ID A0A2K5M3M6_CERAT Unreviewed; 1774 AA.
AC A0A2K5M3M6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=RB binding protein 6, ubiquitin ligase {ECO:0000313|Ensembl:ENSCATP00000019801.1};
GN Name=RBBP6 {ECO:0000313|Ensembl:ENSCATP00000019801.1};
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:ENSCATP00000019801.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000019801.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSCATT00000043985.1; ENSCATP00000019801.1; ENSCATG00000033601.1.
DR GeneTree; ENSGT00940000157561; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000033601; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd16620; vRING-HC-C4C4_RBBP6; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014891; DWNN_domain.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15439:SF29; CELL DIVISION CYCLE AND APOPTOSIS REGULATOR PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR15439; RETINOBLASTOMA-BINDING PROTEIN 6; 1.
DR Pfam; PF08783; DWNN; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF13696; zf-CCHC_2; 1.
DR SMART; SM01180; DWNN; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51282; DWNN; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT DOMAIN 4..76
FT /note="DWNN"
FT /evidence="ECO:0000259|PROSITE:PS51282"
FT DOMAIN 155..169
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 253..294
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 320..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..748
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1732
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1774 AA; 199879 MW; 6F2D749740DD5682 CRC64;
MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADCDLQITN AQTKEEYTDD
NALIPKNSSV IVRRIPIGGV KSTSKTYVIY CSLQDEWCCL WLCGLKCVSN TANLAEANAS
EEDKIKAMMS QSGHEYDPIN YMKKPLGPPP PSYTCFRCGK PGHYIKNCPT NGDKNFESGP
RIKKSTGIPR SFMMEVKDPN MKGAMLTNTG KYAIPTIDAE AYAIGKKEKP PFLPEEPSSS
SEEDDPIPDE LLCLICKDIM TDAVVIPCCG NSYCDECIRT ALLESDEHTC PTCHQNDVSP
DALIANKFLR QAVNNFKNET GYTKRLRKQL PPPPPPIPPP RPLIQRNLQP LMRSPISRQQ
DPLMMPVTSS STHPTPSISS LTSNQSSLAP PVSGNPSSAP APVPDITATV SISVHSEKSD
GPFRDSDNKI LPAAALASEH SKGTSSIAIT ALMEEKGYQV PVLGTPSLLG QSLLHGQLIP
TTGPVRINTA RPGGGRPGWE HLLVSDDFSL KKSINRGRHH SERSQRTQGP SLPATPVFVP
VPPPPLYPPP PHTLPLPTGV PPPQFSPQFP PGQPPPAGYS VPPPGFPPAP TNLSTPWVSS
GVQTAHSNTI PTTQAPPLSR EEFYREQRRL KEEEKKKSKL DEFTNDFAKE LMEYKKIQKE
RRRSFSRSKS PYSGSSYSRS SYTYSKSRSG STRSRSYSRS FSRSHSRSYS RSPPYPRRGR
GKSRNYRSRS RSHGYHRSRS RSPPYRRYHS RSRSPQAFRG QSPNKRNVPQ GETEREYFNR
YREVPPPYDM KAYYGRSVDF RDPFEKERYR EWERKYREWY EKYYKGFAAG AQPRPSANRE
NFSPERFLPL NIRNSPFTRG RREDYVGGQS HRSRNIGSNY PEKLSARDGH NQKDNTKSKE
KESENAPGDG KGNKHKKHRK RRKGEESEGF LNPELLETSR KSREPTGVEE NKTDSLFVLP
SRDDATPVRD EPMDAESITF KSVSEKDKRE RDKPKTKGDK TKRKNDGSAV SKKENIVKPA
KGPQEKVDGE REKSPRSEPP LKKAKEETPK TDNAKSSSSS QKDEKITGTP RKAHSKSAKE
HQETKPVKEE KVKKDYSKDV KSEKLTTKEE KAKKPNEKNK PLDNKGEKRK RKTEEKGVDK
DFESSSMKIS KLEVTEIVKP SPKRKMEPDI EKMDRTPEKD KISSTAPAKK IKLNRETGKK
IGSTENISNT KEPCEKLEST SSKVKQEKVK AKVRRKVTGT EGSSSTLVDY TSTSSTGGSP
VRKSEEKTDT KRTVIKTMEE YNNDNTAPAE DVIIMIQVPQ SKWDKDDFES EEEDVKSTQP
ISSVGKPASV IKNVSTKPSN IVKYPEKESE PSEKIQKFTK DVSLEIIQHE VKSSKNSASS
EKGKTKDRDY SVLEKENAEK RKNNTQPEKE SNLDRLNEQG NFKSLSQSSK EARTSDKHDS
TRASSNKDFT PNRDKKTDYD TREYSSSKRR DEKNELTRRK DSPSRNKDSA SGQKNKPREE
RDLPKKGTGD SKKSNSSPSR DRKPHDHKAT YDTKRPNEET KSVDKNPCKD REKHVLEARN
NKESSGNKLL YILNPPETQV EKEQITGQID KNTAKPKPQL SHSSRLSSDL TRETDEAAFE
PDYNESDSES NVSVKEEETS GNISKDLKDK IVEKAKENLD TAAVVQVGIS RNQSHSSPSV
SPSRSHSPSG SQTRSHSSSA SSAESQDSKK KKKKKEKKKH KKHKKHKKHK KHAGTEVELE
KSQKHKHKKK KSKKNKDKEK EKEKDDQKVK SVTV
//
