ID A0A452EIG7_CAPHI Unreviewed; 1797 AA.
AC A0A452EIG7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=RB binding protein 6, ubiquitin ligase {ECO:0000313|Ensembl:ENSCHIP00000011681.1};
GN Name=RBBP6 {ECO:0000313|Ensembl:ENSCHIP00000011681.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000011681.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000011681.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000011681.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWLT01000031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013830282.2; XM_013974828.2.
DR STRING; 9925.ENSCHIP00000011681; -.
DR Ensembl; ENSCHIT00000019471.1; ENSCHIP00000011681.1; ENSCHIG00000013732.1.
DR GeneID; 102172681; -.
DR KEGG; chx:102172681; -.
DR CTD; 5930; -.
DR GeneTree; ENSGT00940000157561; -.
DR OrthoDB; 150979at2759; -.
DR Proteomes; UP000291000; Chromosome 25.
DR Bgee; ENSCHIG00000013732; Expressed in thymus and 16 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR GO; GO:0061053; P:somite development; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
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:UP000291000};
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 161..175
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 259..300
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 328..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..765
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1755
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1797 AA; 201396 MW; 5F4AAA08B8B165DA CRC64;
MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADCDLQITN AQTKEEYTDD
NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPVMGTSK AIDDSSASIS LAQLTKTANL
AEANASEEDK IKAMMSQSGH EYDPINYMKK PLGPPPPSYT CFRCGKPGHY IKNCPTNGDK
NFESGPRIKK STGIPRSFMM EVKDPNMKGA MLTNTGKYAI PTIDAEAYAI GKKEKPPFLP
EEPSSSSEED DPIPDELLCL ICKDIMTDAV VIPCCGNSYC DECIRTALLE SDEHTCPTCH
QNDVSPDALI ANKFLRQAVN NFKNETGYTK RLRKQLPPPP PPIPPPRPLI QRNLQPLMRS
PISRQQDPLM IPVTSSSTHS ASSMSSLTSN QSSLAPPVPG NPSSAPAPVP DITATVSISV
HSEKSDGPFR DSDNKILPAA ALASEHSKGA SSIAITALME EKGYQVPVLG TPSLLGQSLL
HGQLIPTTGP VRINAARPGG GRPGWEHSNK LGYLVSPPQQ IRRGERSCYR SINRGRHHSE
RSQRTQGPSL PATPVFVPVP PPPLYPPPPH TLPLPGVPPP QFSPQFPPGQ PPPAGYSVPP
PGFPPAPANL SAPWVSSGVQ TAHSNTIPTT QAPPLSREEF YREQRRLKEE EKKKSKLDEF
TNDFAKELME YKKIQKERRR SFSRSKSPYS GSSYSRSSYT YSKSRSGSTR SRSYSRSFSR
SHSRSYSRSP PYPRRGRGKS RNYRSRSRSH GYHRSRSRSP PYRRYHSRSR SPQAFRGQSP
NKRNVPQGET EREYFNRFRE VPPPYDMKAY YGRSVDFRDP FEKERYREWE RKYREWYEKY
YKGYATGAQP RPSANRENFS PERFLPLNLR NSPFTRGRRE DYSGGQSHRS RNIAGNYPEK
LSSRDSHNQK DNTKSKDKEG ESAPGDGKGN KHKKHRKRRK GEESEGFLNP ELLDTSRKSR
EPTSGEESKT DSLFVLPSRD DATPVRDEPM DAESITFKSV SEKDKREKDK PKAKGDKTKR
KNDGSTVSKK ETVVKPAKGP QEKLDGEREK SPRSEPPLKK AKEETPKTDN VKSSSSSQKD
EKTVGTPRKA HSKPVKEHQE TKPVKEEKMK KDYSKDVKSE KGTSKEEKAR KPNEKSKPLD
SKGEKRKRKT EEKSVDKDFE SSSMKISKLE VTEIVKPSPK RKMELDIEKM DRTPEKDKIS
SSAAPAKKIK LNRETGKKIG STENVCNTKE PSEKLESTSG KVKQEKIKGK VRRKVTGTEG
SSSTLVDYTS TSSTGGSPVR KSEEKTDTKR TVIKTMEEYN NDNTAPAEDV IIMIQVPQSK
WDKDDFESEE EDVKSTSQPI SSVGKPASII KNVSTKPPNA IKYTEKESES SEKIQKLTKE
VSHEIAQHEV KSSKNSASSE KGKTKDRDHS VLEKENPEKR KNNSTQPEKD SNLDRLNEQG
NFKSLSQSSK ETRTSGKEDK HDSIRGSSNK DFTPNRDKKA DYDNREHSSS KRRDERNELT
RRKDSPPRSK DSASGQKAKP REERDLPKKG TGESKKSNSS PTRDKKPHDH KATYDPKRLS
EETKSLDKNP CKDREKHVLE AKNNKEPSGN KSLSILNPPD PQIEKEQVTG QIDKNTIKPK
PQVSHSSRLS SDLTRETDEA AFEPDYNESD SESNVSIKEE EAAGKVSKEL KDKVVEKAKE
SLDTAAVSQA GVTRSQSQSS PSVSPSRSHS PSGSQTRSHS SSASSAESQD SKKKKKKKEK
KKHKKHKKHK KHKKHAGTEA ELEKSQKHKH KKKKSKKSKD KEKEKEKDDQ KVKSVTV
//
