ID A0A8C6GN34_MUSSI Unreviewed; 837 AA.
AC A0A8C6GN34;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Zinc finger protein 598 {ECO:0000313|Ensembl:ENSMSIP00000009024.1};
OS Mus spicilegus (Mound-building mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10103 {ECO:0000313|Ensembl:ENSMSIP00000009024.1, ECO:0000313|Proteomes:UP000694415};
RN [1] {ECO:0000313|Ensembl:ENSMSIP00000009024.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMSIP00000009024.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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DR AlphaFoldDB; A0A8C6GN34; -.
DR Ensembl; ENSMSIT00000011510.1; ENSMSIP00000009024.1; ENSMSIG00000008003.1.
DR GeneTree; ENSGT00390000014178; -.
DR Proteomes; UP000694415; Unplaced.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR InterPro; IPR057634; PAH_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 SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000694415}.
FT DOMAIN 115..136
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 220..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..429
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..466
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 91687 MW; D3119C10BB082BA7 CRC64;
VVFGKKLPAF ALIPIHQLQH EKKYDIYFAD GKVFALYRQL LQHECPRCPH LPPFSLFGDL
EQHMRKQHEL FCCKLCLKHL KIFTYERKWY SRKDLARHRM QGDPDDTSHR GHPLCKFCDE
RYLDNDELLK HLRRDHYFCH FCDSDGAQDY YSDYAYLREH FREKHFLCEE GRCSTEQFTH
AFRTEIDLKA HKTACHSRSR AEARQNRQID LQFSFAPRHS RRSEGVVSGE DYEEVDRYNR
QGRAGRASGR GAQQNRRGSW RYKREEEDRE VAAAIRASVA AQQQEETQRV EDREEGSRPK
KEEAAARVPE EPRGHRRLPR AQGEGSGSKE ASANGPVSQE AFPATGPGPV VALSNTLPPP
SPELKEEDFP SLCASTSSCC TAVTPGSVGL ALAYPGPPRG KNTFQEEDFP ALVSSAPKPS
SAPSSLISAW NSGCSKKGNL PTPGSQAVVG GSQPPRKAGK GSRGGRKGGP APVDEEDSGG
LTVQGLRSVP TTIAVSSLLA PATNQSSAKV GKKKKVGSEK PGATSSPLLP PDHTPKPSGA
EQVLEAPLSK AEVPVTIVVN GHSEGSALVR SAPKEPPGLP RPLGPLPCPV PQEDFPALGG
PCPPRMPPPP GFSTVVLLKG TPPPPPPPPG LVPPISKPPP GFSSLLPSSH SACAPSPATT
TTTTTTTTKT PRLAPTPQAY LVPENFRERN LQLIQSIKDF LQSDEACFSK FKSHSGEFRQ
GMISAAQYYK SCRDLLGESF QKIFSELLAL LPDTAKQQEL LSAHTDFCSR EKPPNSRSKK
NKKNVWQTST QQLGLDCCVC PTCQQVLAHG DVSSHQALHA ARDDDFPSLQ AIARIIT
//
