ID M3YUL7_MUSPF Unreviewed; 2544 AA.
AC M3YUL7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Ubiquitin protein ligase E3 component n-recognin 5 {ECO:0000313|Ensembl:ENSMPUP00000015027.1};
GN Name=UBR5 {ECO:0000313|Ensembl:ENSMPUP00000015027.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015027.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000015027.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; AEYP01071266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9669.ENSMPUP00000015027; -.
DR Ensembl; ENSMPUT00000015264.1; ENSMPUP00000015027.1; ENSMPUG00000015136.1.
DR eggNOG; KOG0943; Eukaryota.
DR GeneTree; ENSGT00940000156357; -.
DR HOGENOM; CLU_000257_0_0_1; -.
DR InParanoid; M3YUL7; -.
DR OMA; EKCKCRA; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; IEA:Ensembl.
DR GO; GO:0033696; P:heterochromatin boundary formation; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR CDD; cd19675; UBR-box_UBR5; 1.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 2.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR047503; UBR-box_UBR5.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR46276; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR PANTHER; PTHR46276:SF1; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00658; PABP; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 923..991
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT DOMAIN 2123..2200
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT DOMAIN 2249..2544
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ZN_FING 923..991
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 74..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1863..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2069..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2219..2246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..777
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1323
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1742..1760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2075..2116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2219..2236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2513
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2544 AA; 281907 MW; A0715BFB8D9769B7 CRC64;
MSLLDADIHS AHPSVIIDAD AMFSEDISYF GYPSFRRSSL SRLGSSRERD SELLRERESV
LRLRERRWLD GASFDNERGS TSKEGEPNLD KKNTPVQSPV SLGEDLQWWP DKDGTKFICI
GALYSELLAV SGKGELYQWK WSESEPYRNA QNPSLHHPRA TFLGLTNEKI VLLSANSIRA
TVATENNKVA TWVDETLSSV ASKLEHTAQT YSELQGERIV SLHCCALYTC AQLENNLYWW
GVVPFSQRKK MLEKARAKNK KPKSSAGISS MPNITVGTQV CLRNNPLYHA GAVAFSISAG
IPKVGVLMES VWNMNDSCRF QLRSPESLKS MDKASKTTEA KPESKQEPVK TEMGPPPSPA
STCSDASSIA SSASMPYKRR RSTPAPKEEE KVNEEQWSLR EVVFVEDVKN VPVGKVLKVD
GAYVAVKFPG TSSNTNCQSS SGSDADPSSL LQDCRLLRID ELQVVKTGGT PKVPDCFQRT
PKKLCIPEKT EILAVNVDSK GVHAVLKTGN WVRYCIFDLA TGKAEQENNF PTSSIAFLGQ
NERNVAIFTA GQESPIILRD GNGTIYPMAK DCMGGIRDPD WLDLPPISSL GMGVHSLINL
PANSTIKKKA AIIIMAVEKQ TLMQHILRCD YEACRQYLMN LEQAVVLEQN LQMLQTFIGH
RCDGNRNILH ACVSVCFPTS NKETKEEEEA ERSERNTFAE RLSAVEAIAN AISVVSSNGP
GNRAGSSSSR SLRLREMMRR SLRAAGLGRH EAGASSSDHQ DPVSPPIAPP SWVPDPPAMD
PDGDIDFILA PAVGSLTTAA SGTGQGPSTS TIPGPSTEPS VVESKDRKAN AHFILKLLCD
SVVLQPYLRE LLSAKDARGM TPFMSAVSGR AYPAAITILE TAQKIAKAEV SSSEKEEDVF
MGMVCPSGTN PDDSPLYVLC CNDTCSFTWT GAEHINQDIF ECRTCGLLES LCCCTECARV
CHKGHDCKLK RTSPTAYCDC WEKCKCKTLI AGQKSARLDL LYRLLTATNL VTLPNSRGEH
LLLFLVQTVA RQTVEHCQYR PPRIREDRNR KTANPEDSDM PDHDLEPPRF AQLALERVLQ
DWNALKSMIM FGSQENKDPL SASSRIGHLL PEEQVYLNQQ SGTIRLDCFT HCLIVKCTAD
ILLLDTLLGT LVKELQNKYT PGRREEAIAV TMRFLRSVAR VFVILSVEMA SSKKKNNFIP
QPIGKCKRVF QALLPYAVEE LCNVAESLIV PVRMGIARPT APFTLASTSI DAMQGSEELF
SVEPLPPRPS SDQSSSSSQS QSSYIIRNPQ QRRISQSQPV RGRDEEQDDI VSADVEEVEV
VEGVAGEEDH HDEQEEHGEE NAEAEGQHDE HDEDGSDMEL DLLAAAETES DSESNHSNQD
NASGRRSVVT AATAGSEAGA SSVPAFFSED DSQSNDSSDS DSSSSQSDDI EQETFMLDEP
LERTTNSSHA NGAAQAPRSM QWAVRNTQHQ RAASTAPSST STPAASSAGL IYIDPSNLRR
SGTISTSAAA AAAALEASNA SSYLTSASSL ARAYSIVIRQ ISDLMGLIPK YNHLVYSQIP
AAVKLTYQDA VNLQNYVEEK LIPTWNWMVS IMDSTEAQLR YGSALASAGD PGHPNHPLHA
SQNSARRERM TAREEASLRT LEGRRRATLL SARQGMMSAR GDFLNYALSL MRSHNDEHSD
VLPVLDVCSL KHVAYVFQAL IYWIKAMNQQ TTLDTPQLER KRTRELLELG IDNEDSEHEN
DDDTNQSATL NDKDDDSLPA ETGQNHPFFR RSDSMTFLGC IPPNPFEVPL AEAIPLADQP
HLLQPNARKE DLFGRPSQGL YSSSASSGKC LMEVTVDRNC LEVLPTKMSY AANLKNVMNM
QNRQKKEGEE QNVVPEEAES SKPGPSAHDL AAQLKSSLLA EIGLTESEGP PLTSFRPQCS
FMGMVISHDM LLGRWRLSLE LFGRVFMEDV GAEPGSILTE LGGFEVKESK FRREMEKLRN
QQSRDLSLEV DRDRDLLIQQ TMRQLNNHFG RRCATTPMAV HRVKVTFKDE PGEGSGVARS
FYTAIAQAFL SNEKLPNLDC IQNANKGTHT SLMQRLRNRG ERDRERERER EMRRSSGLRA
GSRRDRDRDF RRQLSIDTRP FRPASEGNPS DDPDPLPAHR QALGERLYPR VQAMQPAFAS
KITGMLLELS PAQLLLLLAS EDSLRARVDE AMELIIAHGR ENGADSILDL GLLDSSEKVQ
ENRKRHGSSR SVVDMDLDDT DDGDDNAPLF YQPGKRGFYT PRPGKNTEAR LNCFRNIGRI
LGLCLLQNEL CPITLNRHVI KVLLGRKVNW HDFAFFDPVM YESLRQLILA SQSSDADAVF
SAMDLAFAID LCKEEGGGQV ELIPNGVNIP VTPQNVYEYV RKYAEHRMLV VAEQPLHAMR
KGLLDVLPKN SLEDLTAEDF RLLVNGCGEV NVQMLISFTS FNDESGENAE KLLQFKRWFW
SIVEKMSMTE RQDLVYFWTS SPSLPASEEG FQPMPSITIR PPDDQHLPTA NTCISRLYVP
LYSSKQILKQ KLLLAIKTKN FGFV
//
