ID A0A8J8Y1H6_CALJA Unreviewed; 315 AA.
AC A0A8J8Y1H6;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=E3 ubiquitin-protein ligase RNF144A {ECO:0000256|ARBA:ARBA00069723};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=RING finger protein 144A {ECO:0000256|ARBA:ARBA00078868};
DE AltName: Full=UbcM4-interacting protein 4 {ECO:0000256|ARBA:ARBA00075379};
DE AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 4 {ECO:0000256|ARBA:ARBA00078433};
GN Name=RNF144A {ECO:0000313|Ensembl:ENSCJAP00000018832.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000018832.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000018832.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000018832.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates. Mediates the ubiquitination and degradation of the DNA
CC damage kinase PRKDC during DNA damage. Positively regulates DNA virus
CC or exogenous cytosolic DNA-triggered innate immune response by
CC mediating STING1 ubiquitination and increasing its 'Lys-6'-linked
CC ubiquitination and translocation from the endoplasmic reticulum to the
CC Golgi leading to downstream signaling pathways. Plays a positive role
CC in EGF-dependent cell proliferation by prolonging EGF/EGFR signaling
CC during EGF stimulation through EGFR ubiquitination. Increases ERK
CC activity independently of EGFR signaling by promoting
CC polyubiquitination and subsequent degradation of VRK3 in the cytosol.
CC {ECO:0000256|ARBA:ARBA00054980}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Self-associates. Interacts with UBE2L3.
CC {ECO:0000256|ARBA:ARBA00064341}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily.
CC {ECO:0000256|ARBA:ARBA00038342}.
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DR Ensembl; ENSCJAT00000019892.5; ENSCJAP00000018832.4; ENSCJAG00000010225.5.
DR GeneTree; ENSGT00940000157701; -.
DR HOGENOM; CLU_053598_1_0_1; -.
DR TreeFam; TF324777; -.
DR Proteomes; UP000008225; Chromosome 14.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20366; BRcat_RBR_RNF144A; 1.
DR CDD; cd16777; mRING-HC-C4C4_RBR_RNF144A; 1.
DR CDD; cd20352; Rcat_RBR_RNF144; 1.
DR FunFam; 1.20.120.1750:FF:000006; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000051; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
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 65..285
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 69..115
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 315 AA; 35396 MW; 4DC7CC417B30F97E CRC64;
MLWAPSMVSW PPPWAPATAR RCDSCHRAGG RQGCGGLTFH ASLISDCSAM TTARYRPTWD
LALDPLVSCK LCLGEYPVEQ MTTIAQCQCI FCTLCLKQYV ELLIKEGLET AISCPDAACP
KQGHLQENEI ECMVAAEIMQ RYKKLQFERE VLFDPCRTWC PASTCQAVCQ LQDVGLQTPQ
PVQCKACHME FCSTCKASWH PGQGCPETMP ITFLPGETSA AFKMEEDDAP IKRCPKCKVY
IERDEGCAQM MCKNCKHAFC WYCLESLDDD FLLIHYDKGP CRNKLGHSRA SVIWHRTQFH
CDHIPVMTAG KCHCG
//
