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 180 (13 Nov 2019)
Sequence version 1 (01 Jun 1994)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Protein DOA1

Gene

DOA1

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

Ubiquitin-binding protein involved in protein ubiquitination, sorting and degradation (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:18508771, PubMed:20508643, PubMed:27044889). Acts as a ubiquitinated substrate-recruiting adapter for chaperone ATPase CDC48 by binding mono- or polyubiquitin chains (PubMed:15096053, PubMed:16427015, PubMed:16428438, PubMed:27044889). Depending on the context, promotes or prevents proteasomal degradation of ubiquitinated proteins (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:27044889). Involved in the ubiquitin fusion degradation (UFD) pathway by promoting the degradation of ubiquitinated proteins (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:27044889). Involved in the mitochondria-associated degradation pathway (MAD) by promoting the degradation of several ubiquitinated membrane proteins (PubMed:27044889). By competing with UFD2 to bind CDC48, prevents the multi-ubiquitination and subsequent degradation of UFD2-dependent substrates (PubMed:16427015). Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation (PubMed:20508643). Involved in the ubiquitin-mediated sorting of membrane proteins into multivesicular bodies (MVBs) (PubMed:18508771). In addition, plays an essential role in maintaining cellular ubiquitin levels (PubMed:7615550, PubMed:16427015, PubMed:16428438, PubMed:18508771, PubMed:19805280). May affect indirectly the degradation of ubiquitinylated proteins by regulating cellular ubiquitin levels (PubMed:7615550, PubMed:23525333).11 Publications

Miscellaneous

Present with 6800 molecules/cell in log phase SD medium.1 Publication

<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

  • protein-containing complex binding Source: UniProtKB
  • ubiquitin binding Source: SGD
  • ubiquitin-dependent protein binding Source: UniProtKB

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

Biological processUbl conjugation pathway

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31971-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-8951664 Neddylation
R-SCE-983168 Antigen processing: Ubiquitination & Proteasome degradation

<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:
Protein DOA11 Publication
Alternative name(s):
Degradation of alpha protein 11 Publication
Ubiquitin fusion degradation protein 31 Publication
<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:DOA11 PublicationImported
Synonyms:UFD31 PublicationImported, ZZZ4Imported
Ordered Locus Names:YKL213CImported
<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 XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YKL213C

Saccharomyces Genome Database

More...
SGDi
S000001696 DOA1

<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

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Severely reduces cell growth in response to misfolded protein, translation inhibition-induced, heat or mitochondrial oxidative stresses but not in response to ER stress (PubMed:16427015, PubMed:18508771, PubMed:16428438, PubMed:27044889).4 Publications

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>Mutagenesisi2 – 425Missing : No binding to ubiquitin but does not affect the interaction with CDC48. 1 PublicationAdd BLAST424
Mutagenesisi2 – 359Missing : No binding to ubiquitin. 1 PublicationAdd BLAST358
Mutagenesisi2 – 353Missing : No binding to ubiquitin. 1 PublicationAdd BLAST352
Mutagenesisi2 – 330Missing : Does not affect binding to ubiquitin. 1 PublicationAdd BLAST329
Mutagenesisi2 – 287Missing : No binding to ubiquitin. 1 PublicationAdd BLAST286
Mutagenesisi5L → S: No binding to ubiquitin. 1 Publication1
Mutagenesisi15D → S: No binding to ubiquitin. Reduces cell growth at high temperatures (37 degrees Celsius). Inhibits cell growth at high temperatures and prevents the degradation of mitochondrial proteins FZO1, MDM34 and MSP1 without affecting the interaction with CDC48 and UFD1; when associated with A-222 and A-265. 2 Publications1
Mutagenesisi158A → E: No binding to ubiquitin. 1 Publication1
Mutagenesisi222F → A: No binding to ubiquitin. Inhibits cell growth at high temperatures and prevents the degradation of mitochondrial proteins FZO1, MDM34 and MSP1 without affecting the interaction with CDC48 and UFD1; when associated with S-15 and A-265. 2 Publications1
Mutagenesisi237C → Y in ufd3-2; severe reduction in the degradation of short-lived ubiquitin-fusion proteins. No defect in the interaction with CDC48. 1 Publication1
Mutagenesisi265W → A: No binding to ubiquitin. Inhibits cell growth at high temperatures and prevents the degradation of mitochondrial proteins FZO1, MDM34 and MSP1 without affecting the interaction with CDC48 and UFD1; when associated with S-15 and A-222. 2 Publications1
Mutagenesisi281D → S: No binding to ubiquitin. 1 Publication1
Mutagenesisi289 – 715Missing : No binding to ubiquitin. 1 PublicationAdd BLAST427
Mutagenesisi417F → D: Prevents binding to mono-ubiquitin, reduces levels of free ubiquitin, prevents the degradation of mitochondrial proteins FZO1, MDM34 and MSP1 and is partially sensitive to misfolded protein or translation inhibition-induced stresses; when associated with D-434. 2 Publications1
Mutagenesisi426 – 715Missing : No binding to ubiquitin and no interaction with CDC48. 2 PublicationsAdd BLAST290
Mutagenesisi434 – 443Missing : Loss of interaction with HSE1 and ubiquitin without affecting general ubquitination levels. Prevents protease CSP1 sorting into the vacuole. 1 Publication10
Mutagenesisi434 – 440FILKNTN → AAAKAAA: Loss of interaction with HSE1 without affecting binding to ubiquitin or general ubquitination levels. Prevents protease CSP1 sorting into the vacuole. 1 Publication7
Mutagenesisi434F → D: Prevents binding to mono-ubiquitin, reduces levels of free ubiquitin, prevents the degradation of mitochondrial proteins FZO1, MDM34 and MSP1 and is partially sensitive to misfolded protein or translation inhibition-induced stresses; when associated with D-417. 2 Publications1
Mutagenesisi451 – 715Missing : Does not affect binding to ubiquitin. 1 PublicationAdd BLAST265
Mutagenesisi495 – 715Missing : Loss of interaction with CDC48 without affecting binding to ubiquitin. 1 PublicationAdd BLAST221
Mutagenesisi541R → A: Depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. Prevents the interaction with CDC48 and UFD1 and thus the degradation of mitochondrial proteins FZO1, MDM34 and MSP1; when associated with A-669. 2 Publications1
Mutagenesisi669R → A: Depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. Prevents the interaction with CDC48 and UFD1 and thus the degradation of mitochondrial proteins FZO1, MDM34 and MSP1; when associated with A-541. 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_00000509581 – 715Protein DOA1Add BLAST715

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 residuei332PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P36037

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

More...
PaxDbi
P36037

PRoteomics IDEntifications database

More...
PRIDEi
P36037

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P36037

<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

Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase OTU1; within the complex interacts with CDC48 (PubMed:16427015).

Interacts (via PUL domain) with CDC48 (via C-terminus); the interaction is direct (PubMed:8890162, PubMed:16427015, PubMed:16428438, PubMed:27044889, PubMed:19805280, PubMed:20508643).

Forms a complex composed of CDC48, DOA1, deubiquitinase UBP3 and probably BRE5; within the complex interacts with CDC48 and UBP3 (PubMed:20508643). May form a complex composed of VPS27, HSE1 and DOA1 (PubMed:18508771).

Interacts with HSE1 (via SH3 domain) (PubMed:18508771).

Interacts (via WD repeats and PFU domain) with ubiquitin; the interaction is direct (PubMed:15096053, PubMed:16427015, PubMed:16428438, PubMed:21070969).

Interacts with ubiquitinated FZO1 but not unmodified FZO1; the interaction recruits FZO1 to CDC48 and promotes FZO1 proteasomal degradation (PubMed:27044889).

9 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33952, 698 interactors

Database of interacting proteins

More...
DIPi
DIP-6274N

Protein interaction database and analysis system

More...
IntActi
P36037, 10 interactors

Molecular INTeraction database

More...
MINTi
P36037

STRING: functional protein association networks

More...
STRINGi
4932.YKL213C

<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

1715
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P36037

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P36037

<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati11 – 40WD 1Sequence analysisAdd BLAST30
Repeati53 – 82WD 2Sequence analysisAdd BLAST30
Repeati97 – 125WD 3Sequence analysisAdd BLAST29
Repeati135 – 166WD 4Sequence analysisAdd BLAST32
Repeati177 – 206WD 5Sequence analysisAdd BLAST30
Repeati218 – 247WD 6Sequence analysisAdd BLAST30
Repeati259 – 288WD 7Sequence analysisAdd BLAST30
<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>Domaini352 – 449PFUPROSITE-ProRule annotationAdd BLAST98
Domaini465 – 715PULPROSITE-ProRule annotationAdd BLAST251
Repeati478 – 512ARM 11 Publication1 PublicationAdd BLAST35
Repeati513 – 543ARM 21 Publication1 PublicationAdd BLAST31
Repeati544 – 582ARM 31 Publication1 PublicationAdd BLAST39
Repeati583 – 635ARM 41 Publication1 PublicationAdd BLAST53
Repeati636 – 680ARM 51 Publication1 PublicationAdd BLAST45
Repeati681 – 715ARM 61 Publication1 PublicationAdd BLAST35

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>Regioni434 – 440Interaction with HSE11 Publication7

<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 WD repeats mediate interaction with ubiquitin.1 Publication
The PUL domain is composed of 6 armadillo-like repeats and mediates the interaction with CDC48 C-terminus.3 Publications
The PFU domain mediates interaction with ubiquitin.2 Publications

<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 WD repeat PLAP family.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000174247

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P36037

KEGG Orthology (KO)

More...
KOi
K14018

Identification of Orthologs from Complete Genome Data

More...
OMAi
STIMVKN

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.150.410, 1 hit
1.25.10.10, 1 hit
2.130.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR020472 G-protein_beta_WD-40_rep
IPR015155 PFU
IPR038122 PFU_sf
IPR033510 PLAA/Doa1/Lub1
IPR013535 PUL_dom
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR19849 PTHR19849, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09070 PFU, 1 hit
PF08324 PUL, 1 hit
PF00400 WD40, 4 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00320 GPROTEINBRPT

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00320 WD40, 6 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 1 hit
SSF50978 SSF50978, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51394 PFU, 1 hit
PS51396 PUL, 1 hit
PS50082 WD_REPEATS_2, 4 hits
PS50294 WD_REPEATS_REGION, 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.

P36037-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGYQLSATLK GHDQDVRDVV AVDDSKVASV SRDGTVRLWS KDDQWLGTVV
60 70 80 90 100
YTGQGFLNSV CYDSEKELLL FGGKDTMING VPLFATSGED PLYTLIGHQG
110 120 130 140 150
NVCSLSFQDG VVISGSWDKT AKVWKEGSLV YNLQAHNASV WDAKVVSFSE
160 170 180 190 200
NKFLTASADK TIKLWQNDKV IKTFSGIHND VVRHLAVVDD GHFISCSNDG
210 220 230 240 250
LIKLVDMHTG DVLRTYEGHE SFVYCIKLLP NGDIVSCGED RTVRIWSKEN
260 270 280 290 300
GSLKQVITLP AISIWSVDCM SNGDIIVGSS DNLVRIFSQE KSRWASEDEI
310 320 330 340 350
NELSTQVEKS TISSKTIEFD ESKLSPYEIL QSPGRKEGQI VVVKSPQGTI
360 370 380 390 400
EAHQFSNSSW KKVGDVVGAG ATGNDKKIEF EGKTYDYVFD VDIEDGKPPL
410 420 430 440 450
KLPINVSDNP YTAADNFLAR YELPMSYRDQ VVQFILKNTN GISLDQPNDN
460 470 480 490 500
ASSSAVSPSK TSVMKVLPVK QYLIMENYNP DTIFNGIVKI NSNEKTFDDE
510 520 530 540 550
ILAQIGGALH DIDESWELLL SFANTIRSNW EIKTPAYDIV RLIVKKLPYS
560 570 580 590 600
SDIKDYIEEG LGNKNITLTM LTVRILVNCF NNENWGVKLL ESNQVYKSIF
610 620 630 640 650
ETIDTEFSQA SAKQSQNLAI AVSTLIFNYS ALVTKGNSDL ELLPIVADAI
660 670 680 690 700
NTKYGPLEEY QECEEAAYRL TVAYGNLATV EPTLRQFANS VTWLANIKRS
710
YGNVPRFKDI FDDLS
Length:715
Mass (Da):79,506
Last modified:June 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:i593B808169283B5F
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 conflicti180D → DI AA sequence (PubMed:15096053).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
U39947 Genomic DNA Translation: AAA82258.1
X75951 Genomic DNA Translation: CAA53560.1
Z28213 Genomic DNA Translation: CAA82058.1
BK006944 Genomic DNA Translation: DAA08956.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S38051

NCBI Reference Sequences

More...
RefSeqi
NP_012709.1, NM_001179778.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKL213C_mRNA; YKL213C; YKL213C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853667

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKL213C

<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
U39947 Genomic DNA Translation: AAA82258.1
X75951 Genomic DNA Translation: CAA53560.1
Z28213 Genomic DNA Translation: CAA82058.1
BK006944 Genomic DNA Translation: DAA08956.1
PIRiS38051
RefSeqiNP_012709.1, NM_001179778.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GAEX-ray1.60A/B464-715[»]
3L3FX-ray1.90X354-715[»]
3ODTX-ray1.35A/B2-300[»]
3PSPX-ray2.42A325-715[»]
3PSTX-ray2.00A325-715[»]
SMRiP36037
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi33952, 698 interactors
DIPiDIP-6274N
IntActiP36037, 10 interactors
MINTiP36037
STRINGi4932.YKL213C

PTM databases

iPTMnetiP36037

Proteomic databases

MaxQBiP36037
PaxDbiP36037
PRIDEiP36037

Genome annotation databases

EnsemblFungiiYKL213C_mRNA; YKL213C; YKL213C
GeneIDi853667
KEGGisce:YKL213C

Organism-specific databases

EuPathDBiFungiDB:YKL213C
SGDiS000001696 DOA1

Phylogenomic databases

HOGENOMiHOG000174247
InParanoidiP36037
KOiK14018
OMAiSTIMVKN

Enzyme and pathway databases

BioCyciYEAST:G3O-31971-MONOMER
ReactomeiR-SCE-8951664 Neddylation
R-SCE-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

EvolutionaryTraceiP36037

Protein Ontology

More...
PROi
PR:P36037

Family and domain databases

Gene3Di1.10.150.410, 1 hit
1.25.10.10, 1 hit
2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR020472 G-protein_beta_WD-40_rep
IPR015155 PFU
IPR038122 PFU_sf
IPR033510 PLAA/Doa1/Lub1
IPR013535 PUL_dom
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR19849 PTHR19849, 1 hit
PfamiView protein in Pfam
PF09070 PFU, 1 hit
PF08324 PUL, 1 hit
PF00400 WD40, 4 hits
PRINTSiPR00320 GPROTEINBRPT
SMARTiView protein in SMART
SM00320 WD40, 6 hits
SUPFAMiSSF48371 SSF48371, 1 hit
SSF50978 SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS51394 PFU, 1 hit
PS51396 PUL, 1 hit
PS50082 WD_REPEATS_2, 4 hits
PS50294 WD_REPEATS_REGION, 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 nameiDOA1_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: P36037
Secondary accession number(s): D6VWZ0
<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: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 13, 2019
This is version 180 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, Complete proteome, Direct protein sequencing, 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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