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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Small ubiquitin-related modifier 3''' is a [[protein]] that in humans is encoded by the ''SUMO3'' [[gene]].<ref name="pmid9119407">{{cite journal | vauthors = Lapenta V, Chiurazzi P, van der Spek P, Pizzuti A, Hanaoka F, Brahe C | title = SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family | journal = Genomics | volume = 40 | issue = 2 | pages = 362–6 | date = March 1997 | pmid = 9119407 | pmc = | doi = 10.1006/geno.1996.4556 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6612| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_SUMO3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1u4a.
| PDB = {{PDB2|1u4a}}, {{PDB2|1wm2}}, {{PDB2|1wm3}}, {{PDB2|1wz0}}, {{PDB2|2awt}}, {{PDB2|2ckh}}, {{PDB2|2d07}}, {{PDB2|2io0}}, {{PDB2|2io1}}, {{PDB2|2io3}}, {{PDB2|2iyd}}
| Name = SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)
| HGNCid = 11124
| Symbol = SUMO3
| AltSymbols =; SMT3A; SMT3H1; SUMO-3
| OMIM = 602231
| ECnumber = 
| Homologene = 38251
| MGIid = 1336201
| GeneAtlas_image1 = PBB_GE_SUMO3_200740_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SUMO3_200739_s_at_tn.png
| Function = {{GNF_GO|id=GO:0019949 |text = SUMO conjugating enzyme activity}}
| Component = {{GNF_GO|id=GO:0000776 |text = kinetochore}}
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0016925 |text = protein sumoylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6612
    | Hs_Ensembl = ENSG00000184900
    | Hs_RefseqProtein = NP_008867
    | Hs_RefseqmRNA = NM_006936
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 45049960
    | Hs_GenLoc_end = 45062472
    | Hs_Uniprot = P55854
    | Mm_EntrezGene = 20610
    | Mm_Ensembl = ENSMUSG00000020265
    | Mm_RefseqmRNA = NM_019929
    | Mm_RefseqProtein = NP_064313
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 77049986
    | Mm_GenLoc_end = 77061092
    | Mm_Uniprot = Q9Z172
  }}
}}
'''SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)''', also known as '''SUMO3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6612| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002).[supplied by OMIM]<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6612| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
SUMO3 has been shown to [[Protein-protein interaction|interact]] with [[ARNTL]]<ref name=pmid18644859>{{cite journal | vauthors = Lee J, Lee Y, Lee MJ, Park E, Kang SH, Chung CH, Lee KH, Kim K | title = Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex | journal = Molecular and Cellular Biology | volume = 28 | issue = 19 | pages = 6056–65 | date = October 2008 | pmid = 18644859 | pmc = 2546997 | doi = 10.1128/MCB.00583-08 }}</ref> and [[Thymine-DNA glycosylase]].<ref name=pmid11889051>{{cite journal | vauthors = Hardeland U, Steinacher R, Jiricny J, Schär P | title = Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover | journal = The EMBO Journal | volume = 21 | issue = 6 | pages = 1456–64 | date = March 2002 | pmid = 11889051 | pmc = 125358 | doi = 10.1093/emboj/21.6.1456 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
| citations =
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
* {{cite journal | vauthors = Saitoh H, Hinchey J | title = Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3 | journal = The Journal of Biological Chemistry | volume = 275 | issue = 9 | pages = 6252–8 | date = March 2000 | pmid = 10692421 | doi = 10.1074/jbc.275.9.6252 }}
*{{cite journal  | author=Lapenta V, Chiurazzi P, van der Spek P, ''et al.'' |title=SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family. |journal=Genomics |volume=40 |issue= 2 |pages= 362-6 |year= 1997 |pmid= 9119407 |doi= 10.1006/geno.1996.4556 }}
* {{cite journal | vauthors = Tatham MH, Jaffray E, Vaughan OA, Desterro JM, Botting CH, Naismith JH, Hay RT | title = Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9 | journal = The Journal of Biological Chemistry | volume = 276 | issue = 38 | pages = 35368–74 | date = September 2001 | pmid = 11451954 | doi = 10.1074/jbc.M104214200 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Lin J, Johannsen E, Robertson E, Kieff E | title = Epstein-Barr virus nuclear antigen 3C putative repression domain mediates coactivation of the LMP1 promoter with EBNA-2 | journal = Journal of Virology | volume = 76 | issue = 1 | pages = 232–42 | date = January 2002 | pmid = 11739688 | pmc = 135708 | doi = 10.1128/JVI.76.1.232-242.2002 }}
*{{cite journal | author=Saitoh H, Hinchey J |title=Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. |journal=J. Biol. Chem. |volume=275 |issue= 9 |pages= 6252-8 |year= 2000 |pmid= 10692421 |doi= }}
* {{cite journal | vauthors = Kadoya T, Yamamoto H, Suzuki T, Yukita A, Fukui A, Michiue T, Asahara T, Tanaka K, Asashima M, Kikuchi A | title = Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin | journal = Molecular and Cellular Biology | volume = 22 | issue = 11 | pages = 3803–19 | date = June 2002 | pmid = 11997515 | pmc = 133821 | doi = 10.1128/MCB.22.11.3803-3819.2002 }}
*{{cite journal  | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
* {{cite journal | vauthors = Su HL, Li SS | title = Molecular features of human ubiquitin-like SUMO genes and their encoded proteins | journal = Gene | volume = 296 | issue = 1-2 | pages = 65–73 | date = August 2002 | pmid = 12383504 | doi = 10.1016/S0378-1119(02)00843-0 }}
*{{cite journal | author=Tatham MH, Jaffray E, Vaughan OA, ''et al.'' |title=Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35368-74 |year= 2001 |pmid= 11451954 |doi= 10.1074/jbc.M104214200 }}
* {{cite journal | vauthors = Subramanian L, Benson MD, Iñiguez-Lluhí JA | title = A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 11 | pages = 9134–41 | date = March 2003 | pmid = 12511558 | doi = 10.1074/jbc.M210440200 }}
*{{cite journal | author=Lin J, Johannsen E, Robertson E, Kieff E |title=Epstein-Barr virus nuclear antigen 3C putative repression domain mediates coactivation of the LMP1 promoter with EBNA-2. |journal=J. Virol. |volume=76 |issue= 1 |pages= 232-42 |year= 2002 |pmid= 11739688 |doi= }}
* {{cite journal | vauthors = Eaton EM, Sealy L | title = Modification of CCAAT/enhancer-binding protein-beta by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 35 | pages = 33416–21 | date = August 2003 | pmid = 12810706 | doi = 10.1074/jbc.M305680200 }}
*{{cite journal | author=Kadoya T, Yamamoto H, Suzuki T, ''et al.'' |title=Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin. |journal=Mol. Cell. Biol. |volume=22 |issue= 11 |pages= 3803-19 |year= 2002 |pmid= 11997515 |doi= }}
* {{cite journal | vauthors = Tatham MH, Kim S, Yu B, Jaffray E, Song J, Zheng J, Rodriguez MS, Hay RT, Chen Y | title = Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation | journal = Biochemistry | volume = 42 | issue = 33 | pages = 9959–69 | date = August 2003 | pmid = 12924945 | doi = 10.1021/bi0345283 }}
*{{cite journal | author=Su HL, Li SS |title=Molecular features of human ubiquitin-like SUMO genes and their encoded proteins. |journal=Gene |volume=296 |issue= 1-2 |pages= 65-73 |year= 2003 |pmid= 12383504 |doi= }}
* {{cite journal | vauthors = Dobreva G, Dambacher J, Grosschedl R | title = SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression | journal = Genes & Development | volume = 17 | issue = 24 | pages = 3048–61 | date = December 2003 | pmid = 14701874 | pmc = 305257 | doi = 10.1101/gad.1153003 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Reverter D, Lima CD | title = A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex | journal = Structure | volume = 12 | issue = 8 | pages = 1519–31 | date = August 2004 | pmid = 15296745 | doi = 10.1016/j.str.2004.05.023 }}
*{{cite journal | author=Subramanian L, Benson MD, Iñiguez-Lluhí JA |title=A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9134-41 |year= 2003 |pmid= 12511558 |doi= 10.1074/jbc.M210440200 }}
* {{cite journal | vauthors = Ayaydin F, Dasso M | title = Distinct in vivo dynamics of vertebrate SUMO paralogues | journal = Molecular Biology of the Cell | volume = 15 | issue = 12 | pages = 5208–18 | date = December 2004 | pmid = 15456902 | pmc = 532004 | doi = 10.1091/mbc.E04-07-0589 }}
*{{cite journal | author=Eaton EM, Sealy L |title=Modification of CCAAT/enhancer-binding protein-beta by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 33416-21 |year= 2003 |pmid= 12810706 |doi= 10.1074/jbc.M305680200 }}
* {{cite journal | vauthors = Xu Z, Au SW | title = Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1 | journal = The Biochemical Journal | volume = 386 | issue = Pt 2 | pages = 325–30 | date = March 2005 | pmid = 15487983 | pmc = 1134797 | doi = 10.1042/BJ20041210 }}
*{{cite journal | author=Tatham MH, Kim S, Yu B, ''et al.'' |title=Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation. |journal=Biochemistry |volume=42 |issue= 33 |pages= 9959-69 |year= 2003 |pmid= 12924945 |doi= 10.1021/bi0345283 }}
* {{cite journal | vauthors = Ding H, Xu Y, Chen Q, Dai H, Tang Y, Wu J, Shi Y | title = Solution structure of human SUMO-3 C47S and its binding surface for Ubc9 | journal = Biochemistry | volume = 44 | issue = 8 | pages = 2790–9 | date = March 2005 | pmid = 15723523 | doi = 10.1021/bi0477586 }}
*{{cite journal | author=Dobreva G, Dambacher J, Grosschedl R |title=SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression. |journal=Genes Dev. |volume=17 |issue= 24 |pages= 3048-61 |year= 2004 |pmid= 14701874 |doi= 10.1101/gad.1153003 }}
* {{cite journal | vauthors = Bossis G, Malnou CE, Farras R, Andermarcher E, Hipskind R, Rodriguez M, Schmidt D, Muller S, Jariel-Encontre I, Piechaczyk M | title = Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation | journal = Molecular and Cellular Biology | volume = 25 | issue = 16 | pages = 6964–79 | date = August 2005 | pmid = 16055710 | pmc = 1190241 | doi = 10.1128/MCB.25.16.6964-6979.2005 }}
*{{cite journal | author=Reverter D, Lima CD |title=A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. |journal=Structure |volume=12 |issue= 8 |pages= 1519-31 |year= 2005 |pmid= 15296745 |doi= 10.1016/j.str.2004.05.023 }}
*{{cite journal | author=Ayaydin F, Dasso M |title=Distinct in vivo dynamics of vertebrate SUMO paralogues. |journal=Mol. Biol. Cell |volume=15 |issue= 12 |pages= 5208-18 |year= 2005 |pmid= 15456902 |doi= 10.1091/mbc.E04-07-0589 }}
*{{cite journal | author=Xu Z, Au SW |title=Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. |journal=Biochem. J. |volume=386 |issue= Pt 2 |pages= 325-30 |year= 2005 |pmid= 15487983 |doi= 10.1042/BJ20041210 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Ding H, Xu Y, Chen Q, ''et al.'' |title=Solution structure of human SUMO-3 C47S and its binding surface for Ubc9. |journal=Biochemistry |volume=44 |issue= 8 |pages= 2790-9 |year= 2005 |pmid= 15723523 |doi= 10.1021/bi0477586 }}
*{{cite journal | author=Bossis G, Malnou CE, Farras R, ''et al.'' |title=Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation. |journal=Mol. Cell. Biol. |volume=25 |issue= 16 |pages= 6964-79 |year= 2005 |pmid= 16055710 |doi= 10.1128/MCB.25.16.6964-6979.2005 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=6612}}


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{{gene-21-stub}}
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Latest revision as of 07:18, 11 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Small ubiquitin-related modifier 3 is a protein that in humans is encoded by the SUMO3 gene.[1][2]

Function

SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002).[supplied by OMIM][2]

Interactions

SUMO3 has been shown to interact with ARNTL[3] and Thymine-DNA glycosylase.[4]

References

  1. ↑ Lapenta V, Chiurazzi P, van der Spek P, Pizzuti A, Hanaoka F, Brahe C (March 1997). "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family". Genomics. 40 (2): 362–6. doi:10.1006/geno.1996.4556. PMID 9119407.
  2. ↑ 2.0 2.1 "Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)".
  3. ↑ Lee J, Lee Y, Lee MJ, Park E, Kang SH, Chung CH, Lee KH, Kim K (October 2008). "Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex". Molecular and Cellular Biology. 28 (19): 6056–65. doi:10.1128/MCB.00583-08. PMC 2546997. PMID 18644859.
  4. ↑ Hardeland U, Steinacher R, Jiricny J, Schär P (March 2002). "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover". The EMBO Journal. 21 (6): 1456–64. doi:10.1093/emboj/21.6.1456. PMC 125358. PMID 11889051.

Further reading


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