SUMO2: Difference between revisions

SUMO2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1WM2, 1WM3, 1WZ0, 2AWT, 2CKH, 2D07, 2IO0, 2IO3, 2IYD, 2RPQ, 3UIN, 3UIO, 3ZO5, 4BKG, 4NPN, 2N9E, 5D2M, 2N1W
Identifiers
Aliases	SUMO2, HSMT3, SMT3B, SMT3H2, SUMO3, Smt3A, small ubiquitin-like modifier 2, small ubiquitin like modifier 2
External IDs	OMIM: 603042 MGI: 2158813 HomoloGene: 87858 GeneCards: SUMO2
Gene location (Human)
Chr.	Chromosome 17 (human)
End	75,182,959 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	115,427,102 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; endothelial cell; ; lower lobe of lung; ; superficial temporal artery; ; islet of Langerhans; ; cerebellar vermis; ; oocyte; ; monocyte; ; cerebellar hemisphere; ; pancreatic ductal cell;
	Top expressed in
	morula; ; neural tube; ; mesencephalon; ; ganglionic eminence; ; ovary; ; thymus; ; olfactory bulb; ; uterus; ; lung; ; lens;
	More reference expression data
	n/a
Gene ontology
Molecular function	protein binding; ubiquitin protein ligase binding; protein tag; RNA binding; transcription corepressor binding; SUMO transferase activity; ubiquitin-like protein ligase binding;
Cellular component	PML body; nucleus; nucleoplasm;
Biological process	global genome nucleotide-excision repair; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein sumoylation; positive regulation of transcription by RNA polymerase II;
	Sources:Amigo / QuickGO
Orthologs
	6613
	170930
	ENSG00000188612
	ENSMUSG00000020738
	P61956
	P61957
	NM_001005849; NM_006937
	NM_133354
	NP_001005849; NP_008868
	NP_579932
	Wikidata
View/Edit Human	View/Edit Mouse

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Revision as of 06:34, 19 November 2007

Template:PBB Controls

SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae), also known as SUMO2, is a human gene.

Template:PBB Summary

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000188612 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020738 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

Template:PBB Further reading

This protein-related article is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000188612 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020738 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

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@@ Line 50: / Line 50: @@
 {{PBB_Summary
 | section_title =
-| summary_text = This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last two amino acids of the carboxy-terminus have been cleaved off. Numerous pseudogenes have been reported for this gene. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref>{{cite web | title = Entrez Gene: SUMO2 SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6613| accessdate = }}</ref>
+| summary_text = This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last two amino acids of the carboxy-terminus have been cleaved off. Numerous pseudogenes have been reported for this gene. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: SUMO2 SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6613| accessdate = }}</ref>
 }}
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 {{PBB_Further_reading
 | citations =
+*{{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  | author=Mannen H, Tseng HM, Cho CL, Li SS |title=Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 1 |pages= 178-80 |year= 1996 |pmid= 8630065 |doi= 10.1006/bbrc.1996.0717 }}
+*{{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  | 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  | author=Kamitani T, Nguyen HP, Kito K, ''et al.'' |title=Covalent modification of PML by the sentrin family of ubiquitin-like proteins. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3117-20 |year= 1998 |pmid= 9452416 |doi=  }}
+*{{cite journal  | author=Kamitani T, Kito K, Nguyen HP, ''et al.'' |title=Characterization of a second member of the sentrin family of ubiquitin-like proteins. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11349-53 |year= 1998 |pmid= 9556629 |doi=  }}
+*{{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  | author=Nishida T, Tanaka H, Yasuda H |title=A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase. |journal=Eur. J. Biochem. |volume=267 |issue= 21 |pages= 6423-7 |year= 2000 |pmid= 11029585 |doi=  }}
+*{{cite journal  | author=Dai KS, Liew CC |title=A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 23992-9 |year= 2001 |pmid= 11283016 |doi= 10.1074/jbc.M011208200 }}
+*{{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  | author=Nishida T, Kaneko F, Kitagawa M, Yasuda H |title=Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39060-6 |year= 2001 |pmid= 11489887 |doi= 10.1074/jbc.M103955200 }}
+*{{cite journal  | author=Hardeland U, Steinacher R, Jiricny J, Schär P |title=Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. |journal=EMBO J. |volume=21 |issue= 6 |pages= 1456-64 |year= 2002 |pmid= 11889051 |doi= 10.1093/emboj/21.6.1456 }}
+*{{cite journal  | author=Kim J, Cantwell CA, Johnson PF, ''et al.'' |title=Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation. |journal=J. Biol. Chem. |volume=277 |issue= 41 |pages= 38037-44 |year= 2002 |pmid= 12161447 |doi= 10.1074/jbc.M207235200 }}
+*{{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  | 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  | author=Petrie K, Guidez F, Howell L, ''et al.'' |title=The histone deacetylase 9 gene encodes multiple protein isoforms. |journal=J. Biol. Chem. |volume=278 |issue= 18 |pages= 16059-72 |year= 2003 |pmid= 12590135 |doi= 10.1074/jbc.M212935200 }}
+*{{cite journal  | author=Hietakangas V, Ahlskog JK, Jakobsson AM, ''et al.'' |title=Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. |journal=Mol. Cell. Biol. |volume=23 |issue= 8 |pages= 2953-68 |year= 2003 |pmid= 12665592 |doi=  }}
+*{{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  | 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  | author=Chung TL, Hsiao HH, Yeh YY, ''et al.'' |title=In vitro modification of human centromere protein CENP-C fragments by small ubiquitin-like modifier (SUMO) protein: definitive identification of the modification sites by tandem mass spectrometry analysis of the isopeptides. |journal=J. Biol. Chem. |volume=279 |issue= 38 |pages= 39653-62 |year= 2004 |pmid= 15272016 |doi= 10.1074/jbc.M405637200 }}
 }}
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