O54965

PR
Gene name
Rnf13 (Rzf)
Protein name
E3 ubiquitin-protein ligase RNF13
Names
RING finger protein 13
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:24017
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

260-337 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O54965

Entry ID Method Resolution Chain Position Source
AF-O54965-F1 Predicted AlphaFoldDB

11 variants for O54965

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388631360 37 L>F No EVA
rs3388629172 170 I>N No EVA
rs3388627256 177 S>C No EVA
rs3388621322 232 K>* No EVA
rs3388633959 233 K>M No EVA
rs3388634578 234 G>R No EVA
rs3393020160 270 W>C No EVA
rs3388613693 298 S>N No EVA
rs3388634592 330 H>Q No EVA
rs16807645 357 E>K No EVA
rs3393181336 360 D>N No EVA

No associated diseases with O54965

3 regional properties for O54965

Type Name Position InterPro Accession
domain Zinc finger, RING-type 239 - 282 IPR001841
domain PA domain 88 - 158 IPR003137
domain ZNRF4 /RNF13/RNF167, PA domain 23 - 180 IPR044744

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass type I membrane protein
  • Late endosome membrane ; Single-pass type I membrane protein
  • Lysosome membrane ; Single-pass type I membrane protein
  • Nucleus inner membrane ; Single-pass type I membrane protein
  • The mature protein is subjected to extensive proteolysis that leads to the shedding of the ectodomain into the lumen of vesicles and the release of the C-terminal fragment into the cytosol (PubMed:20230530)
  • Not detected in early endosomes (PubMed:20230530)
  • Treatment of the cells with either PMA or ionomycin stabilizes the full-length protein which relocalizes to recycling endosomes and to the inner nuclear membrane (PubMed:20230530)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
endosome A vacuole to which materials ingested by endocytosis are delivered.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
late endosome membrane The lipid bilayer surrounding a late endosome.
lysosomal membrane The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
nuclear inner membrane The inner, i.e. lumen-facing, lipid bilayer of the nuclear envelope.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

4 GO annotations of molecular function

Name Definition
JUN kinase binding Binding to JUN kinase, an enzyme that catalyzes the phosphorylation and activation of members of the JUN family.
metal ion binding Binding to a metal ion.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.

4 GO annotations of biological process

Name Definition
organelle localization Any process in which an organelle is transported to, and/or maintained in, a specific location.
positive regulation of stress-activated protein kinase signaling cascade Any process that activates or increases the frequency, rate or extent of signaling via the stress-activated protein kinase signaling cascade.
protein autoubiquitination The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3U2C5 Rnf149 E3 ubiquitin-protein ligase RNF149 Mus musculus (Mouse) PR
10 20 30 40 50 60
MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFED LPARFGYRLP
70 80 90 100 110 120
AEGLKGFLIN SKPENACEPI VPPPLKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI
130 140 150 160 170 180
VHNVDSDDLI SMGSNDIDTL KKIDIPSVFI GESSANSLKD EFTYEKGGHI ILVPELSLPL
190 200 210 220 230 240
EYYLIPFLII VGICLILIVI FMITKFVQDR HRNRRNRLRK DQLKKLPVHK FKKGDEYDVC
250 260 270 280 290 300
AICLEEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ
310 320 330 340 350 360
EENQVSEHTP LLPPSASART QSFGSLSESH SHHNMTESSD YEDDDNEETD SSDADNEITD
370 380
HSVVVQLQPN GEQDYNIANT V