MUB1_YEAST
ID MUB1_YEAST Reviewed; 620 AA.
AC Q03162; D6VZS3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=MYND-type zinc finger protein MUB1;
DE AltName: Full=Multi-budding protein;
GN Name=MUB1; OrderedLocusNames=YMR100W; ORFNames=YM6543.07;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP POSSIBLE FUNCTION.
RX PubMed=9427754; DOI=10.1093/emboj/17.1.204;
RA Kruger M., Fischer R.;
RT "Integrity of a Zn finger-like domain in SamB is crucial for morphogenesis
RT in ascomycetous fungi.";
RL EMBO J. 17:204-214(1998).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, INTERACTION WITH UBR2 AND RPN4, AND DOMAIN.
RX PubMed=18070918; DOI=10.1128/mcb.01787-07;
RA Ju D., Wang X., Xu H., Xie Y.;
RT "Genome-wide analysis identifies MYND-domain protein Mub1 as an essential
RT factor for Rpn4 ubiquitylation.";
RL Mol. Cell. Biol. 28:1404-1412(2008).
CC -!- FUNCTION: Involved in the determination of the onset of polarized
CC growth. Required for the ubiquitin-dependent degradation of RPN4.
CC Cooperates with UBR2 to transfer ubiquitin from RAD6 to RPN4.
CC {ECO:0000269|PubMed:18070918}.
CC -!- SUBUNIT: Interacts with UBR2 and RPN4. {ECO:0000269|PubMed:18070918}.
CC -!- INTERACTION:
CC Q03162; Q03465: RPN4; NbExp=3; IntAct=EBI-28207, EBI-15931;
CC Q03162; Q07963: UBR2; NbExp=2; IntAct=EBI-28207, EBI-34338;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The MYND-type zinc finger is essential for the ubiquitin-
CC dependent degradation of RPN4. {ECO:0000269|PubMed:18070918}.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Is a short-lived protein whose degradation is dependent
CC on the UBR2/RAD6 ubiquitin-protein ligase.
CC -!- SIMILARITY: Belongs to the MUB1/samB family. {ECO:0000305}.
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DR EMBL; Z49807; CAA89901.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09997.1; -; Genomic_DNA.
DR PIR; S55086; S55086.
DR RefSeq; NP_013818.1; NM_001182600.1.
DR AlphaFoldDB; Q03162; -.
DR BioGRID; 35276; 327.
DR ComplexPortal; CPX-2937; MUB1-RAD6-UBR2 ubiquitin ligase complex.
DR DIP; DIP-6429N; -.
DR IntAct; Q03162; 6.
DR MINT; Q03162; -.
DR STRING; 4932.YMR100W; -.
DR MaxQB; Q03162; -.
DR PaxDb; Q03162; -.
DR PRIDE; Q03162; -.
DR EnsemblFungi; YMR100W_mRNA; YMR100W; YMR100W.
DR GeneID; 855126; -.
DR KEGG; sce:YMR100W; -.
DR SGD; S000004706; MUB1.
DR VEuPathDB; FungiDB:YMR100W; -.
DR eggNOG; ENOG502QTM3; Eukaryota.
DR HOGENOM; CLU_014851_1_0_1; -.
DR InParanoid; Q03162; -.
DR OMA; HWCVAAT; -.
DR BioCyc; YEAST:G3O-32800-MON; -.
DR PRO; PR:Q03162; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03162; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990304; C:MUB1-RAD6-UBR2 ubiquitin ligase complex; IPI:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IC:ComplexPortal.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF01753; zf-MYND; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Reference proteome; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..620
FT /note="MYND-type zinc finger protein MUB1"
FT /id="PRO_0000218323"
FT ZN_FING 514..555
FT /note="MYND-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 563..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 620 AA; 72251 MW; E38AA57377082966 CRC64;
MRDSNHRSLT SNKPIVTITS TVYDRRALDI NSSIPLINSL NYLTYLTSNS SKVRETVAND
GALERLVSIL RSCHLSLFEL LDLDLENFNE HENIKDLWKE KRLALCAWKW TLTFQCLVLT
GTRGTEQIRK KVVMSGVLSV LVTVLDNYLL YHKNYDFIKD QTMTFDFKGI TTETMYKFMR
KDENETYQQY IEFITGQDKL KLSTDKNFLN ERLVAPSMTI PTDFSDIWGR FADLASNFEP
DQERHDDDID IDSEVESENF DAHKNFFSQP DINRPTISTP REFFLGRIVP KQDDVIWSLQ
LLAFVSKYTY MKSTLQNVEL VESLSFRSMA YKIKQRISEE NDLEEQERDV TVKLSSLYPY
LSKNPENNSK VKALDTSKMD PFFKELEELS NRCQQEEQNE ICNNHCPVLN LFERYRVPKP
SDDNAYGKDK ERINLRKKIS DNFERRWSYD KMKKELTNIV YKNKVLTNVV NIFPLVEKYT
VSAENTHDVI YWSSVIMRNS CRKNEILGVR QCANFSCGKW EDFPRQFAKC RRCKRTKYCS
RKCQLKAWGY HRYWCHEVGS SHMRSTNTTT GVNTPNEPSS LNATATTAAD VSNSTSTFTP
NISTTVPDEI SNRDENSIPE
