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DNAJA2 Antibody (N-term) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession O60884
Clone Names 100712267
Peptide ID 100712267
Additional Information
Other Names DnaJ homolog subfamily A member 2, Cell cycle progression restoration gene 3 protein, Dnj3, Dj3, HIRA-interacting protein 4, Renal carcinoma antigen NY-REN-14, DNAJA2, CPR3, HIRIP4
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 DNAJA2
Synonyms CPR3, HIRIP4
Function Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877).
Cellular Location Membrane; Lipid-anchor EMBL; AJ001309; CAA04669.1; -; mRNA EMBL; Y13350; CAA73791.1; -; mRNA EMBL; AF011793; AAB69313.1; -; mRNA EMBL; AK313031; BAG35864.1; -; mRNA EMBL; CH471092; EAW82693.1; -; Genomic_DNA EMBL; BC013044; AAH13044.1; -; mRNA EMBL; BC015809; AAH15809.1; -; mRNA CCDS; CCDS10726.1; - RefSeq; NP_005871.1; NM_005880.3 UniGene; Hs.368078; - ProteinModelPortal; O60884; - SMR; O60884; - BioGrid; 115582; 99 CORUM; O60884; - DIP; DIP-33143N; - IntAct; O60884; 61 MINT; O60884; - STRING; 9606.ENSP00000314030; - iPTMnet; O60884; - PhosphoSitePlus; O60884; - SwissPalm; O60884; - BioMuta; DNAJA2; - EPD; O60884; - MaxQB; O60884; - PaxDb; O60884; - PeptideAtlas; O60884; - PRIDE; O60884; - ProteomicsDB; 49650; - DNASU; 10294; - Ensembl; ENST00000317089; ENSP00000314030; ENSG00000069345 GeneID; 10294; - KEGG; hsa:10294; - UCSC; uc002eeo.3; human CTD; 10294; - DisGeNET; 10294; - EuPathDB; HostDB:ENSG00000069345.11; - GeneCards; DNAJA2; - H-InvDB; HIX0173287; - HGNC; HGNC:14884; DNAJA2 HPA; HPA049789; - HPA; HPA060538; - MIM; 611322; gene neXtProt; NX_O60884; - OpenTargets; ENSG00000069345; - PharmGKB; PA27409; - eggNOG; KOG0712; Eukaryota eggNOG; COG0484; LUCA GeneTree; ENSGT00860000133716; - HOGENOM; HOG000226718; - HOVERGEN; HBG066727; - InParanoid; O60884; - KO; K09503; - OMA; KCKGKRT; - OrthoDB; EOG091G0CAC; - PhylomeDB; O60884; - TreeFam; TF105141; - Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) ChiTaRS; DNAJA2; human GeneWiki; DNAJA2; - GenomeRNAi; 10294; - PRO; PR:O60884; - Proteomes; UP000005640; Chromosome 16 Bgee; ENSG00000069345; - CleanEx; HS_DNAJA2; - ExpressionAtlas; O60884; baseline and differential Genevisible; O60884; HS GO; GO:0005829; C:cytosol; IDA:UniProtKB GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell GO; GO:0005524; F:ATP binding; IEA:InterPro GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB GO; GO:0051087; F:chaperone binding; IPI:UniProtKB GO; GO:0031072; F:heat shock protein binding; IEA:InterPro GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc GO; GO:0042026; P:protein refolding; IDA:UniProtKB GO; GO:0009408; P:response to heat; IEA:InterPro CDD; cd06257; DnaJ; 1 CDD; cd10719; DnaJ_zf; 1 Gene3D; 1.10.287.110; -; 1 HAMAP; MF_01152; DnaJ; 1 InterPro; IPR012724; DnaJ InterPro; IPR002939; DnaJ_C InterPro; IPR001623; DnaJ_domain InterPro; IPR018253; DnaJ_domain_CS InterPro; IPR008971; HSP40/DnaJ_pept-bd InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf InterPro; IPR036869; J_dom_sf Pfam; PF00226; DnaJ; 1 Pfam; PF01556; DnaJ_C; 1 Pfam; PF00684; DnaJ_CXXCXGXG; 1 PRINTS; PR00625; JDOMAIN SMART; SM00271; DnaJ; 1 SUPFAM; SSF46565; SSF46565; 1 SUPFAM; SSF49493; SSF49493; 3 SUPFAM; SSF57938; SSF57938; 1 PROSITE; PS00636; DNAJ_1; 1 PROSITE; PS50076; DNAJ_2; 1 PROSITE; PS51188; ZF_CR; 1 1: Evidence at protein level; Acetylation; Chaperone; Complete proteome; Isopeptide bond; Lipoprotein; Membrane; Metal-binding; Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger CHAIN 1 409 DnaJ homolog subfamily A member 2 /FTId=PRO_0000071011 PROPEP 410 412 Removed in mature form. /FTId=PRO_0000393942 DOMAIN 8 70 J REPEAT 143 150 CXXCXGXG motif REPEAT 159 166 CXXCXGXG motif REPEAT 186 193 CXXCXGXG motif REPEAT 202 209 CXXCXGXG motif ZN_FING 130 214 CR-type METAL 143 143 Zinc 1. METAL 146 146 Zinc 1. METAL 159 159 Zinc 2. METAL 162 162 Zinc 2. METAL 186 186 Zinc 2. METAL 189 189 Zinc 2. METAL 202 202 Zinc 1. METAL 205 205 Zinc 1. MOD_RES 39 39 N6-acetyllysine {ECO:0000250|UniProtKB:Q9QYJ0} MOD_RES 78 78 Phosphoserine MOD_RES 123 123 Phosphoserine {ECO:0000250|UniProtKB:O35824} MOD_RES 152 152 N6-acetyllysine {ECO:0000250|UniProtKB:Q9QYJ0} MOD_RES 391 391 Phosphotyrosine MOD_RES 394 394 Phosphoserine MOD_RES 395 395 Phosphoserine MOD_RES 409 409 Cysteine methyl ester. LIPID 409 409 S-farnesyl cysteine CROSSLNK 134 134 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) CONFLICT 17 17 P -> A (in Ref. 2; AAB69313) CONFLICT 42 46 NAGDK -> QMQETN (in Ref. 2; AAB69313) CONFLICT 83 93 GMDDIFSHIFG -> WHGLIFSLTVFC (in Ref. 2; AAB69313). CONFLICT 242 257 GVEPGDIVLLLQEKEH -> EWNPETLFFLLPGEKNM (in Ref. 2; AAB69313). CONFLICT 286 287 FK -> LS (in Ref. 2; AAB69313) CONFLICT 328 328 D -> G (in Ref. 2; AAB69313) SEQUENCE 412 AA; 45746 MW; 8F1BC367425CB428 CRC64; MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA PGVEPGDIVL LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD GRQIVVKYPP GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE VPNIIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ
Research Areas
Citations (0)

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Background

The protein encoded by this gene belongs to theevolutionarily conserved DNAJ/HSP40 family of proteins, whichregulate molecular chaperone activity by stimulating ATPaseactivity. DNAJ proteins may have up to 3 distinct domains: aconserved 70-amino acid J domain, usually at the N terminus; aglycine/phenylalanine (G/F)-rich region; and a cysteine-rich domaincontaining 4 motifs resembling a zinc finger domain. The product ofthis gene works as a cochaperone of Hsp70s in protein folding andmitochondrial protein import in vitro.

References

Walker, V.E., et al. J. Biol. Chem. 285(5):3319-3329(2010)Rosales-Hernandez, A., et al. Cell Stress Chaperones 14(1):71-82(2009)Tzankov, S., et al. J. Biol. Chem. 283(40):27100-27109(2008)Lamesch, P., et al. Genomics 89(3):307-315(2007)Olsen, J.V., et al. Cell 127(3):635-648(2006)

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