SUMOylation of DNA replication proteins (Homo sapiens)

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1, 4, 11, 25, 336, 21, 22, 289, 222, 9, 12, 2214, 16, 22, 26, 272, 3410, 22, 29, 3015, 18, 19, 23, 31nucleoplasmTOP2BNUP37 UBE2I-G92-SUMO3 NDC1 SUMO1-C93-UBE2I TPR SUMO1:TOP2ANUP88 SUMO1:C93-UBE2IUBE2I-G92-SUMO3 SUMO1:TOP1UBE2I-G97-SUMO1 UBE2I-G97-SUMO1 SUMO2-C93-UBE2I SUMO1:TOP2BUBE2I-G97-SUMO1 NUP98-4 NUP43 NUP98-5 NUPL2 NUP133 NUP205 SUMO1-K524-RANGAP1 NUP133 AURKB TPR PCNAUBE2ISEH1L-2 TOP1-G97-SUMO1 UBE2I-G97-SUMO1 K164-PCNA-G97-SUMO1 BIRC5 SUMO2-C93-UBE2I NUP188 NUP214 SUMO1-C93-UBE2I NUP62 NUP88 NUP54 SUMO1-K258-AURKA NUP188 SUMO1:AURKATOP2A-G97-SUMO1 NUP160 NUP214 NUP98-3 NUP107 NUP93 K254-PCNA-G97-SUMO1 UBE2I-G93-SUMO2 AURKA-G97-SUMO1 TOP2AAAAS SUMO1-C93-UBE2I NUP98-5 TOP1NUP205 UBE2INUP155 RANBP2 POM121 NUP85 Nup45 NUP50 Nuclear Pore Complex(NPC)SUMO3-C93-UBE2I K-PCNA-G97-SUMO1 PIAS4RAE1 UBE2I:SUMO2,UBE2I:SUMO3PIAS3NUP107 TOP2B-G97-SUMO1 NUP153 UBE2INUP35 RANBP2 SUMO1:C93-UBE2IINCENP SUMO1-K-TOP2A UBE2INUP98-4 NUP43 NUP54 UBE2I-G97-SUMO1 UBE2I UBE2INUP93 NUP210 NUP153 SUMO2,3-CDCA8 RAE1 AURKAUBE2I:SUMO2,UBE2I:SUMO3SUMO1:C93-UBE2ISUMO1:PCNAINCENP SUMO2,3:Chromosomepassenger complexChromosome passengercomplexSUMO1-K117-TOP1 POM121 NUPL1-2 SUMO1-K-TOP2B Nup45 POM121C NUP160 NUPL2 NDC1 NUP85 RANGAP1-G97-SUMO1 BIRC5 RANBP2:RANGAP1-SUMO1:UBE2I:Nuclear Pore Complex (NPC)SUMO1-K164,K254,K-PCNA POM121C NUP35 NUP37 NUPL1-2 NUP210 SUMO1:C93-UBE2ISUMO1-C93-UBE2I NUP155 NUP98-3 SUMO1:C93-UBE2IUBE2I-G93-SUMO2 CDCA8 SUMO3-C93-UBE2I SUMO1-C93-UBE2I AAAS SUMO2,3-TOP2ASUMO2,3-K202-AURKB UBE2INUP62 SEH1L-2 NUP50 2, 343, 132415, 235, 207, 8, 17, 322, 9, 22322, 26316, 9, 21, 2233, 1310, 22, 29, 30247, 8, 17


The sliding clamp protein PCNA, Aurora-A, Aurora-B, Borealin, and various topoisomerases can be SUMOylated (reviewed in Wan et al. 2012). SUMOylation of PCNA appears to reduce formation of double-strand breaks and inappropriate recombination (reviewed in Watts 2006, Watts 2007, Dieckman et al. 2012, Gazy and Kupiec 2012). SUMOylation of Aurora-A, Aurora-B, and Borealin is necessary for proper chromosome segregation. SUMOylation of topoisomerases is observed in response to damage caused by inhibitors of topoisomerases. View original pathway at:Reactome.


Pathway is converted from Reactome ID: 4615885
Reactome version: 66
Reactome Author 
Reactome Author: May, Bruce

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Ontology Terms



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  1. Watts FZ.; ''The role of SUMO in chromosome segregation.''; PubMed Europe PMC
  2. Mao Y, Desai SD, Liu LF.; ''SUMO-1 conjugation to human DNA topoisomerase II isozymes.''; PubMed Europe PMC
  3. Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMed Europe PMC
  4. Gazy I, Kupiec M.; ''The importance of being modified: PCNA modification and DNA damage response.''; PubMed Europe PMC
  5. Hsiao HH, Meulmeester E, Frank BT, Melchior F, Urlaub H.; ''"ChopNSpice," a mass spectrometric approach that allows identification of endogenous small ubiquitin-like modifier-conjugated peptides.''; PubMed Europe PMC
  6. Agostinho M, Santos V, Ferreira F, Costa R, Cardoso J, Pinheiro I, Rino J, Jaffray E, Hay RT, Ferreira J.; ''Conjugation of human topoisomerase 2 alpha with small ubiquitin-like modifiers 2/3 in response to topoisomerase inhibitors: cell cycle stage and chromosome domain specificity.''; PubMed Europe PMC
  7. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed Europe PMC
  8. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed Europe PMC
  9. Dawlaty MM, Malureanu L, Jeganathan KB, Kao E, Sustmann C, Tahk S, Shuai K, Grosschedl R, van Deursen JM.; ''Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha.''; PubMed Europe PMC
  10. Rallabhandi P, Hashimoto K, Mo YY, Beck WT, Moitra PK, D'Arpa P.; ''Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin.''; PubMed Europe PMC
  11. Dieckman LM, Freudenthal BD, Washington MT.; ''PCNA structure and function: insights from structures of PCNA complexes and post-translationally modified PCNA.''; PubMed Europe PMC
  12. 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
  13. 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
  14. Papouli E, Chen S, Davies AA, Huttner D, Krejci L, Sung P, Ulrich HD.; ''Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.''; PubMed Europe PMC
  15. Ban R, Nishida T, Urano T.; ''Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis.''; PubMed Europe PMC
  16. Freudenthal BD, Brogie JE, Gakhar L, Kondratick CM, Washington MT.; ''Crystal structure of SUMO-modified proliferating cell nuclear antigen.''; PubMed Europe PMC
  17. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC
  18. Werner A, Flotho A, Melchior F.; ''The RanBP2/RanGAP1*SUMO1/Ubc9 complex is a multisubunit SUMO E3 ligase.''; PubMed Europe PMC
  19. Fernández-Miranda G, Pérez de Castro I, Carmena M, Aguirre-Portolés C, Ruchaud S, Fant X, Montoya G, Earnshaw WC, Malumbres M.; ''SUMOylation modulates the function of Aurora-B kinase.''; PubMed Europe PMC
  20. Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD.; ''Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.''; PubMed Europe PMC
  21. Tammsalu T, Matic I, Jaffray EG, Ibrahim AFM, Tatham MH, Hay RT.; ''Proteome-wide identification of SUMO2 modification sites.''; PubMed Europe PMC
  22. Impens F, Radoshevich L, Cossart P, Ribet D.; ''Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.''; PubMed Europe PMC
  23. 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
  24. Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMed Europe PMC
  25. Wan J, Subramonian D, Zhang XD.; ''SUMOylation in control of accurate chromosome segregation during mitosis.''; PubMed Europe PMC
  26. Gali H, Juhasz S, Morocz M, Hajdu I, Fatyol K, Szukacsov V, Burkovics P, Haracska L.; ''Role of SUMO modification of human PCNA at stalled replication fork.''; PubMed Europe PMC
  27. Pfander B, Moldovan GL, Sacher M, Hoege C, Jentsch S.; ''SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase.''; PubMed Europe PMC
  28. Díaz-Martínez LA, Giménez-Abián JF, Azuma Y, Guacci V, Giménez-Martín G, Lanier LM, Clarke DJ.; ''PIASgamma is required for faithful chromosome segregation in human cells.''; PubMed Europe PMC
  29. Mao Y, Sun M, Desai SD, Liu LF.; ''SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage.''; PubMed Europe PMC
  30. Mo YY, Yu Y, Shen Z, Beck WT.; ''Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein.''; PubMed Europe PMC
  31. Klein UR, Haindl M, Nigg EA, Muller S.; ''RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin.''; PubMed Europe PMC
  32. Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMed Europe PMC
  33. Watts FZ.; ''Sumoylation of PCNA: Wrestling with recombination at stalled replication forks.''; PubMed Europe PMC
  34. Isik S, Sano K, Tsutsui K, Seki M, Enomoto T, Saitoh H, Tsutsui K.; ''The SUMO pathway is required for selective degradation of DNA topoisomerase IIbeta induced by a catalytic inhibitor ICRF-193(1).''; PubMed Europe PMC


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101539view11:40, 1 November 2018ReactomeTeamreactome version 66
101074view21:22, 31 October 2018ReactomeTeamreactome version 65
100604view19:57, 31 October 2018ReactomeTeamreactome version 64
100155view16:42, 31 October 2018ReactomeTeamreactome version 63
99705view15:10, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93814view13:38, 16 August 2017ReactomeTeamreactome version 61
93358view11:21, 9 August 2017ReactomeTeamreactome version 61
88419view11:54, 5 August 2016FehrhartOntology Term : 'sumoylation pathway' added !
86441view09:18, 11 July 2016ReactomeTeamNew pathway

External references


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NameTypeDatabase referenceComment
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
AURKA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
AURKAProteinO14965 (Uniprot-TrEMBL)
AURKB ProteinQ96GD4 (Uniprot-TrEMBL)
BIRC5 ProteinO15392 (Uniprot-TrEMBL)
CDCA8 ProteinQ53HL2 (Uniprot-TrEMBL)
Chromosome passenger complexComplexR-HSA-4655348 (Reactome)
INCENP ProteinQ9NQS7 (Uniprot-TrEMBL)
K-PCNA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K164-PCNA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K254-PCNA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
NDC1 ProteinQ9BTX1 (Uniprot-TrEMBL)
NUP107 ProteinP57740 (Uniprot-TrEMBL)
NUP133 ProteinQ8WUM0 (Uniprot-TrEMBL)
NUP153 ProteinP49790 (Uniprot-TrEMBL)
NUP155 ProteinO75694 (Uniprot-TrEMBL)
NUP160 ProteinQ12769 (Uniprot-TrEMBL)
NUP188 ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205 ProteinQ92621 (Uniprot-TrEMBL)
NUP210 ProteinQ8TEM1 (Uniprot-TrEMBL)
NUP214 ProteinP35658 (Uniprot-TrEMBL)
NUP35 ProteinQ8NFH5 (Uniprot-TrEMBL)
NUP37 ProteinQ8NFH4 (Uniprot-TrEMBL)
NUP43 ProteinQ8NFH3 (Uniprot-TrEMBL)
NUP50 ProteinQ9UKX7 (Uniprot-TrEMBL)
NUP54 ProteinQ7Z3B4 (Uniprot-TrEMBL)
NUP62 ProteinP37198 (Uniprot-TrEMBL)
NUP85 ProteinQ9BW27 (Uniprot-TrEMBL)
NUP88 ProteinQ99567 (Uniprot-TrEMBL)
NUP93 ProteinQ8N1F7 (Uniprot-TrEMBL)
NUP98-3 ProteinP52948-3 (Uniprot-TrEMBL)
NUP98-4 ProteinP52948-4 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL1-2 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
Nuclear Pore Complex (NPC)ComplexR-HSA-157689 (Reactome)
Nup45 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
PCNAProteinP12004 (Uniprot-TrEMBL)
PIAS3ProteinQ9Y6X2 (Uniprot-TrEMBL)
PIAS4ProteinQ8N2W9 (Uniprot-TrEMBL)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
POM121C ProteinA8CG34 (Uniprot-TrEMBL)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
RANBP2:RANGAP1-SUMO1:UBE2I:Nuclear Pore Complex (NPC)ComplexR-HSA-5228516 (Reactome)
RANGAP1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
SUMO1-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO1-K-TOP2A ProteinP11388 (Uniprot-TrEMBL)
SUMO1-K-TOP2B ProteinQ02880 (Uniprot-TrEMBL)
SUMO1-K117-TOP1 ProteinP11387 (Uniprot-TrEMBL)
SUMO1-K164,K254,K-PCNA ProteinP12004 (Uniprot-TrEMBL)
SUMO1-K258-AURKA ProteinO14965 (Uniprot-TrEMBL)
SUMO1-K524-RANGAP1 ProteinP46060 (Uniprot-TrEMBL)
SUMO1:AURKAComplexR-HSA-4655329 (Reactome)
SUMO1:C93-UBE2IComplexR-HSA-2993783 (Reactome)
SUMO1:PCNAComplexR-HSA-4616014 (Reactome)
SUMO1:TOP1ComplexR-HSA-4641301 (Reactome)
SUMO1:TOP2AComplexR-HSA-4641318 (Reactome)
SUMO1:TOP2BComplexR-HSA-4641356 (Reactome)
SUMO2,3-CDCA8 ProteinQ53HL2 (Uniprot-TrEMBL)
SUMO2,3-K202-AURKB ProteinQ96GD4 (Uniprot-TrEMBL)
SUMO2,3-TOP2AProteinP11388 (Uniprot-TrEMBL)
SUMO2,3:Chromosome passenger complexComplexR-HSA-4655354 (Reactome)
SUMO2-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO3-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
TOP1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
TOP1ProteinP11387 (Uniprot-TrEMBL)
TOP2A-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
TOP2AProteinP11388 (Uniprot-TrEMBL)
TOP2B-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
TOP2BProteinQ02880 (Uniprot-TrEMBL)
TPR ProteinP12270 (Uniprot-TrEMBL)
UBE2I ProteinP63279 (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)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
AURKAR-HSA-4655404 (Reactome)
Chromosome passenger complexR-HSA-4655355 (Reactome)
Nuclear Pore Complex (NPC)mim-catalysisR-HSA-5228525 (Reactome)
PCNAR-HSA-4615910 (Reactome)
PIAS3mim-catalysisR-HSA-4655355 (Reactome)
PIAS4mim-catalysisR-HSA-4641350 (Reactome)
R-HSA-4615910 (Reactome) PCNA is SUMOylated with SUMO1 at lysine-164, lysine-254, and other residues (Papouli et al. 2005, Pfander et al. 2005, Gali et al. 2012, Impens et al. 2014). SUMO1 is predominant in vivo. SUMOylation prevents double strand break formation and recombination if DNA replication stalls at lesions (Gali et al. 2012). This is comparable to the situation in Saccharomyces cerevisiae where sumoylated PCNA recruits the Srs2 helicase to prevent recombination during S phase (Pfander et al. 2005, Papouli et al. 2005). In the yeast PCNA homolog, SUMO at lysine-164 is located on the opposite face of PCNA from the face that interacts with DNA polymerase (Freudenthal et al. 2011).
R-HSA-4641342 (Reactome) TOP2A is SUMOylated with SUMO1 (Mao et al. 2000, Dawlaty et al. 2008, Matafora et al. 2009, Impens et al. 2014). SUMOylation is observed in response to TOP2A-mediated DNA damage induced by teniposide.
R-HSA-4641345 (Reactome) TOP2B is SUMOylated with SUMO1 (Mao et al. 2000, Isik et al. 2003). SUMOylation is observed in response to topoisomerase-mediated DNA damage induced by teniposide.
R-HSA-4641350 (Reactome) PIAS4 SUMOylates TOP2A with SUMO2,3 (Diaz-Martinez et al. 2006, Agostinho et al. 2008, Impens et al. 2014, Tammsalu et al. 2014). SUMOylation is observed in interphase and mitosis in response to inhibitors of topoisomerase. SUMOylated TOP2A is localized to centromeres during mitosis.
R-HSA-4641362 (Reactome) TOP1 is SUMOylated at lysine-117 with SUMO1 (Mao et al. 2000, Mo et al. 2002, Rallabhandi et al. 2002, Impens et al. 2014). SUMOylation is observed in response to the topoisomerase inhibitor camptothecin and causes nucleolar delocalization of TOP1.
R-HSA-4655355 (Reactome) During early mitosis (before metaphase) RANBP2 in the RANBP2:RANGAP-SUMO:UBC9 complex SUMOylates CDCA8 (Borealin) with SUMO2,3 at unknown lysine residues (Klein et al. 2009, Fernandez-Miranda et al. 2010, Ban et al. 2011, Werner et al. 2012, Hendriks et al. 2014). CDCA8 can also be SUMOylated with SUMO1 but SUMO2,3 is observed to predominate in vivo. At this time PIAS3 also SUMOylates AURKB (Aurora-B) at lysine-202 with SUMO2,3. The SUMOylated complex is observed in the cytosol after the nuclear envelope has broken down. As inferred from mouse, failure to SUMOylate AURKB causes defective centromeric function and abnormal chromosome segregation (Fernandez-Miranda et al. 2010).
R-HSA-4655404 (Reactome) As inferred from mouse homologs, AURKA (Aurora-A) is SUMOylated at lysine-258 with SUMO1. AURKA, SUMO1, and UBE2I (UBC9) colocalize to centrisomes and the mitotic spindle. SUMOylation of AURKA is required for proper localization to the microtubules of the mitotic spindle therefore SUMOylated AURKA is assumed to be located on spindles in the cytosol during metphase.
R-HSA-5228525 (Reactome) RANBP2 of the nuclear pore complex SUMOylates TOP2A with SUMO1 (Dawlaty et al. 2008, Impens et al. 2014). SUMOylated TOP2A is localized to centromeres. As inferred from mouse homologs, SUMOylation of TOP2A by RANBP2 is required for resolution of sister centromeres (Dawlaty et al. 2008).
RANBP2:RANGAP1-SUMO1:UBE2I:Nuclear Pore Complex (NPC)mim-catalysisR-HSA-4655355 (Reactome)
SUMO1:AURKAArrowR-HSA-4655404 (Reactome)
SUMO1:C93-UBE2IR-HSA-4615910 (Reactome)
SUMO1:C93-UBE2IR-HSA-4641342 (Reactome)
SUMO1:C93-UBE2IR-HSA-4641345 (Reactome)
SUMO1:C93-UBE2IR-HSA-4641362 (Reactome)
SUMO1:C93-UBE2IR-HSA-4655404 (Reactome)
SUMO1:C93-UBE2IR-HSA-5228525 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4615910 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4641342 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4641345 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4641362 (Reactome)
SUMO1:PCNAArrowR-HSA-4615910 (Reactome)
SUMO1:TOP1ArrowR-HSA-4641362 (Reactome)
SUMO1:TOP2AArrowR-HSA-4641342 (Reactome)
SUMO1:TOP2AArrowR-HSA-5228525 (Reactome)
SUMO1:TOP2BArrowR-HSA-4641345 (Reactome)
SUMO2,3-TOP2AArrowR-HSA-4641350 (Reactome)
SUMO2,3:Chromosome passenger complexArrowR-HSA-4655355 (Reactome)
TOP1R-HSA-4641362 (Reactome)
TOP2AR-HSA-4641342 (Reactome)
TOP2AR-HSA-4641350 (Reactome)
TOP2AR-HSA-5228525 (Reactome)
TOP2BR-HSA-4641345 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4641350 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4655355 (Reactome)
UBE2IArrowR-HSA-4615910 (Reactome)
UBE2IArrowR-HSA-4641342 (Reactome)
UBE2IArrowR-HSA-4641345 (Reactome)
UBE2IArrowR-HSA-4641350 (Reactome)
UBE2IArrowR-HSA-4641362 (Reactome)
UBE2IArrowR-HSA-4655355 (Reactome)
UBE2IArrowR-HSA-4655404 (Reactome)
UBE2IArrowR-HSA-5228525 (Reactome)
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