ubiquitin chains on FZO1 that have opposing effects on mitochondrial fusion (PubMed:23317502). UBP2 removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit fusion (PubMed:23317502). UBP12 recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization (PubMed:23317502).6 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P38297

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P38297

PRoteomics IDEntifications database

More...
PRIDEi
P38297

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P38297

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P38297

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:16624808, PubMed:21385840, PubMed:19812251). Dimerization depends on GTP binding (PubMed:16624808, PubMed:21385840, PubMed:19812251).

Component of a large multiprotein complex of 800 kDa (PubMed:9685359). Binds the cytoplasmic domain of UGO1 which binds MGM1 through its intermembrane space domain (PubMed:15087460, PubMed:12808034).

Interacts with MDM30 (PubMed:21385840, PubMed:21502136, PubMed:16735578).

Interacts with UBP2 and UBP12 (PubMed:23317502).

Interacts (when ubiquitinated) with DOA1; the interaction recruits FZO1 to CDC48 and promotes FZO1 proteasomal degradation (PubMed:27044889).

10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
32877, 146 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-161 FZO1-MGM1-UGO1 complex

Database of interacting proteins

More...
DIPi
DIP-5581N

Protein interaction database and analysis system

More...
IntActi
P38297, 4 interactors

Molecular INTeraction database

More...
MINTi
P38297

STRING: functional protein association networks

More...
STRINGi
4932.YBR179C

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini184 – 467Dynamin-type GSequence analysisAdd BLAST284

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni91 – 190HRN1 PublicationAdd BLAST100
Regioni484 – 547HR11 PublicationAdd BLAST64
Regioni630 – 843Required for interaction with UGO1Add BLAST214
Regioni769 – 831HR21 PublicationAdd BLAST63

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili798 – 825Sequence analysisAdd BLAST28

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 coiled-coil heptad repeat domains HRN, HR1 and HR2 are required for the oligomerization and function in mitochondrial fusion.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000177197

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P38297

KEGG Orthology (KO)

More...
KOi
K06030

Identification of Orthologs from Complete Genome Data

More...
OMAi
DYVHSNA

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022812 Dynamin_SF
IPR030381 G_DYNAMIN_dom
IPR027094 Mitofusin_fam
IPR027417 P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR10465 PTHR10465, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00350 Dynamin_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51718 G_DYNAMIN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD796DA455E2AE28B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z36048 Genomic DNA Translation: CAA85140.1
BK006936 Genomic DNA Translation: DAA07293.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S46050

NCBI Reference Sequences

More...
RefSeqi
NP_009738.1, NM_001178527.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YBR179C_mRNA; YBR179C; YBR179C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852477

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YBR179C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi32877, 146 interactors
ComplexPortaliCPX-161 FZO1-MGM1-UGO1 complex
DIPiDIP-5581N
IntActiP38297, 4 interactors
MINTiP38297
STRINGi4932.YBR179C

Protein family/group databases

TCDBi1.N.6.1.1 the mitochondrial inner/outer membrane fusion (mmf) family

PTM databases

iPTMnetiP38297

Proteomic databases

MaxQBiP38297
PaxDbiP38297
PRIDEiP38297
TopDownProteomicsiP38297

Genome annotation databases

EnsemblFungiiYBR179C_mRNA; YBR179C; YBR179C
GeneIDi852477
KEGGisce:YBR179C

Organism-specific databases

EuPathDBiFungiDB:YBR179C
SGDiS000000383 FZO1

Phylogenomic databases

HOGENOMiHOG000177197
InParanoidiP38297
KOiK06030
OMAiDYVHSNA

Enzyme and pathway databases

BioCyciYEAST:G3O-29123-MONOMER
ReactomeiR-SCE-983231 Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P38297

Family and domain databases

InterProiView protein in InterPro
IPR022812 Dynamin_SF
IPR030381 G_DYNAMIN_dom
IPR027094 Mitofusin_fam
IPR027417 P-loop_NTPase
PANTHERiPTHR10465 PTHR10465, 1 hit
PfamiView protein in Pfam
PF00350 Dynamin_N, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51718 G_DYNAMIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFZO1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P38297
Secondary accession number(s): D6VQH3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 16, 2019
This is version 157 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again