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UniProtKB - P63281 (UBC9_RAT)

Entry version 146 (25 May 2022)
Sequence version 1 (11 Oct 2004)
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Protein

SUMO-conjugating enzyme UBC9

Gene

Ube2i

Organism
Rattus norvegicus (Rat)
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 and SUMO3 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 (By similarity).

Can catalyze the formation of poly-SUMO chains (By similarity).

Essential for nuclear architecture and chromosome segregation (By similarity).

Necessary for sumoylation of FOXL2 and KAT5 (By similarity).

Sumoylates p53/TP53 at 'Lys-386' (By similarity).

Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity (By similarity).

By similarity

<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 sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
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 <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 sitei93Glycyl thioester intermediatePROSITE-ProRule annotation1
<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 bindingBy similarity2

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-196791, Vitamin D (calciferol) metabolism
R-RNO-3065678, SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-RNO-3108214, SUMOylation of DNA damage response and repair proteins
R-RNO-3108232, SUMO E3 ligases SUMOylate target proteins
R-RNO-3232118, SUMOylation of transcription factors
R-RNO-3232142, SUMOylation of ubiquitinylation proteins
R-RNO-3899300, SUMOylation of transcription cofactors
R-RNO-4085377, SUMOylation of SUMOylation proteins
R-RNO-4090294, SUMOylation of intracellular receptors
R-RNO-4551638, SUMOylation of chromatin organization proteins
R-RNO-4570464, SUMOylation of RNA binding proteins
R-RNO-4615885, SUMOylation of DNA replication proteins
R-RNO-4655427, SUMOylation of DNA methylation proteins
R-RNO-4755510, SUMOylation of immune response proteins
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-5693607, Processing of DNA double-strand break ends
R-RNO-5696395, Formation of Incision Complex in GG-NER
R-RNO-8866904, Negative regulation of activity of TFAP2 (AP-2) family transcription factors
R-RNO-9615933, Postmitotic nuclear pore complex (NPC) reformation

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

More...UniPathwayi		UPA00886

<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:
SUMO-conjugating enzyme UBC9 (EC:2.3.2.-)
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-conjugating enzyme UbcE2A1 Publication
Ubiquitin-protein ligase I
<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:Ube2i
Synonyms:Ubce9
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 10

Organism-specific databases

Rat genome database

More...RGDi		3926, Ube2i

<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 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 methionineiRemovedBy similarity
<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_00000824572 – 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-acetylserineBy similarity1
<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-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei65N6-acetyllysineBy similarity1
Modified residuei71Phosphoserine; by CDK1By similarity1
Cross-linki101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

<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

Phosphorylation at Ser-71 significantly enhances SUMOylation activity.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P63281

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

More...PaxDbi		P63281

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P63281

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

More...PhosphoSitePlusi		P63281

<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

Broadly expressed, with highest levels in spleen and lung (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000017907, Expressed in spleen and 20 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P63281, RN

<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

Forms a complex with SENP6 and UBE2I in response to UV irradiation (By similarity).

Forms a tight complex with RANGAP1 and RANBP2 (By similarity).

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 (By similarity).

Interacts with SETX (By similarity).

Interacts with HIPK1 and HIPK2 (By similarity).

Interacts with PPM1J (By similarity).

Interacts with RASD2 (PubMed:19498170).

Interacts with TCF3 (PubMed:9013644).

Interacts with NR2C1; the interaction promotes its sumoylation (By similarity).

Interacts with SIAH1 (By similarity).

Interacts with PARP (By similarity).

Interacts with various transcription factors such as TFAP2A, TFAP2B, and TFAP2C (By similarity).

Interacts with AR (By similarity).

Interacts with ETS1 (By similarity).

Interacts with SOX4 (By similarity).

Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B (By similarity).

Interacts with FOXL2 (By similarity).

Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain (By similarity).

Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains (By similarity).

Interacts with FHIT (By similarity).

Interacts with PRKRA and p53/TP53 (By similarity).

Interacts with UHRF2 (By similarity).

Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3 (By similarity).

Interacts with MTA1 (By similarity).

Interacts with ZNF451 (By similarity).

Interacts with CPEB3 (By similarity).

Interacts with SUMO1, SUMO2, and SUMO3 (By similarity).

Interacts with IPO13 (By similarity).

Interacts with DNMT1 (By similarity).

By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei4Interaction with RANBP2By similarity1
Sitei25Interaction with RANBP2By similarity1
Sitei57Interaction with RANBP2By similarity1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		247604, 13 interactors

Database of interacting proteins

More...DIPi		DIP-47657N

Protein interaction database and analysis system

More...IntActi		P63281, 2 interactors

Molecular INTeraction database

More...MINTi		P63281

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000024406

<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

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P63281

Biological Magnetic Resonance Data Bank

More...BMRBi		P63281

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

More...SMRi		P63281

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 157UBC corePROSITE-ProRule annotationAdd BLAST154

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 SUMO1By similarity6

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00550000075088

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_030988_12_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P63281

Identification of Orthologs from Complete Genome Data

More...OMAi		QEPAWRA

Database of Orthologous Groups

More...OrthoDBi		1522509at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P63281

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
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, UBC_1, 1 hit
PS50127, UBC_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>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P63281-1 [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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2KB55A0A0G2KB55_RAT
SUMO-conjugating enzyme UBC9
LOC102553386 Ube2i
229Annotation 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>
A0A8I6AG56A0A8I6AG56_RAT
SUMO-conjugating enzyme UBC9
Ube2i
101Annotation 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>

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
U54632 mRNA Translation: AAC98704.1
BC086324 mRNA Translation: AAH86324.1
BC086592 mRNA Translation: AAH86592.1

NCBI Reference Sequences

More...RefSeqi		NP_037182.1, NM_013050.1
XP_006245980.2, XM_006245918.3
XP_006245981.1, XM_006245919.3
XP_006245982.1, XM_006245920.3
XP_008765771.2, XM_008767549.2
XP_017452533.1, XM_017597044.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000104064; ENSRNOP00000085922; ENSRNOG00000066579

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25573

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25573

UCSC genome browser

More...UCSCi		RGD:3926, rat

<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
U54632 mRNA Translation: AAC98704.1
BC086324 mRNA Translation: AAH86324.1
BC086592 mRNA Translation: AAH86592.1
RefSeqiNP_037182.1, NM_013050.1
XP_006245980.2, XM_006245918.3
XP_006245981.1, XM_006245919.3
XP_006245982.1, XM_006245920.3
XP_008765771.2, XM_008767549.2
XP_017452533.1, XM_017597044.1

3D structure databases

AlphaFoldDBiP63281
BMRBiP63281
SMRiP63281
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi247604, 13 interactors
DIPiDIP-47657N
IntActiP63281, 2 interactors
MINTiP63281
STRINGi10116.ENSRNOP00000024406

PTM databases

iPTMnetiP63281
PhosphoSitePlusiP63281

Proteomic databases

jPOSTiP63281
PaxDbiP63281

Genome annotation databases

EnsembliENSRNOT00000104064; ENSRNOP00000085922; ENSRNOG00000066579
GeneIDi25573
KEGGirno:25573
UCSCiRGD:3926, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7329
RGDi3926, Ube2i

Phylogenomic databases

eggNOGiKOG0424, Eukaryota
GeneTreeiENSGT00550000075088
HOGENOMiCLU_030988_12_0_1
InParanoidiP63281
OMAiQEPAWRA
OrthoDBi1522509at2759
PhylomeDBiP63281
TreeFamiTF101122

Enzyme and pathway databases

UniPathwayiUPA00886
ReactomeiR-RNO-196791, Vitamin D (calciferol) metabolism
R-RNO-3065678, SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-RNO-3108214, SUMOylation of DNA damage response and repair proteins
R-RNO-3108232, SUMO E3 ligases SUMOylate target proteins
R-RNO-3232118, SUMOylation of transcription factors
R-RNO-3232142, SUMOylation of ubiquitinylation proteins
R-RNO-3899300, SUMOylation of transcription cofactors
R-RNO-4085377, SUMOylation of SUMOylation proteins
R-RNO-4090294, SUMOylation of intracellular receptors
R-RNO-4551638, SUMOylation of chromatin organization proteins
R-RNO-4570464, SUMOylation of RNA binding proteins
R-RNO-4615885, SUMOylation of DNA replication proteins
R-RNO-4655427, SUMOylation of DNA methylation proteins
R-RNO-4755510, SUMOylation of immune response proteins
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-5693607, Processing of DNA double-strand break ends
R-RNO-5696395, Formation of Incision Complex in GG-NER
R-RNO-8866904, Negative regulation of activity of TFAP2 (AP-2) family transcription factors
R-RNO-9615933, Postmitotic nuclear pore complex (NPC) reformation

Miscellaneous databases

Protein Ontology

More...PROi		PR:P63281

Gene expression databases

BgeeiENSRNOG00000017907, Expressed in spleen and 20 other tissues
GenevisibleiP63281, RN

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, UBC_1, 1 hit
PS50127, UBC_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 nameiUBC9_RAT
<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: P63281
Secondary accession number(s): P50550, Q15698, 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%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: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 25, 2022
This is version 146 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

<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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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