ID A0A663LUL0_ATHCN Unreviewed; 1711 AA.
AC A0A663LUL0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=UBR2 {ECO:0000313|Ensembl:ENSACUP00000003360.1};
OS Athene cunicularia (Burrowing owl) (Speotyto cunicularia).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Strigiformes;
OC Strigidae; Athene.
OX NCBI_TaxID=194338 {ECO:0000313|Ensembl:ENSACUP00000003360.1, ECO:0000313|Proteomes:UP000472269};
RN [1] {ECO:0000313|Ensembl:ENSACUP00000003360.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSACUP00000003360.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the E3 ubiquitin-protein ligase UBR1-like
CC family. {ECO:0000256|ARBA:ARBA00046341, ECO:0000256|RuleBase:RU366018}.
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DR Ensembl; ENSACUT00000003574.1; ENSACUP00000003360.1; ENSACUG00000001572.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000472269; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd16686; RING-H2_UBR2; 1.
DR CDD; cd19679; UBR-box_UBR2; 1.
DR FunFam; 2.10.110.30:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform 1; 1.
DR FunFam; 1.10.10.2670:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform X1; 1.
DR FunFam; 3.30.1390.10:FF:000003; E3 ubiquitin-protein ligase UBR2 isoform X1; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR047508; UBR-box_UBR2.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR055194; UBR1-like_WH.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF28; E3 UBIQUITIN-PROTEIN LIGASE UBR2; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF22960; WHD_UBR1; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472269};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 88..159
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 88..159
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
SQ SEQUENCE 1711 AA; 195631 MW; 93B32A3E051D8921 CRC64;
LVTEATPVAP LLPKSCHKWL QANDLQKEVY QHLAYYVPKI YCRGPNPAPQ REDMLAQHVL
LGPMEWYLCG EDPAFGFPKL EQANKPSHLC GRVFKVGEPT YSCRDCAVDP TCVLCMECFL
GSIHREHRYR MTTSGGGGFC DCGDTEAWKE GPYCQKHELN TSETAEEEDP LVHLPEDMVV
RAYNIFAITF KYAVDILTWE KENELPGLEM IEKSDTYYCM LFNDEVHTYE QVIYTLQKAV
NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC DQAKSVIVRN TSRQTKPLKV QVMHSSIVAH
QSFGLKLLTW LGSVIGYSDG LRRILCQVGL QEGPDGENSS LVDKLMLYDS KLWKGARNVY
HQLFMSSLLM DLKYKKLFAI RFARNYERLQ SDFMKDDHDR EFSIADLSIQ IFTVPSLARM
LITEENLMTT IIKTFMDHLR HRDIQGRFQF ERYTALQAFK FRRVQSLIVD LKYVLISKPT
EWSDDLRHKF LEGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL QMKLTLVISM
MQDWCALDEK VLIEAYKKCL TVLMQCHSGF TDGEQPIVLS MCGHSVETIR YCVSQEKVSI
HLPVSRLLAG LHVLLSKTEV AYKFPELLPL SELSPPMLIE HPLRCLVLCA QVHAGMWRRN
GFSLVNQIYY YHNVKCRREM FDKDIVMLQT GVSMMDPNHF LMIMLSRFEL YQIFSTPDYG
KRFSTENTNK DVVQQNNTLI EEMLYLIIMI VGERFSPGIG QVNATDEIKR EIIHQLSIRP
MAHSELVKAL PEDENRETGM ESVIEEVACF KKPGLTGRGL YELKPECARN FNLYFYHFSR
AEQSKAEEAQ RKLKRQNRED TALPPPALPP FCPLFASLVN ILQSDVMLCI MGTILQWAVE
HNGYAWSESM LQRVLHLLGM ALQEEKQHLE NLNEENVVTF TFTQKISRPG EAPNNSPSIL
AMLETLQNAP HLEVHKDMIR WILKMLKMTE KRKAEIARLR REKIMAQMSE MQRHFINENK
ELFQQTLEEL DTSTSGVHEN SPVISDAKLT ALGPEQTRVA EHRQVVMCIL CQEEQEVKVD
SRAMVLAAFI QRSTVLSKNR NKITPDPEKY DPLFMHPDLS CGTHTGSCGH IMHAHCWQRY
FDAVQAKEQR RQQRLRVHTS YDVENGEFLC PLCECLSNTV IPLLPPPRVL FNRLDFSGQP
NLTQWIKTIS QQIKVLYLLR DEDGASNSGN AEKMDQLQLP EGFRPDFKPK NPYSESIKEM
LTTFGTATYK VGLKVHPNEE DPRVPIMCWG SCAYTIQTIE RILADEDKPL FGHLPCRQDD
CLTSLTRFAA AHWTVSSLPA VQTHFCTLLA SLVPNEKNGN LPCILDIDMF HLLVSLVLSF
PAIHCQDFSG VSLGTGDLHL FHLVTMAHII QILLTSSTEE NGMDQENTNS EEEVAVLTLY
KFLCQCTGSA LKEISSGWHL WRNLKAGIMP FLRCSALFFH YLNGVPAPSE IQVNGTNQFE
HLCSYLSLPN NLTCLFQENS EILNTLIESW CSNSEVKRYL EGKRHAISYA RESNKLIDLP
DDYSCLINQA SNFSCPKSGG DKSRAPTLCL VCGTMLCSQS YCCQTELEGE DVGACTAHTY
TCGSGVGIFL RVRECQVLFL AGKTKGCFYP PPYLDDYGET DQGLRRGNPL HLCKERFKKI
QKLWQQHSIT EEIGHAQEAN QTLVGIDWQH L
//
