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UniProtKB - P22515 (UBA1_YEAST)

Entry version 215 (23 Feb 2022)
Sequence version 2 (01 Jun 1994)
Previous versions | rss
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Protein

Ubiquitin-activating enzyme E1 1

Gene

UBA1

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

Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.

3 Publications

Miscellaneous

There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.1 Publication
Present with 17700 molecules/cell in log phase SD medium.1 Publication

<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

  • ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.2 Publications EC:6.2.1.45

<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.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei444ATP; via amide nitrogen1 Publication1
Binding sitei470ATP1 Publication1
Binding sitei481ATP1 Publication1
Binding sitei494ATP1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei600Glycyl thioester intermediatePROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi544 – 545ATP1 Publication2

<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 functionLigase
Biological processUbl conjugation pathway
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-SCE-983168, Antigen processing: Ubiquitination & Proteasome degradation

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

More...UniPathwayi		UPA00143

<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:
Ubiquitin-activating enzyme E1 1 (EC:6.2.1.452 Publications)
<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:UBA1
Ordered Locus Names:YKL210W
<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 XI

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000001693, UBA1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YKL210W

<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

Keywords - Cellular componenti

Cytoplasm, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi912I → P: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with P-914. 1 Publication1
Mutagenesisi914S → P: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with P-912. 1 Publication1
Mutagenesisi1004E → K: Strongly reduces formation of the thioester intermediate with ubiquitin. 1 Publication1
Mutagenesisi1014D → K: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with K-1016. 1 Publication1
Mutagenesisi1016E → K: Strongly reduces formation of the thioester intermediate with ubiquitin; when associated with K-1014. 1 Publication1

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001949772 – 1024Ubiquitin-activating enzyme E1 1Add BLAST1023

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 residuei2N-acetylserineCombined sources1
Modified residuei265PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki608Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei914PhosphoserineCombined sources1

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

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P22515

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

More...PaxDbi		P22515

PRoteomics IDEntifications database

More...PRIDEi		P22515

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P22515

<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

Monomer. Binds simultaneously two ubiquitin chains.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		33955, 154 interactors

Database of interacting proteins

More...DIPi		DIP-4853N

Protein interaction database and analysis system

More...IntActi		P22515, 29 interactors

Molecular INTeraction database

More...MINTi		P22515

STRING: functional protein association networks

More...STRINGi		4932.YKL210W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P22515, 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

11024
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		P22515

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		P22515

<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>Repeati27 – 1641-1Add BLAST138
Repeati425 – 5791-2Add BLAST155

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>Regioni27 – 5792 approximate repeatsAdd BLAST553

<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 ubiquitin-activating E1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2012, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000166138

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002556_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P22515

Identification of Orthologs from Complete Genome Data

More...OMAi		GANLHAF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.2660, 1 hit
2.40.30.180, 1 hit
3.10.290.60, 1 hit
3.50.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR032420, E1_4HB
IPR032418, E1_FCCH
IPR042302, E1_FCCH_sf
IPR045886, ThiF/MoeB/HesA
IPR000594, ThiF_NAD_FAD-bd
IPR018965, Ub-activating_enz_E1_C
IPR042449, Ub-E1_IAD_1
IPR038252, UBA_E1_C_sf
IPR019572, UBA_E1_SCCH
IPR042063, Ubi_acti_E1_SCCH
IPR035985, Ubiquitin-activating_enz
IPR018075, UBQ-activ_enz_E1
IPR018074, UBQ-activ_enz_E1_CS
IPR033127, UBQ-activ_enz_E1_Cys_AS
IPR000011, UBQ/SUMO-activ_enz_E1-like

The PANTHER Classification System

More...PANTHERi		PTHR10953, PTHR10953, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16191, E1_4HB, 1 hit
PF16190, E1_FCCH, 1 hit
PF09358, E1_UFD, 1 hit
PF00899, ThiF, 2 hits
PF10585, UBA_e1_thiolCys, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01849, UBIQUITINACT

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00985, UBA_e1_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF69572, SSF69572, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01408, Ube1, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00536, UBIQUITIN_ACTIVAT_1, 1 hit
PS00865, UBIQUITIN_ACTIVAT_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%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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P22515-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSNNSGLSA AGEIDESLYS RQLYVLGKEA MLKMQTSNVL ILGLKGLGVE 
        60         70         80         90        100
IAKNVVLAGV KSMTVFDPEP VQLADLSTQF FLTEKDIGQK RGDVTRAKLA 
       110        120        130        140        150
ELNAYVPVNV LDSLDDVTQL SQFQVVVATD TVSLEDKVKI NEFCHSSGIR 
       160        170        180        190        200
FISSETRGLF GNTFVDLGDE FTVLDPTGEE PRTGMVSDIE PDGTVTMLDD 
       210        220        230        240        250
NRHGLEDGNF VRFSEVEGLD KLNDGTLFKV EVLGPFAFRI GSVKEYGEYK 
       260        270        280        290        300
KGGIFTEVKV PRKISFKSLK QQLSNPEFVF SDFAKFDRAA QLHLGFQALH 
       310        320        330        340        350
QFAVRHNGEL PRTMNDEDAN ELIKLVTDLS VQQPEVLGEG VDVNEDLIKE 
       360        370        380        390        400
LSYQARGDIP GVVAFFGGLV AQEVLKACSG KFTPLKQFMY FDSLESLPDP 
       410        420        430        440        450
KNFPRNEKTT QPVNSRYDNQ IAVFGLDFQK KIANSKVFLV GSGAIGCEML 
       460        470        480        490        500
KNWALLGLGS GSDGYIVVTD NDSIEKSNLN RQFLFRPKDV GKNKSEVAAE 
       510        520        530        540        550
AVCAMNPDLK GKINAKIDKV GPETEEIFND SFWESLDFVT NALDNVDART 
       560        570        580        590        600
YVDRRCVFYR KPLLESGTLG TKGNTQVIIP RLTESYSSSR DPPEKSIPLC 
       610        620        630        640        650
TLRSFPNKID HTIAWAKSLF QGYFTDSAEN VNMYLTQPNF VEQTLKQSGD 
       660        670        680        690        700
VKGVLESISD SLSSKPHNFE DCIKWARLEF EKKFNHDIKQ LLFNFPKDAK 
       710        720        730        740        750
TSNGEPFWSG AKRAPTPLEF DIYNNDHFHF VVAGASLRAY NYGIKSDDSN 
       760        770        780        790        800
SKPNVDEYKS VIDHMIIPEF TPNANLKIQV NDDDPDPNAN AANGSDEIDQ 
       810        820        830        840        850
LVSSLPDPST LAGFKLEPVD FEKDDDTNHH IEFITACSNC RAQNYFIETA 
       860        870        880        890        900
DRQKTKFIAG RIIPAIATTT SLVTGLVNLE LYKLIDNKTD IEQYKNGFVN 
       910        920        930        940        950
LALPFFGFSE PIASPKGEYN NKKYDKIWDR FDIKGDIKLS DLIEHFEKDE 
       960        970        980        990       1000
GLEITMLSYG VSLLYASFFP PKKLKERLNL PITQLVKLVT KKDIPAHVST 
      1010       1020 
MILEICADDK EGEDVEVPFI TIHL
Length:1,024
Mass (Da):114,266
Last modified:June 1, 1994 - v2
<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:i8910804DF9156661
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 conflicti526E → K in CAA39056 (PubMed:1989885).Curated1
Sequence conflicti736S → N in CAA39056 (PubMed:1989885).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
X55386 Genomic DNA Translation: CAA39056.1
Z28210 Genomic DNA Translation: CAA82055.1
X15428 Genomic DNA Translation: CAA33468.1
BK006944 Genomic DNA Translation: DAA08959.1

Protein sequence database of the Protein Information Resource

More...PIRi		S38048

NCBI Reference Sequences

More...RefSeqi		NP_012712.1, NM_001179775.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YKL210W_mRNA; YKL210W; YKL210W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853670

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YKL210W

<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
X55386 Genomic DNA Translation: CAA39056.1
Z28210 Genomic DNA Translation: CAA82055.1
X15428 Genomic DNA Translation: CAA33468.1
BK006944 Genomic DNA Translation: DAA08959.1
PIRiS38048
RefSeqiNP_012712.1, NM_001179775.1

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
3CMMX-ray2.70A/C10-1024[»]
4NNJX-ray2.40A/C9-1024[»]
5L6HX-ray2.30A/C1-1024[»]
5L6IX-ray2.76A/C1-1024[»]
5L6JX-ray2.68A/C1-1024[»]
5TR4X-ray2.20A/C9-1024[»]
6NYAX-ray2.06A/D11-1024[»]
6ZQHX-ray2.03A/C1-1024[»]
7K5JX-ray3.42A/C/D/G/I/K/S/U11-1024[»]
SMRiP22515
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi33955, 154 interactors
DIPiDIP-4853N
IntActiP22515, 29 interactors
MINTiP22515
STRINGi4932.YKL210W

PTM databases

iPTMnetiP22515

Proteomic databases

MaxQBiP22515
PaxDbiP22515
PRIDEiP22515

Genome annotation databases

EnsemblFungiiYKL210W_mRNA; YKL210W; YKL210W
GeneIDi853670
KEGGisce:YKL210W

Organism-specific databases

SGDiS000001693, UBA1
VEuPathDBiFungiDB:YKL210W

Phylogenomic databases

eggNOGiKOG2012, Eukaryota
GeneTreeiENSGT00940000166138
HOGENOMiCLU_002556_0_0_1
InParanoidiP22515
OMAiGANLHAF

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-SCE-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-SCE-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

EvolutionaryTraceiP22515

Protein Ontology

More...PROi		PR:P22515
RNActiP22515, protein

Family and domain databases

Gene3Di1.10.10.2660, 1 hit
2.40.30.180, 1 hit
3.10.290.60, 1 hit
3.50.50.80, 1 hit
InterProiView protein in InterPro
IPR032420, E1_4HB
IPR032418, E1_FCCH
IPR042302, E1_FCCH_sf
IPR045886, ThiF/MoeB/HesA
IPR000594, ThiF_NAD_FAD-bd
IPR018965, Ub-activating_enz_E1_C
IPR042449, Ub-E1_IAD_1
IPR038252, UBA_E1_C_sf
IPR019572, UBA_E1_SCCH
IPR042063, Ubi_acti_E1_SCCH
IPR035985, Ubiquitin-activating_enz
IPR018075, UBQ-activ_enz_E1
IPR018074, UBQ-activ_enz_E1_CS
IPR033127, UBQ-activ_enz_E1_Cys_AS
IPR000011, UBQ/SUMO-activ_enz_E1-like
PANTHERiPTHR10953, PTHR10953, 1 hit
PfamiView protein in Pfam
PF16191, E1_4HB, 1 hit
PF16190, E1_FCCH, 1 hit
PF09358, E1_UFD, 1 hit
PF00899, ThiF, 2 hits
PF10585, UBA_e1_thiolCys, 1 hit
PRINTSiPR01849, UBIQUITINACT
SMARTiView protein in SMART
SM00985, UBA_e1_C, 1 hit
SUPFAMiSSF69572, SSF69572, 2 hits
TIGRFAMsiTIGR01408, Ube1, 1 hit
PROSITEiView protein in PROSITE
PS00536, UBIQUITIN_ACTIVAT_1, 1 hit
PS00865, UBIQUITIN_ACTIVAT_2, 1 hit

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 nameiUBA1_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: P22515
Secondary accession number(s): D6VWZ3
<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: August 1, 1991
Last sequence update: June 1, 1994
Last modified: February 23, 2022
This is version 215 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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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