SUMOylation of transcription cofactors (Homo sapiens)

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3, 16, 17, 40257, 28, 3021, 22, 3213, 23, 2995, 12, 249, 3114, 18, 4511, 19515, 26, 33427, 32, 37, 39, 41...46104320, 3628, 303422, 32, 3813, 2324, 32, 471, 6nucleoplasmHIPK2-G97-SUMO1 SUMO1:DDX5SUMO1:DDX17SUMO3-C93-UBE2I SUMO1-K1020,1024-EP300 SUMO1-K53-DDX5 SUMO1-SIN3A UBE2I-G97-SUMO1 SUMO2-C93-UBE2I PPARGC1A-G97-SUMO1 SUMO1:C93-UBE2I2SUMO1:SAFBPIAS1 K1020-EP300-G97-SUMO1 UBE2ISUMO1-C93-UBE2I K1056-CREBBP-G97-SUMO1 SUMO1-C93-UBE2I SUMO2-K53-DDX5SUMO2,3-K231,K294-SAFBUBE2INCOR2-G97-SUMO1 DAXXSUMO1-C93-UBE2I UBE2I-G97-SUMO1 SUMO1:NCOR2UBE2I-G97-SUMO1 SUMO1-K998,K1033,K1056-CREBBP SUMO1-K184-PPARGC1A UBE2I-G97-SUMO1 SUMO1-C93-UBE2I 3SUMO1:NCOA2ZNF131-G97-SUMO1 K575-TRIM28-G97-SUMO1 SUMO2:UBE2I3SUMO1:MKL1UBE2I-G97-SUMO1 K804-TRIM28-G97-SUMO1 TRIM28UBE2I-G97-SUMO1 PIAS1SUMO1-K239,K731,K788-NCOA2 K294-SAFB-G97-SUMO1 SUMO1:NPM1K239-NCOA2-G97-SUMO1 UBE2ISUMO1-C93-UBE2I SUMO1:C93-UBE2ICTBP1-G97-SUMO1 UBE2IPIAS2-1UBE2I-G97-SUMO1 RING1 UBE2I-G97-SUMO1 K499-MKL1-G97-SUMO1 SUMO1:C93-UBE2ISUMO1-K263-NPM1 SCMH1-2 SUMO1:C93-UBE2IUBE2ISUMO1-K195-ING2 PIAS1,3K779-TRIM28-G97-SUMO1 SUMO1-K554,575,676,750,779,804-TRIM28 SUMO1-K1813-CASP8AP2 SUMO1:C93-UBE2IK624-MKL1-G97-SUMO1 K998-CREBBP-G97-SUMO1 UBE2INRIP1SUMO1-K601-ZNF131 SUMO1:SUMO1:NRIP1UBE2IUBE2IK231-SAFB-G97-SUMO1 UBE2I-G97-SUMO1 NCOR2UBE2I-G97-SUMO1 PRC1 complexMKL12SUMO1:NCOA1SUMO1:C93-UBE2IPIAS4 SUMO1:C93-UBE2ICASP8AP2K576-MKL1-G97-SUMO1 UBE2I-G93-SUMO2 CBX4 2SUMO1:EP300TOPORSPIAS1 PIAS1,4DDX5-G97-SUMO1 SAFBSUMO1-K32-HIPK2 SUMO2-C93-UBE2I UBE2IUBE2I2SUMO1:DAXXPHC1 PCGF2 K554-TRIM28-G97-SUMO1 HIPK2RNF2 SUMO1-C93-UBE2I SUMO1:CTBP1SUMO1-C93-UBE2I UBE2I-G93-SUMO2 SUMO1-C93-UBE2I SUMO1-C93-UBE2I UBE2I-G92-SUMO3 UBE2ISUMO1:C93-UBE2IUBE2I-G97-SUMO1 DDX5ZNF350 UBE2I-G97-SUMO1 DDX17CBX4, UHRF2SIN3ASUMO3-C93-UBE2I NPM1SUMO1:PPARGC1APPARGC1AUBE2I-G92-SUMO3 NCOA2MBD1PARK7-G97-SUMO1 SUMO1-K130-PARK7 K1033-CREBBP-G97-SUMO1 CBX4 UHRF2 K676-TRIM28-G97-SUMO1 SUMO1:C93-UBE2IUBE2I:SUMO2,UBE2I:SUMO3SUMO1-K732,K774-NCOA1 SUMO1-C93-UBE2I SUMO1-C93-UBE2I SUMO1-C93-UBE2I 2SUMO1:MBD1UBE2I-G97-SUMO1 UBE2IUBE2IUBE2ISUMO1-K756,K1154-NRIP1 SUMO1:ING2SUMO1-C93-UBE2I PARK7K1024-EP300-G97-SUMO1 SUMO2,3-K428-CTBP1SUMO1:C93-UBE2IK731-NCOA2-G97-SUMO1 SUMO1:C93-UBE2ISUMO1-K630,K631-DAXX SUMO1:C93-UBE2IUBE2I-G97-SUMO1 NPM1-G97-SUMO1 CREBBPUBE2IUBE2I:SUMO2,UBE2I:SUMO3PHC3 ZNF131UBE2IUBE2I-G97-SUMO1 UBE2I-G93-SUMO2 SUMO1:HIPK2SUMO1:ZNF131UBE2I-G92-SUMO3 UBE2IUBE2IK499-MBD1-G97-SUMO1 SUMO1:C93-UBE2ITRIM28 DDX17-G97-SUMO1 SUMO1-C93-UBE2I 3SUMO1:CREBBPSUMO1:C93-UBE2INCOA1SUMO1-K499,K538-MBD1 SUMO1-C93-UBE2I SUMO1-K231,K294-SAFB UBE2ISIN3A-G97-SUMO1 SUMO1-K50-DDX17 UBE2I-G97-SUMO1 SUMO1:SIN3ABMI1 SUMO1:TRIM28:ZNF350SUMO1:C93-UBE2ISUMO1:CASP8AP2K631-DAXX-G97-SUMO1 SUMO1-K672-NCOR2 CASP8AP2-G97-SUMO1 SUMO1:PARK7EP300SUMO1-C93-UBE2I SUMO3-C93-UBE2I K732-NCOA1-G97-SUMO1 ING2UBE2I-G93-SUMO2 UBE2I-G97-SUMO1 PHC2 UBE2I:SUMO2,UBE2I:SUMO3TRIM28:ZNF350K630-DAXX-G97-SUMO1 SUMO1-C93-UBE2I SUMO1:C93-UBE2ISUMO1:C93-UBE2IK774-NCOA1-G97-SUMO1 CBX8 SUMO2-C93-UBE2I SUMO1:C93-UBE2ISUMO1-C93-UBE2I SUMO2-C93-UBE2I K756-NRIP1-G97-SUMO1 SUMO1-C93-UBE2I K1154-NRIP1-G97-SUMO1 ZNF350 PIAS3 UBE2I-G97-SUMO1 SUMO2,3-K263-NPM1UBE2ICTBP1K538-MBD1-G97-SUMO1 CBX2 K788-NCOA2-G97-SUMO1 SUMO1-K499,K576,K624-MKL1 UBE2I-G97-SUMO1 ING2-G97-SUMO1 K750-TRIM28-G97-SUMO1 SUMO1:C93-UBE2ISUMO1-K428-CTBP1 SUMO1:C93-UBE2IUBE2I-G97-SUMO1 SUMO1-C93-UBE2I 1, 615, 332, 4443424, 32, 472913, 231, 65, 12, 248, 3514, 18, 452222, 3220, 36462437, 2852, 44102, 443422, 322, 44253791948, 3522


Description

SUMO1,2, and 3 are predominantly located in the nucleus and targets of SUMOylation are predominantly nuclear. Transcription cofactors are nuclear proteins that generally do not bind DNA themselves but interact with DNA-bound factors and influence transcription. SUMOylation of transcription cofactors usually inhibits the activity of the cofactor (reviewed in Girdwood et al. 2004, Gill 2005, Lyst and Stancheva 2007, Garcia-Dominguez and Reyes 2009). In the cases of coactivators such as PPARGC1A (PGC-1alpha) this results in decreased transcription; in the cases of corepressors such as MBD1 this results in increased transcription. View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 3899300
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: May, Bruce

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Ontology Terms

 

Bibliography

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  1. Gresko E, Möller A, Roscic A, Schmitz ML.; ''Covalent modification of human homeodomain interacting protein kinase 2 by SUMO-1 at lysine 25 affects its stability.''; PubMed Europe PMC
  2. Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMed Europe PMC
  3. Garcia-Dominguez M, Reyes JC.; ''SUMO association with repressor complexes, emerging routes for transcriptional control.''; PubMed Europe PMC
  4. Ythier D, Larrieu D, Binet R, Binda O, Brambilla C, Gazzeri S, Pedeux R.; ''Sumoylation of ING2 regulates the transcription mediated by Sin3A.''; PubMed Europe PMC
  5. Liu X, Liu Z, Jang SW, Ma Z, Shinmura K, Kang S, Dong S, Chen J, Fukasawa K, Ye K.; ''Sumoylation of nucleophosmin/B23 regulates its subcellular localization, mediating cell proliferation and survival.''; PubMed Europe PMC
  6. Hofmann TG, Jaffray E, Stollberg N, Hay RT, Will H.; ''Regulation of homeodomain-interacting protein kinase 2 (HIPK2) effector function through dynamic small ubiquitin-related modifier-1 (SUMO-1) modification.''; PubMed Europe PMC
  7. Alm-Kristiansen AH, Lorenzo PI, Molværsmyr AK, Matre V, Ledsaak M, Sæther T, Gabrielsen OS.; ''PIAS1 interacts with FLASH and enhances its co-activation of c-Myb.''; PubMed Europe PMC
  8. Puigserver P, Wu Z, Park CW, Graves R, Wright M, Spiegelman BM.; ''A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis.''; PubMed Europe PMC
  9. Garee JP, Meyer R, Oesterreich S.; ''Co-repressor activity of scaffold attachment factor B1 requires sumoylation.''; PubMed Europe PMC
  10. Girdwood D, Bumpass D, Vaughan OA, Thain A, Anderson LA, Snowden AW, Garcia-Wilson E, Perkins ND, Hay RT.; ''P300 transcriptional repression is mediated by SUMO modification.''; PubMed Europe PMC
  11. Oh Y, Chung KC.; ''UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131.''; PubMed Europe PMC
  12. Blomster HA, Hietakangas V, Wu J, Kouvonen P, Hautaniemi S, Sistonen L.; ''Novel proteomics strategy brings insight into the prevalence of SUMO-2 target sites.''; PubMed Europe PMC
  13. Yang SH, Sharrocks AD.; ''The SUMO E3 ligase activity of Pc2 is coordinated through a SUMO interaction motif.''; PubMed Europe PMC
  14. Jang MS, Ryu SW, Kim E.; ''Modification of Daxx by small ubiquitin-related modifier-1.''; PubMed Europe PMC
  15. Takahashi K, Taira T, Niki T, Seino C, Iguchi-Ariga SM, Ariga H.; ''DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor.''; PubMed Europe PMC
  16. Gill G.; ''Something about SUMO inhibits transcription.''; PubMed Europe PMC
  17. Lyst MJ, Stancheva I.; ''A role for SUMO modification in transcriptional repression and activation.''; PubMed Europe PMC
  18. Lalioti VS, Vergarajauregui S, Pulido D, Sandoval IV.; ''The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1.''; PubMed Europe PMC
  19. Oh Y, Chung KC.; ''Small ubiquitin-like modifier (SUMO) modification of zinc finger protein 131 potentiates its negative effect on estrogen signaling.''; PubMed Europe PMC
  20. Uchimura Y, Ichimura T, Uwada J, Tachibana T, Sugahara S, Nakao M, Saitoh H.; ''Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation.''; PubMed Europe PMC
  21. Fuller-Pace FV, Nicol SM.; ''DEAD-box RNA helicases as transcription cofactors.''; PubMed Europe PMC
  22. Mooney SM, Grande JP, Salisbury JL, Janknecht R.; ''Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential.''; PubMed Europe PMC
  23. Merrill JC, Melhuish TA, Kagey MH, Yang SH, Sharrocks AD, Wotton D.; ''A role for non-covalent SUMO interaction motifs in Pc2/CBX4 E3 activity.''; PubMed Europe PMC
  24. Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC.; ''Uncovering global SUMOylation signaling networks in a site-specific manner.''; PubMed Europe PMC
  25. Pungaliya P, Kulkarni D, Park HJ, Marshall H, Zheng H, Lackland H, Saleem A, Rubin EH.; ''TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins.''; PubMed Europe PMC
  26. Fan J, Ren H, Fei E, Jia N, Ying Z, Jiang P, Wu M, Wang G.; ''Sumoylation is critical for DJ-1 to repress p53 transcriptional activity.''; PubMed Europe PMC
  27. Zeng L, Yap KL, Ivanov AV, Wang X, Mujtaba S, Plotnikova O, Rauscher FJ, Zhou MM.; ''Structural insights into human KAP1 PHD finger-bromodomain and its role in gene silencing.''; PubMed Europe PMC
  28. Alm-Kristiansen AH, Norman IL, Matre V, Gabrielsen OS.; ''SUMO modification regulates the transcriptional activity of FLASH.''; PubMed Europe PMC
  29. Kagey MH, Melhuish TA, Wotton D.; ''The polycomb protein Pc2 is a SUMO E3.''; PubMed Europe PMC
  30. Vennemann A, Hofmann TG.; ''SUMO regulates proteasome-dependent degradation of FLASH/Casp8AP2.''; PubMed Europe PMC
  31. Liu HW, Banerjee T, Guan X, Freitas MA, Parvin JD.; ''The chromatin scaffold protein SAFB1 localizes SUMO-1 to the promoters of ribosomal protein genes to facilitate transcription initiation and splicing.''; PubMed Europe PMC
  32. Impens F, Radoshevich L, Cossart P, Ribet D.; ''Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.''; PubMed Europe PMC
  33. Shinbo Y, Niki T, Taira T, Ooe H, Takahashi-Niki K, Maita C, Seino C, Iguchi-Ariga SM, Ariga H.; ''Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities.''; PubMed Europe PMC
  34. Rytinki MM, Palvimo JJ.; ''SUMOylation modulates the transcription repressor function of RIP140.''; PubMed Europe PMC
  35. Knutti D, Kaul A, Kralli A.; ''A tissue-specific coactivator of steroid receptors, identified in a functional genetic screen.''; PubMed Europe PMC
  36. Lyst MJ, Nan X, Stancheva I.; ''Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins.''; PubMed Europe PMC
  37. Lee YK, Thomas SN, Yang AJ, Ann DK.; ''Doxorubicin down-regulates Kruppel-associated box domain-associated protein 1 sumoylation that relieves its transcription repression on p21WAF1/CIP1 in breast cancer MCF-7 cells.''; PubMed Europe PMC
  38. Matafora V, D'Amato A, Mori S, Blasi F, Bachi A.; ''Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition.''; PubMed Europe PMC
  39. Li X, Lee YK, Jeng JC, Yen Y, Schultz DC, Shih HM, Ann DK.; ''Role for KAP1 serine 824 phosphorylation and sumoylation/desumoylation switch in regulating KAP1-mediated transcriptional repression.''; PubMed Europe PMC
  40. Girdwood DW, Tatham MH, Hay RT.; ''SUMO and transcriptional regulation.''; PubMed Europe PMC
  41. Ivanov AV, Peng H, Yurchenko V, Yap KL, Negorev DG, Schultz DC, Psulkowski E, Fredericks WJ, White DE, Maul GG, Sadofsky MJ, Zhou MM, Rauscher FJ.; ''PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing.''; PubMed Europe PMC
  42. Mascle XH, Germain-Desprez D, Huynh P, Estephan P, Aubry M.; ''Sumoylation of the transcriptional intermediary factor 1beta (TIF1beta), the Co-repressor of the KRAB Multifinger proteins, is required for its transcriptional activity and is modulated by the KRAB domain.''; PubMed Europe PMC
  43. Chauchereau A, Amazit L, Quesne M, Guiochon-Mantel A, Milgrom E.; ''Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1.''; PubMed Europe PMC
  44. Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET.; ''Characterization of a second member of the sentrin family of ubiquitin-like proteins.''; PubMed Europe PMC
  45. Lin DY, Huang YS, Jeng JC, Kuo HY, Chang CC, Chao TT, Ho CC, Chen YC, Lin TP, Fang HI, Hung CC, Suen CS, Hwang MJ, Chang KS, Maul GG, Shih HM.; ''Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors.''; PubMed Europe PMC
  46. Nakagawa K, Kuzumaki N.; ''Transcriptional activity of megakaryoblastic leukemia 1 (MKL1) is repressed by SUMO modification.''; PubMed Europe PMC
  47. Jacobs AM, Nicol SM, Hislop RG, Jaffray EG, Hay RT, Fuller-Pace FV.; ''SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1.''; PubMed Europe PMC

History

CompareRevisionActionTimeUserComment
101685view14:02, 1 November 2018DeSlOntology Term : 'sumoylation pathway' added !
101620view11:48, 1 November 2018ReactomeTeamreactome version 66
101156view21:34, 31 October 2018ReactomeTeamreactome version 65
100733view20:12, 31 October 2018ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
2SUMO1:DAXXComplexR-HSA-4086032 (Reactome)
2SUMO1:EP300ComplexR-HSA-3899311 (Reactome)
2SUMO1:MBD1ComplexR-HSA-4090342 (Reactome)
2SUMO1:NCOA1ComplexR-HSA-4085307 (Reactome)
2SUMO1:SAFBComplexR-HSA-4085360 (Reactome)
3SUMO1:CREBBPComplexR-HSA-3927867 (Reactome)
3SUMO1:MKL1ComplexR-HSA-3900115 (Reactome)
3SUMO1:NCOA2ComplexR-HSA-4085298 (Reactome)
BMI1 ProteinP35226 (Uniprot-TrEMBL)
CASP8AP2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
CASP8AP2ProteinQ9UKL3 (Uniprot-TrEMBL)
CBX2 ProteinQ14781 (Uniprot-TrEMBL)
CBX4 ProteinO00257 (Uniprot-TrEMBL)
CBX4, UHRF2ComplexR-HSA-3296158 (Reactome)
CBX8 ProteinQ9HC52 (Uniprot-TrEMBL)
CREBBPProteinQ92793 (Uniprot-TrEMBL)
CTBP1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
CTBP1ProteinQ13363 (Uniprot-TrEMBL)
DAXXProteinQ9UER7 (Uniprot-TrEMBL)
DDX17-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
DDX17ProteinQ92841 (Uniprot-TrEMBL)
DDX5-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
DDX5ProteinP17844 (Uniprot-TrEMBL)
EP300ProteinQ09472 (Uniprot-TrEMBL)
HIPK2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
HIPK2ProteinQ9H2X6 (Uniprot-TrEMBL)
ING2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
ING2ProteinQ9H160 (Uniprot-TrEMBL)
K1020-EP300-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K1024-EP300-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K1033-CREBBP-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K1056-CREBBP-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K1154-NRIP1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K231-SAFB-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K239-NCOA2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K294-SAFB-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K499-MBD1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K499-MKL1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K538-MBD1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K554-TRIM28-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K575-TRIM28-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K576-MKL1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K624-MKL1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K630-DAXX-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K631-DAXX-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K676-TRIM28-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K731-NCOA2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K732-NCOA1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K750-TRIM28-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K756-NRIP1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K774-NCOA1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K779-TRIM28-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K788-NCOA2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K804-TRIM28-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K998-CREBBP-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
MBD1ProteinQ9UIS9 (Uniprot-TrEMBL)
MKL1ProteinQ969V6 (Uniprot-TrEMBL)
NCOA1ProteinQ15788 (Uniprot-TrEMBL)
NCOA2ProteinQ15596 (Uniprot-TrEMBL)
NCOR2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
NCOR2ProteinQ9Y618 (Uniprot-TrEMBL)
NPM1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
NPM1ProteinP06748 (Uniprot-TrEMBL)
NRIP1ProteinP48552 (Uniprot-TrEMBL)
PARK7-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
PARK7ProteinQ99497 (Uniprot-TrEMBL)
PCGF2 ProteinP35227 (Uniprot-TrEMBL)
PHC1 ProteinP78364 (Uniprot-TrEMBL)
PHC2 ProteinQ8IXK0 (Uniprot-TrEMBL)
PHC3 ProteinQ8NDX5 (Uniprot-TrEMBL)
PIAS1 ProteinO75925 (Uniprot-TrEMBL)
PIAS1,3ComplexR-HSA-4086016 (Reactome)
PIAS1,4ComplexR-HSA-2997694 (Reactome)
PIAS1ProteinO75925 (Uniprot-TrEMBL)
PIAS2-1ProteinO75928-1 (Uniprot-TrEMBL)
PIAS3 ProteinQ9Y6X2 (Uniprot-TrEMBL)
PIAS4 ProteinQ8N2W9 (Uniprot-TrEMBL)
PPARGC1A-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
PPARGC1AProteinQ9UBK2 (Uniprot-TrEMBL)
PRC1 complexComplexR-HSA-389114 (Reactome)
RING1 ProteinQ06587 (Uniprot-TrEMBL)
RNF2 ProteinQ99496 (Uniprot-TrEMBL)
SAFBProteinQ15424 (Uniprot-TrEMBL)
SCMH1-2 ProteinQ96GD3-2 (Uniprot-TrEMBL)
SIN3A-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
SIN3AProteinQ96ST3 (Uniprot-TrEMBL)
SUMO1-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO1-K1020,1024-EP300 ProteinQ09472 (Uniprot-TrEMBL)
SUMO1-K130-PARK7 ProteinQ99497 (Uniprot-TrEMBL)
SUMO1-K1813-CASP8AP2 ProteinQ9UKL3 (Uniprot-TrEMBL)
SUMO1-K184-PPARGC1A ProteinQ9UBK2 (Uniprot-TrEMBL)
SUMO1-K195-ING2 ProteinQ9H160 (Uniprot-TrEMBL)
SUMO1-K231,K294-SAFB ProteinQ15424 (Uniprot-TrEMBL)
SUMO1-K239,K731,K788-NCOA2 ProteinQ15596 (Uniprot-TrEMBL)
SUMO1-K263-NPM1 ProteinP06748 (Uniprot-TrEMBL)
SUMO1-K32-HIPK2 ProteinQ9H2X6 (Uniprot-TrEMBL) Hoffmann et al. 2005 (205) and Gresko et al. (2005) cite lysine-25 as the SUMO-modified residue, however the motif in their papers indicates lysine-32 of the UniProt sequence is the lysine residue modified.
SUMO1-K428-CTBP1 ProteinQ13363 (Uniprot-TrEMBL)
SUMO1-K499,K538-MBD1 ProteinQ9UIS9 (Uniprot-TrEMBL)
SUMO1-K499,K576,K624-MKL1 ProteinQ969V6 (Uniprot-TrEMBL)
SUMO1-K50-DDX17 ProteinQ92841 (Uniprot-TrEMBL)
SUMO1-K53-DDX5 ProteinP17844 (Uniprot-TrEMBL)
SUMO1-K554,575,676,750,779,804-TRIM28 ProteinQ13263 (Uniprot-TrEMBL)
SUMO1-K601-ZNF131 ProteinP52739 (Uniprot-TrEMBL)
SUMO1-K630,K631-DAXX ProteinQ9UER7 (Uniprot-TrEMBL)
SUMO1-K672-NCOR2 ProteinQ9Y618 (Uniprot-TrEMBL)
SUMO1-K732,K774-NCOA1 ProteinQ15788 (Uniprot-TrEMBL)
SUMO1-K756,K1154-NRIP1 ProteinP48552 (Uniprot-TrEMBL)
SUMO1-K998,K1033,K1056-CREBBP ProteinQ92793 (Uniprot-TrEMBL)
SUMO1-SIN3A ProteinQ96ST3 (Uniprot-TrEMBL)
SUMO1:C93-UBE2IComplexR-HSA-2993783 (Reactome)
SUMO1:CASP8AP2ComplexR-HSA-3927930 (Reactome)
SUMO1:CTBP1ComplexR-HSA-3730765 (Reactome)
SUMO1:DDX17ComplexR-HSA-3900118 (Reactome)
SUMO1:DDX5ComplexR-HSA-3900182 (Reactome)
SUMO1:HIPK2ComplexR-HSA-4090295 (Reactome)
SUMO1:ING2ComplexR-HSA-4086008 (Reactome)
SUMO1:NCOR2ComplexR-HSA-3927913 (Reactome)
SUMO1:NPM1ComplexR-HSA-4086055 (Reactome)
SUMO1:PARK7ComplexR-HSA-4085370 (Reactome)
SUMO1:PPARGC1AComplexR-HSA-3903019 (Reactome)
SUMO1:SIN3AComplexR-HSA-4086080 (Reactome)
SUMO1:SUMO1:NRIP1ComplexR-HSA-4086005 (Reactome)
SUMO1:TRIM28:ZNF350ComplexR-HSA-3782577 (Reactome)
SUMO1:ZNF131ComplexR-HSA-3730857 (Reactome)
SUMO2,3-K231,K294-SAFBProteinQ15424 (Uniprot-TrEMBL)
SUMO2,3-K263-NPM1ProteinP06748 (Uniprot-TrEMBL)
SUMO2,3-K428-CTBP1ProteinQ13363 (Uniprot-TrEMBL)
SUMO2-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO2-K53-DDX5ProteinP17844 (Uniprot-TrEMBL)
SUMO2:UBE2IComplexR-HSA-2993778 (Reactome)
SUMO3-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
TOPORSProteinQ9NS56 (Uniprot-TrEMBL)
TRIM28 ProteinQ13263 (Uniprot-TrEMBL)
TRIM28:ZNF350ComplexR-HSA-3782565 (Reactome)
TRIM28ProteinQ13263 (Uniprot-TrEMBL)
UBE2I-G92-SUMO3 ProteinP55854 (Uniprot-TrEMBL)
UBE2I-G93-SUMO2 ProteinP61956 (Uniprot-TrEMBL)
UBE2I-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
UBE2I:SUMO2,UBE2I:SUMO3ComplexR-HSA-3899312 (Reactome)
UBE2IProteinP63279 (Uniprot-TrEMBL)
UHRF2 ProteinQ96PU4 (Uniprot-TrEMBL)
ZNF131-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
ZNF131ProteinP52739 (Uniprot-TrEMBL)
ZNF350 ProteinQ9GZX5 (Uniprot-TrEMBL)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
2SUMO1:DAXXArrowR-HSA-4085992 (Reactome)
2SUMO1:EP300ArrowR-HSA-3899291 (Reactome)
2SUMO1:MBD1ArrowR-HSA-4090288 (Reactome)
2SUMO1:NCOA1ArrowR-HSA-4085296 (Reactome)
2SUMO1:SAFBArrowR-HSA-4085347 (Reactome)
3SUMO1:CREBBPArrowR-HSA-3927959 (Reactome)
3SUMO1:MKL1ArrowR-HSA-3900070 (Reactome)
3SUMO1:NCOA2ArrowR-HSA-4085318 (Reactome)
CASP8AP2R-HSA-3927824 (Reactome)
CASP8AP2R-HSA-5228521 (Reactome)
CBX4, UHRF2mim-catalysisR-HSA-3296126 (Reactome)
CREBBPR-HSA-3927959 (Reactome)
CTBP1R-HSA-3108203 (Reactome)
CTBP1R-HSA-3108209 (Reactome)
DAXXR-HSA-4085992 (Reactome)
DDX17R-HSA-3900047 (Reactome)
DDX5R-HSA-3900177 (Reactome)
DDX5R-HSA-3900194 (Reactome)
EP300R-HSA-3899291 (Reactome)
HIPK2R-HSA-4090284 (Reactome)
ING2R-HSA-4086083 (Reactome)
MBD1R-HSA-4090288 (Reactome)
MKL1R-HSA-3900070 (Reactome)
NCOA1R-HSA-4085296 (Reactome)
NCOA2R-HSA-4085318 (Reactome)
NCOR2R-HSA-3927886 (Reactome)
NPM1R-HSA-4086059 (Reactome)
NPM1R-HSA-4086088 (Reactome)
NRIP1R-HSA-4086036 (Reactome)
PARK7R-HSA-4085331 (Reactome)
PIAS1,3mim-catalysisR-HSA-4086036 (Reactome)
PIAS1,3mim-catalysisR-HSA-4090288 (Reactome)
PIAS1,4mim-catalysisR-HSA-5228521 (Reactome)
PIAS1mim-catalysisR-HSA-3900194 (Reactome)
PIAS1mim-catalysisR-HSA-4085347 (Reactome)
PIAS1mim-catalysisR-HSA-4085372 (Reactome)
PIAS2-1mim-catalysisR-HSA-4085331 (Reactome)
PPARGC1AR-HSA-3903017 (Reactome)
PRC1 complexmim-catalysisR-HSA-3108203 (Reactome)
PRC1 complexmim-catalysisR-HSA-3108209 (Reactome)
PRC1 complexmim-catalysisR-HSA-3927824 (Reactome)
R-HSA-3108203 (Reactome) CBX4 (Pc2) via its SUMO-interacting motifs recruits both CTBP1 and SUMO2,3:UBE2I (SUMO1:UBC9) to polycomb bodies where CTBP1 is SUMOylated with SUMO2,3 at lysine-428, as inferred from SUMOylation with SUMO1 (Merrill et al. 2010, Yang and Sharrocks 2010).
R-HSA-3108209 (Reactome) CBX4 (Pc2) via its SUMO-interacting motifs recruits both CTBP1 and SUMO1:UBE2I (SUMO1:UBC9) to polycomb bodies where CTBP1 is SUMOylated with SUMO1 at lysine-428 (Kagey et al. 2003, Merrill et al. 2010, Yang and Sharrocks 2010).
R-HSA-3296126 (Reactome) CBX4 (Pc2) and UHRF2 are able to SUMOylate ZNF131 on lysine-601 (lysine-567 in the isoform in Oh and Chung 2012, Oh and Chung 2013) . SUMOylation of ZNF131 increases the inhibition of ERalpha signaling by ZNF131 through suppression of ERalpha homodimerization.
R-HSA-3782535 (Reactome) The PHD domain of TRIM28 (KAP1) acts as a SUMO E3 ligase to SUMOylate the bromodomain of TRIM28 with SUMO1 (Ivanov et al. 2007, Lee et al. 2007, Li et al. 2007, Mascle et al. 2007, Zeng et al. 2008, Impens et al. 2014). SUMOylation enhances repression of p21 transcription by the TRIM28:ZNF350 (KAP1:ZBRK1) complex. SUMOylated TRIM28 recruits SETDB1 and CHD3 (of the NuRD complex).
R-HSA-3899291 (Reactome) EP300 (p300) is SUMOylated at lysine-1020 and lysine-1024 with SUMO1 (Girdwood et al. 2003). SUMOylation of EP300 alleviates transcriptional repression caused by the CRD1 domain.
R-HSA-3900047 (Reactome) DDX17 is SUMOylated at lysine-50 with SUMO1 or SUMO2 (Mooney et al. 2010, Fuller-Pace and Nicol 2012, Impens et al. 2014). SUMOylation reduces the transactivation activity of DDX17 with the estrogen receptor and with p53. SUMOylation also promotes association of DDX17 with HDAC1.
R-HSA-3900070 (Reactome) MKL1 is SUMOylated with SUMO1 at lysine-499, lysine-576, and lysine-624 (Nakagawa and Kuzumaki 2005) SUMOylation represses transcriptional activity of MKL1. MKL1 is a coactivator of SRF.
R-HSA-3900177 (Reactome) DDX5 is SUMOylated at lysine-53 with SUMO1 (Mooney et al. 2010, Matafora et al. 2009, Impens et al. 2014). SUMOylation enhances coactivation activity of DDX5, stability of DDX5, and interaction of DDX5 with HDAC1.
R-HSA-3900194 (Reactome) PIAS1 SUMOylates DDX5 at lysine-53 with SUMO2 (Jacobs et al. 2007, Hendriks et al. 2014, Impens et al. 2014). SUMOylation reduces the coactivation activity of DDX5 with p53 but enhances coactivation of the estrogen receptor. SUMOylation also increases stability of DDX5 and promotes interaction of DDX5 with HDAC1. DDX5 is a coactivator of p53 (TP53).
R-HSA-3903017 (Reactome) As infered from mouse homologs, PPARGC1A (PGC-1alpha) is SUMOylated at lysine-184 with SUMO1. SUMOylation reduces transcription activation by PPARGC1A.
R-HSA-3927824 (Reactome) The CBX3 component of PRC1 SUMOylates CASP8AP2 (FLASH) at lysine-1813 with SUMO1 (Alm-Kristiansen et al. 2009). SUMOylation enhances the transcriptional coactivation activity of CASP8AP2. SUMOylation also appears to trigger proteasomal degradation of CASP8AP2 (Vennemann and Hofmann 2013).
R-HSA-3927886 (Reactome) As inferred from mouse homologs, NCOR2 (SMRT) is sumoylated at lysine-668 with SUMO1. SUMOylation reduces repression of transcription by NCOR2.
R-HSA-3927959 (Reactome) As inferred from mouse homologs, CREBBP (CBP) is SUMOylated at lysine-998, lysine-1033, and lysine-1056 with SUMO1. SUMOylation recruits DAXX and HDAC2 to repress transcription.
R-HSA-4085296 (Reactome) NCOA1 (SRC1) is SUMOylated at lysine-732 and lysine-774 with SUMO1 (Chauchereau et al. 2003). SUMOylation enhances interaction between NCOA1 and the progesterone receptor and causes NCOA1 to be retained in the nucleus.
R-HSA-4085318 (Reactome) As inferred from mouse homologs, NCOA2 is SUMOylated at lysine-239, lysine-731, and lysine-788 with SUMO1. SUMOylation of NCOA2 increases coactivation of transcription by the androgen receptor.
R-HSA-4085331 (Reactome) PIAS2-1 (PIASxalpha) SUMOylates PARK7 (DJ-1) at lysine-130 with SUMO1 (Takahashi et al. 2001, Shinbo et al. 2006). SUMOylation causes PARK7 to be retained in the nucleus where it represses transcription activation by P53 (TP53). A non-SUMOylatable mutant of PARK7 is located in the cytoplasm and fails to repress TP53 (p53) transcriptional activity (Fan et al. 2008).
R-HSA-4085347 (Reactome) PIAS1 SUMOylates SAFB at lysine-231 and lysine-294 with SUMO1 (Garee et al. 2011). SUMOylation of SAFB is required for co-repressor activity of SAFB at promoters regulated by the estrogen receptor (ER). In contrast, SUMOylated SAFB increases transcription of genes encoding ribosomal proteins (Liu 2015).
R-HSA-4085372 (Reactome) PIAS1 SUMOylates SAFB at lysine 231 and lysine 294 with SUMO2,3 (Garee et al. 2011). SUMOylation of SAFB is required for co-repressor activity.
R-HSA-4085992 (Reactome) DAXX is SUMOylated at lysine-630 and lysine-631 with SUMO1 (Jang et al. 2002, Lalioti et al. 2002, Lin et al. 2006). SUMOylation of DAXX does not prevent it from localizing to PML oncogenic domains.
R-HSA-4085994 (Reactome) TOPORS SUMOylates SIN3A at an unknown lysine residue with SUMO1 (Pungaliya et al. 2007).
R-HSA-4086036 (Reactome) PIAS1,3 SUMOylate NRIP1 (RIP140) at lysine 756 and lysine-1154 with SUMO1 (Rytinki et al. 2008). SUMOylation enhances transcription repression by NRIP1.
R-HSA-4086059 (Reactome) NPM1 (Nucleophosmin, B23) is SUMOylated at lysine-263 with SUMO2,3 (Liu et al. 2007, Blomster et al. 2009, Hendriks et al. 2014). SUMOylation enhances binding of NPM1 to Rb and enhances nuclear residency of NPM1.
R-HSA-4086083 (Reactome) ING2 is SUMOylated at lysine-195 with SUMO1 (Ythier et al. 2010). SUMOylation enhances the interaction of ING2 with SIN3A
R-HSA-4086088 (Reactome) NPM1 (Nucleophosmin, B23) is SUMOylated at lysine-263 with SUMO1 (Liu et al. 2007). SUMOylation enhances binding of NPM1 to Rb and enhances nuclear residency of NPM1.
R-HSA-4090284 (Reactome) HIPK2 is SUMOylated at lysine-32 with SUMO1. (Lysine-25 is cited by Hofmann et al. 2005 and Gresko et al. 2005, however the sequence motif listed in Hoffmann et al. 2005 corresponds to lysine-32 of the UniProt reference protein. An alternative isoform having lysine-25 is listed as accession AAG35710 in GenBank.) SUMOylation of HIPK2 disrupts interaction of HIPK2 with GROUCHO corepressor, inhibits JNK activation, and inhibits p53-independent antiproliferative function.
R-HSA-4090288 (Reactome) PIAS1,3 SUMOylates MBD1 at lysine-499 and lysine-538 of the reference sequence (lysine-450 and lysine-489 of isoform 5) with SUMO1 (Lyst et al. 2006, Uchimura et al. 2006). SUMOylated MBD1 does not form a complex with SETDB1 and does not repress transcription.
R-HSA-5228521 (Reactome) PIAS1, PIAS4 SUMOylate CASP8AP2 (FLASH) at lysine-1813 with SUMO1 (Alm-Kristiansen et al. 2009, Alm-Kristiansen et al. 2011). SUMOylation enhances the transcriptional coactivation activity of CASP8AP2. As inferred from mouse homologs, SUMOylation also appears to trigger proteasomal degradation of CASP8AP2 (Vennemann and Hofmann 2013).
SAFBR-HSA-4085347 (Reactome)
SAFBR-HSA-4085372 (Reactome)
SIN3AR-HSA-4085994 (Reactome)
SUMO1:C93-UBE2IR-HSA-3108209 (Reactome)
SUMO1:C93-UBE2IR-HSA-3296126 (Reactome)
SUMO1:C93-UBE2IR-HSA-3782535 (Reactome)
SUMO1:C93-UBE2IR-HSA-3899291 (Reactome)
SUMO1:C93-UBE2IR-HSA-3900047 (Reactome)
SUMO1:C93-UBE2IR-HSA-3900070 (Reactome)
SUMO1:C93-UBE2IR-HSA-3900177 (Reactome)
SUMO1:C93-UBE2IR-HSA-3903017 (Reactome)
SUMO1:C93-UBE2IR-HSA-3927824 (Reactome)
SUMO1:C93-UBE2IR-HSA-3927886 (Reactome)
SUMO1:C93-UBE2IR-HSA-3927959 (Reactome)
SUMO1:C93-UBE2IR-HSA-4085296 (Reactome)
SUMO1:C93-UBE2IR-HSA-4085318 (Reactome)
SUMO1:C93-UBE2IR-HSA-4085331 (Reactome)
SUMO1:C93-UBE2IR-HSA-4085347 (Reactome)
SUMO1:C93-UBE2IR-HSA-4085992 (Reactome)
SUMO1:C93-UBE2IR-HSA-4085994 (Reactome)
SUMO1:C93-UBE2IR-HSA-4086036 (Reactome)
SUMO1:C93-UBE2IR-HSA-4086083 (Reactome)
SUMO1:C93-UBE2IR-HSA-4086088 (Reactome)
SUMO1:C93-UBE2IR-HSA-4090284 (Reactome)
SUMO1:C93-UBE2IR-HSA-4090288 (Reactome)
SUMO1:C93-UBE2IR-HSA-5228521 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-3899291 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-3900047 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-3900070 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-3900177 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-3903017 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-3927886 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-3927959 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4085296 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4085318 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4085992 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4086083 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4086088 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4090284 (Reactome)
SUMO1:CASP8AP2ArrowR-HSA-3927824 (Reactome)
SUMO1:CASP8AP2ArrowR-HSA-5228521 (Reactome)
SUMO1:CTBP1ArrowR-HSA-3108209 (Reactome)
SUMO1:DDX17ArrowR-HSA-3900047 (Reactome)
SUMO1:DDX5ArrowR-HSA-3900177 (Reactome)
SUMO1:HIPK2ArrowR-HSA-4090284 (Reactome)
SUMO1:ING2ArrowR-HSA-4086083 (Reactome)
SUMO1:NCOR2ArrowR-HSA-3927886 (Reactome)
SUMO1:NPM1ArrowR-HSA-4086088 (Reactome)
SUMO1:PARK7ArrowR-HSA-4085331 (Reactome)
SUMO1:PPARGC1AArrowR-HSA-3903017 (Reactome)
SUMO1:SIN3AArrowR-HSA-4085994 (Reactome)
SUMO1:SUMO1:NRIP1ArrowR-HSA-4086036 (Reactome)
SUMO1:TRIM28:ZNF350ArrowR-HSA-3782535 (Reactome)
SUMO1:ZNF131ArrowR-HSA-3296126 (Reactome)
SUMO2,3-K231,K294-SAFBArrowR-HSA-4085372 (Reactome)
SUMO2,3-K263-NPM1ArrowR-HSA-4086059 (Reactome)
SUMO2,3-K428-CTBP1ArrowR-HSA-3108203 (Reactome)
SUMO2-K53-DDX5ArrowR-HSA-3900194 (Reactome)
SUMO2:UBE2IR-HSA-3900194 (Reactome)
TOPORSmim-catalysisR-HSA-4085994 (Reactome)
TRIM28:ZNF350R-HSA-3782535 (Reactome)
TRIM28mim-catalysisR-HSA-3782535 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-3108203 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4085372 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4086059 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3mim-catalysisR-HSA-4086059 (Reactome)
UBE2IArrowR-HSA-3108203 (Reactome)
UBE2IArrowR-HSA-3108209 (Reactome)
UBE2IArrowR-HSA-3296126 (Reactome)
UBE2IArrowR-HSA-3782535 (Reactome)
UBE2IArrowR-HSA-3899291 (Reactome)
UBE2IArrowR-HSA-3900047 (Reactome)
UBE2IArrowR-HSA-3900070 (Reactome)
UBE2IArrowR-HSA-3900177 (Reactome)
UBE2IArrowR-HSA-3900194 (Reactome)
UBE2IArrowR-HSA-3903017 (Reactome)
UBE2IArrowR-HSA-3927824 (Reactome)
UBE2IArrowR-HSA-3927886 (Reactome)
UBE2IArrowR-HSA-3927959 (Reactome)
UBE2IArrowR-HSA-4085296 (Reactome)
UBE2IArrowR-HSA-4085318 (Reactome)
UBE2IArrowR-HSA-4085331 (Reactome)
UBE2IArrowR-HSA-4085347 (Reactome)
UBE2IArrowR-HSA-4085372 (Reactome)
UBE2IArrowR-HSA-4085992 (Reactome)
UBE2IArrowR-HSA-4085994 (Reactome)
UBE2IArrowR-HSA-4086036 (Reactome)
UBE2IArrowR-HSA-4086059 (Reactome)
UBE2IArrowR-HSA-4086083 (Reactome)
UBE2IArrowR-HSA-4086088 (Reactome)
UBE2IArrowR-HSA-4090284 (Reactome)
UBE2IArrowR-HSA-4090288 (Reactome)
UBE2IArrowR-HSA-5228521 (Reactome)
ZNF131R-HSA-3296126 (Reactome)
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