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SUMO network



   

SUMO network consists of enzymes and substrates involved in the dynamic posttranslational modification process of sumoylation (i.e. transfer of SUMO protein to substrates).

Contents

Network members

The SUMO network members (gene name and aliases) as published in the last 100 newest PubMed entries (see below) are depicted hierarchically by Cytoscape in the figure on the right and are listed below as annotated by Gene Ontology.

  • sumo1 = pic1, smt3c, gmp1, sumo1, sumo-1, smt3, ubl1, smt3h3
  • senp1 = senp1
  • nf-kappab = nf-kappa b, nfkb, nf-kappab, nfkappa b, nfkappab
  • atm = ata, atm, atc, atdc, ate
  • ikbkg = nemo, fip-3, ip2, ikbkg, ikk-gamma, fip3, fip3p
  • rasa1 = cmavm, gap, rasa1, rasgap, p120gap, pkws, rasa
  • rgs17 = rgsz2, rgs17, hrgs17
  • rgs20 = rgs20, rgsz1, zgap1
  • efna2 = eplg6, lerk6, elf-1, efna2, hek7-l
  • elf4 = mef, elf4, elfr
  • myog = myf4, myogenin, myog
  • cdkn1a = cdkn1a, sdi1, mda-6, waf1, cip1, cdkn1, cap20, p21
  • skil = snoa, snon, sno, skil
  • rev1l = rev1l, rev1
  • rev3l = polz, rev3, rev3l
  • fus = tls, fus1, fus
  • rad1 = rad1, hrad1
  • rad51 = hsrad51, hrad51, hst16930, reca, rad51, rad51a
  • tp53 = p53, trp53, tp53
  • sumo2 = smt3b, sumo2, hsmt3, sumo-2, smt3h2
  • rad52 = rad52
  • hipk2 = hipk2, pro0593
  • krt6b = k6b, krtl1, ck6b, krt6b, pc2
  • pml = myl, pml, rnf71, trim19
  • fgfr1 = c-fgr, cek, h5, h4, h3, bfgfr, n-sam, fgfr1, flt2, h2
  • znf198 = mym, fim, scll, znf198
  • tdg = tdg
  • crebbp = rts, rsts, crebbp, cbp
  • ep300 = p300, ep300
  • creb1 = creb, mgc9284, creb1
  • setdb1 = kg1t, kiaa0067, setdb1, eset
  • mbd1 = cxxc3, mbd1, rft
  • pias3 = pias3, pias-3, flj14651
  • soat1 = soat1, stat, acact
  • pias1 = ddxbp1, pias1, gu/rh-ii
  • myb = c-myb, myb
  • mapk8 = jnk, sapk1, jnk1, mapk8, jnk1a2, jnk21b1/2, prkm8
  • cdkn3 = cdi1, kap, cip2, kap1, cdkn3
  • znf350 = zfqr, znf350, zbrk1
  • ube2i = c358b7.1, ubc9, ube2i
  • pcna = pcna, mgc8367
  • nbs1 = nbs, at-v2, nibrin, at-v1, nbs1, atv
  • daxx = dap6, bing2, daxx
  • sim2 = sim2, sim
  • sox2 = anop3, mgc2413, sox2
  • fgf4 = hst, hst-1, fgf4, kfgf, hbgf-4, k-fgf, hstf1
  • pou5f1 = oct4, otf4, oct3, otf3, pou5f1, mgc22487
  • src = src, c-src, src-1, src1, asv, p60-src
  • ptpn1 = ptp1b, ptpn1
  • stat1 = stat91, stat1, isgf-3
  • sumo3 = smt3a, sumo3, smt3h1, sumo-3
  • zbtb17 = miz-1, phz-67, miz1, zbtb17, znf151
  • uba2 = uba2, sae2, hrihfb2115
  • sae1 = aos1, hspc140, sae1, sua1
  • cdc2 = cdc2, cdk1
  • klf5 = iklf, bteb2, klf5
  • nr2c1 = tr2-11, tr2, nr2c1
  • pcaf = p/caf, pcaf, gcn5l, caf
  • nrip1 = rip140, nrip1
  • pparg = nr1c3, humpparg, pparg, ppargamma, pparg1, pparg2, ppar-gamma
  • abcc6 = mlp1, moate, ara, mrp6, est349056, abc34, abcc6
  • senp2 = kiaa1331, axam2, senp2, smt3ip2
  • kcna5 = pcn1, kcna5, kv1.5, hpcn1, hck1
  • taf12 = taf12, taf2j, tafii20
  • atf7 = atfa, atf7
  • tbp = tfiid, tbp, gtf2d1, gtf2d, sca17
  • fos = fos
  • jun = jun, ap1
  • hic1 = hic1, zbtb29
  • dynamin = dynamin-1, dynamin, dynamin1
  • pcap = hpc2, prostate cancer susceptibility 2, pcap, prca2
  • ctbp2 = ctbp2
  • ctbp1 = ctbp1
  • senp5 = mgc27076, senp5
  • hmga1 = mgc12816, mgc4854, hmga1, hmgiy, hmg-r, mgc4242
  • pias4 = piasg, mgc35296, flj12419, piasy, pias4
  • yy1 = ucrbp, nf-e1, yin-yang-1, yy1
  • cpa1 = cpa, cpa1
  • klk3 = psa, klk2a1, klk3
  • mdm2 = hdm2, mdm2, mgc71221
  • trps1 = gc79, trps1
  • ube2v1 = uev-1, ube2v, ube2v1, uev1, c-roc1, croc1, croc-1, cir1, uev1a
  • cul2 = cul2
  • dnmt3a = dnmt3a, m.hsaiiia, dnmt3a2
  • cbx4 = cbx4
  • col11a2 = col11a2, dfna13, stl3, hke5
  • sox9 = cmd1, sox9

SUMO antibodies

Comprehensive panel of antibodies to characterize the SUMO network is available by Abgent: SUMO1 Monoclonal Ab(AM1200a), UBC9 Ab(AM1261a), SUMO3 C-term Ab(AP1225a), NEDD8 N-term Ab(AP1226a), SENP1 N-term Ab(AP1230a), SENP2 N-term Ab(AP1232a), SENP3 N-term Ab(AP1234a), SENP5 N-term Ab(AP1236a), SENP6 N-term Ab(AP1238a), SENP7 N-term Ab(AP1240a), PIAS1 C-term Ab(AP1243a), PIAS3 N-term Ab(AP1244a), PIASx1 N-term Ab(AP1248a), PIASy1 N-term Ab(AP1249a), SENP8 N-term Ab(AP1259a), AOS1 Ab(AP1262a), SUMO2 C-term Ab(AP1282a), Pan SUMO Ab(AP1290a).

See also

References

  • Schuster B et al. Purification and identificati...[PMID: 17300217]
  • Makhnevych T et al. The role of karyopherins in t...[PMID: 17403926]
  • Yang XJ et al. A recurrent phospho-sumoyl sw...[PMID: 16973431]
  • Mascle XH et al. Sumoylation of the Transcript...[PMID: 17298944]
  • Miura K et al. SIZ1-Mediated Sumoylation of ...[PMID: 17416732]
  • Zhang PJ et al. CUE domain containing 2 regul...[PMID: 17347654]
  • Maier P et al. Cytokinesis in yeast meiosis ...[PMID: 17347652]
  • Kaiser FJ et al. SUMOylation modulates transcr...[PMID: 17391059]
  • Utsubo-Kuniyoshi R et al. MEK-ERK is involved in SUMO-1...[PMID: 17284251]
  • Zunino R et al. The SUMO protease SENP5 is re...[PMID: 17341580]
  • Stankovic-Valentin N et al. An acetylation/deacetylation-...[PMID: 17283066]
  • Carter S et al. C-terminal modifications regu...[PMID: 17369817]
  • Lee YJ et al. Protein SUMOylation is massiv...[PMID: 16955077]
  • Rodriguez-Munoz M et al. Sumoylated RGS-Rz proteins ac...[PMID: 16900103]
  • Tirard M et al. Sumoylation and proteasomal a...[PMID: 17314004]
  • Boggio R et al. Targeting sumo E1 to ubiquiti...[PMID: 17392274]
  • Meinecke I et al. Modification of nuclear PML p...[PMID: 17360386]
  • Li Y et al. Dual role for sumo E2 conjuga...[PMID: 17350957]
  • Moehren U et al. Alien interacts with the huma...[PMID: 17356171]
  • Deng Z et al. PIASy-mediated sumoylation of...[PMID: 17353273]
  • Janssen K et al. Apoptin is modified by SUMO c...[PMID: 16924230]
  • Wrighton KH et al. Transforming growth factor-be...[PMID: 17202138]
  • Jakobs A et al. Ubc9 fusion-directed SUMOylat...[PMID: 17277783]
  • Lake AN et al. Protein methylation and DNA r...[PMID: 17306845]
  • Scheschonka A et al. Sumoylation in neurons: nucle...[PMID: 17241677]
  • Du JX et al. Protein inhibitor of activate...[PMID: 17178721]
  • Oh YH et al. Chip-based analysis of SUMO (...[PMID: 16820290]
  • Dorval V et al. Modulation of Abeta generatio...[PMID: 17346237]
  • Benson MD et al. SUMO modification regulates i...[PMID: 17261810]
  • Chinnadurai G. Transcriptional regulation by...[PMID: 17336131]
  • Watts FZ. The role of SUMO in chromosom...[PMID: 17031663]
  • Jargin SV. Re: Involvement of ubiquitina...[PMID: 17222684]
  • Izumiya Y et al. Kaposi's sarcoma-associated h...[PMID: 17108053]
  • Langereis MA et al. Production of sumoylated prot...[PMID: 17208312]
  • Woeller CF et al. Evidence for SUMO-dependent n...[PMID: 17446168]
  • Su J et al. Differential regulation of in...[PMID: 16690127]
  • Wuerzberger-Davis SM et al. NF-kappaB activation by combi...[PMID: 16862178]
  • Chiu MW et al. The type 2 dengue virus envel...[PMID: 17265167]
  • Treuter E et al. Wrestling rules in transrepre...[PMID: 17244526]
  • Yokota K et al. Coactivation of the N-termina...[PMID: 17105732]
  • Lee YK et al. Doxorubicin down-regulates Kr...[PMID: 17079232]
  • Ji Z et al. Regulation of the Ets-1 trans...[PMID: 16862185]
  • Xhemalce B et al. Role of SUMO in the dynamics ...[PMID: 17209013]
  • Huang RY et al. Small ubiquitin-related modif...[PMID: 17234788]
  • Ghisletti S et al. Parallel SUMOylation-dependen...[PMID: 17218271]
  • Li B et al. Polycomb protein Cbx4 promote...[PMID: 17439403]
  • Seeler JS et al. SUMO, the three Rs and cancer...[PMID: 17217038]
  • Bono E et al. Thyroid hormones induce sumoy...[PMID: 17053029]
  • Wu F et al. Ubiquitin-like protein modifi...[PMID: 17127330]
  • Chang YL et al. Regulation of nuclear recepto...[PMID: 17336575]
  • Deyrieux AF et al. Sumoylation dynamics during k...[PMID: 17164289]
  • Wang J et al. Myocardin sumoylation transac...[PMID: 17101795]
  • Mohan RD et al. SUMO-1-dependent allosteric r...[PMID: 17060459]
  • Tronnersjo S et al. The jmjN and jmjC domains of ...[PMID: 17043893]
  • Dadke S et al. Regulation of protein tyrosin...[PMID: 17159996]
  • Park SW et al. SUMOylation of Tr2 orphan rec...[PMID: 17187077]
  • Park Y. Functional evaluation of the ...[PMID: 17448564]
  • Hamard PJ et al. Sumoylation delays the ATF7 t...[PMID: 17264123]
  • Lee J et al. Salicylic acid-mediated innat...[PMID: 17163880]
  • Kim KI et al. SUMOylation code in cancer de...[PMID: 17202851]
  • Tsuruzoe S et al. Inhibition of DNA binding of ...[PMID: 17097055]
  • Sramko M et al. Stress-induced inactivation o...[PMID: 17077080]
  • Chen CC et al. Genetic analysis of ionizing ...[PMID: 16990054]
  • Duma D et al. Multiple glucocorticoid recep...[PMID: 17070034]
  • Vertegaal AC et al. Distinct and overlapping sets...[PMID: 17000644]
  • Yoo CY et al. SIZ1 small ubiquitin-like mod...[PMID: 17041025]
  • Li T et al. Expression of SUMO-2/3 induce...[PMID: 17012228]
  • Oh HJ et al. PIAS1 interacts with and repr...[PMID: 17440973]
  • Lyst MJ et al. Regulation of MBD1-mediated t...[PMID: 17066076]
  • Kunapuli P et al. ZNF198, a zinc finger protein...[PMID: 17027752]
  • Reindle A et al. Multiple domains in Siz SUMO ...[PMID: 17077124]
  • Kabil O et al. Human cystathionine beta-synt...[PMID: 17087506]
  • Vitte AL et al. Modulation of HIV-1 Rev prote...[PMID: 17067581]
  • Branzei D et al. Ubc9- and mms21-mediated sumo...[PMID: 17081974]
  • Klein HL. A SUMOry of DNA replication: ...[PMID: 17081966]
  • Hsu YH et al. Sumoylated SnoN represses tra...[PMID: 16966324]
  • Lin DY et al. Role of SUMO-interacting moti...[PMID: 17081986]
  • Shen TH et al. The mechanisms of PML-nuclear...[PMID: 17081985]
  • Kumar A et al. NMR Characterization of the E...[PMID: 17320104]
  • Faus H et al. Post-translational modificati...[PMID: 16949786]
  • Yang SH et al. An extended consensus motif e...[PMID: 17036045]
  • Fan Z et al. SARS-CoV nucleocapsid protein...[PMID: 16998888]
  • Sacher M et al. Control of Rad52 recombinatio...[PMID: 17013376]
  • Sebban H et al. Posttranslational modificatio...[PMID: 16987664]
  • Jones MC et al. Regulation of the SUMO pathwa...[PMID: 17053081]
  • Perkins ND. Post-translational modificati...[PMID: 17072324]
  • Schachtman DP et al. Nutrient Sensing and Signalin...[PMID: 17067284]
  • Liu G et al. The p66 and p12 subunits of D...[PMID: 16934752]
  • Roscic A et al. Phosphorylation-dependent con...[PMID: 17018294]
  • Ihara M et al. Non-covalent binding of SUMO ...[PMID: 17428805]
  • Britanova O et al. Satb2 haploinsufficiency phen...[PMID: 16960803]
  • Wang CY et al. Genetic and functional eviden...[PMID: 17130563]
  • Di Bacco A et al. SUMO-specific proteases and t...[PMID: 17102611]
  • Tomoiu A et al. Functional interaction betwee...[PMID: 17005699]
  • Panse VG et al. Formation and nuclear export ...[PMID: 16978391]
  • Suico MA et al. SUMO down-regulates the activ...[PMID: 16904644]
  • Alkuraya FS et al. SUMO1 haploinsufficiency lead...[PMID: 16990542]
  • Northam MR et al. A novel function of DNA polym...[PMID: 16957771]
  • Chosed R et al. Evolution of a signalling sys...[PMID: 16740136]
  • Xu Z et al. Crystal structure of the SENP...[PMID: 16712526]


 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "SUMO_network". A list of authors is available in Wikipedia.
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