RN19A_HUMAN
ID RN19A_HUMAN Reviewed; 838 AA.
AC Q9NV58; A3KCU9; Q52LG1; Q9H5H9; Q9H8M8; Q9UFG0; Q9UFX6; Q9Y4Y1;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=E3 ubiquitin-protein ligase RNF19A;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
DE AltName: Full=Double ring-finger protein;
DE Short=Dorfin;
DE AltName: Full=RING finger protein 19A;
DE AltName: Full=p38;
GN Name=RNF19A; Synonyms=RNF19;
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), FUNCTION, INTERACTION WITH UBE2L3
RP AND UBE2L6, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Spinal cord;
RX PubMed=11237715; DOI=10.1006/bbrc.2001.4414;
RA Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.;
RT "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase
RT activity.";
RL Biochem. Biophys. Res. Commun. 281:706-713(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-89 (ISOFORM 3).
RA Kim T., Huh J., Kim H.;
RT "Expression and promoter activity of MaLR element of Dorfin gene related to
RT Parkinson disease.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 426-838 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-838 (ISOFORM 2).
RC TISSUE=Hepatoma, Ovarian carcinoma, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 422-824 (ISOFORM 1), AND INTERACTION WITH
RP SP1.
RC TISSUE=Colon;
RX PubMed=10976766; DOI=10.1023/a:1007177623283;
RA Gunther M., Laithier M., Brison O.;
RT "A set of proteins interacting with transcription factor Sp1 identified in
RT a two-hybrid screening.";
RL Mol. Cell. Biochem. 210:131-142(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 524-838 (ISOFORM 1).
RC TISSUE=Fetal kidney, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SOD1.
RX PubMed=12145308; DOI=10.1074/jbc.m206559200;
RA Niwa J., Ishigaki S., Hishikawa N., Yamamoto M., Doyu M., Murata S.,
RA Tanaka K., Taniguchi N., Sobue G.;
RT "Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated
RT neurotoxicity.";
RL J. Biol. Chem. 277:36793-36798(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SNCAIP.
RX PubMed=12750386; DOI=10.1074/jbc.m302763200;
RA Ito T., Niwa J., Hishikawa N., Ishigaki S., Doyu M., Sobue G.;
RT "Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1.";
RL J. Biol. Chem. 278:29106-29114(2003).
RN [9]
RP FUNCTION, INTERACTION WITH VCP, MUTAGENESIS OF CYS-132 AND CYS-135, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15456787; DOI=10.1074/jbc.m406683200;
RA Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S.,
RA Kakizuka A., Tanaka K., Sobue G.;
RT "Physical and functional interaction between dorfin and valosin-containing
RT protein that are colocalized in ubiquitylated inclusions in
RT neurodegenerative disorders.";
RL J. Biol. Chem. 279:51376-51385(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH CASR AND VCP.
RX PubMed=16513638; DOI=10.1074/jbc.m513552200;
RA Huang Y., Niwa J., Sobue G., Breitwieser G.E.;
RT "Calcium-sensing receptor ubiquitination and degradation mediated by the E3
RT ubiquitin ligase dorfin.";
RL J. Biol. Chem. 281:11610-11617(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates, such as SNCAIP or CASR. Specifically ubiquitinates
CC pathogenic SOD1 variants, which leads to their proteasomal degradation
CC and to neuronal protection. {ECO:0000269|PubMed:11237715,
CC ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12750386,
CC ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16513638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with UBE2L3 and UBE2L6. Interacts with transcription
CC factor Sp1. Interacts with VCP, CASR, SNCAIP and with some SOD1
CC variants which cause amyotrophic lateral sclerosis, but not with wild-
CC type SOD1. {ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:11237715,
CC ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12750386,
CC ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16513638}.
CC -!- INTERACTION:
CC Q9NV58; P00441: SOD1; NbExp=3; IntAct=EBI-1390270, EBI-990792;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:11237715,
CC ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12750386,
CC ECO:0000269|PubMed:15456787}. Note=Present in the hyaline inclusion
CC bodies specifically found in motor neurons from amyotrophic lateral
CC sclerosis patients. Present in the Lewy bodies specifically found in
CC neurons from Parkinson disease patients.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NV58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NV58-2; Sequence=VSP_021010, VSP_021011;
CC Name=3;
CC IsoId=Q9NV58-3; Sequence=VSP_028631;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart.
CC Ubiquitously expressed in the central nervous system.
CC {ECO:0000269|PubMed:11237715}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING domain, but require
CC an obligate trans-thiolation step during the ubiquitin transfer,
CC requiring a conserved cysteine residue in the second RING domain.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14581.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB029316; BAB39353.1; -; mRNA.
DR EMBL; BC093938; AAH93938.1; -; mRNA.
DR EMBL; BC093940; AAH93940.1; -; mRNA.
DR EMBL; AB271914; BAF48117.1; -; mRNA.
DR EMBL; AK001774; BAA91900.1; -; mRNA.
DR EMBL; AK023455; BAB14581.1; ALT_INIT; mRNA.
DR EMBL; AK027070; BAB15647.1; ALT_INIT; mRNA.
DR EMBL; AJ242975; CAB45132.1; -; mRNA.
DR EMBL; AL110253; CAB53700.1; -; mRNA.
DR EMBL; AL122096; CAB59264.1; -; mRNA.
DR CCDS; CCDS6286.1; -. [Q9NV58-1]
DR PIR; T34528; T34528.
DR RefSeq; NP_001267468.1; NM_001280539.1. [Q9NV58-1]
DR RefSeq; NP_056250.3; NM_015435.4. [Q9NV58-1]
DR RefSeq; NP_904355.1; NM_183419.3. [Q9NV58-1]
DR RefSeq; XP_005250910.1; XM_005250853.3.
DR RefSeq; XP_016868791.1; XM_017013302.1. [Q9NV58-1]
DR RefSeq; XP_016868792.1; XM_017013303.1. [Q9NV58-1]
DR AlphaFoldDB; Q9NV58; -.
DR BioGRID; 117405; 24.
DR IntAct; Q9NV58; 14.
DR MINT; Q9NV58; -.
DR STRING; 9606.ENSP00000428968; -.
DR iPTMnet; Q9NV58; -.
DR PhosphoSitePlus; Q9NV58; -.
DR BioMuta; RNF19A; -.
DR DMDM; 116242764; -.
DR EPD; Q9NV58; -.
DR jPOST; Q9NV58; -.
DR MassIVE; Q9NV58; -.
DR MaxQB; Q9NV58; -.
DR PaxDb; Q9NV58; -.
DR PeptideAtlas; Q9NV58; -.
DR PRIDE; Q9NV58; -.
DR ProteomicsDB; 82747; -. [Q9NV58-1]
DR ProteomicsDB; 82748; -. [Q9NV58-2]
DR ProteomicsDB; 82749; -. [Q9NV58-3]
DR Antibodypedia; 3140; 222 antibodies from 29 providers.
DR DNASU; 25897; -.
DR Ensembl; ENST00000341084.7; ENSP00000342667.2; ENSG00000034677.13. [Q9NV58-1]
DR Ensembl; ENST00000519449.5; ENSP00000428968.1; ENSG00000034677.13. [Q9NV58-1]
DR GeneID; 25897; -.
DR KEGG; hsa:25897; -.
DR MANE-Select; ENST00000341084.7; ENSP00000342667.2; NM_183419.4; NP_904355.1.
DR UCSC; uc003yjj.3; human. [Q9NV58-1]
DR CTD; 25897; -.
DR DisGeNET; 25897; -.
DR GeneCards; RNF19A; -.
DR HGNC; HGNC:13432; RNF19A.
DR HPA; ENSG00000034677; Low tissue specificity.
DR MIM; 607119; gene.
DR neXtProt; NX_Q9NV58; -.
DR OpenTargets; ENSG00000034677; -.
DR PharmGKB; PA162401601; -.
DR VEuPathDB; HostDB:ENSG00000034677; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000158703; -.
DR HOGENOM; CLU_016793_1_0_1; -.
DR InParanoid; Q9NV58; -.
DR OMA; LMSDLDM; -.
DR OrthoDB; 257621at2759; -.
DR PhylomeDB; Q9NV58; -.
DR TreeFam; TF324777; -.
DR PathwayCommons; Q9NV58; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9NV58; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 25897; 64 hits in 1111 CRISPR screens.
DR ChiTaRS; RNF19A; human.
DR GeneWiki; RNF19A; -.
DR GenomeRNAi; 25897; -.
DR Pharos; Q9NV58; Tbio.
DR PRO; PR:Q9NV58; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NV58; protein.
DR Bgee; ENSG00000034677; Expressed in calcaneal tendon and 185 other tissues.
DR ExpressionAtlas; Q9NV58; baseline and differential.
DR Genevisible; Q9NV58; HS.
DR GO; GO:0005813; C:centrosome; TAS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
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:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; TAS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0099576; P:regulation of protein catabolic process at postsynapse, modulating synaptic transmission; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..838
FT /note="E3 ubiquitin-protein ligase RNF19A"
FT /id="PRO_0000056061"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 132..179
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 199..264
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 301..332
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 41..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..351
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 622..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..838
FT /note="Interaction with CASR"
FT /evidence="ECO:0000269|PubMed:16513638"
FT REGION 700..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_028631"
FT VAR_SEQ 572..604
FT /note="RYSLSGESGTVSLGTVSDNASTKAMAGSILNSY -> AAVAAAGRWAYSPAT
FT LRCRRSEELKNIHDSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021010"
FT VAR_SEQ 605..838
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021011"
FT VARIANT 835
FT /note="Q -> H (in dbSNP:rs9642785)"
FT /id="VAR_028045"
FT MUTAGEN 132
FT /note="C->S: Abolishes interaction with VCP and E3 ligase
FT activity toward mutant SOD1; when associated with S-135."
FT /evidence="ECO:0000269|PubMed:15456787"
FT MUTAGEN 135
FT /note="C->S: Abolishes interaction with VCP and E3 ligase
FT activity toward mutant SOD1; when associated with S-132."
FT /evidence="ECO:0000269|PubMed:15456787"
FT CONFLICT 645
FT /note="H -> Y (in Ref. 1; BAB39353)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="S -> R (in Ref. 6; CAB53700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 838 AA; 90696 MW; 00A7DED5023FDC06 CRC64;
MQEQEIGFIS KYNEGLCVNT DPVSILTSIL DMSLHRQMGS DRDLQSSASS VSLPSVKKAP
KKRRISIGSL FRRKKDNKRK SRELNGGVDG IASIESIHSE MCTDKNSIFS TNTSSDNGLT
SISKQIGDFI ECPLCLLRHS KDRFPDIMTC HHRSCVDCLR QYLRIEISES RVNISCPECT
ERFNPHDIRL ILSDDVLMEK YEEFMLRRWL VADPDCRWCP APDCGYAVIA FGCASCPKLT
CGREGCGTEF CYHCKQIWHP NQTCDAARQE RAQSLRLRTI RSSSISYSQE SGAAADDIKP
CPRCAAYIIK MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW GKKPWSRKKK
ILWQLGTLVG APVGIALIAG IAIPAMIIGI PVYVGRKIHN RYEGKDVSKH KRNLAIAGGV
TLSVIVSPVV AAVTVGIGVP IMLAYVYGVV PISLCRSGGC GVSAGNGKGV RIEFDDENDI
NVGGTNTAVD TTSVAEARHN PSIGEGSVGG LTGSLSASGS HMDRIGAIRD NLSETASTMA
LAGASITGSL SGSAMVNCFN RLEVQADVQK ERYSLSGESG TVSLGTVSDN ASTKAMAGSI
LNSYIPLDKE GNSMEVQVDI ESKPSKFRHN SGSSSVDDGS ATRSHAGGSS SGLPEGKSSA
TKWSKEATAG KKSKSGKLRK KGNMKINETR EDMDAQLLEQ QSTNSSEFEA PSLSDSMPSV
ADSHSSHFSE FSCSDLESMK TSCSHGSSDY HTRFATVNIL PEVENDRLEN SPHQCSISVV
TQTASCSEVS QLNHIAEEHG NNGIKPNVDL YFGDALKETN NNHSHQTMEL KVAIQTEI
