ID I3MK61_ICTTR Unreviewed; 873 AA.
AC I3MK61;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 28-JAN-2026, entry version 66.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=ZNF598 {ECO:0000313|Ensembl:ENSSTOP00000011646.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000011646.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000011646.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSSTOP00000011646.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AGTP01095360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MK61; -.
DR FunCoup; I3MK61; 1267.
DR STRING; 43179.ENSSTOP00000011646; -.
DR Ensembl; ENSSTOT00000012996.3; ENSSTOP00000011646.3; ENSSTOG00000012994.3.
DR eggNOG; KOG2231; Eukaryota.
DR GeneTree; ENSGT00390000014178; -.
DR HOGENOM; CLU_015828_0_0_1; -.
DR InParanoid; I3MK61; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR056437; Znf-C2H2_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23230; zf-C2H2_13; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 160..181
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 265..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..302
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..467
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..498
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..508
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..708
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 95851 MW; 4FB059FB3739352E CRC64;
VLCCGDLEAT ALGRCDHPVC YRCSTKMRVL CEQRYCAVCR EELRQVVFGK KLPAFATIPI
HQLQHEKKYD IYFADGKVFA LYRQLLQHEC PQCPQLPPFG LFGDLEQHMR KQHELFCCKL
CLKHLKIFTY ERKWYSRKDL ARHRMQGDPD DTSHRGHPLC KFCDERYLDN DELLKHLRRD
HYFCHFCDSD GAQDYYSDYA YLREHFREKH FLCEEGRCST EQFTHAFRTE IDLKAHRTAC
HSRSRAEARQ NRQIDLQFSF APRHSRRSEG VVSGEDYEEV DRYNRQGRAG RASGRGAQQN
RRGSWRYKRE EEDREVAAAI RASVAAQQEE IRRSEDREEV GRPKKEEAVA RGPEEPRGPR
RLTRAQGEGP GPKEASTNGP ASQEDCPGPG PGPTPPSTLL LSTPKLKDED FPSLCASTSS
CCTAAVPGPM GLALVYPGPA RGRNTFQEED FPALVSSASK PSTAPPSLIS AWNSSCSKKG
APPTPGAQAA GGSSQTSRKA GKGSRGGRKG GLPPTEEEGS GLGAQELRSM PTGAAASLLG
PASTQTSTKV GKKKKVGSEK LGATPSPPLP SDRTPKPPGA EQAPEAPVSR AEGPVGVIVN
GHTEGPALAR STPKEPPGLP RPLGPLPCPT PQEDFPALGG PCPPRMPPPP GFNTVVLLKG
TPPPPPPGLA PPVSKPPPGF SSLLPSPHPA SVPSPTTTTT TTTTKAPRLT PTPRAYLVPE
NFRERNLQLI QSIKNFVQSD EARFSKFKSH SGEFRQGMIS AAQYYKSCRD LLGENFQKIF
SELLVLLPDT AKQQELLSAH TDFRSREKPP GTKSKRNKKS AWQASTQQVG LDCCVCPTCQ
QVLAHGDVSS HQALHAARDD DFPSLQAIAR IIT
//
