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RN114_PANTR
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   03-AUG-2022, entry version 98.
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; Q6J212; -.
DR   GeneID; 470029; -.
DR   KEGG; ptr:470029; -.
DR   CTD; 55905; -.
DR   eggNOG; ENOG502QW3F; Eukaryota.
DR   InParanoid; Q6J212; -.
DR   OrthoDB; 1097558at2759; -.
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; -; 1.
DR   InterPro; IPR008598; Di19_Zn-bd.
DR   InterPro; IPR042716; RNF114_RING-HC.
DR   InterPro; IPR034734; ZF_C2HC_RNF.
DR   InterPro; IPR027370; Znf-RING_LisH.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
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   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
 
 
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