ID A0A2K5NIN4_CERAT Unreviewed; 1085 AA.
AC A0A2K5NIN4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TOPORS {ECO:0000313|Ensembl:ENSCATP00000037297.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000037297.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000037297.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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};
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DR AlphaFoldDB; A0A2K5NIN4; -.
DR STRING; 9531.ENSCATP00000037297; -.
DR Ensembl; ENSCATT00000061594.1; ENSCATP00000037297.1; ENSCATG00000041380.1.
DR GeneTree; ENSGT00530000064170; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000041380; Expressed in heart and 12 other cell types or tissues.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0000930; C:gamma-tubulin complex; IEA:Ensembl.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:InterPro.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0003823; F:antigen binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0044547; F:DNA topoisomerase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IEA:Ensembl.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR CDD; cd16574; RING-HC_Topors; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019174; NADH_DH_b-subcmplx_su6.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR PANTHER; PTHR46077:SF2; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR Pfam; PF09782; NDUF_B6; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 143..182
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 493..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..685
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..939
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 125260 MW; 5FA83B2BAEB2A44F CRC64;
MTGYTPDEKL RLQQLRELRR RWLKDQELSP REPVLPPQKM WPMEKFWNKF LENKSPWRRT
VHGVYQKGIF IFTHILVPAW IIHYYLKYHV SEKPYGIVET KAGIFPIMAS AAKEFKMDNF
SPKAGTSKLQ QTVPADASPD SKCPICLDRF DNVSYLDRCL HKFCFRCVQE WSKNKAECPL
CKQPFDSIFH SVRAEDDFKE YVLRPSYNGS FVTPDRRFRY RTTLTRERNA SVYSPSGPVN
RRTTTPPDSG VLFEGLGIST RPRDAEIPQF MRQIAVRRPT TADERSLRKI QEQDIINFRR
TLYRAGARVR NIEDGGRYRD ISAEFFRRNP ACLHRLVPWL KRELTVLFGA HGSLVNIVQH
IIMSNVTRYD LESQAFVSDL RPFLLNRTEH FIHEFISFAR SPFNMAAFDQ HANYDCPAPS
YEEGSHSDSS VITISPDEAE TQELDINVAT VSQAPWDDET PGPSYSSSEQ VHVTMSSLLN
TSDSSDEELV TGGATSQIQG VQTNEDLNND SDDSSDNCVI VGFVKPLAER TPELVELSSD
SEDLGSYEKM ETVKTQEQEQ SYSSGDSDVS RYSSPHSVLG KDEEINKGHC DSSTRIKSKK
EEKRSTSLSS PRNLSSSVRG DRVYSPYNHR HRKRGRSRSS DSRSQSRSGH DQKNHRKHHG
KKRMKSKRSR SRESSRPRGR RDKKRSRTRD SSWSRRSQTL SLSSESTSRS RSRSSDHGKR
RSRSRNRDRY YLRNNYGSRY KWEYTYYSRN KDRDGYESSY RRRTLSRAHY SRQSSSPEFR
VQSFSERTNA RKKNNHSERK YYYYERHRSR SLSSNRSRTA STGTDRVRNE KPGGKRKYKT
RHLEGTNEVA QPSREFASKA KDSHYQKSSS KLDGNYKNES DTFSDSRSSD RETKHKRRKR
KTRSLSVEIV YEGKATDTTK HHKKKKKKHK KKHKKHHGDN ASRSPVVITI DSDSDKDSEI
KEDTECDNSG PQDPLQNEFL APSLEPFETK DVVTIEDEFG VLDKECDIAT LSNNLNNANK
TVDNIPFPAA SVEQTLDVRE ESTFVSDLEN QPSNIVSIQT EPSRQLPSPR TSLMSVCLGR
DCDMS
//