UBR1_DROME
ID UBR1_DROME Reviewed; 1824 AA.
AC Q9VX91; B5RIU9; Q8SX71;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase UBR1;
DE EC=2.3.2.27;
DE AltName: Full=N-recognin;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR1;
DE AltName: Full=Ubiquitin-protein ligase E3-alpha;
GN Name=Ubr1 {ECO:0000312|FlyBase:FBgn0030809};
GN ORFNames=CG9086 {ECO:0000312|FlyBase:FBgn0030809};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase 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:0000250}.
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 -!- 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 -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48687.2; -; Genomic_DNA.
DR EMBL; AY094815; AAM11168.1; -; mRNA.
DR EMBL; BT044223; ACH92288.1; -; mRNA.
DR RefSeq; NP_001245723.1; NM_001258794.2.
DR RefSeq; NP_001285356.1; NM_001298427.1.
DR RefSeq; NP_573184.1; NM_132956.3.
DR AlphaFoldDB; Q9VX91; -.
DR SMR; Q9VX91; -.
DR BioGRID; 59018; 2.
DR IntAct; Q9VX91; 6.
DR STRING; 7227.FBpp0074189; -.
DR PaxDb; Q9VX91; -.
DR PRIDE; Q9VX91; -.
DR DNASU; 32687; -.
DR EnsemblMetazoa; FBtr0074415; FBpp0074189; FBgn0030809.
DR EnsemblMetazoa; FBtr0308839; FBpp0300996; FBgn0030809.
DR EnsemblMetazoa; FBtr0346190; FBpp0312009; FBgn0030809.
DR GeneID; 32687; -.
DR KEGG; dme:Dmel_CG9086; -.
DR UCSC; CG9086-RA; d. melanogaster.
DR CTD; 197131; -.
DR FlyBase; FBgn0030809; Ubr1.
DR VEuPathDB; VectorBase:FBgn0030809; -.
DR eggNOG; KOG1140; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_001801_2_0_1; -.
DR InParanoid; Q9VX91; -.
DR OMA; ILCQEDQ; -.
DR OrthoDB; 81415at2759; -.
DR PhylomeDB; Q9VX91; -.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9VX91; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 32687; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 32687; -.
DR PRO; PR:Q9VX91; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030809; Expressed in saliva-secreting gland and 24 other tissues.
DR ExpressionAtlas; Q9VX91; baseline and differential.
DR Genevisible; Q9VX91; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
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; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; ISS:FlyBase.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR Gene3D; 1.10.10.2670; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 2.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1824
FT /note="E3 ubiquitin-protein ligase UBR1"
FT /id="PRO_0000056139"
FT ZN_FING 107..178
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1126..1220
FT /note="RING-type; atypical"
FT REGION 1006..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1661
FT /note="E -> V (in Ref. 3; AAM11168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1824 AA; 208361 MW; 79992C11175E82A0 CRC64;
MDRYDMEDVV VAPPAECSSP LKEWRLKRQA GTLDRSDIIE FLKRESPKYF DYQTSATVKD
TNVITLKCMF KESLAKEEII DVVVEFMLGD NPSSALEKLR LEGNTATVCG KVFKNGEPTY
SCRECGVDPT CVLCVNCFKR SAHRFHKYKM STSGGGGCCD CGDDEAWKKD QYCELHLANR
KNPLESKILT DAVLERVEIC FGAILAFCVS YLEIEPNASL QCLDGNVEGG QVDGAQYCTV
LYNDESHTFD QVIQTLTKIA KCRAKDAMEI VAAIDREGRA VVKCDTFEEC NKLKVSIENQ
MILPTSLVST ARNNQSLRTS VLHIGAVACQ QFALQLLGWF QEFLVRHYLF RKTFSELVQR
KQETFCIRHI LEYDVKLWKT ARTCWHRLLI SGMLMEYDNK MILAQEFSRR YATIVEDFIS
DDHDHAFSIV SLSVQLFTVP SIAHHLIAHE GIFDKLLHTF YHVAIEKFIR NKTLHFSKNI
ASLTFFKRAN YILYDLRYLL SLKPDVLSND LRNGFLEGCR ALMRVLNVMQ GMESMTRQTG
QHMDYEPEWE CAFNLHIKLA TTISQVIDWA SGDVKLLRKL YKMTMRALVS NSFIVGGEKV
MQPKKVADHV ANCLVYDISV QPVSIHLPLS RFFAGIYLHL GAHDLTYDGL QTETEALSIK
LTPREIIEPV LCTQAMIAQV GAGLWRRNGY TLLHQLYFYR NVRCRVEMLD RDIACLQIGA
SLMESNEFLI HVLNRFNTIP WLQENYWSLL SGNEMNDDII REASIFDEFL ELLIVIIGER
WMPGVSMVTE EDRLRKEIIQ LLCIKPYSHS ELSRALPDGN SGNSDNVFEE VINTVAVFKK
PVGADSKGVY ELKEHLLKEF NMYFYHYTKE DKSKAEELQR ERRKAKKQLV CCPPPMLPKL
TPAFTPMANI LQCPVFLNIC SLIMERALNA YSRSFTESHL QKVLHLLGYA IQEELSEHYP
FLSFYERSQE YGILEKLEEL ARCPRLEAHY DFVLWTIERF KQLQAKQAPS DGRAGPSCSQ
QGTGGKLSLS AEEQAREERE NRARLAAERR AHIMAQMQKA QKSFISSNAE MFADTENETR
KESASTGPMD WEDIPPEEEQ GAVALESKVA CLGPDRKFYH GTDDTFKCIL CFENCAISRG
GRQLVSSAFV QTSRVIFTTP NLRNSQSALH ISCCGHVMHY SCWLEYFTNE EFKELRRPHR
NRAALAQAAN VEFQCPYCRT LSNAIIPVTE TLPAFSAPPS PNESYLPLDS FVEIMSTLAI
ELGNVKDHEL TTLPSVSNIL RLSGVVGGLA QFERSVQLIK NPPRLHADYI EGIEFLKKAL
LNTMKIQQSH LKDHPAIESI EMVPILWDSC SYTLQALEIY LYAVEKPLKA ELSMRHQSCA
RNLVRACSRS SALEWETDLP LLPPMRSQAE FSSRLLDTIF NQNDTSVLEW DCFRVLVPFQ
FGVLNLMVPE KGYKTIIPSG SMFDFYIMQT MFLAQLTKAV LCFDVEKEKA KRAEKAPNSE
LTQLDYIEQL PSRIRDNMID FYRRYNIPAR VLQKTKQKQL VEEESEENQG HGQTVVIPCE
SHHLALLLEY VQRQMSSFLR CSCLFYRFLT DVDFPDTFPT DQPDRFDLMC QYLGLDPMLG
VYFDMETVYA TMMHSFASHP HIDREVEQRC QPDARRSLQV EPCLRPLPRL KVLCDDFSDL
INSVSDIFCP NNEREEMKTP TMCLICGLIL CGQSYCCQPE LGKVSVGACT HHAHACGAEV
GIFLRIRDCQ VVYLGRGKGC FVPPPYLDEY GETDMGLRRG NPLRLSQAAY RKIYLQWLGH
GLHGEIARLN DNANVAAAAQ WHHM
