HAKAI_XENLA
ID HAKAI_XENLA Reviewed; 496 AA.
AC Q4V7X9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=E3 ubiquitin-protein ligase Hakai {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9JIY2};
DE AltName: Full=Casitas B-lineage lymphoma-transforming sequence-like protein 1 {ECO:0000250|UniProtKB:Q9JIY2};
DE Short=c-Cbl-like protein 1 {ECO:0000250|UniProtKB:Q9JIY2};
DE AltName: Full=RING-type E3 ubiquitin transferase Hakai {ECO:0000305};
GN Name=cbll1 {ECO:0000250|UniProtKB:Q9JIY2};
GN Synonyms=hakai {ECO:0000250|UniProtKB:Q9JIY2};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC several tyrosine-phosphorylated Src substrates. Associated component of
CC the WMM complex, a complex that mediates N6-methyladenosine (m6A)
CC methylation of RNAs, a modification that plays a role in the efficiency
CC of mRNA splicing and RNA processing. {ECO:0000250|UniProtKB:Q75N03,
CC ECO:0000250|UniProtKB:Q9JIY2}.
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:0000250|UniProtKB:Q9JIY2};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9JIY2}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with tyrosine-
CC phosphorylated SRC substrates (By similarity). Component of the WMM
CC complex, a N6-methyltransferase complex composed of a catalytic
CC subcomplex, named MAC, and of an associated subcomplex, named MACOM.
CC Component of the MACOM subcomplex (By similarity).
CC {ECO:0000250|UniProtKB:Q75N03, ECO:0000250|UniProtKB:Q9JIY2}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q75N03}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q75N03}.
CC -!- DOMAIN: The HYB domain forms a phosphotyrosine-binding pocket upon
CC dimerization, and mediates as well the recognition of its flanking
CC acidic amino acids. {ECO:0000250|UniProtKB:Q9JIY2}.
CC -!- SIMILARITY: Belongs to the Hakai family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC097670; AAH97670.1; -; mRNA.
DR RefSeq; NP_001089473.1; NM_001096004.1.
DR AlphaFoldDB; Q4V7X9; -.
DR SMR; Q4V7X9; -.
DR DNASU; 734524; -.
DR GeneID; 734524; -.
DR KEGG; xla:734524; -.
DR CTD; 734524; -.
DR Xenbase; XB-GENE-17337556; cbll1.S.
DR OrthoDB; 765364at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 734524; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISS:UniProtKB.
DR CDD; cd16508; RING-HC_HAKAI_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040380; HAKAI-like_RING-HC.
DR InterPro; IPR040383; HAKAI/CBLL2.
DR InterPro; IPR041042; Znf_Hakai.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13480; PTHR13480; 1.
DR Pfam; PF18408; zf_Hakai; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..496
FT /note="E3 ubiquitin-protein ligase Hakai"
FT /id="PRO_0000284052"
FT ZN_FING 104..144
FT /note="RING-type; degenerate"
FT ZN_FING 173..199
FT /note="C2H2-type"
FT REGION 35..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..215
FT /note="HYB domain"
FT /evidence="ECO:0000250|UniProtKB:Q9JIY2"
FT REGION 304..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..364
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..433
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 55539 MW; EA57D917C3D476C4 CRC64;
MDHNDNDLQG TNSMGSLSGL DVRRRIPIKL ISKHPNKIKP APRPQRNMNR IPTKPQPGFD
YNEEERYENK GDVFNNQRRF SAHLFWDFKL NLIGEKEDTP VHFCDKCGLP IKIYGRMIPC
KHVFCYDCAL MHEKKADKLC PGTLVEDSTD TFKRMSCNDP VQRIEQCARG SLFMCSIVQG
CKRTYLSQRD LQAHINHRHM RASKPTARPQ PEPIHPPLAP PPAEIPDRFI MPPDKHHLSH
MPPKQHILMP PPPMQHVPHE HFSQQHDDIR PSPADISLAP PPPRSVNQDA FRISTRQHSN
LITVPIQDDS NSGARETPQA PGPTLHHPEY PGQPVVAHPH HIMPPQQHYA PPPPPPPPIS
HPMQHPPQAA GTPHMVYSQG PPPPMTTAPP PITPPPGHII AQIPPYMNHP PPGPPPQHGG
PPVNAPPPHH YNPSSMPQFN EDQGTLSPPF TQPGGMSPGM WPAPRGPPPR MQGPPSQAPM
PGPHHPDQAR YRPYYQ
