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Database: UniProt
Entry: A0A3Q2X4L2_HAPBU
LinkDB: A0A3Q2X4L2_HAPBU
Original site: A0A3Q2X4L2_HAPBU 
ID   A0A3Q2X4L2_HAPBU        Unreviewed;      1152 AA.
AC   A0A3Q2X4L2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Ubiquitination factor E4B {ECO:0000313|Ensembl:ENSHBUP00000033656.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000033656.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000033656.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
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DR   AlphaFoldDB; A0A3Q2X4L2; -.
DR   Ensembl; ENSHBUT00000027739.1; ENSHBUP00000033656.1; ENSHBUG00000020910.1.
DR   GeneTree; ENSGT00390000009300; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; 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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   CDD; cd16658; RING-Ubox_UBE4B; 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; 2.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT   DOMAIN          1076..1149
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..56
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1152 AA;  130551 MW;  1319A3A529C05AAB CRC64;
     MMEELSADEI RRRRLARLAG GQTSQPSTPL STPLTSPQRE TPPGPLPGPS GAAPQPVPPA
     ASQSLGLNVH SGTPATSPMG TSGVAYGSQS SEGVSSLSSS PSNSLETQSQ SLSRSQSMDI
     DPASCEKSMS QVDVDSGIEN MEVEDSDRRE KRNLTEKETS ANSDVSEEQA LQLICKILRV
     SWKEQDRDVI FLPSLAAEFH QNPKEVYSDF KDLISQILME VLMMSTQSRV HNPFASLTAT
     SQPIAAAKSP DHRLTLVQPS SQGGSPMGPS AGSFGASSLS SLGACGGGMS CESASDRFTI
     ETCKETEMLN YLIERFDSVG MEERKAPKMC SQPNVSQLLS NIRSQCISHV ALVLQGALTQ
     PRSPLQQSLL VPYMLCRNLP YGFIQELVRI THQEDEVFRQ IFIPILHGLA LAVKECSFDS
     DNFKFPLMAL AELCEIKFGK THPVCNLVTS LPLWCPKPLS PGCGREIQRL SYLGAFFGLS
     VFAEDDTKVG DKYFSGPAIT MENTRVVSQS LQHYLESARG DMFKVLHNIL LNSETRELAL
     NYMAALVNYN VKKAQMQTDD KLVSTDGFML NFLWVLQQLS MKIKLETVDP YYIFHPRCRL
     VVSLEETRLK ATMDELKAWL SELHKDPAKF TEPKFPTECF FLTLHTHHLS ILPGCRRYIR
     RLRAIRELNR TVEELKNSES QWKDSPLASR HREMLKRCKT QLKKLVRAKA CADVGLLDEN
     LLRRCLQFYS TVIQLILRMV DPTYPKYSPQ VLYEPCVQDI VTFLVVFICS QNYIRNPYLI
     AKLVEVLFVT NPAVQPRTQR FSEMMENHPL SVKHLVPALM KFYTDVEHTG ATSEFYDKFT
     IRYHISTIFK SLWQNIAHHG TFMEEFNSGK QFVRYINMLI NDTTFLLDES LESLKRIHEV
     QEEMKNKEQW EQLPREQQQS RQSQLTQDER VSRSYLALAT ETVEMFHILT KQVQKPFLRP
     ELGPRLAAML NFNLQQLCGP KCRDLKVENP EKYGFEPKKL LDQLTDIYLQ LDCARFAKAI
     ADDQRSYSRE LFEEVISKMR KAGIKSSIAI EKFKLLSEKV EEIVAKNSQS EMDYSDAPDE
     FKDPLMDTLM TDPVMLPSGN IMDRSIILRH LLNSPTDPFN RQPLTENMLE SVPELKERIH
     TWMREKQGGR GV
//
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