ID A0A6P5BQL6_BOSIN Unreviewed; 492 AA.
AC A0A6P5BQL6;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=E3 ubiquitin-protein ligase Hakai {ECO:0000256|ARBA:ARBA00041081};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Casitas B-lineage lymphoma-transforming sequence-like protein 1 {ECO:0000256|ARBA:ARBA00076432};
DE AltName: Full=RING-type E3 ubiquitin transferase Hakai {ECO:0000256|ARBA:ARBA00079012};
GN Name=CBLL1 {ECO:0000313|RefSeq:XP_019814245.1};
OS Bos indicus (Zebu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9915 {ECO:0000313|Proteomes:UP001652663, ECO:0000313|RefSeq:XP_019814245.1};
RN [1] {ECO:0000313|RefSeq:XP_019814245.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_019814245.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC several tyrosine-phosphorylated Src substrates, including CDH1, CTTN
CC and DOK1. Targets CDH1 for endocytosis and degradation. Associated
CC component of the WMM complex, a complex that mediates N6-
CC methyladenosine (m6A) methylation of RNAs, a modification that plays a
CC role in the efficiency of mRNA splicing and RNA processing. Its
CC function in the WMM complex is unknown.
CC {ECO:0000256|ARBA:ARBA00057512}.
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 -!- SUBUNIT: Homodimer. Interacts with tyrosine-phosphorylated SRC
CC substrates. Component of the WMM complex, a N6-methyltransferase
CC complex composed of a catalytic subcomplex, named MAC, and of an
CC associated subcomplex, named MACOM. The MAC subcomplex is composed of
CC METTL3 and METTL14. The MACOM subcomplex is composed of WTAP, ZC3H13,
CC CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B). Also
CC a component of a MACOM-like complex, named WTAP complex, composed of
CC WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3.
CC {ECO:0000256|ARBA:ARBA00062699}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the Hakai family.
CC {ECO:0000256|ARBA:ARBA00038499}.
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DR RefSeq; XP_019814245.1; XM_019958686.2.
DR AlphaFoldDB; A0A6P5BQL6; -.
DR SMR; A0A6P5BQL6; -.
DR GeneID; 109557391; -.
DR KEGG; biu:109557391; -.
DR CTD; 79872; -.
DR OrthoDB; 547746at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP001652663; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IEA:UniProtKB-ARBA.
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:UniProtKB-UniPathway.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:TreeGrafter.
DR CDD; cd16508; RING-HC_HAKAI-like; 1.
DR FunFam; 3.30.40.10:FF:000140; E3 ubiquitin-protein ligase Hakai isoform X2; 1.
DR FunFam; 6.10.140.2210:FF:000001; Putative e3 ubiquitin-protein ligase hakai; 1.
DR Gene3D; 6.10.140.2210; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR040380; HAKAI-like_RING-HC.
DR InterPro; IPR040383; HAKAI/CBLL2.
DR InterPro; IPR041042; Znf_Hakai.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13480:SF0; E3 UBIQUITIN-PROTEIN LIGASE HAKAI; 1.
DR PANTHER; PTHR13480; E3 UBIQUITIN-PROTEIN LIGASE HAKAI-RELATED; 1.
DR Pfam; PF18408; zf_Hakai; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP001652663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 109..149
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..479
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 54505 MW; 78E756843C2FFF52 CRC64;
MDHTDNELQG TNSSGSLGGL DVRRRIPIKL ISKQGNKAKA SPRTPRTINR MPAKAPAGDE
EGFDYNEEER YDCKGGELFG NQRRFPGHLF WDFQINILGE KDDTPVHFCD KCGLPIKIYG
RMIPCKHVFC YDCAILHEKK GDKMCPGCSD PVQRIEQCTR GSLFMCSIVQ GCKRTYLSQR
DLQAHINHRH MRAGKPVTRA SLENVHPPPI APPPAEIPDR FIMPPDKHHM SHIPPKQHIM
MPPPPLQHVP HEHYNQPHED IRAPPAELSM APPPPRSVSQ ETFRISTRKH SNLITVPIQD
DSNPGAREPP PPAPAPAHHH PEYQGQPVVS HPHHIMPPQQ HYAPPPPPPP PISHPMPHPP
QAAGTPHLVY SQAPPPPMTS APPPITPPPG HIIAQMPPYM NHPPPGPPPP QHGGPPVTAP
PPHHYNPNSL PQFTEDQGTL SPPFTQPGGM SPGIWPAPRG PPPPPRMQGP PSQTPLPGPH
HPDQTRYRPY YQ
//
