UBR2_YEAST
ID UBR2_YEAST Reviewed; 1872 AA.
AC Q07963; D6VY26;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase UBR2;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR2;
DE AltName: Full=Ubiquitin-protein ligase E3 component N-recognin-1 homolog;
GN Name=UBR2; OrderedLocusNames=YLR024C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 INTERACTION WITH UBC2.
RX PubMed=10581257; DOI=10.1093/emboj/18.23.6832;
RA Xie Y., Varshavsky A.;
RT "The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3
RT is required for the synthesis of multiubiquitin chain.";
RL EMBO J. 18:6832-6844(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-709.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [7]
RP INTERACTION WITH UBC2 AND RPN4, AND FUNCTION.
RX PubMed=15504724; DOI=10.1074/jbc.m410085200;
RA Wang L., Mao X., Ju D., Xie Y.;
RT "Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.";
RL J. Biol. Chem. 279:55218-55223(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH MUB1.
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1218 AND SER-1222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which probably functions outside
CC the N-end rule pathway, since it lacks the residues essential for the
CC degradation of N-end rule substrates. Mediates RPN4 ubiquitination and
CC subsequent degradation. {ECO:0000269|PubMed:15504724,
CC ECO:0000269|PubMed:18070918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with MUB1, RPN4 and UBC2.
CC {ECO:0000269|PubMed:10581257, ECO:0000269|PubMed:15504724,
CC ECO:0000269|PubMed:18070918}.
CC -!- INTERACTION:
CC Q07963; Q03162: MUB1; NbExp=2; IntAct=EBI-34338, EBI-28207;
CC Q07963; P06104: RAD6; NbExp=6; IntAct=EBI-34338, EBI-19722;
CC Q07963; Q03465: RPN4; NbExp=2; IntAct=EBI-34338, EBI-15931;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His
CC ligand in place of the fourth Cys of the classical motif.
CC -!- MISCELLANEOUS: Present with 49 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Deletion produces no detectable phenotype.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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DR EMBL; Z73196; CAA97547.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09342.1; -; Genomic_DNA.
DR PIR; S64851; S64851.
DR RefSeq; NP_013124.1; NM_001181911.2.
DR AlphaFoldDB; Q07963; -.
DR SMR; Q07963; -.
DR BioGRID; 31298; 442.
DR ComplexPortal; CPX-2935; RAD6-UBR2 ubiquitin ligase complex.
DR ComplexPortal; CPX-2937; MUB1-RAD6-UBR2 ubiquitin ligase complex.
DR DIP; DIP-6593N; -.
DR IntAct; Q07963; 6.
DR MINT; Q07963; -.
DR STRING; 4932.YLR024C; -.
DR iPTMnet; Q07963; -.
DR MaxQB; Q07963; -.
DR PaxDb; Q07963; -.
DR PRIDE; Q07963; -.
DR EnsemblFungi; YLR024C_mRNA; YLR024C; YLR024C.
DR GeneID; 850711; -.
DR KEGG; sce:YLR024C; -.
DR SGD; S000004014; UBR2.
DR VEuPathDB; FungiDB:YLR024C; -.
DR eggNOG; KOG1140; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_004097_0_0_1; -.
DR InParanoid; Q07963; -.
DR OMA; TKYSMRE; -.
DR BioCyc; YEAST:G3O-32185-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q07963; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07963; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:1990304; C:MUB1-RAD6-UBR2 ubiquitin ligase complex; IPI:SGD.
DR GO; GO:1990305; C:RAD6-UBR2 ubiquitin ligase complex; IPI:ComplexPortal.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IGI:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
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; IBA:GO_Central.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1872
FT /note="E3 ubiquitin-protein ligase UBR2"
FT /id="PRO_0000056142"
FT ZN_FING 96..172
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1241..1362
FT /note="RING-type; atypical"
FT REGION 1134..1240
FT /note="Interaction with UBC2"
FT REGION 1203..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
SQ SEQUENCE 1872 AA; 216778 MW; 1F60CC41EB88752F CRC64;
MEDSDLSITN IRDFLTELPK LAKCEYSETT SYLLWKTLNL RLKHSDNDIN WRSLVSILNS
EAWENEKYRD ILNGRKWRTL EFENDHHSVG NMHIGTACTR LCFPSETIYY CFTCSTNPLY
EICELCFDKE KHVNHSYVAK VVMRPEGRIC HCGDPFAFND PSDAFKCKNE LNNIPISNDN
SNVTDDENVI SLLNYVLDFL IDVTVSYKEE AEAHSSERKA SSLMHPNQNS ITDDIMEKHE
CEPLVNDENF VFFDNNWSNT RKEAHMEWAI QIEEEECNVH YMDLASTITR ILNTPVEYAI
SITKALEDSH DVVTVLQSEN FFEIDQIAKE FQKENIVVHV RKADDIFKRK LTDDLTDWLY
SLCFKAATSL QNKYALRISM LDVWYSHFSK MRVSPTNTNP DFSKINLLGG FLISNEDSDE
SWFKPWSLEN IEDERISKIL TNYNERLIRA HSPNTVSHFY NFYGSRFQYI IINSINILSK
KSKFKMLKIM ASLFSLRDES RKFLAAQYID VYLSVLYDAV ASDAKECQVT LMSILGQYTF
QDPSIANMTI SSGFIERTIR FAFTLMAFNP EDLMSYLPIS LYNGFKLPTE TIRNRRTIIC
FKDLCTIMSA NTVPEELLSN EAIFNAIIES FSEFSNVLPL KRETKEHVEV ENFDFSAFYF
FFSSILIMTD GYTRSISLVK DAAFRKQIVL KLLDVAQTRE FESLTNSRKA ISPDNASTNE
NDSNKATLST VRETICNYVA ETINFQVGVN TQYFFNPMSY LFKFVIQWSQ CGRYEPIPAS
LTNYINLFEV FQDKQKALYI SESALSTLVL IGQINVGFWV RNGTPITHQA RMYTKYSMRE
FTYISDIFNV QFSMAMCNPD ELMVTYLSRW GLKHWANGVP MYDYPDTETT VAVVNECILL
LIQLLTEVRS LVMKSSKEGF ERTFKSEIIH ALCFDTCSYA QIVNCIPEHI TKHPSFDIYL
EKYANYTSPV SLTDNGIFVL KEKYKDEIDP YYIGLSSSRR YDVEKNIRLN MANLKKMKYE
DTFVPAKKVK DLLKNTLFSG LYSISSVNTF GLFLKNTLDH IIKYDYDNLL PRVVHLIHLC
VVNNLNEFMG ILWHEYAIVD TEFCHYHSIG SILYYCLLKD NFSESHGKIR EIFRYLMETA
PHVNVNSYLR EQTTSYTPGI LWPTKEDKSH KDKEFERKKH LARLRKKKLM KKLAQQQMKF
MENNSVDTSD ISTPRTTSPS LSPTRINAEN SSNTINSCCD DDCVFCKMPK DDDVFVYFSY
QERNICDHGI DFTNPTDVNR INSLFSGKQT KDSAIQENPQ DDDGTRLKFT SCEPVLRACG
HGSHTKCLSG HMKSIRGIQN QTTKNIPLSY GSGLIYCPVC NSLSNSFLPK TNDIDKRTSS
QFFMCIEKRS EAEENLDPMS SICIKAAMIL GDLQGKKVTT IEDAYKVVNS VFINTISNTE
LRLRSHKKEG KIVNMERISS QCILTLHLVC ELKSFIYKKF VNSKTFSSEI SRKIWNWNEF
LIKGNNVNLL LYMSQNFDNI DGGKTPQPPN LCIYEMFKRR FHQLLLLLAR DMMRVNFYKD
CRNKIKISSN GSEEPSTSFS YLFNTFKKYV DLFKPDDVRF DFTSLEKIKD FICSLLLESL
SIFCRRTFLL FNIQYDDDGD GDNNNNRSNN FMDVKQREIE LIFRYFKLPN LTHFLKDFFY
NELTQNIERY NDGNDNLRIQ QVIYDMVQNI NTRAYPSPEH IQLIELPLNL SKFSLDNDEI
SNKCDKYEIA VCLLCGQKCH IQKSIALQGY LQGECTDHMR NGCEITSAYG VFLMTGTNAI
YLSYGKRGTF YAAPYLSKYG ETNEDYKFGT PVYLNRARYA NLANEIVFGN MIPHIVFRLT
DGSADLGGWE TM
