SUMO2

SUMO2

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

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.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 = ]

References

Further reading

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

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать курсовую

Look at other dictionaries:

  • AMD Fusion — Codename(s) Fusion Desna Ontario Zacate Llano Hondo (cancelled) Wichita (cancelled) Krishna (cancelled) Trinity Weatherford Richland IGP Wrestler WinterPark BeaverCreek ATI/Radeon Driver related BTC[1] [2] …   Wikipedia

  • SUMO network — consists of enzymes and substrates involved in the dynamic posttranslational modification process of sumoylation (i.e. transfer of SUMO protein to substrates). Network membersThe SUMO network members (gene name and aliases) as published in the… …   Wikipedia

  • Proteine SUMO — Protéine SUMO Les protéines SUMO (pour Small Ubiquitin like MOdifier) sont une famille de petites protéines de 12 kDa (ou une centaine d acides aminés). Elles sont structuralement proches de l ubiquitine ou de la protéine NEDD8, mais… …   Wikipédia en Français

  • Protéine SUMO — Les protéines SUMO (pour Small Ubiquitin like MOdifier) sont une famille de petites protéines de 12 kDa (ou une centaine d acides aminés). Elles sont structuralement proches de l ubiquitine ou de la protéine NEDD8, mais fonctionnellement… …   Wikipédia en Français

  • Sumo — (Del lat. summus.) ► adjetivo 1 Que es superior en su especie o clase: ■ está considerado como la suma autoridad en literatura medieval. SINÓNIMO máximo 2 Muy grande o muy intenso: ■ lo que has dicho es una suma tontería. SINÓNIMO enorme ANTÓNIMO …   Enciclopedia Universal

  • SUMO protein — Small Ubiquitin like Modifier or SUMO proteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function. SUMOylation is a post translational modification involved in various …   Wikipedia

  • SENP6 — SUMO1/sentrin specific peptidase 6, also known as SENP6, is a human gene.cite web | title = Entrez Gene: SENP6 SUMO1/sentrin specific peptidase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=26054|… …   Wikipedia

  • K-bZIP — K bZIP, aussi connue sous le nom de RAP et K8α, est une phosphoprotéine homodimérique de 237 acides aminés. Elle fait partie de la famille des basic leucine zipper protein (bZIP). Elle se localise dans le cytoplasme, mais surtout dans le noyau de …   Wikipédia en Français

  • Ubiquitina — HUGO 12468 Símbolo UBC Datos genéticos …   Wikipedia Español

  • SUMO (proteína) — Saltar a navegación, búsqueda Para otros usos de este término, véase Sumo (desambiguación). SUMO (small ubiquitin like modifier) es una pequeña proteína de aproximadamente 100 amino ácidos (unos 12 kDa) que modifica covalente a otras proteínas en …   Wikipedia Español

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”