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COMMD9 Antibody (C-term) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession Q9P000
Clone Names 100406051
Peptide ID 100406051
Additional Information
Other Names COMM domain-containing protein 9, COMMD9
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
Function May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966). Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits (PubMed:23637203).
Cellular Location Nucleus. Cytoplasmic vesicle
Tissue Location Ubiquitous.. EMBL; AY542164; AAS22246.1; -; mRNA EMBL; AF161515; AAF29130.1; -; mRNA EMBL; AL136688; CAB66623.1; -; mRNA EMBL; AC087277; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BC010892; AAH10892.1; -; mRNA CCDS; CCDS44571.1; -. [Q9P000-2] CCDS; CCDS7900.1; -. [Q9P000-1] RefSeq; NP_001294866.1; NM_001307937.1 RefSeq; NP_054905.2; NM_014186.3. [Q9P000-1] UniGene; Hs.279836; - UniGene; Hs.99443; - PDB; 4NKN; X-ray; 2.79 A; A/B/C/D/E/F=1-116 PDB; 4OE9; X-ray; 1.55 A; A/B=1-117 PDBsum; 4NKN; - PDBsum; 4OE9; - ProteinModelPortal; Q9P000; - SMR; Q9P000; - BioGrid; 118867; 23 CORUM; Q9P000; - IntAct; Q9P000; 10 STRING; 9606.ENSP00000263401; - iPTMnet; Q9P000; - PhosphoSitePlus; Q9P000; - SwissPalm; Q9P000; - BioMuta; COMMD9; - DMDM; 124056492; - EPD; Q9P000; - MaxQB; Q9P000; - PaxDb; Q9P000; - PeptideAtlas; Q9P000; - PRIDE; Q9P000; - ProteomicsDB; 83528; - ProteomicsDB; 83529; -. [Q9P000-2] DNASU; 29099; - Ensembl; ENST00000263401; ENSP00000263401; ENSG00000110442. [Q9P000-1] Ensembl; ENST00000452374; ENSP00000392510; ENSG00000110442. [Q9P000-2] GeneID; 29099; - KEGG; hsa:29099; - UCSC; uc001mwn.5; human. [Q9P000-1] CTD; 29099; - EuPathDB; HostDB:ENSG00000110442.11; - GeneCards; COMMD9; - HGNC; HGNC:25014; COMMD9 HPA; HPA009142; - MIM; 612299; gene neXtProt; NX_Q9P000; - OpenTargets; ENSG00000110442; - PharmGKB; PA134930445; - eggNOG; ENOG410II5T; Eukaryota eggNOG; ENOG4111H94; LUCA GeneTree; ENSGT00390000006218; - HOGENOM; HOG000232004; - HOVERGEN; HBG080522; - InParanoid; Q9P000; - KO; K22565; - OMA; VSTWRTE; - OrthoDB; EOG091G1AK9; - PhylomeDB; Q9P000; - TreeFam; TF323880; - Reactome; R-HSA-6798695; Neutrophil degranulation Reactome; R-HSA-8951664; Neddylation ChiTaRS; COMMD9; human GeneWiki; COMMD9; - GenomeRNAi; 29099; - PRO; PR:Q9P000; - Proteomes; UP000005640; Chromosome 11 Bgee; ENSG00000110442; - CleanEx; HS_COMMD9; - ExpressionAtlas; Q9P000; baseline and differential Genevisible; Q9P000; HS GO; GO:0005829; C:cytosol; IDA:HPA GO; GO:0005576; C:extracellular region; TAS:Reactome GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome GO; GO:0005794; C:Golgi apparatus; IDA:HPA GO; GO:0005634; C:nucleus; IDA:HPA GO; GO:0034774; C:secretory granule lumen; TAS:Reactome GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW InterPro; IPR017920; COMM InterPro; IPR037360; COMMD9 PANTHER; PTHR15663; PTHR15663; 1 Pfam; PF07258; COMM_domain; 1 PROSITE; PS51269; COMM; 1 1: Evidence at protein level; 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasmic vesicle; Ion transport; Nucleus; Reference proteome; Sodium; Sodium transport; Transcription; Transcription regulation; Transport; Ubl conjugation pathway INIT_MET 1 1 Removed. CHAIN 2 198 COMM domain-containing protein 9 /FTId=PRO_0000077403 DOMAIN 122 196 COMM. {ECO:0000255|PROSITE- ProRule:PRU00602} MOD_RES 2 2 N-acetylalanine VAR_SEQ 18 59 Missing (in isoform 2). /FTId=VSP_041499 CONFLICT 45 45 V -> F (in Ref. 3; CAB66623) CONFLICT 161 161 G -> R (in Ref. 1; AAS22246 and 2; AAF29130). HELIX 6 12 {ECO:0000244|PDB:4OE9} HELIX 13 17 {ECO:0000244|PDB:4OE9} HELIX 21 33 {ECO:0000244|PDB:4OE9} HELIX 36 42 {ECO:0000244|PDB:4OE9} HELIX 43 50 {ECO:0000244|PDB:4OE9} HELIX 54 74 {ECO:0000244|PDB:4OE9} HELIX 79 83 {ECO:0000244|PDB:4OE9} HELIX 92 114 {ECO:0000244|PDB:4OE9} SEQUENCE 198 AA; 21819 MW; 54DA2FE525C3A24F CRC64; MAALTAEHFA ALQSLLKASS KDVVRQLCQE SFSSSALGLK KLLDVTCSSL SVTQEEAEEL LQALHRLTRL VAFRDLSSAE AILALFPENF HQNLKNLLTK IILEHVSTWR TEAQANQISL PRLVDLDWRV DIKTSSDSIS RMAVPTCLLQ MKIQEDPSLC GDKPSISAVT VELSKETLDT MLDGLGRIRD QLSAVASK
Research Areas
Citations (0)

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The function of this protein remains unknown.


Burstein, E., et al. J. Biol. Chem. 280(23):22222-22232(2005)

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Cat# BP17500b
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