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E3 ubiquitin-protein ligase UBR2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase UBR2) (Ubiquitin-protein ligase E3 component N-recognin-1 homolog)

 UBR2_YEAST              Reviewed;        1872 AA.
Q07963; D6VY26;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 140.
RecName: Full=E3 ubiquitin-protein ligase UBR2;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase UBR2;
AltName: Full=Ubiquitin-protein ligase E3 component N-recognin-1 homolog;
Name=UBR2; OrderedLocusNames=YLR024C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
INTERACTION WITH UBC2.
PubMed=10581257; DOI=10.1093/emboj/18.23.6832;
Xie Y., Varshavsky A.;
"The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger
of E3 is required for the synthesis of multiubiquitin chain.";
EMBO J. 18:6832-6844(1999).
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-709.
STRAIN=SUB592;
PubMed=12872131; DOI=10.1038/nbt849;
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,
Marsischky G., Roelofs J., Finley D., Gygi S.P.;
"A proteomics approach to understanding protein ubiquitination.";
Nat. Biotechnol. 21:921-926(2003).
[7]
INTERACTION WITH UBC2 AND RPN4, AND FUNCTION.
PubMed=15504724; DOI=10.1074/jbc.M410085200;
Wang L., Mao X., Ju D., Xie Y.;
"Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.";
J. Biol. Chem. 279:55218-55223(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
FUNCTION, AND INTERACTION WITH MUB1.
PubMed=18070918; DOI=10.1128/MCB.01787-07;
Ju D., Wang X., Xu H., Xie Y.;
"Genome-wide analysis identifies MYND-domain protein Mub1 as an
essential factor for Rpn4 ubiquitylation.";
Mol. Cell. Biol. 28:1404-1412(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1218 AND SER-1222, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: E3 ubiquitin-protein ligase which probably functions
outside the N-end rule pathway, since it lacks the residues
essential for the degradation of N-end rule substrates. Mediates
RPN4 ubiquitination and subsequent degradation.
{ECO:0000269|PubMed:15504724, ECO:0000269|PubMed:18070918}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with MUB1, RPN4 and UBC2.
{ECO:0000269|PubMed:10581257, ECO:0000269|PubMed:15504724,
ECO:0000269|PubMed:18070918}.
-!- INTERACTION:
Q03162:MUB1; NbExp=2; IntAct=EBI-34338, EBI-28207;
P06104:RAD6; NbExp=6; IntAct=EBI-34338, EBI-19722;
Q03465:RPN4; NbExp=2; IntAct=EBI-34338, EBI-15931;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a
His ligand in place of the fourth Cys of the classical motif.
-!- MISCELLANEOUS: Present with 49 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: Deletion produces no detectable phenotype.
-!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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EMBL; Z73196; CAA97547.1; -; Genomic_DNA.
EMBL; BK006945; DAA09342.1; -; Genomic_DNA.
PIR; S64851; S64851.
RefSeq; NP_013124.1; NM_001181911.2.
ProteinModelPortal; Q07963; -.
SMR; Q07963; -.
BioGrid; 31298; 432.
DIP; DIP-6593N; -.
IntAct; Q07963; 6.
MINT; Q07963; -.
STRING; 4932.YLR024C; -.
iPTMnet; Q07963; -.
MaxQB; Q07963; -.
PaxDb; Q07963; -.
PRIDE; Q07963; -.
EnsemblFungi; YLR024C; YLR024C; YLR024C.
GeneID; 850711; -.
KEGG; sce:YLR024C; -.
EuPathDB; FungiDB:YLR024C; -.
SGD; S000004014; UBR2.
GeneTree; ENSGT00530000063055; -.
HOGENOM; HOG000141750; -.
InParanoid; Q07963; -.
OMA; SMREFTY; -.
OrthoDB; EOG092C01SD; -.
BioCyc; YEAST:G3O-32185-MONOMER; -.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q07963; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:1990304; C:MUB1-RAD6-UBR2 ubiquitin ligase complex; IPI:SGD.
GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IGI:SGD.
GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
InterPro; IPR003126; Znf_UBR.
Pfam; PF02207; zf-UBR; 1.
SMART; SM00396; ZnF_UBR1; 1.
PROSITE; PS51157; ZF_UBR; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Isopeptide bond; Metal-binding;
Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1872 E3 ubiquitin-protein ligase UBR2.
/FTId=PRO_0000056142.
ZN_FING 96 172 UBR-type. {ECO:0000255|PROSITE-
ProRule:PRU00508}.
ZN_FING 1241 1362 RING-type; atypical.
REGION 1134 1240 Interaction with UBC2.
MOD_RES 1218 1218 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1222 1222 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
CROSSLNK 709 709 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:12872131}.
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


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