RNF13_HUMAN
ID RNF13_HUMAN Reviewed; 381 AA.
AC O43567; A6NC87; B3KR12; Q05D66; Q6IBJ9;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase RNF13 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:24387786};
DE AltName: Full=RING finger protein 13;
DE Flags: Precursor;
GN Name=RNF13 {ECO:0000303|PubMed:18794910, ECO:0000312|HGNC:HGNC:10057};
GN Synonyms=RZF {ECO:0000303|Ref.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lomax M.I., Warner S.J., Bersirli C.G., Gong T.-W.L.;
RT "The gene for a RING zinc finger protein is expressed in the inner chick
RT ear after noise exposure.";
RL Prim. Sens. Neuron 2:305-316(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Glial tumor, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Skeletal muscle, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AUTOUBIQUITINATION, GLYCOSYLATION AT ASN-88, AND MUTAGENESIS OF ASN-43;
RP ASN-88; CYS-258; HIS-260 AND TRP-270.
RX PubMed=18794910; DOI=10.1038/cr.2008.285;
RA Zhang Q., Meng Y., Zhang L., Chen J., Zhu D.;
RT "RNF13: a novel RING-type ubiquitin ligase over-expressed in pancreatic
RT cancer.";
RL Cell Res. 19:348-357(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ERN1, MUTAGENESIS OF
RP 1-MET--TYR-183; 52-PRO--PHE-162; 165-GLU--VAL-381; 184-LEU--VAL-207 AND
RP CYS-243, AND DOMAIN.
RX PubMed=23378536; DOI=10.1074/jbc.m112.368829;
RA Arshad M., Ye Z., Gu X., Wong C.K., Liu Y., Li D., Zhou L., Zhang Y.,
RA Bay W.P., Yu V.C., Li P.;
RT "RNF13, a RING finger protein, mediates endoplasmic reticulum stress-
RT induced apoptosis through the inositol-requiring enzyme (IRE1alpha)/c-Jun
RT NH2-terminal kinase pathway.";
RL J. Biol. Chem. 288:8726-8736(2013).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, VARIANTS PRO-114;
RP TYR-243 AND 246-GLU--VAL-381 DEL, AND CHARACTERIZATION OF VARIANTS PRO-114;
RP TYR-243 AND 246-GLU--VAL-381 DEL.
RX PubMed=24387786; DOI=10.1042/bj20131067;
RA van Dijk J.R., Yamazaki Y., Palmer R.H.;
RT "Tumour-associated mutations of PA-TM-RING ubiquitin ligases RNF167/RNF13
RT identify the PA domain as a determinant for endosomal localization.";
RL Biochem. J. 459:27-36(2014).
RN [12]
RP FUNCTION, INVOLVEMENT IN DEE73, VARIANTS DEE73 SER-311 AND PRO-312, AND
RP CHARACTERIZATION OF VARIANT DEE73 SER-311.
RX PubMed=30595371; DOI=10.1016/j.ajhg.2018.11.018;
RA Edvardson S., Nicolae C.M., Noh G.J., Burton J.E., Punzi G., Shaag A.,
RA Bischetsrieder J., De Grassi A., Pierri C.L., Elpeleg O., Moldovan G.L.;
RT "Heterozygous RNF13 gain-of-function variants are associated with
RT congenital microcephaly, epileptic encephalopathy, blindness, and failure
RT to thrive.";
RL Am. J. Hum. Genet. 104:179-185(2019).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates cell proliferation
CC (PubMed:18794910, PubMed:23378536, PubMed:30595371). Involved in
CC apoptosis regulation (PubMed:23378536, PubMed:30595371). Mediates ER
CC stress-induced activation of JNK signaling pathway and apoptosis by
CC promoting ERN1 activation and splicing of XBP1 mRNA (PubMed:23378536,
CC PubMed:30595371). Also involved in protein trafficking and localization
CC (PubMed:24387786). {ECO:0000269|PubMed:18794910,
CC ECO:0000269|PubMed:23378536, ECO:0000269|PubMed:24387786,
CC ECO:0000269|PubMed:30595371}.
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:0000269|PubMed:18794910,
CC ECO:0000269|PubMed:24387786};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:24387786}.
CC -!- SUBUNIT: Interacts with ERN1. {ECO:0000269|PubMed:23378536}.
CC -!- INTERACTION:
CC O43567; P61088: UBE2N; NbExp=2; IntAct=EBI-2129183, EBI-1052908;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:23378536,
CC ECO:0000269|PubMed:24387786}; Single-pass type I membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000305|PubMed:24387786};
CC Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein
CC {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:O54965};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Under certain
CC conditions, relocalizes to recycling endosomes and to the inner nuclear
CC membrane. {ECO:0000250|UniProtKB:O54965}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43567-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43567-2; Sequence=VSP_055430, VSP_055431;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). In normal
CC pancreas, expressed in islets, but not in ducts, nor in acini (at
CC protein level). {ECO:0000269|PubMed:18794910}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity and for promoting ER stress-induced JNK activation and
CC apoptosis. {ECO:0000269|PubMed:23378536}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:18794910}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 73 (DEE73)
CC [MIM:618379]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE73 is an autosomal dominant form with onset at
CC birth. {ECO:0000269|PubMed:30595371}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17878.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF037204; AAC03769.1; -; mRNA.
DR EMBL; AF070558; AAC28641.1; -; mRNA.
DR EMBL; AK313304; BAG36109.1; -; mRNA.
DR EMBL; AK090638; BAG52202.1; -; mRNA.
DR EMBL; AK090771; BAG52224.1; -; mRNA.
DR EMBL; CR456804; CAG33085.1; -; mRNA.
DR EMBL; AC069216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78858.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78859.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78860.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78861.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78862.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78863.1; -; Genomic_DNA.
DR EMBL; BC009803; AAH09803.1; -; mRNA.
DR EMBL; BC009781; AAH09781.1; -; mRNA.
DR EMBL; BC017878; AAH17878.1; ALT_SEQ; mRNA.
DR CCDS; CCDS3146.1; -. [O43567-1]
DR CCDS; CCDS87154.1; -. [O43567-2]
DR RefSeq; NP_009213.1; NM_007282.4. [O43567-1]
DR RefSeq; NP_899237.1; NM_183381.2. [O43567-1]
DR RefSeq; XP_005247149.1; XM_005247092.3.
DR RefSeq; XP_011510675.1; XM_011512373.2. [O43567-1]
DR RefSeq; XP_011510676.1; XM_011512374.2. [O43567-1]
DR RefSeq; XP_011510678.1; XM_011512376.2. [O43567-2]
DR RefSeq; XP_016861143.1; XM_017005654.1.
DR RefSeq; XP_016861144.1; XM_017005655.1.
DR RefSeq; XP_016861145.1; XM_017005656.1.
DR RefSeq; XP_016861146.1; XM_017005657.1.
DR RefSeq; XP_016861147.1; XM_017005658.1.
DR RefSeq; XP_016861148.1; XM_017005659.1.
DR PDB; 5ZBU; X-ray; 3.20 A; A/D=216-290.
DR PDB; 5ZC4; X-ray; 1.91 A; A/D=216-290.
DR PDBsum; 5ZBU; -.
DR PDBsum; 5ZC4; -.
DR AlphaFoldDB; O43567; -.
DR SMR; O43567; -.
DR BioGRID; 116470; 57.
DR IntAct; O43567; 30.
DR STRING; 9606.ENSP00000341361; -.
DR GlyGen; O43567; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O43567; -.
DR PhosphoSitePlus; O43567; -.
DR BioMuta; RNF13; -.
DR EPD; O43567; -.
DR jPOST; O43567; -.
DR MassIVE; O43567; -.
DR MaxQB; O43567; -.
DR PaxDb; O43567; -.
DR PeptideAtlas; O43567; -.
DR PRIDE; O43567; -.
DR ProteomicsDB; 3575; -.
DR ProteomicsDB; 49058; -. [O43567-1]
DR Antibodypedia; 2251; 137 antibodies from 28 providers.
DR DNASU; 11342; -.
DR Ensembl; ENST00000344229.7; ENSP00000341361.3; ENSG00000082996.20. [O43567-1]
DR Ensembl; ENST00000361785.10; ENSP00000355268.6; ENSG00000082996.20. [O43567-2]
DR Ensembl; ENST00000392894.8; ENSP00000376628.3; ENSG00000082996.20. [O43567-1]
DR GeneID; 11342; -.
DR KEGG; hsa:11342; -.
DR MANE-Select; ENST00000392894.8; ENSP00000376628.3; NM_183381.3; NP_899237.1.
DR UCSC; uc003exn.5; human. [O43567-1]
DR CTD; 11342; -.
DR DisGeNET; 11342; -.
DR GeneCards; RNF13; -.
DR HGNC; HGNC:10057; RNF13.
DR HPA; ENSG00000082996; Low tissue specificity.
DR MalaCards; RNF13; -.
DR MIM; 609247; gene.
DR MIM; 618379; phenotype.
DR neXtProt; NX_O43567; -.
DR OpenTargets; ENSG00000082996; -.
DR Orphanet; 544503; RNF13-related severe early-onset epileptic encephalopathy.
DR PharmGKB; PA34422; -.
DR VEuPathDB; HostDB:ENSG00000082996; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000154942; -.
DR HOGENOM; CLU_035275_1_1_1; -.
DR InParanoid; O43567; -.
DR OMA; FMIVRCI; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; O43567; -.
DR TreeFam; TF317486; -.
DR PathwayCommons; O43567; -.
DR SignaLink; O43567; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 11342; 17 hits in 1088 CRISPR screens.
DR ChiTaRS; RNF13; human.
DR GeneWiki; RNF13; -.
DR GenomeRNAi; 11342; -.
DR Pharos; O43567; Tbio.
DR PRO; PR:O43567; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O43567; protein.
DR Bgee; ENSG00000082996; Expressed in corpus callosum and 215 other tissues.
DR ExpressionAtlas; O43567; baseline and differential.
DR Genevisible; O43567; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008432; F:JUN kinase binding; IDA:UniProtKB.
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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0051640; P:organelle localization; IMP:UniProtKB.
DR GO; GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd02123; PA_C_RZF_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Endoplasmic reticulum;
KW Endosome; Epilepsy; Glycoprotein; Lysosome; Membrane; Metal-binding;
KW Nucleus; Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..381
FT /note="E3 ubiquitin-protein ligase RNF13"
FT /id="PRO_0000056054"
FT TOPO_DOM 35..182
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 65..160
FT /note="PA"
FT ZN_FING 240..282
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 285..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18794910"
FT VAR_SEQ 1..18
FT /note="MLLSIGMLMLSATQVYTI -> MLILMTSLAWDPTTVSTV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055430"
FT VAR_SEQ 19..137
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055431"
FT VARIANT 114
FT /note="A -> P (found in a tumor sample; unknown
FT pathological significance; abolished localization to
FT endosomes)"
FT /evidence="ECO:0000269|PubMed:24387786"
FT /id="VAR_086368"
FT VARIANT 243
FT /note="C -> Y (found in a tumor sample; unknown
FT pathological significance; abolished ability to regulate
FT protein trafficking and localization)"
FT /evidence="ECO:0000269|PubMed:24387786"
FT /id="VAR_086369"
FT VARIANT 246..381
FT /note="Missing (found in a tumor sample; unknown
FT pathological significance; abolished ability to regulate
FT protein trafficking and localization)"
FT /evidence="ECO:0000269|PubMed:24387786"
FT /id="VAR_086370"
FT VARIANT 311
FT /note="L -> S (in DEE73; gain-of-function variant;
FT increased ER stress-induced apoptosis)"
FT /evidence="ECO:0000269|PubMed:30595371"
FT /id="VAR_082117"
FT VARIANT 312
FT /note="L -> P (in DEE73)"
FT /evidence="ECO:0000269|PubMed:30595371"
FT /id="VAR_082118"
FT MUTAGEN 1..183
FT /note="Missing: No effect on ER stress-induced JNK
FT activation and apoptosis."
FT /evidence="ECO:0000269|PubMed:23378536"
FT MUTAGEN 43
FT /note="N->A: No effect on glycosylation."
FT /evidence="ECO:0000269|PubMed:18794910"
FT MUTAGEN 52..162
FT /note="Missing: No effect on ER stress-induced JNK
FT activation and apoptosis. No effect on interaction with
FT ERN1."
FT /evidence="ECO:0000269|PubMed:23378536"
FT MUTAGEN 88
FT /note="N->A: Loss of glycosylation."
FT /evidence="ECO:0000269|PubMed:18794910"
FT MUTAGEN 165..381
FT /note="Missing: Abolishes ER stress-induced JNK activation
FT and apoptosis."
FT /evidence="ECO:0000269|PubMed:23378536"
FT MUTAGEN 184..207
FT /note="Missing: Abolishes ER stress-induced JNK activation
FT and apoptosis. Disrupts localization to endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:23378536"
FT MUTAGEN 243
FT /note="C->W: Abolishes ER stress-induced JNK activation and
FT apoptosis. Abolishes interaction with ERN1. Does not affect
FT localization to endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:23378536"
FT MUTAGEN 258
FT /note="C->A: Complete loss of E3 ligase activity; when
FT associated with A-260."
FT /evidence="ECO:0000269|PubMed:18794910"
FT MUTAGEN 260
FT /note="H->A: Complete loss of E3 ligase activity; when
FT associated with A-258."
FT /evidence="ECO:0000269|PubMed:18794910"
FT MUTAGEN 270
FT /note="W->A: Drastically reduces E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:18794910"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:5ZC4"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5ZC4"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:5ZC4"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5ZC4"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5ZC4"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:5ZC4"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:5ZC4"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:5ZBU"
SQ SEQUENCE 381 AA; 42814 MW; 4600727D0F197653 CRC64;
MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFDD LPARFGYRLP
AEGLKGFLIN SKPENACEPI VPPPVKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI
VHNVDSDDLI SMGSNDIEVL KKIDIPSVFI GESSANSLKD EFTYEKGGHL ILVPEFSLPL
EYYLIPFLII VGICLILIVI FMITKFVQDR HRARRNRLRK DQLKKLPVHK FKKGDEYDVC
AICLDEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ
EENEVTEHTP LLRPLASVSA QSFGALSESR SHQNMTESSD YEEDDNEDTD SSDAENEINE
HDVVVQLQPN GERDYNIANT V
