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UniProtKB - P40318 (DOA10_YEAST)

Entry version 182 (10 Feb 2021)
Sequence version 1 (01 Feb 1995)
Previous versions | rss
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Protein

ERAD-associated E3 ubiquitin-protein ligase DOA10

Gene

SSM4

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

E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Mediates the degradation of a broad range of substrates, including endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC) (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains (PubMed:16873066). ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1 (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Also recognizes the N-terminally acetylated residue of proteins as degradation signal (degron) (PubMed:20110468). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8 (PubMed:20110468). Catalyzes ubiquitination of mislocalized tail-anchored proteins that are extracted from the mitochondrion membrane by MSP1: following extraction, mistargeted proteins are transferred to the endoplasmic retuculum, where they are ubiquitinated by DOA10 and degraded by the proteasome (PubMed:31445887).8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri31 – 100RING-CH-typePROSITE-ProRule annotationAdd BLAST70

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:G3O-31303-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

Protein family/group databases

Transport Classification Database

More...TCDBi		3.A.16.1.2, the endoplasmic reticular retrotranslocon (er-rt) 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%5Fand%5Ftaxonomy%5Fsection">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:
ERAD-associated E3 ubiquitin-protein ligase DOA10 (EC:2.3.2.271 Publication)
Alternative name(s):
RING-type E3 ubiquitin transferase DOA10Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:SSM4
Synonyms:DOA10
Ordered Locus Names:YIL030C
ORF Names:YI3299.01C, YI9905.18C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 IX

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000001292, SSM4

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YIL030C

<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%5Flocation%5Fsection">'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 – 131CytoplasmicSequence analysisAdd BLAST131
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei132 – 152HelicalSequence analysisAdd BLAST21
Topological domaini153 – 203LumenalSequence analysisAdd BLAST51
Transmembranei204 – 224HelicalSequence analysisAdd BLAST21
Topological domaini225 – 468CytoplasmicSequence analysisAdd BLAST244
Transmembranei469 – 489HelicalSequence analysisAdd BLAST21
Topological domaini490 – 491LumenalSequence analysis2
Transmembranei492 – 512HelicalSequence analysisAdd BLAST21
Topological domaini513 – 626CytoplasmicSequence analysisAdd BLAST114
Transmembranei627 – 647HelicalSequence analysisAdd BLAST21
Topological domaini648 – 660LumenalSequence analysisAdd BLAST13
Transmembranei661 – 681HelicalSequence analysisAdd BLAST21
Topological domaini682 – 739CytoplasmicSequence analysisAdd BLAST58
Transmembranei740 – 760HelicalSequence analysisAdd BLAST21
Topological domaini761 – 777LumenalSequence analysisAdd BLAST17
Transmembranei778 – 797HelicalSequence analysisAdd BLAST20
Topological domaini798 – 965CytoplasmicSequence analysisAdd BLAST168
Transmembranei966 – 986HelicalSequence analysisAdd BLAST21
Topological domaini987 – 1019LumenalSequence analysisAdd BLAST33
Transmembranei1020 – 1040HelicalSequence analysisAdd BLAST21
Topological domaini1041 – 1113CytoplasmicSequence analysisAdd BLAST73
Transmembranei1114 – 1134HelicalSequence analysisAdd BLAST21
Topological domaini1135 – 1168LumenalSequence analysisAdd BLAST34
Transmembranei1169 – 1189HelicalSequence analysisAdd BLAST21
Topological domaini1190 – 1213CytoplasmicSequence analysisAdd BLAST24
Transmembranei1214 – 1234HelicalSequence analysisAdd BLAST21
Topological domaini1235 – 1270LumenalSequence analysisAdd BLAST36
Transmembranei1271 – 1291HelicalSequence analysisAdd BLAST21
Topological domaini1292 – 1319CytoplasmicSequence analysisAdd BLAST28

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000722141 – 1319ERAD-associated E3 ubiquitin-protein ligase DOA10Add BLAST1319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P40318

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

More...PaxDbi		P40318

PRoteomics IDEntifications database

More...PRIDEi		P40318

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P40318

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the DOA10 complex which contains SSM4/DOA10, CDC48, NPL4, UFD1 AND UBX2/SEL1. The complex is composed of the membrane integral E3 ligase SSM4/DOA10 and the heterotrimeric UFD1-NPL4-CDC48/p97 (UNC) ATPase complex recruited by UBX2/SEL1.

Interacts with UBX2/SEL1.

Interacts also with its associated ubiquitin conjugating enzymesh UBC6 and UBC7 with its membrane anchor CUE1.

Interacts with PEX29.

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34959, 255 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3074, Doa10 ubiquitin ligase complex

Database of interacting proteins

More...DIPi		DIP-7286N

Protein interaction database and analysis system

More...IntActi		P40318, 83 interactors

Molecular INTeraction database

More...MINTi		P40318

STRING: functional protein association networks

More...STRINGi		4932.YIL030C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P40318, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P40318

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P40318

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi288 – 291Poly-Ala4
Compositional biasi293 – 296Poly-Asn4
Compositional biasi332 – 341Asp/Gln/Ser-rich (acidic)10
Compositional biasi369 – 374Poly-Gln6

<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 RING-CH-type zinc finger domain is required for E3 ligase activity.

<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

Belongs to the DOA10/MARCH6 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 100RING-CH-typePROSITE-ProRule annotationAdd BLAST70

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1609, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155171

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_006729_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P40318

Identification of Orthologs from Complete Genome Data

More...OMAi		LRLSHFI

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011016, Znf_RING-CH
IPR013083, Znf_RING/FYVE/PHD

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12906, RINGv, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00744, RINGv, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51292, ZF_RING_CH, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P40318-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDVDSDVNVS RLRDELHKVA NEETDTATFN DDAPSGATCR ICRGEATEDN 
        60         70         80         90        100
PLFHPCKCRG SIKYMHESCL LEWVASKNID ISKPGADVKC DICHYPIQFK 
       110        120        130        140        150
TIYAENMPEK IPFSLLLSKS ILTFFEKARL ALTIGLAAVL YIIGVPLVWN 
       160        170        180        190        200
MFGKLYTMML DGSSPYPGDF LKSLIYGYDQ SATPELTTRA IFYQLLQNHS 
       210        220        230        240        250
FTSLQFIMIV ILHIALYFQY DMIVREDVFS KMVFHKIGPR LSPKDLKSRL 
       260        270        280        290        300
KERFPMMDDR MVEYLAREMR AHDENRQEQG HDRLNMPAAA ADNNNNVINP 
       310        320        330        340        350
RNDNVPPQDP NDHRNFENLR HVDELDHDEA TEEHENNDSD NSLPSGDDSS 
       360        370        380        390        400
RILPGSSSDN EEDEEAEGQQ QQQQPEEEAD YRDHIEPNPI DMWANRRAQN 
       410        420        430        440        450
EFDDLIAAQQ NAINRPNAPV FIPPPAQNRA GNVDQDEQDF GAAVGVPPAQ 
       460        470        480        490        500
ANPDDQGQGP LVINLKLKLL NVIAYFIIAV VFTAIYLAIS YLFPTFIGFG 
       510        520        530        540        550
LLKIYFGIFK VILRGLCHLY YLSGAHIAYN GLTKLVPKVD VAMSWISDHL 
       560        570        580        590        600
IHDIIYLYNG YTENTMKHSI FIRALPALTT YLTSVSIVCA SSNLVSRGYG 
       610        620        630        640        650
RENGMSNPTR RLIFQILFAL KCTFKVFTLF FIELAGFPIL AGVMLDFSLF 
       660        670        680        690        700
CPILASNSRM LWVPSICAIW PPFSLFVYWT IGTLYMYWFA KYIGMIRKNI 
       710        720        730        740        750
IRPGVLFFIR SPEDPNIKIL HDSLIHPMSI QLSRLCLSMF IYAIFIVLGF 
       760        770        780        790        800
GFHTRIFFPF MLKSNLLSVP EAYKPTSIIS WKFNTILLTL YFTKRILESS 
       810        820        830        840        850
SYVKPLLERY WKTIFKLCSR KLRLSSFILG KDTPTERGHI VYRNLFYKYI 
       860        870        880        890        900
AAKNAEWSNQ ELFTKPKTLE QAEELFGQVR DVHAYFVPDG VLMRVPSSDI 
       910        920        930        940        950
VSRNYVQTMF VPVTKDDKLL KPLDLERIKE RNKRAAGEFG YLDEQNTEYD 
       960        970        980        990       1000
QYYIVYVPPD FRLRYMTLLG LVWLFASILM LGVTFISQAL INFVCSFGFL 
      1010       1020       1030       1040       1050
PVVKLLLGER NKVYVAWKEL SDISYSYLNI YYVCVGSVCL SKIAKDILHF 
      1060       1070       1080       1090       1100
TEGQNTLDEH AVDENEVEEV EHDIPERDIN NAPVNNINNV EEGQGIFMAI 
      1110       1120       1130       1140       1150
FNSIFDSMLV KYNLMVFIAI MIAVIRTMVS WVVLTDGILA CYNYLTIRVF 
      1160       1170       1180       1190       1200
GNSSYTIGNS KWFKYDESLL FVVWIISSMV NFGTGYKSLK LFFRNRNTSK 
      1210       1220       1230       1240       1250
LNFLKTMALE LFKQGFLHMV IYVLPIIILS LVFLRDVSTK QIIDISHGSR 
      1260       1270       1280       1290       1300
SFTLSLNESF PTWTRMQDIY FGLLIALESF TFFFQATVLF IQWFKSTVQN 
      1310 
VKDEVYTKGR ALENLPDES
Length:1,319
Mass (Da):151,455
Last modified:February 1, 1995 - 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:i3EDFF7F9D90A0C8C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti241L → F in CAA54133 (PubMed:7816042).Curated1
Sequence conflicti743A → T in CAA54133 (PubMed:7816042).Curated1
Sequence conflicti1085N → D in CAA54133 (PubMed:7816042).Curated1
Sequence conflicti1186Y → F in CAA54133 (PubMed:7816042).Curated1

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
X76715 Genomic DNA Translation: CAA54133.1
Z46881 Genomic DNA Translation: CAA86961.1
Z46861 Genomic DNA Translation: CAA86921.1
BK006942 Genomic DNA Translation: DAA08517.1

Protein sequence database of the Protein Information Resource

More...PIRi		S49951

NCBI Reference Sequences

More...RefSeqi		NP_012234.3, NM_001179380.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YIL030C_mRNA; YIL030C; YIL030C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854781

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YIL030C

<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
X76715 Genomic DNA Translation: CAA54133.1
Z46881 Genomic DNA Translation: CAA86961.1
Z46861 Genomic DNA Translation: CAA86921.1
BK006942 Genomic DNA Translation: DAA08517.1
PIRiS49951
RefSeqiNP_012234.3, NM_001179380.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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Protein Data Bank RCSB

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Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M6MNMR-A19-101[»]
BMRBiP40318
SMRiP40318
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34959, 255 interactors
ComplexPortaliCPX-3074, Doa10 ubiquitin ligase complex
DIPiDIP-7286N
IntActiP40318, 83 interactors
MINTiP40318
STRINGi4932.YIL030C

Protein family/group databases

TCDBi3.A.16.1.2, the endoplasmic reticular retrotranslocon (er-rt) family

PTM databases

iPTMnetiP40318

Proteomic databases

MaxQBiP40318
PaxDbiP40318
PRIDEiP40318

Genome annotation databases

EnsemblFungiiYIL030C_mRNA; YIL030C; YIL030C
GeneIDi854781
KEGGisce:YIL030C

Organism-specific databases

SGDiS000001292, SSM4
VEuPathDBiFungiDB:YIL030C

Phylogenomic databases

eggNOGiKOG1609, Eukaryota
GeneTreeiENSGT00940000155171
HOGENOMiCLU_006729_0_0_1
InParanoidiP40318
OMAiLRLSHFI

Enzyme and pathway databases

UniPathwayiUPA00143
BioCyciMetaCyc:G3O-31303-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:P40318
RNActiP40318, protein

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR011016, Znf_RING-CH
IPR013083, Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF12906, RINGv, 1 hit
SMARTiView protein in SMART
SM00744, RINGv, 1 hit
PROSITEiView protein in PROSITE
PS51292, ZF_RING_CH, 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 nameiDOA10_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: P40318
Secondary accession number(s): D6VVQ1
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 10, 2021
This is version 182 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

3D-structure, Reference proteome

Documents

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