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UniProtKB - P63166 (SUMO1_MOUSE)

Entry version 150 (08 May 2019)
Sequence version 1 (27 Sep 2004)
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Protein

Small ubiquitin-related modifier 1

Gene

Sumo1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (By similarity).By similarity1 Publication

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

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

Biological processStress response, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-MMU-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-MMU-3065679 SUMO is proteolytically processed
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3232118 SUMOylation of transcription factors
R-MMU-3232142 SUMOylation of ubiquitinylation proteins
R-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-4085377 SUMOylation of SUMOylation proteins
R-MMU-4090294 SUMOylation of intracellular receptors
R-MMU-4551638 SUMOylation of chromatin organization proteins
R-MMU-4570464 SUMOylation of RNA binding proteins
R-MMU-4615885 SUMOylation of DNA replication proteins
R-MMU-4655427 SUMOylation of DNA methylation proteins
R-MMU-4755510 SUMOylation of immune response proteins
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693571 Nonhomologous End-Joining (NHEJ)
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-69473 G2/M DNA damage checkpoint
R-MMU-877312 Regulation of IFNG signaling
R-MMU-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors

<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:
Small ubiquitin-related modifier 1
Short name:
SUMO-1
Alternative name(s):
SMT3 homolog 3
Ubiquitin-homology domain protein PIC1
Ubiquitin-like protein SMT3C
Short name:
Smt3C
<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:Sumo1
Synonyms:Smt3c, Smt3h3, Ubl1
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 1

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1197010 Sumo1

<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

Cell membrane, Cytoplasm, Membrane, 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_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 methionineiRemovedBy similarity
<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_00000359412 – 97Small ubiquitin-related modifier 1Add BLAST96
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000003594298 – 101By similarity4

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
Modified residuei2PhosphoserineCombined 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-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei9PhosphoserineBy similarity1
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei32PhosphoserineBy similarity1
Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki45Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

<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

Cleavage of precursor form by SENP1 or SENP2 is necessary for function.By similarity
Polymeric SUMO1 chains undergo polyubiquitination by RNF4.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P63166

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P63166

MaxQB - The MaxQuant DataBase

More...MaxQBi		P63166

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

More...PaxDbi		P63166

PeptideAtlas

More...PeptideAtlasi		P63166

PRoteomics IDEntifications database

More...PRIDEi		P63166

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P63166

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

More...PhosphoSitePlusi		P63166

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P63166

<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

Ubiquitous.

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed at 13.5 dpc strongly in the upper lip, primary palate and medial edge epithelia of the secondary palate. At 14.5 dpc expression could be seen in the medial edge epithelial seam.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

By hypoxia.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000026021 Expressed in 45 organ(s), highest expression level in cerebellum

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P63166 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P63166 MM

<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 USP25 (via ts SIM domain) the interaction weakly sumoylates USP25. Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity). Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PRKN. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei36Interaction with PIAS2By similarity1

<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		204420, 8 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3046 activated SUMO1-E1 ligase complex
CPX-3052 sumoylated E2 ligase complex (SUMO1)

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P63166

Database of interacting proteins

More...DIPi		DIP-29278N

Protein interaction database and analysis system

More...IntActi		P63166, 14 interactors

Molecular INTeraction database

More...MINTi		P63166

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000088935

<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

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

More...SMRi		P63166

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini20 – 97Ubiquitin-likePROSITE-ProRule annotationAdd BLAST78

<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 family. SUMO subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1769 Eukaryota
COG5227 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154319

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000207495

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P63166

KEGG Orthology (KO)

More...KOi		K12160

Identification of Orthologs from Complete Genome Data

More...OMAi		GQRISDH

Database of Orthologous Groups

More...OrthoDBi		1583700at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P63166

TreeFam database of animal gene trees

More...TreeFami		TF315116

Family and domain databases

Conserved Domains Database

More...CDDi		cd01763 Sumo, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR022617 Rad60/SUMO-like_dom
IPR033950 Sumo
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF11976 Rad60-SLD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00213 UBQ, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54236 SSF54236, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50053 UBIQUITIN_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 1 potential isoform that is computationally mapped.Show allAlign All

P63166-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES 
        60         70         80         90        100
YCQRQGVPMN SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST 

V
Length:101
Mass (Da):11,557
Last modified:September 27, 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:i89BE97D2D054FB33
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WRQ4A0A087WRQ4_MOUSE
Small ubiquitin-related modifier 1
Sumo1
75Annotation 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
AF033353 mRNA Translation: AAC39959.1
AK002536 mRNA Translation: BAB22172.1
AK011074 mRNA Translation: BAB27379.1
AK089081 mRNA Translation: BAC40739.1
AK159366 mRNA Translation: BAE35024.1
BC082566 mRNA Translation: AAH82566.1
BC083158 mRNA Translation: AAH83158.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS35586.1

NCBI Reference Sequences

More...RefSeqi		NP_033486.1, NM_009460.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021

Database of genes from NCBI RefSeq genomes

More...GeneIDi		22218

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:22218

UCSC genome browser

More...UCSCi		uc007bdx.1 mouse

<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
AF033353 mRNA Translation: AAC39959.1
AK002536 mRNA Translation: BAB22172.1
AK011074 mRNA Translation: BAB27379.1
AK089081 mRNA Translation: BAC40739.1
AK159366 mRNA Translation: BAE35024.1
BC082566 mRNA Translation: AAH82566.1
BC083158 mRNA Translation: AAH83158.1
CCDSiCCDS35586.1
RefSeqiNP_033486.1, NM_009460.2

3D structure databases

SMRiP63166
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204420, 8 interactors
ComplexPortaliCPX-3046 activated SUMO1-E1 ligase complex
CPX-3052 sumoylated E2 ligase complex (SUMO1)
CORUMiP63166
DIPiDIP-29278N
IntActiP63166, 14 interactors
MINTiP63166
STRINGi10090.ENSMUSP00000088935

PTM databases

iPTMnetiP63166
PhosphoSitePlusiP63166
SwissPalmiP63166

Proteomic databases

EPDiP63166
jPOSTiP63166
MaxQBiP63166
PaxDbiP63166
PeptideAtlasiP63166
PRIDEiP63166

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021
GeneIDi22218
KEGGimmu:22218
UCSCiuc007bdx.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7341
MGIiMGI:1197010 Sumo1

Phylogenomic databases

eggNOGiKOG1769 Eukaryota
COG5227 LUCA
GeneTreeiENSGT00940000154319
HOGENOMiHOG000207495
InParanoidiP63166
KOiK12160
OMAiGQRISDH
OrthoDBi1583700at2759
PhylomeDBiP63166
TreeFamiTF315116

Enzyme and pathway databases

ReactomeiR-MMU-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-MMU-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-MMU-3065679 SUMO is proteolytically processed
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3232118 SUMOylation of transcription factors
R-MMU-3232142 SUMOylation of ubiquitinylation proteins
R-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-4085377 SUMOylation of SUMOylation proteins
R-MMU-4090294 SUMOylation of intracellular receptors
R-MMU-4551638 SUMOylation of chromatin organization proteins
R-MMU-4570464 SUMOylation of RNA binding proteins
R-MMU-4615885 SUMOylation of DNA replication proteins
R-MMU-4655427 SUMOylation of DNA methylation proteins
R-MMU-4755510 SUMOylation of immune response proteins
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693571 Nonhomologous End-Joining (NHEJ)
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-69473 G2/M DNA damage checkpoint
R-MMU-877312 Regulation of IFNG signaling
R-MMU-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors

Miscellaneous databases

Protein Ontology

More...PROi		PR:P63166

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000026021 Expressed in 45 organ(s), highest expression level in cerebellum
ExpressionAtlasiP63166 baseline and differential
GenevisibleiP63166 MM

Family and domain databases

CDDicd01763 Sumo, 1 hit
InterProiView protein in InterPro
IPR022617 Rad60/SUMO-like_dom
IPR033950 Sumo
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF11976 Rad60-SLD, 1 hit
SMARTiView protein in SMART
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS50053 UBIQUITIN_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 nameiSUMO1_MOUSE
<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: P63166
Secondary accession number(s): P55856, Q3TX92, Q93068
<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: September 27, 2004
Last sequence update: September 27, 2004
Last modified: May 8, 2019
This is version 150 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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