SCUD (Saccharomyces Cerevisiae Ubiquitination Database)


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Enzyme Information

General Information
Standard nameRSP5
Systematic nameYER125W
AliasMDP1, MUT2, NPI1, UBY1, SMM1
DescriptionUbiquitin-protein ligase involved in ubiquitin-mediated protein degradation; functions in multivesicular body sorting, heat shock response and ubiquitination of arrested RNAPII; contains a hect (homologous to E6-AP carboxyl terminus) domain.

Ubiquitination Features
Num. of substrates Total 69 wild-typeand 4 mutant known substrates.
Wild-type substrate
KeywordDescription
ACK1Activator of C kinase protein 1
ALG6Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
ALR1Magnesium transporter ALR1
ARN1Siderophore iron transporter ARN1
BSC5Bypass of stop codon protein 5
BUL1Ubiquitin ligase-binding protein BUL1
CDC3Cell division control protein 3
CPS1Carboxypeptidase S
CSR2Transcription factor CSR2
CTR1Copper transport protein CTR1
CUE5Ubiquitin-binding protein CUE5
DIA1Protein DIA1
EAF7Chromatin modification-related protein EAF7
EAR1Protein EAR1
ECM21Protein ECM21
ENT2Epsin-2
FUR4Uracil permease
GAL2Galactose transporter
GAP1General amino-acid permease GAP1
HPR1THO complex subunit HPR1
LSB1LAS seventeen-binding protein 1
MAL11General alpha-glucoside permease
MAL61Maltose permease MAL61
MGA2Protein MGA2
MUP1High-affinity methionine permease
NOP3Nucleolar protein 3
NTG2DNA base excision repair N-glycosylase 2
PGI1Glucose-6-phosphate isomerase
PPN1Endopolyphosphatase
PUT4Proline-specific permease
RCR1Protein RCR1
RCR2Protein RCR2
ROD1Protein ROD1
ROG1Putative lipase ROG1
ROG3Protein ROG3
RPB1DNA-directed RNA polymerase II subunit RPB1
RPB7DNA-directed RNA polymerase II subunit RPB7
RPC25DNA-directed RNA polymerase III subunit RPC8
RSA1Ribosome assembly 1 protein
RVS167Reduced viability upon starvation protein 167
SGT1Protein SGT1
SIP5Protein SIP5
SMF1Manganese transporter SMF1
SNA3Protein SNA3
SNA4Protein SNA4
SPT23Protein SPT23
SRP40Suppressor protein SRP40
STE2Pheromone alpha factor receptor
TAT2Tryptophan permease
TRE1Uncharacterized protein TRE1
TRM1N(2),N(2)-dimethylguanosine tRNA methyltransferase, mitochondrial
VPS9Vacuolar protein sorting-associated protein 9
YDL012CUncharacterized protein YDL012C
YFL010CWW domain-containing protein YFL010C
YGR068CUncharacterized protein YGR068C
YHL024WUncharacterized RNA-binding protein YHL024W
YHR131CPH domain-containing protein YHR131C
YIP5Protein YIP5
YJL084CUncharacterized protein YJL084C
YKL023WUncharacterized protein YKL023W
YKR021WUncharacterized protein YKR021W
YLH47LETM1 domain-containing protein YLH47, mitochondrial
YLR326WUncharacterized membrane protein YLR326W
YLR392CUncharacterized protein YLR392C
YMR181CUncharacterized protein YMR181C
YNL305CUncharacterized vacuolar membrane protein YNL305C
YPL146CUncharacterized protein YPL146C
YPR084WUncharacterized protein YPR084W
ZRT1Zinc-regulated transporter 1
Mutant substrate
KeywordWild type description
mPEP4Saccharopepsin [Precursor]
mPMA1Plasma membrane ATPase 1
mPRC1Carboxypeptidase Y [Precursor]
mSEC61Protein transport protein SEC61

Cross References
Swiss-Prot accessionP39940
SGD YER125W
Gene Ontology (GO)
Cellular componentGO:0010008endosome membraneIDA:SGD.
Cellular componentGO:0005794Golgi apparatusIDA:SGD.
Cellular componentGO:0005739mitochondrionIDA:SGD.
Cellular componentGO:0005886plasma membraneIDA:SGD.
Cellular componentGO:0000151ubiquitin ligase complexIDA:MGI.
Molecular functionGO:0042802identical protein bindingIPI:IntAct.
Molecular functionGO:0004842ubiquitin-protein ligase activityIDA:MGI.
Biological processGO:0006333chromatin assembly or disassemblyIMP:SGD.
Biological processGO:0006897endocytosisTAS:SGD.
Biological processGO:0010142farnesyl diphosphate biosynthetic process, ...IMP:SGD.
Biological processGO:0006406mRNA export from nucleusIMP:SGD.
Biological processGO:0006513protein monoubiquitinationIDA:SGD.
Biological processGO:0000209protein polyubiquitinationIDA:SGD.
Biological processGO:0006350transcriptionTAS:SGD.
Biological processGO:0006511ubiquitin-dependent protein catabolic processIDA:MGI.
EC number 6.3.2.-

Additional Features
Post Translational Modifications (PTM) PTM sites are not determined.

Sequence Information
Sequence length809
Molecular weight91816

	---------+----------+----------+----------+----------+
MPSSISVKLV AAESLYKRDV FRSPDPFAVL TIDGYQTKST SAAKKTLNPY   50
WNETFKFDDI NENSILTIQV FDQKKFKKKD QGFLGVVNVR VGDVLGHLDE   100
DTATSSGRPR EETITRDLKK SNDGMAVSGR LIVVLSKLPS SSPHSQAPSG   150
HTASSSTNTS STTRTNGHST SSTRNHSTSH PSRGTAQAVE STLQSGTTAA   200
TNTATTSHRS TNSTSSATRQ YSSFEDQYGR LPPGWERRTD NFGRTYYVDH   250
NTRTTTWKRP TLDQTEAERG NQLNANTELE RRQHRGRTLP GGSSDNSSVT   300
VQVGGGSNIP PVNGAAAAAF AATGGTTSGL GELPSGWEQR FTPEGRAYFV   350
DHNTRTTTWV DPRRQQYIRT YGPTNTTIQQ QPVSQLGPLP SGWEMRLTNT   400
ARVYFVDHNT KTTTWDDPRL PSSLDQNVPQ YKRDFRRKVI YFRSQPALRI   450
LPGQCHIKVR RKNIFEDAYQ EIMRQTPEDL KKRLMIKFDG EEGLDYGGVS   500
REFFFLLSHE MFNPFYCLFE YSAYDNYTIQ INPNSGINPE HLNYFKFIGR   550
VVGLGVFHRR FLDAFFVGAL YKMMLRKKVV LQDMEGVDAE VYNSLNWMLE   600
NSIDGVLDLT FSADDERFGE VVTVDLKPDG RNIEVTDGNK KEYVELYTQW   650
RIVDRVQEQF KAFMDGFNEL IPEDLVTVFD ERELELLIGG IAEIDIEDWK   700
KHTDYRGYQE SDEVIQWFWK CVSEWDNEQR ARLLQFTTGT SRIPVNGFKD   750
LQGSDGPRRF TIEKAGEVQQ LPKSHTCFNR VDLPQYVDYD SMKQKLTLAV   800
EETIGFGQE                                                809