ID RN114_PANTR Reviewed; 228 AA.
AC Q6J212;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE RecName: Full=E3 ubiquitin-protein ligase RNF114;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9Y508};
DE AltName: Full=RING finger protein 114;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF114 {ECO:0000305};
DE AltName: Full=Zinc finger protein 313;
GN Name=RNF114; Synonyms=ZNF313;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Ma Y.-X., Wu Q., Zhang S., Sun Y., Wang C., Liu Y., He G., Dong J.,
RA Hong Z., Peng Y.;
RT "Molecular cloning and characterization of chimpanzee Znf313 gene.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC of various substrates. In turn, participates in the regulation of many
CC biological processes including cell cycle, apoptosis,
CC osteoclastogenesis as well as innate or adaptive immunity. Acts as
CC negative regulator of NF-kappa-B-dependent transcription by promoting
CC the ubiquitination and stabilization of the NF-kappa-B inhibitor
CC TNFAIP3. May promote the ubiquitination of TRAF6 as well. Acts also as
CC a negative regulator of T-cell activation. Inhibits cellular dsRNA
CC responses and interferon production by targeting MAVS component for
CC proteasomal degradation. Ubiquitinates the CDK inhibitor CDKN1A leading
CC to its degradationand probably also CDKN1B and CDKN1C. This activity
CC stimulates cell cycle G1-to-S phase transition and suppresses cellular
CC senescence. May play a role in spermatogenesis.
CC {ECO:0000250|UniProtKB:Q9Y508}.
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:Q9Y508};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9Y508}.
CC -!- SUBUNIT: Interacts with XAF1, the interaction increases XAF1 stability
CC and proapoptotic effects, and may regulate IFN signaling.
CC {ECO:0000250|UniProtKB:Q9Y508}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y508}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y508}.
CC -!- PTM: Autoubiquitinated. Polyubiquitinated in the presence of E2 enzymes
CC UBE2D1, UBE2D2 and UBE2D3, but only monoubiquitinated in the presence
CC of UBE2E1. {ECO:0000250|UniProtKB:Q9Y508}.
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DR EMBL; AY604723; AAT38454.1; -; Transcribed_RNA.
DR RefSeq; NP_001120978.1; NM_001127506.1.
DR AlphaFoldDB; Q6J212; -.
DR STRING; 9598.ENSPTRP00000023416; -.
DR PaxDb; 9598-ENSPTRP00000023416; -.
DR GeneID; 470029; -.
DR KEGG; ptr:470029; -.
DR CTD; 55905; -.
DR eggNOG; ENOG502QW3F; Eukaryota.
DR InParanoid; Q6J212; -.
DR OrthoDB; 26661at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16540; RING-HC_RNF114; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR042716; RNF114_RING-HC.
DR InterPro; IPR034734; ZF_C2HC_RNF.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46016:SF3; E3 UBIQUITIN-PROTEIN LIGASE RNF114; 1.
DR PANTHER; PTHR46016; ZINC FINGER, RING/FYVE/PHD-TYPE; 1.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR Pfam; PF18574; zf_C2HC_14; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Developmental protein; Differentiation;
KW Metal-binding; Nucleus; Reference proteome; Spermatogenesis; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..228
FT /note="E3 ubiquitin-protein ligase RNF114"
FT /id="PRO_0000056309"
FT ZN_FING 29..68
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 91..110
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y508"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y508"
SQ SEQUENCE 228 AA; 25708 MW; DF5EC7283FC64A21 CRC64;
MAAQQRDCGG AAQLAGPAAE ADPLGRFTCP VCLEVYEKPV QVPCGHVFCS ACLQECLKPK
KPVCGVCRSA LAPGVRAVEL ERQIESTETS CHGCRKKFFL SKIRSHVATC SKYQNYIMEG
VKATIKDASL QPRNVPNRYT FPCPYCPEKN FDQEGLVEHC KLFHSTDTKS VVCPICASMP
WGDPNYRSAN FREHIQRRHR FSYDTFVDYD VDEEDMMNQV LQRSIIDQ
//
