SCUD (Saccharomyces Cerevisiae Ubiquitination Database)


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Substrate Information

General Information
Standard nameAHP1
Systematic nameYLR109W
DescriptionPeroxiredoxin type-2

Ubiquitination Features
NumberSiteTypeE2E3 ClassE3 SubclassSubstrate ReceptorUbiquitin ReceptorDUBEffect
1         
2        Proteasomal Degradation
* Blank: not determined, NA: not applicable.

References
[1]EvidencePurification & Protein ID
Methodpurification (HB-ubiquitin (a tandem affinity tag under denaturing conditions)), LC/MS
Reference"A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking."
Tagwerker C, Flick K, Cui M, Guerrero C, Dou Y, Auer B, Baldi P, Huang L, Kaiser P.
Mol Cell Proteomics. 5(4):737-48 (2006) [16432255]
[2]EvidencePurification & Protein ID
Methodpurification (ubiquitin-chain by UBA domain-containing protein, 6xHis-ubiquitin (two-step)), LC/MS, validation (statistical quantitative analysis)
Reference"Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway."
Mayor T, Graumann J, Bryan J, MacCoss MJ, Deshaies RJ.
Mol Cell Proteomics. 6(11):1885-95 (2007) [17644757]

Cross References
Swiss-Prot accessionP38013
SGD YLR109W
Gene Ontology (GO)
Cellular componentGO:0005737cytoplasmIDA:SGD.
Molecular functionGO:0005515protein bindingIPI:IntAct.
Molecular functionGO:0008379thioredoxin peroxidase activityIDA:SGD.
Biological processGO:0030503regulation of cell redox homeostasisIDA:SGD.
Biological processGO:0010038response to metal ionIMP:SGD.
Biological processGO:0006979response to oxidative stressIGI:SGD.
EC number 1.11.1.15

Additional Features
Other Post Translational Modifications (PTM)
Residue indexType
2N-acetylserine.
2Phosphoserine.
22Phosphoserine.

Sequence Information
Sequence length176
Molecular weight19115

	---------+----------+----------+----------+----------+
MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI   50
ITGAPAAFSP TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW   100
AKSLGVKDTT HIKFASDPGC AFTKSIGFEL AVGDGVYWSG RWAMVVENGI   150
VTYAAKETNP GTDVTVSSVE SVLAHL                             176