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Entry version 183 (18 Sep 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Ubiquitin-conjugating enzyme E2 R1

Gene

CDC34

Organism
Homo sapiens (Human)
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

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed:22496338). Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes (PubMed:10329681, PubMed:10373550, PubMed:10871850, PubMed:11675391, PubMed:12037680, PubMed:15652359, PubMed:17461777, PubMed:17698585, PubMed:19112177, PubMed:19126550, PubMed:19945379, PubMed:20061386, PubMed:20347421).14 Publications

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

CDC34-catalyzed polyubiquitin chain assembly activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF E3 ligase complex subunit.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.11 µM for beta-catenin-monoubiquin1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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.PROSITE-ProRule annotation
    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_section">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 sitei93Glycyl thioester intermediate1

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

    GO - Biological processi

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

    Molecular functionTransferase
    Biological processCell cycle, Ubl conjugation pathway
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.3.2.B6 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-202424 Downstream TCR signaling
    R-HSA-2871837 FCERI mediated NF-kB activation
    R-HSA-5607764 CLEC7A (Dectin-1) signaling
    R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
    R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

    SignaLink: a signaling pathway resource with multi-layered regulatory networks

    More...
    SignaLinki
    P49427

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P49427

    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_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:
    Ubiquitin-conjugating enzyme E2 R1 (EC:2.3.2.234 Publications)
    Alternative name(s):
    (E3-independent) E2 ubiquitin-conjugating enzyme R1 (EC:2.3.2.241 Publication)
    E2 ubiquitin-conjugating enzyme R1
    Ubiquitin-conjugating enzyme E2-32 kDa complementing
    Ubiquitin-conjugating enzyme E2-CDC34
    Ubiquitin-protein ligase R1
    <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:CDC34
    Synonyms:UBCH3, UBE2R1
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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
    • UP000005640 <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 19

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:1734 CDC34

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    116948 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P49427

    <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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    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_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>Mutagenesisi70Y → R: Loss of RBX1-binding. 1 Publication1
    Mutagenesisi85N → Q: Inhibits both mono and polyubiquitination of NFKBIA. 1 Publication1
    Mutagenesisi87Y → A: Decreases polyubiquitination of NFKBIA. 1 Publication1
    Mutagenesisi93C → S or A: Loss of function. 2 Publications1
    Mutagenesisi95S → D: Inhibits both mono and polyubiquitination of NFKBIA. 1 Publication1
    Mutagenesisi97L → S: Loss of function. 1 Publication1
    Mutagenesisi102D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-103. 1 Publication1
    Mutagenesisi103D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-102. 1 Publication1
    Mutagenesisi108E → A: Inhibits both mono and polyubiquitination of NFKBIA; when associated with A-112. 1 Publication1
    Mutagenesisi112E → A: Inhibits both mono andpolyubiquitination of NFKBIA; when associated with A-108. 1 Publication1
    Mutagenesisi117T → E: Loss of RBX1-binding. 1 Publication1
    Mutagenesisi129S → L: No effect on activity, when assayed in a Sic1-SCF-cdc4 ubiquitination assay. 1 Publication1
    Mutagenesisi129S → R: Complete loss of activity, when assayed in a Sic1-SCF-cdc4 ubiquitination assay. 1 Publication1
    Mutagenesisi133E → R: No effect on activity, when assayed in a Sic1-SCF-cdc4 ubiquitination assay. 1 Publication1
    Mutagenesisi138S → A: Decreases monoubiquitination of NFKBIA and inhibits polyubiquitination of NFKBIA. 1 Publication1
    Mutagenesisi143D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-149; A-150 and A-153. 1 Publication1
    Mutagenesisi147M → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-149; A-150 and A-153. 1 Publication1
    Mutagenesisi149R → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-147; A-150 and A-153. 1 Publication1
    Mutagenesisi150K → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-153. 1 Publication1
    Mutagenesisi153E → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-150. 1 Publication1
    Mutagenesisi203S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-222; A-231; A-233 and A-236. 1 Publication1
    Mutagenesisi222S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-231; A-233 and A-236. 1 Publication1
    Mutagenesisi231S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-233 and A-236. 2 Publications1
    Mutagenesisi233T → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-236. 1 Publication1
    Mutagenesisi236S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-233. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    997

    Open Targets

    More...
    OpenTargetsi
    ENSG00000099804

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA26265

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    CDC34

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    2507505

    <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_00000824511 – 236Ubiquitin-conjugating enzyme E2 R1Add BLAST236

    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 residuei203Phosphoserine; by CK22 Publications1
    Modified residuei222Phosphoserine; by CK22 Publications1
    Modified residuei231Phosphoserine; by CK23 Publications1
    Modified residuei233Phosphothreonine; by CK21 Publication1
    Modified residuei236Phosphoserine; by CK21 Publication1

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

    Autoubiquitinated (PubMed:22496338, PubMed:11805320, PubMed:12060736). Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin-proteasomal pathway (PubMed:11805320, PubMed:12060736).3 Publications
    Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controles the nuclear localization.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P49427

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P49427

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P49427

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P49427

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

    More...
    PaxDbi
    P49427

    PeptideAtlas

    More...
    PeptideAtlasi
    P49427

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P49427

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    56009

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P49427

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P49427

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in testes during spermatogenesis to regulate repression of cAMP-induced transcription.1 Publication

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Negatively regulated by the let-7 microRNA.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000099804 Expressed in 214 organ(s), highest expression level in testis

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P49427 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P49427 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB005109
    CAB047311
    HPA002382

    <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

    Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex.

    Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and RBX1. When cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened (PubMed:10918611, PubMed:11675391, PubMed:18851830, PubMed:19945379, PubMed:19112177, PubMed:24316736). When phosphorylated, interacts with beta-TrCP (BTRC) (PubMed:12037680).

    Interacts with human herpes virus 1 protein ICP0 and associates with the proteasome for degradation (PubMed:11447293, PubMed:11805320, PubMed:12060736).

    Interacts with casein kinase subunit CSNK2B (PubMed:11546811).

    11 Publications

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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    107432, 301 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P49427

    Database of interacting proteins

    More...
    DIPi
    DIP-37783N

    Protein interaction database and analysis system

    More...
    IntActi
    P49427, 20 interactors

    Molecular INTeraction database

    More...
    MINTi
    P49427

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000215574

    <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

    1236
    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
    P49427

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P49427

    <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

    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>Regioni190 – 236SCF-bindingAdd BLAST47

    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 biasi200 – 236Asp/Glu-rich (acidic)Add BLAST37

    <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 C-terminal acidic tail is required for nuclear localization and is involved in the binding to SCF E3 ligase complexes, and more specifically with the CUL1 subunit.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 ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0425 Eukaryota
    COG5078 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000160356

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000233454

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P49427

    KEGG Orthology (KO)

    More...
    KOi
    K02207

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CVKTKTP

    Database of Orthologous Groups

    More...
    OrthoDBi
    1116856at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P49427

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF101107

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00195 UBCc, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.110.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000608 UBQ-conjugat_E2
    IPR023313 UBQ-conjugating_AS
    IPR016135 UBQ-conjugating_enzyme/RWD

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00179 UQ_con, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF54495 SSF54495, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00183 UBIQUITIN_CONJUGAT_1, 1 hit
    PS50127 UBIQUITIN_CONJUGAT_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <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.

    This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

    P49427-1 [UniParc]FASTAAdd to basket
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            10         20         30         40         50
    MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN
    60 70 80 90 100
    TYYEGGYFKA RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP
    110 120 130 140 150
    VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK
    160 170 180 190 200
    WKESKGKDRE YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD
    210 220 230
    EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES
    Length:236
    Mass (Da):26,737
    Last modified:November 1, 1997 - 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:i258960666B589DB3
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    U3KQ77U3KQ77_HUMAN
    Ubiquitin-conjugating enzyme E2 R1
    CDC34
    119Annotation score:

    Annotation score:1 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>
    U3KPV8U3KPV8_HUMAN
    Ubiquitin-conjugating enzyme E2 R1
    CDC34
    146Annotation score:

    Annotation score:1 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>
    U3KQP9U3KQP9_HUMAN
    Ubiquitin-conjugating enzyme E2 R1
    CDC34
    107Annotation score:

    Annotation score:1 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>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAC37534 differs from that shown. Reason: Erroneous initiation.Curated

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_021277227D → H1 PublicationCorresponds to variant dbSNP:rs16990650Ensembl.1

    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
    L22005 mRNA Translation: AAC37534.1 Different initiation.
    BT006659 mRNA Translation: AAP35305.1
    AY650399 Genomic DNA Translation: AAT46688.1
    AK291554 mRNA Translation: BAF84243.1
    CH471242 Genomic DNA Translation: EAW61190.1
    BC009850 mRNA Translation: AAH09850.1
    BC018143 mRNA Translation: AAH18143.1
    BC023979 mRNA Translation: AAH23979.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS12030.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A49630

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_004350.1, NM_004359.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000215574; ENSP00000215574; ENSG00000099804

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    997

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:997

    UCSC genome browser

    More...
    UCSCi
    uc002lov.4 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L22005 mRNA Translation: AAC37534.1 Different initiation.
    BT006659 mRNA Translation: AAP35305.1
    AY650399 Genomic DNA Translation: AAT46688.1
    AK291554 mRNA Translation: BAF84243.1
    CH471242 Genomic DNA Translation: EAW61190.1
    BC009850 mRNA Translation: AAH09850.1
    BC018143 mRNA Translation: AAH18143.1
    BC023979 mRNA Translation: AAH23979.1
    CCDSiCCDS12030.1
    PIRiA49630
    RefSeqiNP_004350.1, NM_004359.1

    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
    2OB4X-ray2.40A7-184[»]
    3RZ3X-ray2.30A/B/C/D7-184[»]
    4MDKX-ray2.61A/B/C/D7-184[»]
    SMRiP49427
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi107432, 301 interactors
    CORUMiP49427
    DIPiDIP-37783N
    IntActiP49427, 20 interactors
    MINTiP49427
    STRINGi9606.ENSP00000215574

    PTM databases

    iPTMnetiP49427
    PhosphoSitePlusiP49427

    Polymorphism and mutation databases

    BioMutaiCDC34
    DMDMi2507505

    Proteomic databases

    EPDiP49427
    jPOSTiP49427
    MassIVEiP49427
    MaxQBiP49427
    PaxDbiP49427
    PeptideAtlasiP49427
    PRIDEiP49427
    ProteomicsDBi56009

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    997
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000215574; ENSP00000215574; ENSG00000099804
    GeneIDi997
    KEGGihsa:997
    UCSCiuc002lov.4 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    997
    DisGeNETi997

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    CDC34
    HGNCiHGNC:1734 CDC34
    HPAiCAB005109
    CAB047311
    HPA002382
    MIMi116948 gene
    neXtProtiNX_P49427
    OpenTargetsiENSG00000099804
    PharmGKBiPA26265

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0425 Eukaryota
    COG5078 LUCA
    GeneTreeiENSGT00940000160356
    HOGENOMiHOG000233454
    InParanoidiP49427
    KOiK02207
    OMAiCVKTKTP
    OrthoDBi1116856at2759
    PhylomeDBiP49427
    TreeFamiTF101107

    Enzyme and pathway databases

    UniPathwayiUPA00143
    BRENDAi2.3.2.B6 2681
    ReactomeiR-HSA-202424 Downstream TCR signaling
    R-HSA-2871837 FCERI mediated NF-kB activation
    R-HSA-5607764 CLEC7A (Dectin-1) signaling
    R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
    R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
    SignaLinkiP49427
    SIGNORiP49427

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    CDC34 human
    EvolutionaryTraceiP49427

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    CDC34

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    997

    Pharos

    More...
    Pharosi
    P49427

    Protein Ontology

    More...
    PROi
    PR:P49427

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000099804 Expressed in 214 organ(s), highest expression level in testis
    ExpressionAtlasiP49427 baseline and differential
    GenevisibleiP49427 HS

    Family and domain databases

    CDDicd00195 UBCc, 1 hit
    Gene3Di3.10.110.10, 1 hit
    InterProiView protein in InterPro
    IPR000608 UBQ-conjugat_E2
    IPR023313 UBQ-conjugating_AS
    IPR016135 UBQ-conjugating_enzyme/RWD
    PfamiView protein in Pfam
    PF00179 UQ_con, 1 hit
    SUPFAMiSSF54495 SSF54495, 1 hit
    PROSITEiView protein in PROSITE
    PS00183 UBIQUITIN_CONJUGAT_1, 1 hit
    PS50127 UBIQUITIN_CONJUGAT_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

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

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiUB2R1_HUMAN
    <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: P49427
    Secondary accession number(s): A8K689
    <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: February 1, 1996
    Last sequence update: November 1, 1997
    Last modified: September 18, 2019
    This is version 183 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 programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <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, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    7. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
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