RNF11_BOVIN
ID RNF11_BOVIN Reviewed; 154 AA.
AC Q08DI6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=RING finger protein 11;
GN Name=RNF11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of a ubiquitin-editing protein complex,
CC comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient
CC nature of inflammatory signaling pathways. Promotes the association of
CC TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-
CC 63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-
CC 48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation
CC and consequently termination of the TNF- or LPS-mediated activation of
CC NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for
CC ubiquitination, leading to its degradation by the 26S proteasome (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (when phosphorylated) with 14-3-3. Interacts with
CC the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 (By similarity).
CC Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and
CC UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350,
CC EPS15 and STAMBP (By similarity). After TNF stimulation, interacts with
CC TAX1BP1, TNFAIP3 and RIPK1; these interaction are transient and they
CC are lost after 1 hour of stimulation with TNF (By similarity).
CC Interacts with GGA1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic, when unphosphorylated, and nuclear,
CC when phosphorylated by PKB/AKT1. {ECO:0000250}.
CC -!- DOMAIN: The PPxY motif mediates interaction with NEDD4. {ECO:0000250}.
CC -!- PTM: Ubiquitinated in the presence of ITCH, SMURF2 and UBE2D1, as well
CC as WWP1. {ECO:0000250}.
CC -!- PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the
CC proteasome. {ECO:0000250}.
CC -!- PTM: Acylation at both Gly-2 and Cys-4 is required for proper
CC localization to the endosomes. {ECO:0000250}.
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DR EMBL; BC123728; AAI23729.1; -; mRNA.
DR RefSeq; NP_001071421.1; NM_001077953.1.
DR AlphaFoldDB; Q08DI6; -.
DR SMR; Q08DI6; -.
DR IntAct; Q08DI6; 3.
DR STRING; 9913.ENSBTAP00000017277; -.
DR PaxDb; Q08DI6; -.
DR Ensembl; ENSBTAT00000086641; ENSBTAP00000059090; ENSBTAG00000054545.
DR GeneID; 522791; -.
DR KEGG; bta:522791; -.
DR CTD; 26994; -.
DR VEuPathDB; HostDB:ENSBTAG00000054545; -.
DR VGNC; VGNC:34009; RNF11.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00730000110988; -.
DR HOGENOM; CLU_123539_1_1_1; -.
DR InParanoid; Q08DI6; -.
DR OMA; HLDCIDN; -.
DR OrthoDB; 1261762at2759; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000054545; Expressed in occipital lobe and 102 other tissues.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
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:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16468; RING-H2_RNF11; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042981; RNF11_RING-H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endosome; Lipoprotein; Metal-binding; Myristate; Nucleus;
KW Palmitate; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3C5"
FT CHAIN 2..154
FT /note="RING finger protein 11"
FT /id="PRO_0000285208"
FT ZN_FING 99..140
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..40
FT /note="PPxY motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3C5"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYK7"
FT MOD_RES 135
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3C5"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 154 AA; 17444 MW; C368E38148FC1D0D CRC64;
MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH PTPSQTRLAT
QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV ICMMDFVYGD PIRFLPCMHI
YHLDCIDDWL MRSFTCPSCM EPVDAALLSS YETN
