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UniProtKB - P63279 (UBC9_HUMAN)

Entry version 174 (10 Apr 2019)
Sequence version 1 (11 Oct 2004)
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Protein

SUMO-conjugating enzyme UBC9

Gene

UBE2I

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 the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'.9 Publications

<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 sumoylation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei100 – 101Substrate binding2

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular functionTransferase
Biological processCell cycle, Cell division, Chromosome partition, Host-virus interaction, Mitosis, Ubl conjugation pathway
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1221632 Meiotic synapsis
R-HSA-196791 Vitamin D (calciferol) metabolism
R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232118 SUMOylation of transcription factors
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4085377 SUMOylation of SUMOylation proteins
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-4655427 SUMOylation of DNA methylation proteins
R-HSA-4755510 SUMOylation of immune response proteins
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors

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

More...SignaLinki		P63279

SIGNOR Signaling Network Open Resource

More...SIGNORi		P63279

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

More...UniPathwayi
UPA00886

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P63279 Predicted

Transport Classification Database

More...TCDBi		3.A.20.1.1 the peroxisomal protein importer (ppi) family

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
SUMO-conjugating enzyme UBC9 (EC:2.3.2.-1 Publication)
Alternative name(s):
RING-type E3 SUMO transferase UBC9
SUMO-protein ligase
Ubiquitin carrier protein 9
Ubiquitin carrier protein I
Ubiquitin-conjugating enzyme E2 I
Ubiquitin-protein ligase I
p18
<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:UBE2I
Synonyms:UBC9, UBCE9
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000103275.18

Human Gene Nomenclature Database

More...HGNCi		HGNC:12485 UBE2I

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601661 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P63279

<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>Mutagenesisi13 – 14RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication2
Mutagenesisi17 – 18RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication2
Mutagenesisi22F → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi25V → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi27V → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi42E → A: Slightly impairs binding to RANBP2. 1 Publication1
Mutagenesisi48K → A: Slightly impairs binding to RANBP2. 1 Publication1
Mutagenesisi54E → A: Slightly impairs binding to RANBP2. 1 Publication1
Mutagenesisi57L → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi59K → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi61R → A: Slightly impairs binding to RANBP2. 1 Publication1
Mutagenesisi85N → Q: Impairs catalytic activity. 1 Publication1
Mutagenesisi87Y → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi93C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels. 1
Mutagenesisi100 – 101DK → AA: Impairs catalytic activity. 1 Publication2
Mutagenesisi127D → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi127D → S: No effect on catalytic activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		7329

Open Targets

More...OpenTargetsi		ENSG00000103275

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA37134

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1741191

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		UBE2I

Domain mapping of disease mutations (DMDM)

More...DMDMi		54039791

<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_processing_section">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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000824542 – 158SUMO-conjugating enzyme UBC9Add BLAST157

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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei65N6-acetyllysineCombined sources1
Modified residuei71Phosphoserine; by CDK1Combined sources1 Publication1
Cross-linki101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<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

Phosphorylation at Ser-71 significantly enhances SUMOylation activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P63279

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P63279

MaxQB - The MaxQuant DataBase

More...MaxQBi		P63279

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

More...PaxDbi		P63279

PeptideAtlas

More...PeptideAtlasi		P63279

PRoteomics IDEntifications database

More...PRIDEi		P63279

ProteomicsDB human proteome resource

More...ProteomicsDBi		12715
57517

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P63279

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P63279

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

More...PhosphoSitePlusi		P63279

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P63279

<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 heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000103275 Expressed in 235 organ(s), highest expression level in oocyte

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P63279 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P63279 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB009021
HPA003909

<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 SETX (PubMed:24105744). Interacts with HIPK1, HIPK2, PPM1J, RASD2 and TCF3 Interacts with NR2C1; the interaction promotes its sumoylation (By similarity). Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1 and PARP. Interacts with various transcription factors such as TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B. Interacts with DNMT1. Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PML-RARA oncoprotein (via the coiled-colied domain); the interaction is required for sumoylation of the PML-RARA oncoprotein. Interacts with IPO13. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Interacts with FHIT. Interacts with PRKRA and p53/TP53 (By similarity). Interacts with UHRF2. Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1. Interacts with ZNF451. Identified in a complex with SUMO2 and UBE2I, where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one bound to the UBE2I active site and the other to another region of the same UBE2I molecule. Interacts with CPEB3 (By similarity). Interacts with SUMO1P1/SUMO5 (PubMed:27211601).By similarityCurated28 Publications
(Microbial infection) Interacts with human herpesvirus 6 IE2.1 Publication
(Microbial infection) Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation.2 Publications
(Microbial infection) Interacts with Epstein-barr virus protein LMP1.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei4Interaction with RANBP21
Sitei25Interaction with RANBP21
Sitei57Interaction with RANBP21

<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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113177, 519 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3043 sumoylated E2 ligase complex (SUMO1)
CPX-3049 sumoylated E2 ligase complex (SUMO2)
CPX-3050 sumoylated E2 ligase complex (SUMO3)
CPX-3051 sumoylated E2 ligase complex (SUMO4)

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P63279

Database of interacting proteins

More...DIPi		DIP-29078N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P63279

Protein interaction database and analysis system

More...IntActi		P63279, 198 interactors

Molecular INTeraction database

More...MINTi		P63279

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000348056

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P63279

<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

1158
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1A3SX-ray2.80A1-158[»]
1KPSX-ray2.50A/C1-158[»]
1Z5Qmodel-A1-158[»]
1Z5SX-ray3.01A1-158[»]
2GRNX-ray1.80A1-158[»]
2GROX-ray1.70A1-158[»]
2GRPX-ray2.05A1-158[»]
2GRQX-ray1.70A1-158[»]
2GRRX-ray1.30A1-158[»]
2O25X-ray2.60C/D1-158[»]
2PE6X-ray2.40A1-158[»]
2PX9NMR-B1-158[»]
2XWUX-ray2.80A1-158[»]
3A4SX-ray2.70A/B1-158[»]
3UINX-ray2.60A1-158[»]
3UIOX-ray2.60A1-158[»]
3UIPX-ray2.29A1-158[»]
4W5VX-ray2.50A1-158[»]
4Y1LX-ray2.70A/B1-158[»]
5D2MX-ray2.40A/D1-158[»]
5F6DX-ray1.55A2-158[»]
5F6EX-ray1.12A2-158[»]
5F6UX-ray1.55A2-158[»]
5F6VX-ray1.49A2-158[»]
5F6WX-ray1.70A2-158[»]
5F6XX-ray1.56A2-158[»]
5F6YX-ray1.14A2-158[»]
5FQ2X-ray2.20A1-158[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P63279

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

More...SMRi		P63279

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P63279

<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>Regioni13 – 18Interaction with SUMO16

<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		KOG0424 Eukaryota
COG5078 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00550000075088

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000233454

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG063308

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P63279

KEGG Orthology (KO)

More...KOi		K10577

Identification of Orthologs from Complete Genome Data

More...OMAi		KCKFTPP

Database of Orthologous Groups

More...OrthoDBi		1110467at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P63279

TreeFam database of animal gene trees

More...TreeFami		TF101122

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
IPR027230 Ubc9
IPR000608 UBQ-conjugat_E2
IPR023313 UBQ-conjugating_AS
IPR016135 UBQ-conjugating_enzyme/RWD

The PANTHER Classification System

More...PANTHERi		PTHR43927 PTHR43927, 1 hit

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>.<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.

<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 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.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P63279-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG 
        60         70         80         90        100
TPWEGGLFKL RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED 
       110        120        130        140        150
KDWRPAITIK QILLGIQELL NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA 

QAKKFAPS
Length:158
Mass (Da):18,007
Last modified:October 11, 2004 - 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:iE2C826E9C8D0683D
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B0QYN7B0QYN7_HUMAN
SUMO-conjugating enzyme UBC9
UBE2I
184Annotation score:

Annotation score:2 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>
H3BQQ9H3BQQ9_HUMAN
SUMO-conjugating enzyme UBC9
UBE2I
137Annotation score:

Annotation score:2 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>
H3BPC4H3BPC4_HUMAN
SUMO-conjugating enzyme UBC9
UBE2I
70Annotation 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>
H3BRD1H3BRD1_HUMAN
SUMO-conjugating enzyme UBC9
UBE2I
29Annotation 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 AAH51289 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD92225 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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 conflicti18K → P in AAC50603 (PubMed:8668125).Curated1
Sequence conflicti86 – 89VYPS → GVPF in AAC50603 (PubMed:8668125).Curated4

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
X96427 mRNA Translation: CAA65287.1
U45328 mRNA Translation: AAA86662.1
D45050 mRNA Translation: BAA08091.1
U29092 mRNA Translation: AAC51361.1
U31933 mRNA Translation: AAB02181.1
U31882 mRNA Translation: AAC50603.1
U66867 mRNA Translation: AAC50716.1
U66818 mRNA Translation: AAC50715.1
U38785 mRNA Translation: AAB09410.1
AJ002385 mRNA Translation: CAA05359.1
BT006932 mRNA Translation: AAP35578.1
AB208988 mRNA Translation: BAD92225.1 Different initiation.
AE006466 Genomic DNA Translation: AAK61274.1
AL031714 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85673.1
CH471112 Genomic DNA Translation: EAW85676.1
CH471112 Genomic DNA Translation: EAW85677.1
CH471112 Genomic DNA Translation: EAW85678.1
CH471112 Genomic DNA Translation: EAW85679.1
BC000427 mRNA Translation: AAH00427.1
BC004429 mRNA Translation: AAH04429.1
BC051289 mRNA Translation: AAH51289.3 Different initiation.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10433.1

Protein sequence database of the Protein Information Resource

More...PIRi		JC6056

NCBI Reference Sequences

More...RefSeqi		NP_003336.1, NM_003345.4
NP_919235.1, NM_194259.2
NP_919236.1, NM_194260.2
NP_919237.1, NM_194261.2
XP_016879129.1, XM_017023640.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.302903

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000325437; ENSP00000324897; ENSG00000103275
ENST00000355803; ENSP00000348056; ENSG00000103275
ENST00000397514; ENSP00000380649; ENSG00000103275
ENST00000397515; ENSP00000380650; ENSG00000103275
ENST00000403747; ENSP00000385009; ENSG00000103275
ENST00000406620; ENSP00000384568; ENSG00000103275
ENST00000566587; ENSP00000457064; ENSG00000103275

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7329

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7329

UCSC genome browser

More...UCSCi		uc002clc.2 human

<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
X96427 mRNA Translation: CAA65287.1
U45328 mRNA Translation: AAA86662.1
D45050 mRNA Translation: BAA08091.1
U29092 mRNA Translation: AAC51361.1
U31933 mRNA Translation: AAB02181.1
U31882 mRNA Translation: AAC50603.1
U66867 mRNA Translation: AAC50716.1
U66818 mRNA Translation: AAC50715.1
U38785 mRNA Translation: AAB09410.1
AJ002385 mRNA Translation: CAA05359.1
BT006932 mRNA Translation: AAP35578.1
AB208988 mRNA Translation: BAD92225.1 Different initiation.
AE006466 Genomic DNA Translation: AAK61274.1
AL031714 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85673.1
CH471112 Genomic DNA Translation: EAW85676.1
CH471112 Genomic DNA Translation: EAW85677.1
CH471112 Genomic DNA Translation: EAW85678.1
CH471112 Genomic DNA Translation: EAW85679.1
BC000427 mRNA Translation: AAH00427.1
BC004429 mRNA Translation: AAH04429.1
BC051289 mRNA Translation: AAH51289.3 Different initiation.
CCDSiCCDS10433.1
PIRiJC6056
RefSeqiNP_003336.1, NM_003345.4
NP_919235.1, NM_194259.2
NP_919236.1, NM_194260.2
NP_919237.1, NM_194261.2
XP_016879129.1, XM_017023640.1
UniGeneiHs.302903

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A3SX-ray2.80A1-158[»]
1KPSX-ray2.50A/C1-158[»]
1Z5Qmodel-A1-158[»]
1Z5SX-ray3.01A1-158[»]
2GRNX-ray1.80A1-158[»]
2GROX-ray1.70A1-158[»]
2GRPX-ray2.05A1-158[»]
2GRQX-ray1.70A1-158[»]
2GRRX-ray1.30A1-158[»]
2O25X-ray2.60C/D1-158[»]
2PE6X-ray2.40A1-158[»]
2PX9NMR-B1-158[»]
2XWUX-ray2.80A1-158[»]
3A4SX-ray2.70A/B1-158[»]
3UINX-ray2.60A1-158[»]
3UIOX-ray2.60A1-158[»]
3UIPX-ray2.29A1-158[»]
4W5VX-ray2.50A1-158[»]
4Y1LX-ray2.70A/B1-158[»]
5D2MX-ray2.40A/D1-158[»]
5F6DX-ray1.55A2-158[»]
5F6EX-ray1.12A2-158[»]
5F6UX-ray1.55A2-158[»]
5F6VX-ray1.49A2-158[»]
5F6WX-ray1.70A2-158[»]
5F6XX-ray1.56A2-158[»]
5F6YX-ray1.14A2-158[»]
5FQ2X-ray2.20A1-158[»]
ProteinModelPortaliP63279
SMRiP63279
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113177, 519 interactors
ComplexPortaliCPX-3043 sumoylated E2 ligase complex (SUMO1)
CPX-3049 sumoylated E2 ligase complex (SUMO2)
CPX-3050 sumoylated E2 ligase complex (SUMO3)
CPX-3051 sumoylated E2 ligase complex (SUMO4)
CORUMiP63279
DIPiDIP-29078N
ELMiP63279
IntActiP63279, 198 interactors
MINTiP63279
STRINGi9606.ENSP00000348056

Chemistry databases

BindingDBiP63279
ChEMBLiCHEMBL1741191

Protein family/group databases

MoonDBiP63279 Predicted
TCDBi3.A.20.1.1 the peroxisomal protein importer (ppi) family

PTM databases

iPTMnetiP63279
PhosphoSitePlusiP63279
SwissPalmiP63279

Polymorphism and mutation databases

BioMutaiUBE2I
DMDMi54039791

Proteomic databases

EPDiP63279
jPOSTiP63279
MaxQBiP63279
PaxDbiP63279
PeptideAtlasiP63279
PRIDEiP63279
ProteomicsDBi12715
57517
TopDownProteomicsiP63279

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		7329
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325437; ENSP00000324897; ENSG00000103275
ENST00000355803; ENSP00000348056; ENSG00000103275
ENST00000397514; ENSP00000380649; ENSG00000103275
ENST00000397515; ENSP00000380650; ENSG00000103275
ENST00000403747; ENSP00000385009; ENSG00000103275
ENST00000406620; ENSP00000384568; ENSG00000103275
ENST00000566587; ENSP00000457064; ENSG00000103275
GeneIDi7329
KEGGihsa:7329
UCSCiuc002clc.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7329
DisGeNETi7329
EuPathDBiHostDB:ENSG00000103275.18

GeneCards: human genes, protein and diseases

More...GeneCardsi		UBE2I
HGNCiHGNC:12485 UBE2I
HPAiCAB009021
HPA003909
MIMi601661 gene
neXtProtiNX_P63279
OpenTargetsiENSG00000103275
PharmGKBiPA37134

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0424 Eukaryota
COG5078 LUCA
GeneTreeiENSGT00550000075088
HOGENOMiHOG000233454
HOVERGENiHBG063308
InParanoidiP63279
KOiK10577
OMAiKCKFTPP
OrthoDBi1110467at2759
PhylomeDBiP63279
TreeFamiTF101122

Enzyme and pathway databases

UniPathwayi
UPA00886

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-196791 Vitamin D (calciferol) metabolism
R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232118 SUMOylation of transcription factors
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4085377 SUMOylation of SUMOylation proteins
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-4655427 SUMOylation of DNA methylation proteins
R-HSA-4755510 SUMOylation of immune response proteins
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors
SignaLinkiP63279
SIGNORiP63279

Miscellaneous databases

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

More...ChiTaRSi		UBE2I human
EvolutionaryTraceiP63279

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		UBE2I

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

More...GenomeRNAii		7329

Protein Ontology

More...PROi		PR:P63279

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000103275 Expressed in 235 organ(s), highest expression level in oocyte
ExpressionAtlasiP63279 baseline and differential
GenevisibleiP63279 HS

Family and domain databases

CDDicd00195 UBCc, 1 hit
Gene3Di3.10.110.10, 1 hit
InterProiView protein in InterPro
IPR027230 Ubc9
IPR000608 UBQ-conjugat_E2
IPR023313 UBQ-conjugating_AS
IPR016135 UBQ-conjugating_enzyme/RWD
PANTHERiPTHR43927 PTHR43927, 1 hit
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...

<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 nameiUBC9_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: P63279
Secondary accession number(s): D3DU69
, P50550, Q15698, Q59GX1, Q86VB3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: April 10, 2019
This is version 174 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 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. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
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