ID A0A8C1P055_CYPCA Unreviewed; 1274 AA.
AC A0A8C1P055;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Ubiquitin conjugation factor E4 B {ECO:0000256|ARBA:ARBA00072779};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING-type E3 ubiquitin transferase E4 B {ECO:0000256|ARBA:ARBA00083610};
DE AltName: Full=Ubiquitin fusion degradation protein 2 {ECO:0000256|ARBA:ARBA00081821};
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:ENSCCRP00010099116.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010099116.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010099116.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC ligase in conjunction with specific E1 and E2 ligases. May also
CC function as an E4 ligase mediating the assembly of polyubiquitin chains
CC on substrates ubiquitinated by another E3 ubiquitin ligase. May
CC regulate myosin assembly in striated muscles together with STUB1 and
CC VCP/p97 by targeting myosin chaperone UNC45B for proteasomal
CC degradation. {ECO:0000256|ARBA:ARBA00056267}.
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 Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000256|ARBA:ARBA00007434}.
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DR AlphaFoldDB; A0A8C1P055; -.
DR Ensembl; ENSCCRT00010109934.1; ENSCCRP00010099116.1; ENSCCRG00010043071.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000694427; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR GO; GO:0036503; P:ERAD pathway; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:TreeGrafter.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16658; RING-Ubox_UBE4B; 1.
DR FunFam; 3.30.40.10:FF:000060; ubiquitin conjugation factor E4 B; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR045132; UBE4.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13931:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 1.
DR PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694427};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 1198..1272
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..68
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..290
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..314
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..330
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1048
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 143094 MW; 01DB6A6C0BFA819D CRC64;
STPLRPSGAS SQPVPPAPSH TLGLNAQNVT PATSPVGASG VAYRSQSSEG VSSLSSSPSN
SLETQSQSLS RSQSMDIDTA SCEKSMSQVD VDSGIENMEV EESDRREKRN LAEKDSSSSS
DVSEEQALHL ICKILRVSWK EQDRDVIFLP SLAAEFQKNP GDVYSDFRDL IGQILMEALM
MSTRSRDCNP FASLTATSQP ITAARSPDCH LTLVPPSSQS GSPMMPCAGS FGASSLSSLY
GCSPNPLALS SARMSAPSVP LAPAAALPGP PSPPVSRPPA SLPPPSPSTP LPISQRYRPY
SLSSSIPISP SHRSTQSGML TPPTTSGIPS SPSPRHRSTN SSVPFPILPG SPSTMARRTA
LAARMPSRYL SHPVRCEVAS FLGASGGGMA GDSGNDRFTI ESCKETEMLN YLIERFDSVG
MEERKALKVA ADNHYRHVST VLILNTGNII MAPLQPSLLV PYMLCRNLPY GFIQELVRMT
HQEEDVFKQI FVPILQGLTL AVKECSFDSD NFKFPLMALV ELCEIKFGKT HPVCNLITSL
PLWCPDPLSP GTGREIQRLS FLGAFFSLSV FAEDDTKVGD KFFSGPAITV ENTRVVSQSL
QHYLESARGD LFKILHNILL NGETREAALS YMAALVNRNV KKAQMQTDDK LVSTDGFMMN
FLWVLQQLSM KIKLDTVDAL YIFHPKCRLN VSTEETRLNA TMEDLKSWLS ELHEDPSKFS
EPKFPTECFF LTLHAHHLSI LPCCRRYIRR LRAIRDLNRT VEELKNSENQ WKDSPLASRH
REMLKRCKTQ LKKLVRSKAC ADAGLLDENL LRRCLQFFSM VIQLILRMVE PAYPGVTLPL
NPEIPKCFAA LPEFYIEDVA EFLLFIVQYF PQVLYETCTE DIVTFLVVFI SSQNYIKNPY
LIAKLVEVLF VTNPAVQPRT QRFFEMMENH PLSINQLVPA LMKFYTDVEH TGATSEFYDK
FTIRYHISTI FKSLWQNINH QGTFLEEFNS GKQFVRYINM LINDTTFLLD ESLESLKRIH
EVQEEMKNKE QWDQLPRDQQ QSRQSQLTQD ERVSRSYLAL ATETVDMFHI LTKQVQKPFL
RPELGPRLAA MLNYNLQQLC GPKCRDLKVE NPEKYGFEPK KLLDQLTDIY LQLDCARFAK
AIADDQRSYS RELFEEVISK MRKAGIKSTI AIEKFKLLLE KVEEIVARNS QSEMDYNDAP
DEFKDPLMDT LMTDPVQLPS GNIMDRAIIL RHLLNSPTDP FNRQPLTESM LEPGTHQNSE
RIQAWMRGKQ SGRV
//
