HAKAI_CHICK
ID HAKAI_CHICK Reviewed; 493 AA.
AC Q5ZHZ4;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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};
GN ORFNames=RCJMB04_31p12 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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DR EMBL; AJ720990; CAG32649.1; -; mRNA.
DR RefSeq; NP_001007849.1; NM_001007848.1.
DR AlphaFoldDB; Q5ZHZ4; -.
DR SMR; Q5ZHZ4; -.
DR STRING; 9031.ENSGALP00000041156; -.
DR PaxDb; Q5ZHZ4; -.
DR GeneID; 417701; -.
DR KEGG; gga:417701; -.
DR CTD; 79872; -.
DR VEuPathDB; HostDB:geneid_417701; -.
DR eggNOG; KOG2932; Eukaryota.
DR InParanoid; Q5ZHZ4; -.
DR OrthoDB; 765364at2759; -.
DR PhylomeDB; Q5ZHZ4; -.
DR TreeFam; TF332910; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5ZHZ4; -.
DR Proteomes; UP000000539; Unplaced.
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; IBA:GO_Central.
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 GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
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; IPR001841; Znf_RING.
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.
DR PROSITE; PS50089; ZF_RING_2; 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..493
FT /note="E3 ubiquitin-protein ligase Hakai"
FT /id="PRO_0000284051"
FT ZN_FING 109..149
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 164..190
FT /note="C2H2-type"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..206
FT /note="HYB domain"
FT /evidence="ECO:0000250|UniProtKB:Q9JIY2"
FT REGION 253..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 54851 MW; E88B2C7C9E5F65B1 CRC64;
MDHNDNDLQG TNSSASLGGL DVRRRIPIKL ISKQTNKTKP APRAPRAMNR MPAKTQAGDE
EEFDFNEEER YECKGGEMFG NQRRFPGPIF WDYKINLLGE KDDTPVHFCD KCGLPIKMYG
RMIPCKHVFC YDCAILHEKK GDKMCPGCNE PVQRIEQCVR GSLFMCSIVQ GCKRTYLSQR
DLQAHINHRH MRAGKPVTRP PLEPVHPPIA PPPAEIPERF IMPPEKHHMS HIPPKQHIMM
PPPPLQHVPH EHYNQPHEDI RPPPAEMSMA PPPPRPVSQD TFRISTRKHS NLITVPIQDD
SNSGAREPPP PAPAPAHHHP EYQGQPVVTH PHHIMPPQQH YAPPPPPPPP ISHPLQHPPQ
AAGTPHMVYS QAPPPPMTSA PPPITPPPGH IIAQMPPYMN HPPPGPPPPQ HGGPPVNVSA
PPPHHYNPNS LPQFSEDQGT LSPPFTQPGG MSPGIWPAPR GPPPPPRMQG PPAQAPLAGP
HHPDQARYRP YYQ
