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RNF5 Antibody (Center) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession Q99942
Clone Names 100318163
Peptide ID 100318163
Additional Information
Other Names E3 ubiquitin-protein ligase RNF5, 632-, Protein G16, RING finger protein 5, Ram1 homolog, HsRma1, RNF5, G16, NG2, RMA1
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name RNF5
Synonyms G16, NG2, RMA1
Function Has E2-dependent E3 ubiquitin-protein ligase activity. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin and Salmonella type III secreted protein sopA. May be involved in regulation of cell motility and localization of PXN/paxillin. Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of TMEM173 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurs in mitochondria after viral transfection and regulates antiviral responses.
Cellular Location Membrane; Multi-pass membrane protein. Mitochondrion membrane. Endoplasmic reticulum membrane Note=Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles
Tissue Location Widely expressed. EMBL; AB056869; BAB39359.1; -; mRNA EMBL; AJ243936; CAB51286.1; -; mRNA EMBL; AK311859; BAG34800.1; -; mRNA EMBL; BT007105; AAP35769.1; -; mRNA EMBL; U89336; AAB47492.1; -; Genomic_DNA EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AL662830; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BC004155; AAH04155.1; -; mRNA EMBL; BC111392; AAI11393.1; -; mRNA EMBL; BC119741; AAI19742.1; -; mRNA EMBL; BC119742; AAI19743.1; -; mRNA EMBL; BC127651; AAI27652.1; -; mRNA EMBL; BC127652; AAI27653.1; -; mRNA EMBL; BC148255; AAI48256.1; -; mRNA CCDS; CCDS4745.1; - RefSeq; NP_008844.1; NM_006913.3 UniGene; Hs.731774; - ProteinModelPortal; Q99942; - SMR; Q99942; - BioGrid; 111975; 60 DIP; DIP-29268N; - IntAct; Q99942; 64 MINT; Q99942; - STRING; 9606.ENSP00000364235; - iPTMnet; Q99942; - PhosphoSitePlus; Q99942; - BioMuta; RNF5; - DMDM; 74762702; - EPD; Q99942; - MaxQB; Q99942; - PaxDb; Q99942; - PeptideAtlas; Q99942; - PRIDE; Q99942; - ProteomicsDB; 78533; - TopDownProteomics; Q99942; - DNASU; 6048; - Ensembl; ENST00000375094; ENSP00000364235; ENSG00000204308 Ensembl; ENST00000413786; ENSP00000387879; ENSG00000225452 Ensembl; ENST00000432616; ENSP00000413131; ENSG00000183574 Ensembl; ENST00000445885; ENSP00000401172; ENSG00000227277 Ensembl; ENST00000449794; ENSP00000415784; ENSG00000223767 Ensembl; ENST00000453473; ENSP00000415127; ENSG00000228907 Ensembl; ENST00000456167; ENSP00000388795; ENSG00000228405 GeneID; 6048; - KEGG; hsa:6048; - UCSC; uc003oaj.5; human CTD; 6048; - DisGeNET; 6048; - EuPathDB; HostDB:ENSG00000204308.7; - GeneCards; RNF5; - H-InvDB; HIX0034363; - HGNC; HGNC:10068; RNF5 HPA; CAB034107; - HPA; HPA065032; - MIM; 602677; gene neXtProt; NX_Q99942; - OpenTargets; ENSG00000204308; - PharmGKB; PA34442; - eggNOG; KOG0823; Eukaryota eggNOG; ENOG4111IHV; LUCA GeneTree; ENSGT00390000014107; - HOGENOM; HOG000238304; - HOVERGEN; HBG054495; - InParanoid; Q99942; - KO; K10666; - OMA; TVFNTND; - OrthoDB; EOG091G0W2I; - PhylomeDB; Q99942; - TreeFam; TF317334; - Reactome; R-HSA-382556; ABC-family proteins mediated transport Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC) UniPathway; UPA00143; - GeneWiki; RNF5; - GenomeRNAi; 6048; - PRO; PR:Q99942; - Proteomes; UP000005640; Chromosome 6 Bgee; ENSG00000204308; - CleanEx; HS_RNF5; - ExpressionAtlas; Q99942; baseline and differential Genevisible; Q99942; HS GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell GO; GO:0042802; F:identical protein binding; IPI:IntAct GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:ParkinsonsUK-UCL GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IBA:GO_Central GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB GO; GO:0008270; F:zinc ion binding; TAS:ProtInc GO; GO:0044257; P:cellular protein catabolic process; IMP:UniProtKB GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:UniProtKB GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl GO; GO:0031648; P:protein destabilization; IEA:Ensembl GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB GO; GO:2000785; P:regulation of autophagosome assembly; IEA:Ensembl GO; GO:0009617; P:response to bacterium; IEA:Ensembl GO; GO:0055085; P:transmembrane transport; TAS:Reactome GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IGI:ParkinsonsUK-UCL Gene3D; 3.30.40.10; -; 1 InterPro; IPR001841; Znf_RING InterPro; IPR013083; Znf_RING/FYVE/PHD InterPro; IPR017907; Znf_RING_CS SMART; SM00184; RING; 1 PROSITE; PS00518; ZF_RING_1; 1 PROSITE; PS50089; ZF_RING_2; 1 1: Evidence at protein level; Acetylation; Complete proteome; Endoplasmic reticulum; Membrane; Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome; Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger INIT_MET 1 1 Removed. CHAIN 2 180 E3 ubiquitin-protein ligase RNF5 /FTId=PRO_0000240393 TRANSMEM 118 138 Helical. TRANSMEM 160 180 Helical. ZN_FING 27 68 RING-type. {ECO:0000255|PROSITE- ProRule:PRU00175} MOD_RES 2 2 N-acetylalanine MOD_RES 84 84 Phosphoserine MOD_RES 94 94 Phosphothreonine MOD_RES 107 107 Phosphoserine MUTAGEN 42 42 C->S: Loss of E3 ubiquitin-protein ligase activity. CONFLICT 22 22 G -> S (in Ref. 3; CAB51286) CONFLICT 60 60 E -> D (in Ref. 3; CAB51286) CONFLICT 117 117 T -> A (in Ref. 3; CAB51286) CONFLICT 148 148 T -> A (in Ref. 3; CAB51286) SEQUENCE 180 AA; 19881 MW; E5AFA4DE6DE85942 CRC64; MAAAEEEDGG PEGPNRERGG AGATFECNIC LETAREAVVS VCGHLYCWPC LHQWLETRPE RQECPVCKAG ISREKVVPLY GRGSQKPQDP RLKTPPRPQG QRPAPESRGG FQPFGDTGGF HFSFGVGAFP FGFFTTVFNA HEPFRRGTGV DLGQGHPASS WQDSLFLFLA IFFFFWLLSI
Research Areas
Citations (0)

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Background

The protein encoded by this gene contains a RING finger,which is a motif known to be involved in protein-proteininteractions. This protein is a membrane-bound ubiquitin ligase. Itcan regulate cell motility by targeting paxillin ubiquitination andaltering the distribution and localization of paxillin in cytoplasmand cell focal adhesions.

References

Barcellos, L.F., et al. PLoS Genet. 5 (10), E1000696 (2009) :Tcherpakov, M., et al. J. Biol. Chem. 284(18):12099-12109(2009)Zhong, B., et al. Immunity 30(3):397-407(2009)McKinnon, E., et al. Diabetes Obes Metab 11 SUPPL 1, 92-100 (2009) :Bromberg, K.D., et al. Cancer Res. 67(17):8172-8179(2007)

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$ 80.00
Cat# BP12440c
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