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SUMO3 small ubiquitin like modifier 3 [ Homo sapiens (human) ]

Gene ID: 6612, updated on 15-Jun-2019

Summary

Official Symbol
SUMO3provided by HGNC
Official Full Name
small ubiquitin like modifier 3provided by HGNC
Primary source
HGNC:HGNC:11124
See related
Ensembl:ENSG00000184900 MIM:602231
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
SMT3A; Smt3B; SMT3H1; SUMO-3
Summary
This gene encodes a member of the small ubiquitin-related modifier (SUMO) family of eukaryotic proteins. The encoded protein is covalently conjugated to other proteins via a post-translation modification known as sumoylation. Sumoylation may play a role in a wide variety of cellular processes, including nuclear transport, DNA replication and repair, mitosis, transcriptional regulation, and signal transduction. Alternatively spliced transcript variants encoding distinct proteins have been described. [provided by RefSeq, Feb 2014]
Expression
Ubiquitous expression in brain (RPKM 42.6), bone marrow (RPKM 40.3) and 25 other tissues See more
Orthologs

Genomic context

See SUMO3 in Genome Data Viewer
Location:
21q22.3
Exon count:
4
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 21 NC_000021.9 (44805617..44818129, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 21 NC_000021.8 (46225532..46238044, complement)

Chromosome 21 - NC_000021.9Genomic Context describing neighboring genes Neighboring gene ubiquitin conjugating enzyme E2 G2 Neighboring gene long intergenic non-protein coding RNA 1424 Neighboring gene PTTG1 interacting protein Neighboring gene integrin subunit beta 2 Neighboring gene uncharacterized LOC107987303

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

HIV-1 interactions

Protein interactions

Protein Gene Interaction Pubs
Tat tat Expression of HIV-1 Tat downregulates the abundance of SMT3 suppressor of mif two 3 homolog 3 (SUMO3) in the nucleoli of Jurkat T-cells PubMed
integrase gag-pol SUMOylation of HIV-1 IN at positions K46, K136, and K244 by SUMO involves HIV-1 infectivity PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

  • DNA Repair, organism-specific biosystem (from REACTOME)
    DNA Repair, organism-specific biosystemDNA repair is a phenomenal multi-enzyme, multi-pathway system required to ensure the integrity of the cellular genome. Living organisms are constantly exposed to harmful metabolic by-products, enviro...
  • Diurnally Regulated Genes with Circadian Orthologs, organism-specific biosystem (from WikiPathways)
    Diurnally Regulated Genes with Circadian Orthologs, organism-specific biosystemHuman genes regulated in the diurnal comparison with orthologues that display circadian regulation in mouse heart and liver (Panda 2002, Storch 2002), and SCN (Panda 2002). The 608 significantly regu...
  • Fluid shear stress and atherosclerosis, organism-specific biosystem (from KEGG)
    Fluid shear stress and atherosclerosis, organism-specific biosystemShear stress represents the frictional force that the flow of blood exerts at the endothelial surface of the vessel wall and plays a central role in vascular biology and contributes to the progress o...
  • Fluid shear stress and atherosclerosis, conserved biosystem (from KEGG)
    Fluid shear stress and atherosclerosis, conserved biosystemShear stress represents the frictional force that the flow of blood exerts at the endothelial surface of the vessel wall and plays a central role in vascular biology and contributes to the progress o...
  • Formation of Incision Complex in GG-NER, organism-specific biosystem (from REACTOME)
    Formation of Incision Complex in GG-NER, organism-specific biosystemAfter the XPC complex and the UV-DDB complex bind damaged DNA, a basal transcription factor TFIIH is recruited to the nucleotide excision repair (NER) site (Volker et al. 2001, Riedl et al. 2003). DN...
  • Global Genome Nucleotide Excision Repair (GG-NER), organism-specific biosystem (from REACTOME)
    Global Genome Nucleotide Excision Repair (GG-NER), organism-specific biosystemThe DNA damage in GG-NER is recognized by the joint action of two protein complexes. The first complex is composed of XPC, RAD23A or RAD23B and CETN2. The second complex, known as the UV-DDB complex,...
  • Metabolism of proteins, organism-specific biosystem (from REACTOME)
    Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
  • Nuclear pore complex, organism-specific biosystem (from KEGG)
    Nuclear pore complex, organism-specific biosystemStructural complex; Genetic information processing; RNA processing
  • Nuclear pore complex, conserved biosystem (from KEGG)
    Nuclear pore complex, conserved biosystemStructural complex; Genetic information processing; RNA processing
  • Nucleotide Excision Repair, organism-specific biosystem (from REACTOME)
    Nucleotide Excision Repair, organism-specific biosystemNucleotide excision repair (NER) was first described in the model organism E. coli in the early 1960s as a process whereby bulky base damage is enzymatically removed from DNA, facilitating the recove...
  • Post-translational protein modification, organism-specific biosystem (from REACTOME)
    Post-translational protein modification, organism-specific biosystemAfter translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the...
  • Processing and activation of SUMO, organism-specific biosystem (from REACTOME)
    Processing and activation of SUMO, organism-specific biosystemThe initial translation products of SUMO1, SUMO2, and SUMO3 are precursors that have extra amino acid residues at the C-terminus (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun ...
  • RNA transport, organism-specific biosystem (from KEGG)
    RNA transport, organism-specific biosystemRNA transport from the nucleus to the cytoplasm is fundamental for gene expression. The different RNA species that are produced in the nucleus are exported through the nuclear pore complexes (NPCs) ...
  • RNA transport, conserved biosystem (from KEGG)
    RNA transport, conserved biosystemRNA transport from the nucleus to the cytoplasm is fundamental for gene expression. The different RNA species that are produced in the nucleus are exported through the nuclear pore complexes (NPCs) ...
  • SUMO E3 ligases SUMOylate target proteins, organism-specific biosystem (from REACTOME)
    SUMO E3 ligases SUMOylate target proteins, organism-specific biosystemSUMO proteins are conjugated to lysine residues of target proteins via an isopeptide bond with the C-terminal glycine of SUMO (reviewed in Zhao 2007, Gareau and Lima 2010, Hannoun et al. 2010, Citro ...
  • SUMO is conjugated to E1 (UBA2:SAE1), organism-specific biosystem (from REACTOME)
    SUMO is conjugated to E1 (UBA2:SAE1), organism-specific biosystemThe UBA2:SAE1 complex catalyzes the formation of a thioester linkage between the C-terminal glycine of the mature SUMO and a cysteine residue (cysteine-173) in UBA2 (SAE2) (reviewed in Wang and Dasso...
  • SUMO is proteolytically processed, organism-specific biosystem (from REACTOME)
    SUMO is proteolytically processed, organism-specific biosystemSUMO1, 2, and 3 are initially expressed as propeptides containing extra residues at the C-terminus. (SUMO1 has 4 residues, SUMO2 has 2 residues, and SUMO3 has 11 residues,) SENP1, 2, and 5 are endopr...
  • SUMO is transferred from E1 to E2 (UBE2I, UBC9), organism-specific biosystem (from REACTOME)
    SUMO is transferred from E1 to E2 (UBE2I, UBC9), organism-specific biosystemSUMO is transferred from cysteine-173 of UBA2 to cysteine-93 of UBC9 (UBE2I) in a transthiolation reaction (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and...
  • SUMOylation, organism-specific biosystem (from REACTOME)
    SUMOylation, organism-specific biosystemSmall Ubiquitin-like MOdifiers (SUMOs) are a family of 3 proteins (SUMO1,2,3) that are reversibly conjugated to lysine residues of target proteins via a glycine-lysine isopeptide bond (reviewed in Ha...
  • SUMOylation of DNA damage response and repair proteins, organism-specific biosystem (from REACTOME)
    SUMOylation of DNA damage response and repair proteins, organism-specific biosystemSeveral factors that participate in DNA damage response and repair are SUMOylated (reviewed in Dou et al. 2011, Bekker-Jensen and Mailand 2011, Ulrich 2012, Psakhye and Jentsch 2012, Bologna and Ferr...
  • SUMOylation of DNA replication proteins, organism-specific biosystem (from REACTOME)
    SUMOylation of DNA replication proteins, organism-specific biosystemThe sliding clamp protein PCNA, Aurora-A, Aurora-B, Borealin, and various topoisomerases can be SUMOylated (reviewed in Wan et al. 2012). SUMOylation of PCNA appears to reduce formation of double-str...
  • SUMOylation of transcription factors, organism-specific biosystem (from REACTOME)
    SUMOylation of transcription factors, organism-specific biosystemProteins classified as transcription factors constitute a disproportionate number of SUMOylation targets. In most cases SUMOylation inhibits transcriptional activation, however in some cases such as ...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enzyme binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein tag IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
ubiquitin-like protein ligase binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
Process Evidence Code Pubs
negative regulation of DNA binding IDA
Inferred from Direct Assay
more info
PubMed 
protein sumoylation IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein sumoylation IDA
Inferred from Direct Assay
more info
PubMed 
Component Evidence Code Pubs
PML body IEA
Inferred from Electronic Annotation
more info
 
cytoplasm IEA
Inferred from Electronic Annotation
more info
 
kinetochore TAS
Traceable Author Statement
more info
PubMed 
nucleoplasm TAS
Traceable Author Statement
more info
 
nucleus IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
nucleus IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
small ubiquitin-related modifier 3
Names
SMT3 suppressor of mif two 3 homolog 1
SMT3 suppressor of mif two 3 homolog 3
ubiquitin-like protein SMT3B

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_033969.1 RefSeqGene

    Range
    5001..17513
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001286416.1NP_001273345.1  small ubiquitin-related modifier 3 isoform 2

    See identical proteins and their annotated locations for NP_001273345.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) uses an alternate in-frame acceptor splice site compared to variant 1. The resulting longer isoform (2) has an internal protein segment not found in isoform 1.
    Source sequence(s)
    AK300822, BC000036, BC008420
    Consensus CDS
    CCDS68220.1
    UniProtKB/Swiss-Prot
    P55854
    Related
    ENSP00000409666.2, ENST00000411651.6
    Conserved Domains (2) summary
    cd01763
    Location:7130
    Sumo; Small ubiquitin-related modifier (SUMO)
    smart00213
    Location:17123
    UBQ; Ubiquitin homologues
  2. NM_006936.3NP_008867.2  small ubiquitin-related modifier 3 isoform 1 precursor

    See identical proteins and their annotated locations for NP_008867.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the predominant transcript and encodes the shorter isoform (1).
    Source sequence(s)
    BC000036, BC008420
    Consensus CDS
    CCDS33587.1
    UniProtKB/Swiss-Prot
    P55854
    Related
    ENSP00000330343.6, ENST00000332859.10
    Conserved Domains (1) summary
    cd01763
    Location:792
    Sumo; Small ubiquitin-related modifier (SUMO)

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p13 Primary Assembly

Genomic

  1. NC_000021.9 Reference GRCh38.p13 Primary Assembly

    Range
    44805617..44818129 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
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