ID A0A8C1YD18_CYPCA Unreviewed; 947 AA.
AC A0A8C1YD18;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|Ensembl:ENSCCRP00010119110.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010119110.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010119110.1}
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}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR AlphaFoldDB; A0A8C1YD18; -.
DR Ensembl; ENSCCRT00010132304.1; ENSCCRP00010119110.1; ENSCCRG00010052122.1.
DR Proteomes; UP000694427; Unplaced.
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; 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:UP000694427};
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 60..100
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..763
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 106417 MW; B975E5E32B1AC722 CRC64;
MHCAERLRTQ ERASPGLTAR TVVYNPSKSQ RITARKPPHT QPVPSSSMGS SAKRDAESSC
VLCCQDIDLF AVGKCDHPVC YRCSTKMRVL CEQKYCAVCR EQLDKVVFIK KLEPFAALNI
HQFQCEKKYD VYFADGNIYA QFRKILLNEC PQCPEPKVFS RFEELEQHMR KQHELFCCKL
CAKHLKIFSY ERKWYSRKDL ARHRTQGDPD DTSHRGHPLC KFCDDRYLDN DELLKHLRRD
HYFCHFCDAD GAQEYYSDYQ YLSEHFRESH YLCQEGRCST EQFTHAFRTE IDYKAHKAAA
HSKNRAEARQ NRQIDIQFNY APRQQRRNDG QIVGGDDYEE ADRFSRQGRP GRGRAPGGQQ
NVRSWRYIRE EEDREIAAAL RASIVSHQEE RSHVQERSSQ KPRKEEKMEP DDTRNNRSTA
KQTNEIQARS VKSNASLAGQ DFPVLGAAAP PAPVQSKIKQ TSVSLKEDDF PSLSGSVVSS
PMTPAYTNQP RKHSSFQEED FPALVSKIKP LKPQSNTTSA WSQAGSKPAV VSNKPVVLPT
KTVSSSILSA SDPLPSGSVP QPLTASSSRR KKKLTSAETH RAPPKVRCPS SSDDEDPQTG
KTAQEIRTVP TMLDISTLLT VKDGSSQPNP KTNKKKKQAT ASSLGSPSHT LEFVSKMAHK
ENVPETKPPD NSLPSKTNSF INGLPEKPAE ALSPTSFPEN IPSPLKQPVA DQPPPPKEEE
FPALISRKPP PGFKSAFPLK STPSVGPPPP PGLGPAVSKP PPGFTGIPLN SNVEESDVNR
VTPAFGSYLI PDNFQQRNMD LIQSIKNYLQ NDETKFNEFK NYSGQFRQGI IPAVQYYKSC
QELLGENFNR VFNELLVLLP DTCKQQELLT AHADFKALEK QQQGSKPKKN KKKAWQTGTS
SNSLELDCQV CPTCKQVLAL KDFNTHKTLH IGDDDFPSLQ AISKIIS
//
