UniProt: A0A2K6CTB1

Database: UniProt
Entry: A0A2K6CTB1_MACNE

LinkDB:  A0A2K6CTB1_MACNE 
Original site:  A0A2K6CTB1_MACNE

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (29)   

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ID   A0A2K6CTB1_MACNE        Unreviewed;      1749 AA.
AC   A0A2K6CTB1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN   Name=UBR1 {ECO:0000313|Ensembl:ENSMNEP00000026910.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000026910.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000026910.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC       ECO:0000256|RuleBase:RU366018}.
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DR   RefSeq; XP_011756334.1; XM_011758032.1.
DR   STRING; 9545.ENSMNEP00000026910; -.
DR   Ensembl; ENSMNET00000051198.1; ENSMNEP00000026910.1; ENSMNEG00000036851.1.
DR   GeneID; 105491520; -.
DR   KEGG; mni:105491520; -.
DR   CTD; 197131; -.
DR   GeneTree; ENSGT00950000183075; -.
DR   OMA; TWMKLLA; -.
DR   OrthoDB; 51389at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000036851; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR   GO; GO:0000502; C:proteasome complex; IEA:Ensembl.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0070728; F:leucine binding; IEA:Ensembl.
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:0071233; P:cellular response to leucine; IEA:Ensembl.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; IEA:Ensembl.
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; cd19678; UBR-box_UBR1; 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; IPR047507; UBR-box_UBR1.
DR   InterPro; IPR039164; UBR1-like.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR21497:SF27; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR   PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
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; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366018};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
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|RuleBase:RU366018}.
FT   DOMAIN          97..168
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         97..168
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          842..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..861
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1749 AA;  200055 MW;  E16BC2740DC57D7B CRC64;
     MADEEAGGAE RMEISAELPQ TPQRLACWWD QQVDFYTAFL HHLAQLVPEI YFAEMDPDLE
     KQEQSVQMSI FTPLEWYLFG EDPDICLEKL KHSGAFQLCG KVFKSGETTY SCRDCAIDPT
     CVLCMDCFQN SVHKNHRYKM HTSTGGGFCD CGDTEAWKTG PFCVNHEPGR AGTIKENSRC
     PLNEEVIAQA RKIFPSVIKY VVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH
     VIYSLQRALD CELAEAQLHT TAIDKEGRRA VKAGAYAACQ EAKEDIKSHS ENVSQHPLHV
     EVLHSEIMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL REEPDSENPC LISRLMLWDA
     KLYKGARKIL HELIFSSFFM EMEYKKLFAM EFVKYYKQLQ KEYISDDHDR SISITALSVQ
     MFTVPTLARH LIEEQNVISV ITETLLEVLP EYLDRNNKFN FQGYSQDKLG RVYAVICDLK
     YILISKPTIW TERLRMQFLE GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM
     QLKNILLMFQ EWCACDEELL LVAYKECHKA VMRCSTSFIS SSKTIVQLCG HSLETKSYRV
     SEDLVSIHLP LSRTLAGLHV RLSRLGAVSR LHEFVSFEDF QVEVLVEYPL RCLVLVAQVV
     AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS LMDPNKFLLL VLQRYELAEA
     FNKTLSTKDQ DLIKQYNTLI EEMLQVLIYI VGERYVPGVG NVTKEEVTMR EIIHLLCIEP
     MPHSAIAKNL PENENNETGL ESVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK
     TQHSKAEHMQ KKRRKQENKD EALPPPPPPE FCPAFSKVIN LLNCDVMMYI LRTVFERAID
     TDSNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVTFD FYHKASRLGS SAMNIQMLLE
     KLKGIPQLEG QKDMITWILQ MFDTVKRLRE KSCLIVATTS GSESVKNDEI THDKEKAERK
     RKAEAARLHR QKIMAQMSAL QKNFIETHKL MYDNTTEMPG KEDSIMEEES TPAVSDYSRI
     ALGPKRGPSV TEKEVLTCIL CQEEQEVKIE NNAMVLSACV QKSTALTQHR GKPIELSGET
     LDPLFMDPDL AYGTYTGSCG HVMHAVCWQK YFEAVQLSSQ QRIHVDLFDL ESGEYLCPLC
     KSLCNTVIPI IPLQPQKINS ENADALAQLL TLAQWIQTVL ARISGYNIRH AKGENPIPVF
     FNQGMGDSTF EFTSILSFGV QSSIKYSNSI KEMVILFATT IYRIGLKVPP DETDPRVPML
     TWSTCAFTIQ AIENLLGDEG KPLFGALQNR QHNGLKALMQ FAVAQRITCP QVLIQKHLLR
     LLSVVLPNLK SEDTPCLLSI DLFHVLVGAV LAFPSLYWDE TVDLQPSSVS SSYNHLYLFH
     LITMAHMLQI LLTIDTGVPL AQVQEDSEEA HSASSFFAEI SQYTSGCIGC SIPGWYLWVS
     LKNGITPYLR CAALFFHYLL GVTPPEDLHT NSAEGEYSAL CSYLSLPTNL FLLFQEYWDT
     VRPLLQRWCA DPALLNCLKQ KNTVVRYPRK RNSLIELPDD YSCLLNQASH FRCPRSADDE
     RKHPVLCLFC GAILCSQNIC CQEIVNGEEV GACIFHALHC GAGVCIFLKI RECRVVLVEG
     KARGCAYPAP YLDEYGETDP GLKRGNPLHL SHERYRKLHL VWQQHCIIEE IARSQETNQM
     LFGFNWQLL
//

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