ID H2MCS1_ORYLA Unreviewed; 917 AA.
AC H2MCS1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 28-JAN-2026, entry version 73.
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:ENSORLP00000016358.2};
GN Synonyms=znf598 {ECO:0000313|Ensembl:ENSORLP00000016358.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000016358.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000016358.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016358.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000016358.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016358.2};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSORLP00000016358.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016358.2};
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}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR RefSeq; XP_011476737.1; XM_011478435.3.
DR AlphaFoldDB; H2MCS1; -.
DR Ensembl; ENSORLT00000016359.2; ENSORLP00000016358.2; ENSORLG00000013053.2.
DR GeneID; 101162451; -.
DR CTD; 90850; -.
DR eggNOG; KOG2231; Eukaryota.
DR GeneTree; ENSGT00390000014178; -.
DR HOGENOM; CLU_015828_0_0_1; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000001038; Chromosome 8.
DR Bgee; ENSORLG00000013053; Expressed in animal zygote and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR InterPro; IPR001841; Znf_RING.
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; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
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:UP000001038};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 11..51
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 291..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..490
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..508
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 102631 MW; BF62EACD54F11F6F CRC64;
MDPAKDPEKT CVLCCQDVEI FALGKCDHPV CYRCSTKMRV LCEQKYCAVC REELDKVVFV
KKLEAFQSLS YQNFPCEKTY DIYFGDEMIY SQYRRLLFSE CPRCPEPKIF CTFEELEKHM
RKQHELFCCK LCTKHLKIFS HERKWYNRKE LARHRAHGDT DDTSHRGHPL CKFCDDRYLD
NDELLKHLRR DHYFCHFCDA DGSQEYYSDY QYLSEHFRES HYLCEEGRCA TEQFTHAFRS
EIDYKAHKAA AHSKNRAEAR QNRQIELQFN YATRQQRRNE GMLTGEDYEE MRQNRGGRGR
PPGGQKSWRY SREREEEDRQ VEAALRASMA MRRQAERAAV QERSTPKHCR EDRVDRTEPE
EPKANTGHKT VNRPPVKTLK SSNPGDDEFP VLGATALIPS VKPASVGGAA TLKEEEYPSL
SAAAVSAPMT PAYSAQPRKT SSFQEEDFPA LVPKVRPRKP AASTSSAWSN HTAVAAPITH
PPPFSRPTPP VSLSTSGPEL LSSSNSVSSR KKKKVGENIK AASRHSPSLS DDESSGMTQR
EFRSVPTMLD ISSLLTVKTD NSKSSTVHAP PSNSTASADS PAPKNSKKKK QKNAGAASTS
AFTAPGMTAD VNPISVETAA QKENLPEKTR NKPNSSVTAP AEMSRLANGY PDPPQSVGKE
NPLLIPVSST EPPPDQEEEF PALATKKPPP GFRASFPLTA SVPPSALPMP PPPPGLGIAA
PKPPPGFTGI PLNSNVVEVA PSAVNSAPKA LSSGYLVPDD FQQRNLELIQ SIKKYLNNDE
SKFNQFKNYS AQFRQSVISA AQYHCCCEDL LGDNFNRIFN ELLVLLPDTT KQQELLTAHA
DCKAVERQAG RGRKNRNRNN AWHTPHSAAN TAAELDCQVC PTCRQVLAPK DFNSHKTLHI
TENEEFPSLQ SISRIIR
//
