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Database: UniProt
Entry: G3HYT4_CRIGR
LinkDB: G3HYT4_CRIGR
Original site: G3HYT4_CRIGR 
ID   G3HYT4_CRIGR            Unreviewed;      1563 AA.
AC   G3HYT4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=I79_016226 {ECO:0000313|EMBL:EGW09324.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW09324.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR   EMBL; JH000944; EGW09324.1; -; Genomic_DNA.
DR   STRING; 10029.G3HYT4; -.
DR   PaxDb; 10029-XP_007647139-1; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   InParanoid; G3HYT4; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd20347; BRcat_RBR_CUL9; 1.
DR   CDD; cd20359; Rcat_RBR_CUL9; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR004939; APC_su10/DOC_dom.
DR   InterPro; IPR048962; ARIH1-like_UBL.
DR   InterPro; IPR047561; BRcat_RBR_CUL9.
DR   InterPro; IPR045093; Cullin.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047560; Rcat_RBR_CUL9.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22771:SF2; CULLIN-9; 1.
DR   Pfam; PF03256; ANAPC10; 1.
DR   Pfam; PF21235; ARI1_UBAl; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM01337; APC10; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS50069; CULLIN_2; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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          234..413
FT                   /note="DOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51284"
FT   DOMAIN          635..903
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   DOMAIN          1114..1331
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          1284..1327
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          18..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1490..1563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1490..1506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1508..1525
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1563 AA;  176598 MW;  CF2F5D7B6EB6C50A CRC64;
     MPTTRTILMM LLNRYSEPRG SPERAALESP STQGQDGSPE LLIRSLVGDP SAELFLDLER
     VLCCEGSPQG AVRPLLKRLQ QETQPFLLLL RTLDAPGPNR SLLLTVLRVT MRLLDYPEAM
     VLPWHEVLEP CLNCLSGPSS DSEIIQELVC FLHRLALTHK DYAVVLCCLG AREVLSKVLD
     KHSAQLLLAS ELRDLVTECE KHAQLYSKLT SSILAGCIQM VLGQIEDHRR THQPINIPFF
     DVFLRHLCQG SSVEVKEDKC WEKVEVSSNP HRASKLTDRN PKTFWESNGS TGSHSITLYM
     HRGVLIRQLT LLVASEDSSY MPARVVVFGG DSVSCINTEL NTVNVMPSAS RVVLLENLNR
     FWPIIQIRIK RCQQGGIDTR VRGVEVLGPK PTFWPLFREQ LCRRTCLFYT IRAQAWSQDI
     AEDRQRLLQL CPRLNRVLRH EQNFADRFLP DDEAAQALGK TCWEALVSPL VQNITSPDAE
     SVSSLGWLLD QYLERRESVQ SSQSQAPSFA SRVRRLCHLL VHVEPPPGSS PESSTQLFGK
     NSKSQNGSPV LSPVLPSSSL RNITQCWLSV VQEQVSRFLA AAWRASDFVP RYCSLYERLQ
     RAGLELFGPR AAFTVALRSG FSGALLQQSF LTATHMSEQF ARHIDQQIQG GLLGGASGVA
     MLGHLQQYLE PITVLSGLEL ATTFEHFYQH YMADRLLSLG SSWLEGAVLE QIGLCFPNRL
     PQLMLQSLHT SEELQRQFHV YQLRQLDRQL LEQEDQEEWR LEEVEEEDKG QETEKEILKE
     DPGPEVSVLV LSPRCWPVSP LCYLHNPRQH LPTEFCDALD RFSSFYSHSQ NYPVLNMGPH
     RRLQWTWLGW AELQFGDQTL HVSTVQMWLL LTFNQTEEVS VESLLKTSGL SPELLHQALL
     PLIEDSGPLT LEEAQNLPQA GMLRLREPRS QPLEEVLWLI PPQTYFSVEK DEGRTLEQKR
     NLLSCLLVRI LKAHGEKGLH IDQLVCLVLE AWKKGPNPPG SLGRTVSGGV ACSSTDVLSC
     ILHLLGQGYV ERRDDRPQLP AGRTMSPQEV EGLMEQTVQQ VQETLNLEPD VARHLLAHSH
     WGTEQLLQSY SDDPEPLLLA AGLRVPQAQV VPTRPDHCPV CVSPLGPNDD APSLCCLHCC
     CKSCWNEYLT TRIEQNFVLN CTCPIADCPA QPTGAFIRDI VSSPEVISKY EKALLRAYVE
     SCSNLTWCTN PQGCDRILCR QGLGSGTTCS KCGWASCFNC SFPEAHYPAS CGHMSQWVDD
     GGYYEGMSVE AQSKHLAKLI SKRCPSCQAP IEKNEGCLHM TCARCNHGFC WRCLKSWKPS
     HKDYYNCSAM VSKAARQEKR FQDYNERCTF HHQAREFAVN LRNQASAIHE VPPPKSFTFL
     HDACRALEQA RKVLAYACVY SFYSQDTEYM DVVEQQTENL ELHTNALQIL LEESLLRCQD
     LASSLRFLRA DCLSTGTELL RRIQERLLAI LQHSTQDFRV GLQSPSVEVR EVKGSNVPSN
     QPQGSLGLEA EEEEEEEEDV PEWHHDFDEE LDNDSFSYDE ESENLDRETF FFGDEDDDDE
     SYD
//
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