SCUD (Saccharomyces Cerevisiae Ubiquitination Database)


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Enzyme Information

General Information
Standard nameUBR1
Systematic nameYGR184C
AliasPTR1
DescriptionUbiquitin-protein ligase (E3) that interacts with Rad6p/Ubc2p to ubiquitinate substrates of the N-end rule pathway; binds to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle of the 26S proteasome.

Ubiquitination Features
Num. of substrates Total 1 wild-type known substrates.
Wild-type substrate
KeywordDescription
CUP9Homeobox protein CUP9

Cross References
Swiss-Prot accessionP19812
SGD YGR184C
Gene Ontology (GO)
Cellular componentGO:0000502proteasome complex (sensu Eukaryota)IPI:SGD.
Molecular functionGO:0004842ubiquitin-protein ligase activityTAS:SGD.
Biological processGO:0006513protein monoubiquitinationTAS:SGD.
Biological processGO:0000209protein polyubiquitinationTAS:SGD.
EC number 6.3.2.-

Additional Features
Post Translational Modifications (PTM)
Residue indexType
296Phosphoserine.
300Phosphoserine.

Sequence Information
Sequence length1950
Molecular weight224838

	---------+----------+----------+----------+----------+
MSVADDDLGS LQGHIRRTLR SIHNLPYFRY TRGPTERADM SRALKEFIYR   50
YLYFVISNSG ENLPTLFNAH PKQKLSNPEL TVFPDSLEDA VDIDKITSQQ   100
TIPFYKIDES RIGDVHKHTG RNCGRKFKIG EPLYRCHECG CDDTCVLCIH   150
CFNPKDHVNH HVCTDICTEF TSGICDCGDE EAWNSPLHCK AEEQENDISE   200
DPATNADIKE EDVWNDSVNI ALVELVLAEV FDYFIDVFNQ NIEPLPTIQK   250
DITIKLREMT QQGKMYERAQ FLNDLKYEND YMFDGTTTAK TSPSNSPEAS   300
PSLAKIDPEN YTVIIYNDEY HNYSQATTAL RQGVPDNVHI DLLTSRIDGE   350
GRAMLKCSQD LSSVLGGFFA VQTNGLSATL TSWSEYLHQE TCKYIILWIT   400
HCLNIPNSSF QTTFRNMMGK TLCSEYLNAT ECRDMTPVVE KYFSNKFDKN   450
DPYRYIDLSI LADGNQIPLG HHKILPESST HSLSPLINDV ETPTSRTYSN   500
TRLQHILYFD NRYWKRLRKD IQNVIIPTLA SSNLYKPIFC QQVVEIFNHI   550
TRSVAYMDRE PQLTAIRECV VQLFTCPTNA KNIFENQSFL DIVWSIIDIF   600
KEFCKVEGGV LIWQRVQKSN LTKSYSISFK QGLYTVETLL SKVHDPNIPL   650
RPKEIISLLT LCKLFNGAWK IKRKEGEHVL HEDQNFISYL EYTTSIYSII   700
QTAEKVSEKS KDSIDSKLFL NAIRIISSFL GNRSLTYKLI YDSHEVIKFS   750
VSHERVAFMN PLQTMLSFLI EKVSLKDAYE ALEDCSDFLK ISDFSLRSVV   800
LCSQIDVGFW VRNGMSVLHQ ASYYKNNPEL GSYSRDIHLN QLAILWERDD   850
IPRIIYNILD RWELLDWFTG EVDYQHTVYE DKISFIIQQF IAFIYQILTE   900
RQYFKTFSSL KDRRMDQIKN SIIYNLYMKP LSYSKLLRSV PDYLTEDTTE   950
FDEALEEVSV FVEPKGLADN GVFKLKASLY AKVDPLKLLN LENEFESSAT   1000
IIKSHLAKDK DEIAKVVLIP QVSIKQLDKD ALNLGAFTRN TVFAKVVYKL   1050
LQVCLDMEDS TFLNELLHLV HGIFRDDELI NGKDSIPEAY LSKPICNLLL   1100
SIANAKSDVF SESIVRKADY LLEKMIMKKP NELFESLIAS FGNQYVNDYK   1150
DKKLRQGVNL QETEKERKRR LAKKHQARLL AKFNNQQTKF MKEHESEFDE   1200
QDNDVDMVGE KVYESEDFTC ALCQDSSSTD FFVIPAYHDH SPIFRPGNIF   1250
NPNEFMPMWD GFYNDDEKQA YIDDDVLEAL KENGSCGSRK VFVSCNHHIH   1300
HNCFKRYVQK KRFSSNAFIC PLCQTFSNCT LPLCQTSKAN TGLSLDMFLE   1350
SELSLDTLSR LFKPFTEENY RTINSIFSLM ISQCQGFDKA VRKRANFSHK   1400
DVSLILSVHW ANTISMLEIA SRLEKPYSIS FFRSREQKYK TLKNILVCIM   1450
LFTFVIGKPS MEFEPYPQQP DTVWNQNQLF QYIVRSALFS PVSLRQTVTE   1500
ALTTFSRQFL RDFLQGLSDA EQVTKLYAKA SKIGDVLKVS EQMLFALRTI   1550
SDVRMEGLDS ESIIYDLAYT FLLKSLLPTI RRCLVFIKVL HELVKDSENE   1600
TLVINGHEVE EELEFEDTAE FVNKALKMIT EKESLVDLLT TQESIVSHPY   1650
LENIPYEYCG IIKLIDLSKY LNTYVTQSKE IKLREERSQH MKNADNRLDF   1700
KICLTCGVKV HLRADRHEMT KHLNKNCFKP FGAFLMPNSS EVCLHLTQPP   1750
SNIFISAPYL NSHGEVGRNA MRRGDLTTLN LKRYEHLNRL WINNEIPGYI   1800
SRVMGDEFRV TILSNGFLFA FNREPRPRRI PPTDEDDEDM EEGEDGFFTE   1850
GNDEMDVDDE TGQAANLFGV GAEGIAGGGV RDFFQFFENF RNTLQPQGNG   1900
DDDAPQNPPP ILQFLGPQFD GATIIRNTNP RNLDEDDSDD NDDSDEREIW   1950